[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"_public_publisher_byId_b7b8595e-6ad3-492d-9f68-22c0b8181a81":3,"_public_publication_all{\"sortAscending\":false,\"sortField\":\"updateTime\",\"page\":0,\"size\":10,\"facet\":true,\"searchKey\":\"publisherId:b7b8595e-6ad3-492d-9f68-22c0b8181a81,\"}":212},{"code":4,"data":5,"meta":20},"SUCCESS",{"id":6,"createTime":7,"updateTime":8,"relativeEntities":9,"slug":10,"properties":11,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":22,"manageAffiliations":47,"indexDatabases":63,"url":100,"thumbnailPath":20,"statistic":101,"gsStatistic":20,"type":211,"analyzePriority":20},"b7b8595e-6ad3-492d-9f68-22c0b8181a81","2024-04-11T08:24:59.621+00:00","2025-11-21T09:49:19.652+00:00",[],"Biology-of-Metals",{"issn":12,"title":14,"eissn":16},{"VOID":13},"1572-8773",{"EN":15},"Biology of Metals",{"VOID":17},"0933-5854","PUBLISHER","PENDING",null,0,[23,29,35,41],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":25,"label":26,"description":28,"parentId":20,"standard":20,"scholarHubFieldId":20},"d685790f-7c6d-40e3-a211-948b6942dd3a",[],{"EN":27},"Agricultural and Biological Sciences (miscellaneous)",{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":31,"label":32,"description":34,"parentId":20,"standard":20,"scholarHubFieldId":20},"8b99c4f7-9e3a-4557-9a16-ed40d924bde3",[],{"EN":33},"Metals and Alloys",{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":37,"label":38,"description":40,"parentId":20,"standard":20,"scholarHubFieldId":20},"97cdf9a1-b6ca-4a4d-aa74-b136947bc142",[],{"EN":39},"Biochemistry, Genetics and Molecular Biology (miscellaneous)",{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":43,"label":44,"description":46,"parentId":20,"standard":20,"scholarHubFieldId":20},"fa7cc0d7-835f-4e75-8db2-b781f243f317",[],{"EN":45},"Biomaterials",{},[48,56],{"id":49,"createTime":20,"updateTime":20,"relativeEntities":50,"slug":20,"properties":51,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":54,"statistic":20},"b2bfac93-563a-4fa4-bd81-e546a66bf9bd",[],{"title":52},{"EN":53},"Springer Netherlands",[55],"9a7c7208-b28a-42c2-a634-5a7f90eee3ab",{"id":57,"createTime":20,"updateTime":20,"relativeEntities":58,"slug":20,"properties":59,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":62,"statistic":20},"26a19206-5cad-4456-bb2f-49abd254fbc6",[],{"title":60},{"EN":61},"SPRINGER",[],[64,80],{"id":65,"indexDatabase":66,"url":20,"indexYears":20,"academicFieldIds":78,"indexDatabaseRanking":20},"6af723a3-26ba-4a31-a88f-171e525100c2",{"id":67,"createTime":20,"updateTime":20,"relativeEntities":68,"label":69,"description":71,"key":74,"publicationTags":75,"standard":20},"a4921856-b128-4d9f-8f1f-e80813d3bbd4",[],{"EN":70,"VI":70},"ISI\u002FSCIE - Science Citation Index Expanded",{"EN":72,"VI":73},"SCIE database","Cơ sở dữ liệu SCIE","scie",[76,77],"SCIE","ISI",[79],"10e9c71e-2256-419c-bdd2-a39e436e76e3",{"id":81,"indexDatabase":82,"url":92,"indexYears":93,"academicFieldIds":94,"indexDatabaseRanking":99},"ff1993bc-b7a8-463b-9fd9-cc6b14d2c685",{"id":83,"createTime":20,"updateTime":20,"relativeEntities":84,"label":85,"description":87,"key":89,"publicationTags":90,"standard":20},"3c7051d4-eb7d-4c57-a56b-36fc74c5d1e9",[],{"EN":86,"VI":86},"Scopus - Elsevier",{"EN":86,"VI":88},"Cơ sở dữ liệu Scopus thuộc Elsevier","scopus",[91],"SCOPUS","https:\u002F\u002Fwww.scopus.com\u002Fsourceid\u002F16919","1992-2025",[95,96,97,98],"8e5f5f89-df86-44a7-bb58-d8bad424ac5f","bf9d84ae-c584-4211-b4aa-5016d0d5d064","46e59dee-8fba-48b3-99a3-4ef8dad73953","570c01f4-de10-4d9b-b20a-a406753e4d65","SCOPUS__Q1","https:\u002F\u002Flink.springer.com\u002Fjournal\u002F10534",{"impactFactor":21,"impactFactorByYear":102,"i10Index":113,"i10IndexLast5Year":114,"totalPublication":115,"totalPublicationByYear":116,"totalCitation":151,"totalCitationByYear":152,"totalCitationPerPublication":181,"totalCitationPerPublicationByYear":182,"hindexLast5Year":123,"hindex":123},{"2012":103,"2013":104,"2014":105,"2015":103,"2016":106,"2017":107,"2018":108,"2019":105,"2020":109,"2021":110,"2022":111,"2023":112},0.65,0.39,0.7,0.36,0.47,0.58,0.57,0.42,0.32,0.93,368,38,3575,{"1988":117,"1989":118,"1990":119,"1991":120,"1992":121,"1993":122,"1994":123,"1995":124,"1996":125,"1997":126,"1998":127,"1999":128,"2000":129,"2001":130,"2002":131,"2003":132,"2004":133,"2005":134,"2006":135,"2007":136,"2008":132,"2009":137,"2010":138,"2011":139,"2012":140,"2013":141,"2014":142,"2015":143,"2016":143,"2017":144,"2018":145,"2019":146,"2020":129,"2021":147,"2022":148,"2023":149,"2024":150},23,29,85,62,53,44,56,92,94,45,72,69,64,51,59,75,147,83,127,138,152,146,151,145,125,171,122,130,115,87,144,167,126,42,14267,{"1989":153,"1990":154,"1991":155,"1992":156,"1993":157,"1994":158,"1995":159,"1996":160,"2004":161,"2005":162,"2006":163,"2007":164,"2008":165,"2009":166,"2010":167,"2011":168,"2012":169,"2013":170,"2014":171,"2015":172,"2016":173,"2017":174,"2018":175,"2019":176,"2020":177,"2021":178,"2022":179,"2023":180},166,18,168,326,78,335,253,580,4,1177,252,1568,202,1121,1618,787,774,926,728,491,778,601,304,242,76,223,284,185,3.99,{"1989":183,"1990":184,"1991":185,"1992":186,"1993":187,"1994":188,"1995":189,"1996":190,"2004":191,"2005":192,"2006":193,"2007":194,"2008":195,"2009":196,"2010":197,"2011":198,"2012":199,"2013":200,"2014":201,"2015":202,"2016":203,"2017":204,"2018":205,"2019":206,"2020":207,"2021":208,"2022":209,"2023":210},5.72,0.21,2.71,6.15,1.77,5.98,2.75,6.17,0.03,14.18,1.98,11.36,2.69,7.38,11.08,5.21,5.34,7.41,4.26,4.02,6.38,4.62,2.64,2.78,1.19,1.55,1.7,1.47,"JOURNAL",{"meta":213,"data":215},{"total":214},"1658",[216,363,465,622,974,1121,1221,1389,2042,2327],{"id":217,"createTime":218,"updateTime":219,"relativeEntities":220,"slug":221,"properties":222,"entityType":233,"verifyStatus":234,"verifyTime":235,"verifyNote":236,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":237,"fullTextUrl":20,"authors":238,"publicationType":291,"publisherRelationship":292,"citationCount":352,"citationInfo":353,"publishDate":358,"publishYear":354,"citationAnalyzeStatus":359,"lastCitationAnalyze":360,"indexDatabases":361,"openAccess":20,"references":20,"isForceReanalyzing":362},"688e5828-f475-491f-8166-a5adaa77320e","2023-12-02T19:26:02.546+00:00","2026-07-27T20:55:04.510+00:00",[],"Metal-responsive-gene-regulation-and-metal-transport-in-Helicobacter-species",{"abstract":223,"title":225,"gsPaper":227,"references":229,"doi":231},{"EN":224},"\n                        Helicobacter species are among the most successful colonizers of the mammalian gastrointestinal and hepatobiliary tract. Colonization is usually lifelong, indicating that Helicobacter species have evolved intricate mechanisms of dealing with stresses encountered during colonization of host tissues, like restriction of essential metal ions. The recent availability of genome sequences of the human gastric pathogen Helicobacter pylori, the murine enterohepatic pathogen Helicobacter hepaticus and the unannotated genome sequence of the ferret gastric pathogen Helicobacter mustelae has allowed for comparitive genome analyses. In this review we present such analyses for metal transporters, metal-storage and metal-responsive regulators in these three Helicobacter species, and discuss possible contributions of the differences in metal metabolism in adaptation to the gastric or enterohepatic niches occupied by Helicobacter species.",{"EN":226},"Metal-responsive gene regulation and metal transport in Helicobacter species",{"VOID":228},"[\"207429816219721871\"]",{"VOID":230},"Alm RA, Ling LS, Moir DT, King BL, Brown ED, Doig PC, Smith DR, Noonan B, Guild BC, deJonge BL, Carmel G, Tummino PJ, Caruso A, Uria-Nickelsen M, Mills DM, Ives C, Gibson R, Merberg D, Mills SD, Jiang Q, Taylor DE, Vovis GF, Trust TJ (1999) Genomic-sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori. Nature 397:176–180\nAndrews SC, Robinson AK, Rodriguez-Quinones F (2003) Bacterial iron homeostasis. FEMS Microbiol Rev 27:215–237\nBaker LM, Raudonikiene A, Hoffman PS, Poole LB (2001) Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization. J Bacteriol 183:1961–1973\nBarnard FM, Loughlin MF, Fainberg HP, Messenger MP, Ussery DW, Williams P, Jenks PJ (2004) Global regulation of virulence and the stress response by CsrA in the highly adapted human gastric pathogen Helicobacter pylori. Mol Microbiol 51:15–32\nBauerfeind P, Garner RM, Mobley HLT (1996) Allelic exchange mutagenesis of nixA in Helicobacter pylori results in reduced nickel transport and urease activity. Infect Immun 64:2877–2880\nBayle D, Wangler S, Weitzenegger T, Steinhilber W, Volz J, Przybylski M, Schafer KP, Sachs G, Melchers K (1998) Properties of the P-type ATPases encoded by the copAP operons of Helicobacter pylori and Helicobacter felis. J Bacteriol 180:317–329\nBeckwith CS, McGee DJ, Mobley HL, Riley LK (2001) Cloning, expression, and catalytic activity of Helicobacter hepaticus urease. Infect Immun 69:5914–5920\nBeier D, Spohn G, Rappuoli R, Scarlato V (1997) Identification and characterization of an operon of Helicobacter pylori that is involved in motility and stress adaptation. J Bacteriol 179:4676–4683\nBelzer C, Stoof J, Beckwith CS, Kuipers EJ, Kusters JG, van Vliet AHM (2005a) Differential regulation of urease activity in Helicobacter hepaticus and Helicobacter pylori. Microbiology 151:3989–3995\nBelzer C, van Schendel BAM, Kuipers EJ, Hoogenboezem T, Hermans PWM, Kusters JG, van Vliet AHM (2005b) PerR is a regulator of oxidative stress defense in Helicobacter hepaticus. Helicobacter 10:548\nBelzer C, van Schendel BAM, Kuipers EJ, Kusters JG, van Vliet AHM (2007) Iron-responsive repression of urease expression in Helicobacter hepaticus is mediated by the transcriptional regulator Fur. Infect Immun 75:745–752\nBereswill S, Strobel S, Lichte F, Fassbinder F, Hantke K, Kist M (1997) Evaluation of microbiological parameters for the study of iron metabolism in Helicobacter pylori. Gut 41(S1):A10\nBereswill S, Lichte F, Vey T, Fassbinder F, Kist M (1998a) Cloning and characterization of the fur gene from Helicobacter pylori. FEMS Microbiol Lett 159:193–200\nBereswill S, Waidner U, Odenbreit S, Lichte F, Fassbinder F, Bode G, Kist M (1998b) Structural, functional and mutational analysis of the pfr gene encoding a ferritin from Helicobacter pylori. Microbiology 144:2505–2516\nBlaser MJ, Atherton JC (2004) Helicobacter pylori persistence: biology and disease. J Clin Invest 113:321–333\nBsat N, Herbig A, Casillas-Martinez L, Setlow P, Helmann JD (1998) Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors. Mol Microbiol 29:189–198\nBury-Mone S, Thiberge JM, Contreras M, Maitournam A, Labigne A, De Reuse H (2004) Responsiveness to acidity via metal ion regulators mediates virulence in the gastric pathogen Helicobacter pylori. Mol Microbiol 53:623–638\nCarson SD, Klebba PE, Newton SM, Sparling PF (1999) Ferric enterobactin binding and utilization by Neisseria gonorrhoeae. J Bacteriol 181:2895–2901\nChivers PT, Sauer RT (2000) Regulation of high-affinity nickel uptake in bacteria: Ni2+- dependent interaction of NikR with wild-type and mutant operator sites. J␣Biol Chem 275:19735–19741\nChristensen JM, Kristiansen J, Nielsen NH, Menne T, Byrialsen K (1999) Nickel concentrations in serum and urine of patients with nickel eczema. Toxicol Lett 108:185–189\nDavis GS, Mobley HL (2005) Contribution of dppA to urease activity in Helicobacter pylori 26695. Helicobacter 10:416–423\nDe Pina K, Desjardin V, Mandrand-Berthelot MA, Giordano G, Wu LF (1999) Isolation and characterization of the nikR gene encoding a nickel-responsive regulator in Escherichia coli. J Bacteriol 181:670–674\nDelany I, Pacheco ABF, Spohn G, Rappuoli R, Scarlato V (2001a) Iron-dependent transcription of the frpB gene of Helicobacter pylori is controlled by the Fur protein. J Bacteriol 183:4932–4937\nDelany I, Spohn G, Rappuoli R, Scarlato V (2001b) The Fur repressor controls transcription of iron-activated and -repressed genes in Helicobacter pylori. Mol Microbiol 42:1297–1309\nDelany I, Ieva R, Soragni A, Hilleringmann M, Rappuoli R, Scarlato V (2005) In vitro analysis of protein-operator interactions of the NikR and Fur metal-responsive regulators of coregulated genes in Helicobacter pylori. J Bacteriol 187:7703–7715\nDhaenens L, Szczebara F, Van Nieuwenhuyse S, Husson MO (1999) Comparison of iron uptake in different Helicobacter species. Res Microbiol 150:475–481\nEppinger M, Baar C, Raddatz G, Huson DH, Schuster SC (2004) Comparative analysis of four Campylobacterales. Nat Rev Microbiol 2:872–885\nErnst FD, Homuth G, Stoof J, Mader U, Waidner B, Kuipers EJ, Kist M, Kusters JG, Bereswill S, van Vliet AHM (2005a) Iron-responsive regulation of the Helicobacter pylori iron-cofactored superoxide dismutase SodB is mediated by Fur. J Bacteriol 187:3687–3692\nErnst FD, Stoof J, Horrevoets JM, Kuipers EJ, Kusters JG, van Vliet AHM (2006) NikR mediates nickel-responsive transcriptional repression of the Helicobacter pylori outer merribrane proteins FecA3 (HP1400) and FrpB4 (HP1512). Infect Immun 74: 6821–6828\nErnst FD, Kuipers EJ, Heijens A, Sarwari R, Stoof J, Penn CW, Kusters JG, van Vliet AHM (2005c) The nickel-responsive regulator NikR controls activation and repression of gene transcription in Helicobacter pylori. Infect Immun 73:7252–7258\nEscolar L, Perez-Martin J, de Lorenzo V (1999) Opening the iron-box: transcriptional metalloregulation by the Fur protein. J Bacteriol 181:6223–6229\nFox JG (2002) The non- H. pylori helicobacters: their expanding role in gastrointestinal and systemic diseases. Gut 50:273–283\nGe R, Watt RM, Sun X, Tanner JA, He QY, Huang JD, Sun H (2006) Expression and characterization of a histidine-rich protein, Hpn: potential for Ni2+ storage in Helicobacter pylori. Biochem J 393:285–293\nGilbert JV, Ramakrishna J, Sunderman FW Jr, Wright A, Plaut AG (1995) Protein Hpn: cloning and characterization of a histidine-rich metal–binding polypeptide in Helicobacter pylori and Helicobacter mustelae. Infect Immun 63:2682–2688\nHantke K (2001) Iron and metal regulation in bacteria. Curr Opin Microbiol 4:172–177\nHarris AG, Hinds FE, Beckhouse AG, Kolesnikow T, Hazell SL (2002) Resistance to hydrogen peroxide in Helicobacter pylori: role of catalase (KatA) and Fur, and functional analysis of a novel gene product designated ‘KatA-associated protein’ KapA (HP0874). Microbiology 148:3813–3825\nHarris AG, Wilson JE, Danon SJ, Dixon MF, Donegan K, Hazell SL (2003) Catalase (KatA) and KatA-associated protein (KapA) are essential to persistent colonization in the Helicobacter pylori SS1 mouse model. Microbiology 149:665–672\nHendricks JK, Mobley HL (1997) Helicobacter pylori ABC transporter: effect of allelic exchange mutagenesis on urease activity. J Bacteriol 179:5892–5902\nHerbig AF, Helmann JD (2001) Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA. Mol Microbiol 41:849–859\nHerrmann L, Schwan D, Garner R, Mobley HL, Haas R, Schafer KP, Melchers K (1999) Helicobacter pylori cadA encodes an essential Cd(II)-Zn(II)-Co(II) resistance factor influencing urease activity. Mol Microbiol 33:524–536\nHong Y, Wang G, Maier RJ (2006) Helicobacter hepaticus Dps protein plays an important role in protecting DNA from oxidative damage. Free Radic Res Suppl:1\nKansau I, Guillain F, Thiberge JM, Labigne A (1996) Nickel binding and immunological properties of the C-terminal domain of the Helicobacter pylori GroES homologue (HspA). Mol Microbiol 22:1013–1023\nLoh JT, Cover TL (2006) Requirement of histidine kinases HP0165 and HP1364 for acid resistance in Helicobacter pylori. Infect Immun 74:3052–3059\nMaier RJ, Olson J, Olczak A (2003) Hydrogen-oxidizing capabilities of Helicobacter hepaticus and in␣vivo availability of the substrate. J Bacteriol 185:2680–2682\nMasse E, Gottesman S (2002) A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc Natl Acad Sci USA 99:4620–4625\nMaurer KJ, Ihrig MM, Rogers AB, Ng V, Bouchard G, Leonard MR, Carey MC, Fox JG (2005) Identification of cholelithogenic enterohepatic Helicobacter species and their role in murine cholesterol gallstone formation. Gastroenterology 128:1023–1033\nMehta NS, Benoit S, Mysore JV, Sousa RS, Maier RJ (2005) Helicobacter hepaticus hydrogenase mutants are deficient in hydrogen-supported amino acid uptake and in causing liver lesions in A\u002FJ mice. Infect Immun 73:5311–5318\nMelchers K, Weitzenegger T, Buhmann A, Steinhilber W, Sachs G, Schafer KP (1996) Cloning and membrane topology of a P type ATPase from Helicobacter pylori. J Biol Chem 271:446–457\nMelchers K, Herrmann L, Mauch F, Bayle D, Heuermann D, Weitzenegger T, Schuhmacher A, Sachs G, Haas R, Bode G, Bensch K, Schafer KP (1998) Properties and function of the P type ion pumps cloned from Helicobacter pylori. Acta Physiol Scand Suppl 643:123–135\nMobley HL, Garner RM, Bauerfeind P (1995) Helicobacter pylori nickel-transport gene nixA: synthesis of catalytically active urease in Escherichia coli independent of growth conditions. Mol Microbiol 16:97–109\nMobley HL, Garner RM, Chippendale GR, Gilbert JV, Kane AV, Plaut AG (1999) Role of Hpn and NixA of Helicobacter pylori in susceptibility and resistance to bismuth and other metal ions. Helicobacter 4:162–169\nNavarro C, Wu LF, Mandrand-Berthelot MA (1993) The nik operon of Escherichia coli encodes a periplasmic binding-protein-dependent transport system for nickel. Mol Microbiol 9:1181–1191\nNolan KJ, McGee DJ, Mitchell HM, Kolesnikow T, Harro JM, O’Rourke J, Wilson JE, Danon SJ, Moss ND, Mobley HL, Lee A (2002) In vivo behavior of a Helicobacter pylori SS1 nixA mutant with reduced urease activity. Infect Immun 70:685–691\nOlczak AA, Olson JW, Maier RJ (2002) Oxidative-stress resistance mutants of Helicobacter pylori. J Bacteriol 184:3186–3193\nOlczak AA, Seyler RW Jr, Olson JW, Maier RJ (2003) Association of Helicobacter pylori antioxidant activities with host colonization proficiency. Infect Immun 71:580–583\nPalyada K, Threadgill D, Stintzi A (2004) Iron acquisition and regulation in Campylobacter jejuni. J Bacteriol 186:4714–4729\nPanthel K, Dietz P, Haas R, Beier D (2003) Two-component systems of Helicobacter pylori contribute to virulence in a mouse infection model. Infect Immun 71:5381–5385\nParkhill J, Wren BW, Mungall K, Ketley JM, Churcher C, Basham D, Chillingworth T, Davies RM, Feltwell T, Holroyd S, Jagels K, Karlyshev AV, Moule S, Pallen MJ, Penn CW, Quail MA, Rajandream MA, Rutherford KM, van Vliet AHM, Whitehead S, Barrell BG (2000) The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences. Nature 403:665–668\nPerez-Perez GI, Gower CB, Blaser MJ (1994) Effects of cations on Helicobacter pylori urease activity, release, and stability. Infect Immun 62:299–302\nSeyler RW Jr, Olson JW, Maier RJ (2001) Superoxide dismutase-deficient mutants of Helicobacter pylori are hypersensitive to oxidative stress and defective in host colonization. Infect Immun 69:4034–4040\nSolnick JV, Schauer DB (2001) Emergence of diverse Helicobacter species in the pathogenesis of gastric and enterohepatic diseases. Clin Microbiol Rev 14:59–97\nStähler FN, Odenbreit S, Haas R, Wilrich J, van Vliet AHM, Kusters JG, Kist M, Bereswill S (2006) The novel Helicobacter pylori CznABC metal efflux pump is required for cadmium, zinc and nickel resistance, for urease modulation and for gastric colonization. Infect Immun 74:3845–3852\nStoof J, Kuipers EJ, Kusters JG, van Vliet AHM (2005) Fur mediates regulation of iron-uptake genes in Helicobacter mustelae. Helicobacter 10:465\nSuerbaum S, Josenhans C, Sterzenbach T, Drescher B, Brandt P, Bell M, Droge M, Fartmann B, Fischer HP, Ge Z, Horster A, Holland R, Klein K, Konig J, Macko L, Mendz GL, Nyakatura G, Schauer DB, Shen Z, Weber J, Frosch M, Fox JG (2003) The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus. Proc Natl Acad Sci USA 100:7901–7906\nSunderman FW (1993) Biological monitoring of nickel in humans. Scand J Work Environm Health 19:34–38\nTomb JF, White O, Kerlavage AR, Clayton RA, Sutton GG, Fleischmann RD, Ketchum KA, Klenk HP, Gill S, Dougherty BA, Nelson K, Quackenbush J, Zhou L, Kirkness EF, Peterson S, Loftus B, Richardson D, Dodson R, Khalak HG, Glodek A, McKenney K, Fitzegerald LM, Lee N, Adams MD, Hickey EK, Berg DE, Gocayne JD, Utterback TR, Peterson JD, Kelley JM, Cotton MD, Weidman JM, Fujii C, Bowman C, Watthey L, Wallin E, Hayes WS, Borodovsky M, Karpk PD, Smith HO, Fraser CM, Venter JC (1997) The complete genome sequence of the gastric pathogen Helicobacter pylori. Nature 388:539–547\nTonello F, Dundon WG, Satin B, Molinari M, Tognon G, Grandi G, del Guicide G, Rappuoli R, Montecucco C (1999) The Helicobacter pylori neutrophil-activating protein is an iron-binding protein with dodecameric structure. Mol Microbiol 34:238–246\nvan Amsterdam K, Bart A, van der Ende A (2005) A Helicobacter pylori TolC efflux pump confers resistance to metronidazole. Antimicrob Agents Chemother 49:1477–1482\nvan Vliet AHM, Wooldridge KG, Ketley JM (1998) Iron-responsive gene regulation in a Campylobacter jejuni fur mutant. J Bacteriol 180:5291–5298\nvan Vliet AH, Baillon ML, Penn CW, Ketley JM (1999) Campylobacter jejuni contains two Fur homologs: characterization of iron-responsive regulation of peroxide stress defense genes by the PerR repressor. J␣Bacteriol 181:6371–6376\nvan Vliet AHM, Bereswill S, Kusters JG (2001) Ion metabolism and transport. In: Mobley HLT, Mendz GL, Hazell SL (eds) Helicobacter pylori: physiology and genetics. ASM Press, Washington, DC, pp 193–206\nvan Vliet AHM, Poppelaars SW, Davies BJ, Stoof J, Bereswill S, Kist M, Kuipers EJ, Penn CW, Kusters JG (2002a) NikR mediates nickel-responsive transcriptional induction of urease expression in Helicobacter pylori. Infect Immun 70:2846–2852\nvan Vliet AHM, Stoof J, Vlasblom R, Wainwright SA, Hughes NJ, Kelly DJ, Bereswill S, Bijlsma JJE, Hoogenboezem T, Vandenbroucke-Grauls CMJE, Kist M, Kuipers EJ, Kusters JG (2002b) The role of the ferric uptake regulator (Fur) in regulation of Helicobacter pylori iron uptake. Helicobacter 7:237–244\nvan Vliet AHM, Stoof J, Poppelaars SW, Bereswill S, Homuth G, Kist M, Kuipers EJ, Kusters JG (2003) Differential regulation of amidase- and formamidase-mediated ammonia production by the Helicobacter pylori Fur repressor. J Biol Chem 278:9052–9057\nvan Vliet AHM, Ernst FD, Kusters JG (2004a) NikR-mediated regulation of Helicobacter pylori acid adaptation. Trends Microbiol 12:489–494\nvan Vliet AHM, Kuipers EJ, Stoof J, Poppelaars SW, Kusters JG (2004b) Acid-responsive gene induction of ammonia-producing enzymes in Helicobacter pylori is mediated via a metal-responsive repressor cascade. Infect Immun 72:766–773\nVelayudhan J, Hughes NJ, McColm AA, Bagshaw J, Clayton CL, Andrews SC, Kelly DJ (2000) Iron acquisition and virulence in Helicobacter pylori: a major role for FeoB, a high-affinity ferrous iron transporter. Mol Microbiol 37:274–286\nWaidner B, Greiner S, Odenbreit S, Kavermann H, Velayudhan J, Stähler F, Bisse E, van Vliet AHM, Andrews SC, Kusters JG, Kelly DJ, Haas R, Kist M, Bereswill S (2002a) Essential role of ferritin Pfr in Helicobacter pylori iron metabolism and gastric colonization. Infect Immun 70:3923–3929\nWaidner B, Melchers K, Ivanov I, Loferer H, Bensch KW, Kist M, Bereswill S (2002b) Identification by RNA profiling and mutational analysis of the novel copper resistance determinants CrdA (HP1326), CrdB (HP1327), and CzcB (HP1328) in Helicobacter pylori. J Bacteriol 184:6700–6708\nWaidner B, Melchers K, Stahler FN, Kist M, Bereswill S (2005) The Helicobacter pylori CrdRS two-component regulation system (HP1364\u002FHP1365) is required for copper-mediated induction of the copper resistance determinant CrdA. J Bacteriol 187:4683–4688\nWang G, Conover RC, Benoit S, Olczak AA, Olson JW, Johnson MK, Maier RJ (2004) Role of a bacterial organic hydroperoxide detoxification system in preventing catalase inactivation. J Biol Chem 279:51908–51914",{"VOID":232},"10.1007\u002Fs10534-006-9028-9","PUBLICATION","VERIFIED","2024-09-13T09:03:23.046+00:00","Auto Verify","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10534-006-9028-9",[239,257,275],{"id":240,"sortIndex":21,"researcher":20,"roles":241,"affiliations":243,"properties":252},"3c6268fd-0948-49f5-b99f-dd58e531b585",[242],"AUTHOR",[244],{"id":245,"sortIndex":21,"affiliation":246,"properties":20},"e25a925f-5689-4be6-8d68-56b807c0bdff",{"id":245,"createTime":20,"updateTime":20,"relativeEntities":247,"slug":20,"properties":248,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":251,"statistic":20},[],{"title":249},{"VI":250},"Department of Gastroenterology and Hepatology, Erasmus MC-University Medical Center, Rotterdam, the Netherlands",[],{"title":253,"gsAuthor":255},{"VI":254},"Clara Belzer",{"VOID":256},"[\"psmY03gAAAAJ\"]",{"id":258,"sortIndex":259,"researcher":20,"roles":260,"affiliations":261,"properties":270},"d2c9f419-ce74-497e-9261-788b6c56ee91",1,[242],[262],{"id":263,"sortIndex":21,"affiliation":264,"properties":20},"18013677-618b-476a-89e6-1a93f6c50535",{"id":263,"createTime":20,"updateTime":20,"relativeEntities":265,"slug":20,"properties":266,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":269,"statistic":20},[],{"title":267},{"VI":268},"Department of Gastroenterology and Hepatology, ERASMUS MC, University Medical Center Rotterdam, The Netherlands",[],{"title":271,"gsAuthor":273},{"VI":272},"Jeroen Stoof",{"VOID":274},"[\"LsClSL4AAAAJ\"]",{"id":276,"sortIndex":277,"researcher":20,"roles":278,"affiliations":279,"properties":286},"87ccc655-9b0f-4994-8cda-e02398729525",2,[242],[280],{"id":245,"sortIndex":21,"affiliation":281,"properties":20},{"id":245,"createTime":20,"updateTime":20,"relativeEntities":282,"slug":20,"properties":283,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":285,"statistic":20},[],{"title":284},{"VI":250},[],{"title":287,"gsAuthor":289},{"VI":288},"Arnoud H. M. van Vliet",{"VOID":290},"[\"k2ybOhoAAAAJ\"]","ARTICLE",{"url":237,"publisher":293,"properties":347},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":294,"slug":10,"properties":295,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":299,"manageAffiliations":316,"indexDatabases":327,"url":100,"thumbnailPath":20,"statistic":342,"gsStatistic":20,"type":211,"analyzePriority":20},[],{"issn":296,"title":297,"eissn":298},{"VOID":13},{"EN":15},{"VOID":17},[300,304,308,312],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":301,"label":302,"description":303,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":305,"label":306,"description":307,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":309,"label":310,"description":311,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":313,"label":314,"description":315,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},[317,322],{"id":49,"createTime":20,"updateTime":20,"relativeEntities":318,"slug":20,"properties":319,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":321,"statistic":20},[],{"title":320},{"EN":53},[55],{"id":57,"createTime":20,"updateTime":20,"relativeEntities":323,"slug":20,"properties":324,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":326,"statistic":20},[],{"title":325},{"EN":61},[],[328,335],{"id":65,"indexDatabase":329,"url":20,"indexYears":20,"academicFieldIds":334,"indexDatabaseRanking":20},{"id":67,"createTime":20,"updateTime":20,"relativeEntities":330,"label":331,"description":332,"key":74,"publicationTags":333,"standard":20},[],{"EN":70,"VI":70},{"EN":72,"VI":73},[76,77],[79],{"id":81,"indexDatabase":336,"url":92,"indexYears":93,"academicFieldIds":341,"indexDatabaseRanking":99},{"id":83,"createTime":20,"updateTime":20,"relativeEntities":337,"label":338,"description":339,"key":89,"publicationTags":340,"standard":20},[],{"EN":86,"VI":86},{"EN":86,"VI":88},[91],[95,96,97,98],{"impactFactor":21,"impactFactorByYear":343,"i10Index":113,"i10IndexLast5Year":114,"totalPublication":115,"totalPublicationByYear":344,"totalCitation":151,"totalCitationByYear":345,"totalCitationPerPublication":181,"totalCitationPerPublicationByYear":346,"hindexLast5Year":123,"hindex":123},{"2012":103,"2013":104,"2014":105,"2015":103,"2016":106,"2017":107,"2018":108,"2019":105,"2020":109,"2021":110,"2022":111,"2023":112},{"1988":117,"1989":118,"1990":119,"1991":120,"1992":121,"1993":122,"1994":123,"1995":124,"1996":125,"1997":126,"1998":127,"1999":128,"2000":129,"2001":130,"2002":131,"2003":132,"2004":133,"2005":134,"2006":135,"2007":136,"2008":132,"2009":137,"2010":138,"2011":139,"2012":140,"2013":141,"2014":142,"2015":143,"2016":143,"2017":144,"2018":145,"2019":146,"2020":129,"2021":147,"2022":148,"2023":149,"2024":150},{"1989":153,"1990":154,"1991":155,"1992":156,"1993":157,"1994":158,"1995":159,"1996":160,"2004":161,"2005":162,"2006":163,"2007":164,"2008":165,"2009":166,"2010":167,"2011":168,"2012":169,"2013":170,"2014":171,"2015":172,"2016":173,"2017":174,"2018":175,"2019":176,"2020":177,"2021":178,"2022":179,"2023":180},{"1989":183,"1990":184,"1991":185,"1992":186,"1993":187,"1994":188,"1995":189,"1996":190,"2004":191,"2005":192,"2006":193,"2007":194,"2008":195,"2009":196,"2010":197,"2011":198,"2012":199,"2013":200,"2014":201,"2015":202,"2016":203,"2017":204,"2018":205,"2019":206,"2020":207,"2021":208,"2022":209,"2023":210},{"pages":348,"volume":350},{"VOID":349},"417-429",{"VOID":351},"20",22,{"total":352,"publishYear":354,"statisticByYear":355},2007,{"2008":356,"2009":357,"2010":277,"2011":277,"2012":259,"2013":259,"2014":259,"2015":161,"2016":259,"2018":259,"2021":259},5,3,"2007-02-09","DONE_ANALYZE_CITATION","2026-07-27T20:55:04.509+00:00",[76,99],false,{"id":364,"createTime":365,"updateTime":366,"relativeEntities":367,"slug":368,"properties":369,"entityType":233,"verifyStatus":234,"verifyTime":380,"verifyNote":236,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":381,"fullTextUrl":20,"authors":382,"publicationType":291,"publisherRelationship":400,"citationCount":21,"citationInfo":460,"publishDate":463,"publishYear":461,"citationAnalyzeStatus":19,"lastCitationAnalyze":366,"indexDatabases":464,"openAccess":20,"references":20,"isForceReanalyzing":362},"c92bad71-dbc9-4585-8133-194fe71b210a","2024-01-14T17:21:19.494+00:00","2026-07-21T07:12:36.972+00:00",[],"Mercury-resistance-in-Sporosarcina-sp-G3",{"abstract":370,"title":372,"gsPaper":374,"references":376,"doi":378},{"EN":371},"Mercuric reductase (MerA) enzyme plays an important role in biogeochemical cycling and detoxification of Hg and recently, has also been shown to be useful in clean up of Hg-contaminated effluents. Present study describes isolation of a heavy metal-resistant isolate of Sporosarcina, which could tolerate up to 40, 525, 210, 2900 and 370 μM of Cd, Co, Zn, Cr and Hg respectively. It was found to reduce and detoxify redox-active metals like Cr and Hg. The chromate reductase and MerA activities in the crude cell extract of the culture were 1.5 and 0.044 units\u002Fmg protein respectively. The study also describes designing of a new set of highly degenerate primers based on a dataset of 23 Firmicute merA genes. As the primers encompass the known diversity of merA genes within the phylum Firmicutes, they can be very useful for functional diversity analysis. They were successfully used to amplify a 787 bp merA fragment from the current isolate. A 1174 bp merA fragment was further cloned by designing an additional downstream primer. It was found to show 92% similarity to the putative merA gene from Bacillus cereus AH820. To the best of our knowledge, this is the first report of mercury resistance and merA gene sequence from Sporosarcina.",{"EN":373},"Mercury resistance in Sporosarcina sp. G3",{"VOID":375},"[\"766079713174398850\"]",{"VOID":377},"Altschul SF, Madden TL, Schäffer AA et al (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25:3389–3402\nAPHA (1989) Standard methods for the examination of water and wastewater, 17th edn. American Public Health Association, Washington, DC\nAttwood TK, Bradley P, Flower DR et al (2003) PRINTS and its automatic supplement, prePRINTS. Nucleic Acids Res 31:400–402\nBailey TL, Elkan C (1994) Fitting a mixture model by expectation maximization to discover motifs in biopolymers. Proc Int Conf Intell Syst Mol Biol 2:28–36\nChadhain SMN, Schaefer JK, Crane S et al (2006) Analysis of mercuric reductase (merA) gene diversity in an anaerobic mercury-contaminated sediment enrichment. Environ Microbiol 8:1746–1752\nChatziefthimiou AD, Crespo-Medina M, Wang Y et al (2007) The isolation and initial characterization of mercury resistant chemolithotrophic thermophilic bacteria from mercury rich geothermal springs. Extremophiles 11:469–479\nEdwards U, Rogall T, Blöcker H et al (1989) Isolation and direct complete nucleotide determination of entire genes. Characterization of a gene coding for 16S ribosomal RNA. Nucleic Acids Res 17:7843–7853\nFelsenstein J (2009) PHYLIP (phylogeny inference package) version 3.69. Distributed by the author. Department of Genetics, University of Washington, Seattle\nFox B, Walsh CT (1982) Mercuric reductase: purification and characterization of a transposon-encoded flavoprotein containing an oxidation-reduction-active disulfide. J Biol Chem 257:2498–2503\nHylander LD, Goodsite ME (2006) Environmental costs of mercury pollution. Sci Total Environ 368:352–370\nJan AT, Murtaza I, Ali A et al (2009) Mercury pollution: an emerging problem and potential bacterial remediation strategies. World J Microbiol Biotechnol 25:1529–1537\nLarkin MA, Blackshields G, Brown NP et al (2007) ClustalW and ClustalX version 2. Bioinformatics 23:2947–2948\nLyyra S, Meagher RB, Kim T et al (2007) Coupling two mercury resistance genes in Eastern cottonwood enhances the processing of organomercury. Plant Biotechnol J 5:254–262\nNarita M, Chiba K, Nishizawa H et al (2003) Diversity of mercury resistance determinants among Bacillus strains isolated from sediment of Minamata Bay. FEMS Microbiol Lett 223:73–82\nNies DH (1999) Microbial heavy-metal resistance. Appl Microbiol Biotechnol 51:730–750\nOregaard G, Sørensen SJ (2007) High diversity of bacterial mercuric reductase genes from surface and sub-surface floodplain soil (Oak Ridge, USA). ISME J 1:453–467\nPark CH, Keyhan M, Wielinga B et al (2000) Purification to homogeneity and characterization of a novel Pseudomonas putida chromate reductase. Appl Environ Microbiol 66:1788–1795\nPathak A, Dastidar MG, Sreekrishnan TR (2009) Bioleaching of heavy metals from sewage sludge: a review. J Environ Manage 90:2343–2353\nRuta L, Paraschivescu C, Matache M et al (2010) Removing heavy metals from synthetic effluents using “kamikaze” Saccharomyces cerevisiae cells. Appl Microbiol Biotechnol 85:763–771\nSigrist CJ, Cerutti L, de Castro E et al (2010) PROSITE, a protein domain database for functional characterization and annotation. Nucleic Acids Res 38:161–166",{"VOID":379},"10.1007\u002Fs10534-010-9396-z","2024-06-23T19:05:53.837+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10534-010-9396-z",[383],{"id":384,"sortIndex":21,"researcher":20,"roles":385,"affiliations":386,"properties":395},"8dc9eeb2-c6af-499f-8016-98e625cd9d5c",[242],[387],{"id":388,"sortIndex":21,"affiliation":389,"properties":20},"5360ac5f-ea3f-491f-bdeb-d4b28baa24d7",{"id":388,"createTime":20,"updateTime":20,"relativeEntities":390,"slug":20,"properties":391,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":394,"statistic":20},[],{"title":392},{"VI":393},"Biotechnology Division, Institute of Himalayan Bioresource Technology (IHBT), Council of Scientific and Industrial Research (CSIR), Palampur, India",[],{"title":396,"gsAuthor":398},{"VI":397},"Amit Bafana",{"VOID":399},"[\"xWbx5MkAAAAJ\"]",{"url":381,"publisher":401,"properties":455},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":402,"slug":10,"properties":403,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":407,"manageAffiliations":424,"indexDatabases":435,"url":100,"thumbnailPath":20,"statistic":450,"gsStatistic":20,"type":211,"analyzePriority":20},[],{"issn":404,"title":405,"eissn":406},{"VOID":13},{"EN":15},{"VOID":17},[408,412,416,420],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":409,"label":410,"description":411,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":413,"label":414,"description":415,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":417,"label":418,"description":419,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":421,"label":422,"description":423,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},[425,430],{"id":49,"createTime":20,"updateTime":20,"relativeEntities":426,"slug":20,"properties":427,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":429,"statistic":20},[],{"title":428},{"EN":53},[55],{"id":57,"createTime":20,"updateTime":20,"relativeEntities":431,"slug":20,"properties":432,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":434,"statistic":20},[],{"title":433},{"EN":61},[],[436,443],{"id":65,"indexDatabase":437,"url":20,"indexYears":20,"academicFieldIds":442,"indexDatabaseRanking":20},{"id":67,"createTime":20,"updateTime":20,"relativeEntities":438,"label":439,"description":440,"key":74,"publicationTags":441,"standard":20},[],{"EN":70,"VI":70},{"EN":72,"VI":73},[76,77],[79],{"id":81,"indexDatabase":444,"url":92,"indexYears":93,"academicFieldIds":449,"indexDatabaseRanking":99},{"id":83,"createTime":20,"updateTime":20,"relativeEntities":445,"label":446,"description":447,"key":89,"publicationTags":448,"standard":20},[],{"EN":86,"VI":86},{"EN":86,"VI":88},[91],[95,96,97,98],{"impactFactor":21,"impactFactorByYear":451,"i10Index":113,"i10IndexLast5Year":114,"totalPublication":115,"totalPublicationByYear":452,"totalCitation":151,"totalCitationByYear":453,"totalCitationPerPublication":181,"totalCitationPerPublicationByYear":454,"hindexLast5Year":123,"hindex":123},{"2012":103,"2013":104,"2014":105,"2015":103,"2016":106,"2017":107,"2018":108,"2019":105,"2020":109,"2021":110,"2022":111,"2023":112},{"1988":117,"1989":118,"1990":119,"1991":120,"1992":121,"1993":122,"1994":123,"1995":124,"1996":125,"1997":126,"1998":127,"1999":128,"2000":129,"2001":130,"2002":131,"2003":132,"2004":133,"2005":134,"2006":135,"2007":136,"2008":132,"2009":137,"2010":138,"2011":139,"2012":140,"2013":141,"2014":142,"2015":143,"2016":143,"2017":144,"2018":145,"2019":146,"2020":129,"2021":147,"2022":148,"2023":149,"2024":150},{"1989":153,"1990":154,"1991":155,"1992":156,"1993":157,"1994":158,"1995":159,"1996":160,"2004":161,"2005":162,"2006":163,"2007":164,"2008":165,"2009":166,"2010":167,"2011":168,"2012":169,"2013":170,"2014":171,"2015":172,"2016":173,"2017":174,"2018":175,"2019":176,"2020":177,"2021":178,"2022":179,"2023":180},{"1989":183,"1990":184,"1991":185,"1992":186,"1993":187,"1994":188,"1995":189,"1996":190,"2004":191,"2005":192,"2006":193,"2007":194,"2008":195,"2009":196,"2010":197,"2011":198,"2012":199,"2013":200,"2014":201,"2015":202,"2016":203,"2017":204,"2018":205,"2019":206,"2020":207,"2021":208,"2022":209,"2023":210},{"pages":456,"volume":458},{"VOID":457},"301-309",{"VOID":459},"24",{"total":21,"publishYear":461,"statisticByYear":462},2010,{},"2010-12-23",[76,99],{"id":466,"createTime":467,"updateTime":468,"relativeEntities":469,"slug":470,"properties":471,"entityType":233,"verifyStatus":234,"verifyTime":482,"verifyNote":236,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":483,"fullTextUrl":20,"authors":484,"publicationType":291,"publisherRelationship":556,"citationCount":21,"citationInfo":616,"publishDate":619,"publishYear":617,"citationAnalyzeStatus":359,"lastCitationAnalyze":620,"indexDatabases":621,"openAccess":20,"references":20,"isForceReanalyzing":362},"a488ec19-9a8b-4329-80a7-ccb602ec1a8e","2024-01-09T23:42:25.167+00:00","2026-07-18T19:09:04.925+00:00",[],"Effect-of-bovine-apo-lactoferrin-on-the-growth-and-virulence-of-Actinobacillus-pleuropneumoniae",{"abstract":472,"title":474,"gsPaper":476,"references":478,"doi":480},{"EN":473},"\n                Actinobacillus pleuropneumoniae (App) is a Gram-negative bacterium that causes porcine pleuropneumonia, leading to economic losses in the swine industry. Due to bacterial resistance to antibiotics, new treatments for this disease are currently being sought. Lactoferrin (Lf) is an innate immune system glycoprotein of mammals that is microbiostatic and microbicidal and affects several bacterial virulence factors. The aim of this study was to investigate whether bovine iron-free Lf (BapoLf) has an effect on the growth and virulence of App. Two serotype 1 strains (reference strain S4074 and the isolate BC52) and a serotype 7 reference strain (WF83) were analyzed. First, the ability of App to grow in iron-charged BLf was discarded because in vivo, BapoLf sequesters iron and could be a potential source of this element favoring the infection. The minimum inhibitory concentration of BapoLf was 14.62, 11.78 and 10.56 µM for the strain BC52, S4074 and WF83, respectively. A subinhibitory concentration (0.8 µM) was tested by assessing App adhesion to porcine buccal epithelial cells, biofilm production, and the secretion and function of toxins and proteases. Decrease in adhesion (24–42 %) was found in the serotype 1 strains. Biofilm production decreased (27 %) for only the strain 4074 of serotype 1. Interestingly, biofilm was decreased (60–70 %) in the three strains by BholoLf. Hemolysis of erythrocytes and toxicity towards HeLa cells were not affected by BapoLf. In contrast, proteolytic activity in all strains was suppressed in the presence of BapoLf. Finally, oxytetracycline produced synergistic effect with BapoLf against App. Our results suggest that BapoLf affects the growth and several of the virulence factors in App.",{"EN":475},"Effect of bovine apo-lactoferrin on the growth and virulence of Actinobacillus pleuropneumoniae",{"VOID":477},"[\"2035929418855650631\"]",{"VOID":479},"Ammendolia MG, Bertuccini L, Iosi F, Minelli F, Berlutti F, Valenti P, Superti F (2010) Bovine lactoferrin interacts with cable pili of Burkholderia cenocepacia. Biometals 23:531–542. doi:10.1007\u002Fs10534-010-9333-1\nAppelmelk BJ, An YQ, Geerts M, Thijs BG, de Boer HA, MacLaren DM, de Graaf J, Nujiens JH (1994) Lactoferrin is a lipid A-binding protein. Infect Immun 62:2628–2632\nArchambault M, Harel J, Goure J, Tremblay YD, Jacques M (2012) Antimicrobial susceptibilities and resistance genes of Canadian isolates of Actinobacillus pleuropneumoniae. Microb Drug Resist 18:198–206. doi:10.1089\u002Fmdr.2011.0150\nArslan SY, Leung KP, Wu CD (2009) The effect of lactoferrin on oral bacterial attachment. Oral Microbiol Immunol 24:411–416\nBaker HM, Baker EN (2004) Lactoferrin and iron: structural and dynamic aspects of binding and release. Biometals 17:209–216\nBlackall PJ, Klaasen HL, van den Bosch H, Kuhnert P, Frey J (2002) Proposal of a new serovar of Actinobacillus pleuropneumoniae: serovar 15. Vet Microbiol 84:47–52\nBoekema BK, Van Putten JP, Stockhofe-Zurwieden N, Smith HE (2004) Host cell contact-induced transcription of the type IV fimbria gene cluster of Actinobacillus pleuropneumoniae. Infect Immun 72:691–700\nBradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254\nChen HL, Yen CC, Lu CY, Yu CH, Chen CM (2006) Synthetic porcine lactoferricin with a 20-residue peptide exhibits antimicrobial activity against Escherichia coli, Staphylococcus aureus, and Candida albicans. J Agric Food Chem 54:3277–3282. doi:10.1021\u002Fjf053031s\nChiers K, De Waele T, Pasmans F, Ducatelle R, Haesebrouck F (2010) Virulence factors of Actinobacillus pleuropneumoniae involved in colonization, persistence and induction of lesions in its porcine host. Vet Res 41:65. doi:10.1051\u002Fvetres\u002F2010037\nDashper SG, Pan Y, Veith PD, Chen YY, Toh EC, Liu SW, Cross KJ, Reynolds EC (2012) Lactoferrin inhibits Porphyromonas gingivalis proteinases and has sustained biofilm inhibitory activity. Antimicrob Agents Chemother 56:1548–1556\nDeneer HG, Potter AA (1989) Effect of iron restriction on the outer membrane proteins of Actinobacillus (Haemophilus) pleuropneumoniae. Infect Immun 57:798–804\nDom P, Hommez J, Castryck F, Devriese LA, Haesebrouck F (1994) Serotyping and quantitative determination of in vitro antibiotic susceptibility of Actinobacillus pleuropneumoniae strains isolated in Belgium (July 1991–August 1992. Vet Q 16:10–13. doi:10.1080\u002F01652176.1994.9694407\nDonlan RM, Costerton JW (2002) Biofilms: survival mechanisms of clinically relevant microorganisms. Clin Microbiol Rev 15:167–193\nDrago-Serrano ME, de la Garza-Amaya M, Luna JS, Campos-Rodriguez R (2012) Lactoferrin-lipopolysaccharide (LPS) binding as key to antibacterial and antiendotoxic effects. Int Immunopharmacol 12:1–9. doi:10.1016\u002Fj.intimp.2011.11.002\nD’Silva CG, Archibald FS, Niven DF (1995) Comparative study of iron acquisition by biotype 1 and biotype 2 strains of Actinobacillus pleuropneumoniae. Vet Microbiol 44:11–23\nDubin G, Koziel J, Pyrc K, Wladyka B, Potempa J (2013) Bacterial proteases in disease - role in intracellular survival, evasion of coagulation\u002Ffibrinolysis innate defenses, toxicoses and viral infections. Curr Pharm Des 19:1090–1113\nEllison RT 3rd, Giehl TJ, LaForce FM (1988) Damage of the outer membrane of enteric Gram-negative bacteria by lactoferrin and transferrin. Infect Immun 56:2774–2781\nEnriquez-Verdugo I, Guerrero AL, Serrano JJ, Godinez D, Rosales JL, Tenorio V, de la Garza M (2004) Adherence of Actinobacillus pleuropneumoniae to swine-lung collagen. Microbiology 150:2391–2400. doi:10.1099\u002Fmic.0.27053-0\nFlores-Villasenor H, Canizalez-Roman A, de la Garza M, Nazmi K, Bolscher JG, Leon-Sicairos N (2012) Lactoferrin and lactoferrin chimera inhibit damage caused by enteropathogenic Escherichia coli in HEp-2 cells. Biochimie 94:1935–1942\nFrey J (2011) The role of RTX toxins in host specificity of animal pathogenic Pasteurellaceae. Vet Microbiol 153:51–58\nFrey J, Bosse JT, Chang YF, Cullen JM, Fenwick B, Gerlach GF, Gygi D, Haesebrouck F, Inzana TJ, Jansen R (1993) Actinobacillus pleuropneumoniae RTX-toxins: uniform designation of haemolysins, cytolysins, pleurotoxin and their genes. J Gen Microbiol 139:1723–1728\nGarcia Gonzalez O, de la Garza M, Vaca S, Paniagua GL, Mejia R, Tenorio VR, Negrete-Abascal E (2004) Actinobacillus pleuropneumoniae metalloprotease: cloning and in vivo expression. FEMS Microbiol Lett 234:81–86. doi:10.1016\u002Fj.femsle.2004.03.012\nGarcia-Cuellar C, Montanez C, Tenorio V, Reyes-Esparza J, Duran MJ, Negrete E, Guerrero A, de la Garza M (2000) A 24-kDa cloned zinc metalloprotease from Actinobacillus pleuropneumoniae is common to all serotypes and cleaves actin in vitro. Can J Vet Res 64:88–95\nGonzalez GC, Caamano DL, Schryvers AB (1990) Identification and characterization of a porcine-specific transferrin receptor in Actinobacillus pleuropneumoniae. Mol Microbiol 4:1173–1179\nGrasteau A, Tremblay YD, Labrie J, Jacques M (2011) Novel genes associated with biofilm formation of Actinobacillus pleuropneumoniae. Vet Microbiol 153:134–143\nGutierrez-Martin CB, del Blanco NG, Blanco M, Navas J, Rodriguez-Ferri EF (2006) Changes in antimicrobial susceptibility of Actinobacillus pleuropneumoniae isolated from pigs in Spain during the last decade. Vet Microbiol 115:218–222\nHamer-Barrera R, Godinez D, Enrique VL, Vaca-Pacheco S, Matinez-Zuniga R, Tamás-Rohana P, Suarez-Guemez F, de la Garza M (2004) Adherence of Actinobacillus pleuropneumoniae serotype 1 to swine buccal epithelial cells involves fibronectin. Can J Vet Res 68:33–41\nInvestigación Aplicada SA (2010). Acontecer porcino 86-87\nInzana TJ (1991) Virulence properties of Actinobacillus pleuropneumoniae. Microb Pathog 11:305–316\nJacques M (2004) Surface polysaccharides and iron-uptake systems of Actinobacillus pleuropneumoniae. Can J Vet Res 68:81–85\nKamiya H, Ehara T, Matsumoto T (2012) Inhibitory effects of lactoferrin on biofilm formation in clinical isolates of Pseudomonas aeruginosa. J Infect Chemother 18:47–52. doi:10.1007\u002Fs10156-011-0287-1\nKaplan JB, Mulks MH (2005) Biofilm formation is prevalent among field isolates of Actinobacillus pleuropneumoniae. Vet Microbiol 108:89–94\nKawasaki Y, Shimizu K, Matsuzawa H, Dosako S, Isoda H, Tsukiji M, Fujimura R, Muranaka Y, Isihida H (2000) Inhibitory effects of bovine lactoferrin on the adherence of enterotoxigenic Escherichia coli to host cells. Biosci Biotechnol Biochem 64:348–354\nKomine Y, Komine K, Kai K, Itagaki M, Kuroishi T, Aso H, Obara Y, Kumagai K (2006) Effect of combination therapy with lactoferrin and antibiotics against staphylococcal mastitis on drying cows. J Vet Med Sci 68:205–211\nKutta H, Willer A, Steven P, Brauer L, Tsokos M, Paulsen F (2008) Distribution of mucins and antimicrobial substances lysozyme and lactoferrin in the laryngeal subglottic region. J Anat 213:473–481\nLacasse P, Lauzon K, Diarra MS, Petitclerc D (2008) Utilization of lactoferrin to fight antibiotic-resistant mammary gland pathogens. J Anim Sci 86:66–71\nLee TT, Chang CC, Juang RS, Chen RB, Yang HY, Chu LW, Wang SR, Tseng TH, Wang CS, Chen LJ, Yu B (2010) Porcine lactoferrin expression in transgenic rice and its effects as a feed additive on early weaned piglets. J Agric Food Chem 58:5166–5173. doi:10.1021\u002Fjf903904s\nLeitch EC, Willcox MD (1999) Elucidation of the antistaphylococcal action of lactoferrin and lysozyme. J Med Microbiol 48:867–871\nLeon-Sicairos N, Canizales-Roman A, de la Garza M, Reyes-Lopez M, Zazueta-Beltrán J, Nazmi K, Gomez-Gil B, Bolscher JG (2009) Bactericidal effect of lactoferrin and lactoferrin chimera against halophilic Vibrio parahaemolyticus. Biochimie 91:133–140\nLeon-Sicairos N, Lopez-Soto F, Reyes-Lopez M, Godinez-Vargas D, Ordaz-Pichardo C, de la Garza M (2006) Amoebicidal activity of milk, apo-lactoferrin, sIgA and lysozyme. Clin Med Res 4:106–113\nLi L, Mou X, Nelson DR (2013) Characterization of Plp, a phosphatidylcholine-specific phospholipase and hemolysin of Vibrio anguillarum. BMC Microbiol 13:271\nLloyd DH (2012) Alternatives to conventional antimicrobial drugs: a review of future prospects. Vet Dermatol 23(299–304):e259–e260. doi:10.1111\u002Fj.1365-3164.2012.01042.x\nLópez-Ruiz B, Vaca S, de la Garza M, Negrete-Abascal E (2013) Actinobacillus pleuropneumoniae secretes a metalloprotease that degrades porcine fibrinogen. Afr J Microbiol Res 7:2803–2807\nMorioka A, Asai T, Nitta H, Yamamoto K, Ogikubo Y, Takahashi T, Suzuki S (2008) Recent trends in antimicrobial susceptibility and the presence of the tetracycline resistance gene in Actinobacillus pleuropneumoniae isolates in Japan. J Vet Med Sci 70:1261–1264\nMosquito S, Zegarra G, Villanueva C, Ruiz J, Ochoa TJ (2012) Effect of bovine lactoferrin on the minimum inhibitory concentrations of ampicillin and trimethoprim-sulfamethoxazole for clinical Shigella spp. strains. Biochem Cell Biol 90:412–416. doi:10.1139\u002Fo11-066\nMurdock CA, Cleveland J, Matthews KR, Chikindas ML (2007) The synergistic effect of nisin and lactoferrin on the inhibition of Listeria monocytogenes and Escherichia coli O157:H7. Lett Appl Microbiol 44:255–261\nNedbalcova K, Satran P, Jaglic Z, Ondriasova R, Kucerova Z (2005) Monitoring of antibiotic resistance in isolates of Actinobacillus pleuropneumoniae in the Czech Republic between 2001 and 2003. Vet Med Czech 50:181–185\nNegrete-Abascal E, Tenorio VR, Serrano JJ, Garcia C, de la Garza M (1994) Secreted proteases from Actinobacillus pleuropneumoniae serotype 1 degrade porcine gelatin, hemoglobin and immunoglobulin A. Can J Vet Res 58:83–86\nNegrete-Abascal E, Tenorio VR, Guerrero AL, Garcia RM, Reyes ME, de la Garza M (1998) Purification and characterization of a protease from Actinobacillus pleuropneumoniae serotype 1, an antigen common to all the serotypes. Can J Vet Res 62:183–190\nOchoa TJ, Brown EL, Guion CE, Chen JZ, McMahon RJ, Cleary TG (2006) Effect of lactoferrin on enteroaggregative E. coli (EAEC). Biochem Cell Biol 84:369–376. doi:10.1139\u002Fo06-053\nOho T, Mitoma M, Koga T (2002) Functional domain of bovine milk lactoferrin which inhibits the adherence of Streptococcus mutans cells to a salivary film. Infect Immun 70:5279–5282\nO’May CY, Sanderson K, Roddam LF, Kirov SM, Reid DW (2009) Iron-binding compounds impair Pseudomonas aeruginosa biofilm formation, especially under anaerobic conditions. J Med Microbiol 58:765–773\nOrsi N (2004) The antimicrobial activity of lactoferrin: current status and perspectives. Biometals 17:189–196\nPlaut AG, Qiu J, St Geme JW 3rd (2000) Human lactoferrin proteolytic activity: analysis of the cleaved region in the IgA protease of Haemophilus influenzae. Vaccine 19(Suppl 1):S148–S152\nPohl S, Bertschinger U, Frederiksen W, Mannheim W (1983) Transfer of Haemophilus pleuropneumoniae and the Pasteurella haemolytica-like organism causing porcine necrotic pleuropneumonia to the genus Actinobacillus (Actinobacillus pleuropneumoniae comb. Nov.) on the basis of phenotypic and deoxyribonucleic acid relatedness. Int J Syst Bacteriol 33:510–514\nQiu J, Hendrixson DR, Baker EN, Murphy TF, St Geme JW 3rd, Plaut AG (1998) Human milk lactoferrin inactivates two putative colonization factors expressed by Haemophilus influenzae. Proc Natl Acad Sci U S A 95:12641–12646\nRamos-Clamont G, Rodríguez-Franco D, Guzmán-Partida A, Acedo-Félix E, Vázquez-Moreno L (2010) Actividad antibacteriana de lactoferrina bovina y lactoferrina porcina sobre Escherichia coli K88 +. Rev Cient-Fac Cienc Vet 5:473–479\nSanchez L, Aranda P, Perez MD, Calvo M (1988) Concentration of lactoferrin and transferrin throughout lactation in cow’s colostrum and milk. Biol Chem Hoppe Seyler 369:1005–1008\nSandkvist M (2001) Type II secretion and pathogenesis Infect Immun 69:3523–3535. doi:10.1128\u002FIAI.69.6.3523-3535.2001\nSchryvers AB (1989) Identification of the transferrin- and lactoferrin-binding proteins in Haemophilus influenzae. J Med Microbiol 29:121–130\nSchryvers AB, Morris LJ (1988) Identification and characterization of the transferrin receptor from Neisseria meningitidis. Mol Microbiol 2:281–288\nShi Y, Kong W, Nakayama K (2000) Human lactoferrin binds and removes the hemoglobin receptor protein of the periodontopathogen Porphyromonas gingivalis. J Biol Chem 275:30002–30008. doi:10.1074\u002Fjbc.M001518200\nSingh PK, Tack BF, McCray PB Jr, Welsh MJ (2000) Synergistic and additive killing by antimicrobial factors found in human airway surface liquid. Am J Physiol Lung Cell Mol Physiol 279:L799–L805\nSojar HT, Hamada N, Genco RJ (1998) Structures involved in the interaction of Porphyromonas gingivalis fimbriae and human lactoferrin. FEBS Lett 422:205–208\nTeraguchi S, Shin K, Fukuwatari Y, Shimamura S (1996) Glycans of bovine lactoferrin function as receptors for the type 1 fimbrial lectin of Escherichia coli. Infect Immun 64:1075–1077\nTian H, Maddox IS, Ferguson LR, Shu Q (2010) Influence of bovine lactoferrin on selected probiotic bacteria and intestinal pathogens. Biometals 23:593–596. doi:10.1007\u002Fs10534-010-9318-0\nVan Meerloo J, Kaspers G, Cloos J (2011) Cell sensitivity assays: the MTT assay. In: Cree IA (ed) Cancer cell culture: methods and protocols, 2nd edn. Humana Press, New York, pp 237–245\nVanni M, Merenda M, Barigazzi G, Garbarino C, Luppi A, Tognetti R, Intorre L (2012) Antimicrobial resistance of Actinobacillus pleuropneumoniae isolated from swine. Vet Microbiol 156:172–177\nVogel HJ (2012) Lactoferrin, a bird’s eye view. Biochem Cell Biol 90:233–244. doi:10.1139\u002Fo2012-016\nWakabayashi H, Yamauchi K, Kobayashi T, Yaeshima T, Iwatsuki K, Yoshie H (2009) Inhibitory effects of lactoferrin on growth and biofilm formation of Porphyromonas gingivalis and Prevotella intermedia. Antimicrob Agents Chemother 53:3308–3316\nWilliams J, Salazar-Fajardo M, Ramírez-Porras R, Mosqueda-Ara Z (2001) Sensibilidad in vitro de cepas de Actinobacillus pleuropneumoniae y Pasteurella multocida tipo “A” ante diferentes antimicrobianos. Rev Biomed 12:172–179\nXiao L, Zhou L, Sun C, Feng X, Du C, Gao Y, Ji Q, Yang S, Wang Y, Han W, Langford PR, Lei L (2012) Apa is a trimeric autotransporter adhesin of Actinobacillus pleuropneumoniae responsible for autoagglutination and host cell adherence. J Basic Microbiol 52:598–607. doi:10.1002\u002Fjobm.201100365\nYang TS, Wu SC, Wang SR (2000) Serum and milk lactoferrin concentration and the correlation with some blood components in lactating sows. Res Vet Sci 69:95–97. doi:10.1053\u002Frvsc.2000.0393\nYu RH, Schryvers AB (2002) Bacterial lactoferrin receptors: insights from characterizing the Moraxella bovis receptors. Biochem Cell Biol 80:81–90",{"VOID":481},"10.1007\u002Fs10534-014-9752-5","2024-05-06T21:59:17.924+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10534-014-9752-5",[485,502,517,530,543],{"id":486,"sortIndex":21,"researcher":20,"roles":487,"affiliations":488,"properties":497},"bccbbeae-5bf3-48e6-91b7-a15498390d9b",[242],[489],{"id":490,"sortIndex":21,"affiliation":491,"properties":20},"45793432-7f4b-44c5-b46f-9ada7bc0a6cc",{"id":490,"createTime":20,"updateTime":20,"relativeEntities":492,"slug":20,"properties":493,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":496,"statistic":20},[],{"title":494},{"VI":495},"Departamento de Biología Celular, Centro de Investigación y de Estudios Avanzados del IPN (CINVESTAV-IPN), México DF, Mexico",[],{"title":498,"gsAuthor":500},{"VI":499},"Sarahí Luna-Castro",{"VOID":501},"[\"sRCzJGwAAAAJ\"]",{"id":503,"sortIndex":259,"researcher":20,"roles":504,"affiliations":505,"properties":514},"920dd53d-50d9-43d3-8f6f-0bbd1d58ce04",[242],[506],{"id":507,"sortIndex":21,"affiliation":508,"properties":20},"a0deab05-ab6b-435e-9ab1-939f652d06c8",{"id":507,"createTime":20,"updateTime":20,"relativeEntities":509,"slug":20,"properties":510,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":513,"statistic":20},[],{"title":511},{"VI":512},"Centro Nacional de Investigación Disciplinaria-Microbiología Animal, México DF, Mexico",[],{"title":515},{"VI":516},"Francisco Aguilar-Romero",{"id":518,"sortIndex":277,"researcher":20,"roles":519,"affiliations":520,"properties":527},"7580673a-2463-4fee-805c-8bc1b42c5692",[242],[521],{"id":490,"sortIndex":21,"affiliation":522,"properties":20},{"id":490,"createTime":20,"updateTime":20,"relativeEntities":523,"slug":20,"properties":524,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":526,"statistic":20},[],{"title":525},{"VI":495},[],{"title":528},{"VI":529},"Luisa Samaniego-Barrón",{"id":531,"sortIndex":357,"researcher":20,"roles":532,"affiliations":533,"properties":540},"bba92b96-6cf4-490b-8fdd-d03e67567cfc",[242],[534],{"id":490,"sortIndex":21,"affiliation":535,"properties":20},{"id":490,"createTime":20,"updateTime":20,"relativeEntities":536,"slug":20,"properties":537,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":539,"statistic":20},[],{"title":538},{"VI":495},[],{"title":541},{"VI":542},"Delfino Godínez-Vargas",{"id":544,"sortIndex":161,"researcher":20,"roles":545,"affiliations":546,"properties":553},"fca54c3b-031a-43e1-ba07-0b59f0969a17",[242],[547],{"id":490,"sortIndex":21,"affiliation":548,"properties":20},{"id":490,"createTime":20,"updateTime":20,"relativeEntities":549,"slug":20,"properties":550,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":552,"statistic":20},[],{"title":551},{"VI":495},[],{"title":554},{"VI":555},"Mireya de la Garza",{"url":483,"publisher":557,"properties":611},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":558,"slug":10,"properties":559,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":563,"manageAffiliations":580,"indexDatabases":591,"url":100,"thumbnailPath":20,"statistic":606,"gsStatistic":20,"type":211,"analyzePriority":20},[],{"issn":560,"title":561,"eissn":562},{"VOID":13},{"EN":15},{"VOID":17},[564,568,572,576],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":565,"label":566,"description":567,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":569,"label":570,"description":571,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":573,"label":574,"description":575,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":577,"label":578,"description":579,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},[581,586],{"id":49,"createTime":20,"updateTime":20,"relativeEntities":582,"slug":20,"properties":583,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":585,"statistic":20},[],{"title":584},{"EN":53},[55],{"id":57,"createTime":20,"updateTime":20,"relativeEntities":587,"slug":20,"properties":588,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":590,"statistic":20},[],{"title":589},{"EN":61},[],[592,599],{"id":65,"indexDatabase":593,"url":20,"indexYears":20,"academicFieldIds":598,"indexDatabaseRanking":20},{"id":67,"createTime":20,"updateTime":20,"relativeEntities":594,"label":595,"description":596,"key":74,"publicationTags":597,"standard":20},[],{"EN":70,"VI":70},{"EN":72,"VI":73},[76,77],[79],{"id":81,"indexDatabase":600,"url":92,"indexYears":93,"academicFieldIds":605,"indexDatabaseRanking":99},{"id":83,"createTime":20,"updateTime":20,"relativeEntities":601,"label":602,"description":603,"key":89,"publicationTags":604,"standard":20},[],{"EN":86,"VI":86},{"EN":86,"VI":88},[91],[95,96,97,98],{"impactFactor":21,"impactFactorByYear":607,"i10Index":113,"i10IndexLast5Year":114,"totalPublication":115,"totalPublicationByYear":608,"totalCitation":151,"totalCitationByYear":609,"totalCitationPerPublication":181,"totalCitationPerPublicationByYear":610,"hindexLast5Year":123,"hindex":123},{"2012":103,"2013":104,"2014":105,"2015":103,"2016":106,"2017":107,"2018":108,"2019":105,"2020":109,"2021":110,"2022":111,"2023":112},{"1988":117,"1989":118,"1990":119,"1991":120,"1992":121,"1993":122,"1994":123,"1995":124,"1996":125,"1997":126,"1998":127,"1999":128,"2000":129,"2001":130,"2002":131,"2003":132,"2004":133,"2005":134,"2006":135,"2007":136,"2008":132,"2009":137,"2010":138,"2011":139,"2012":140,"2013":141,"2014":142,"2015":143,"2016":143,"2017":144,"2018":145,"2019":146,"2020":129,"2021":147,"2022":148,"2023":149,"2024":150},{"1989":153,"1990":154,"1991":155,"1992":156,"1993":157,"1994":158,"1995":159,"1996":160,"2004":161,"2005":162,"2006":163,"2007":164,"2008":165,"2009":166,"2010":167,"2011":168,"2012":169,"2013":170,"2014":171,"2015":172,"2016":173,"2017":174,"2018":175,"2019":176,"2020":177,"2021":178,"2022":179,"2023":180},{"1989":183,"1990":184,"1991":185,"1992":186,"1993":187,"1994":188,"1995":189,"1996":190,"2004":191,"2005":192,"2006":193,"2007":194,"2008":195,"2009":196,"2010":197,"2011":198,"2012":199,"2013":200,"2014":201,"2015":202,"2016":203,"2017":204,"2018":205,"2019":206,"2020":207,"2021":208,"2022":209,"2023":210},{"pages":612,"volume":614},{"VOID":613},"891-903",{"VOID":615},"27",{"total":21,"publishYear":617,"statisticByYear":618},2014,{},"2014-05-31","2026-07-18T19:09:04.924+00:00",[76,99],{"id":623,"createTime":624,"updateTime":625,"relativeEntities":626,"slug":627,"properties":628,"entityType":233,"verifyStatus":234,"verifyTime":637,"verifyNote":236,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":638,"fullTextUrl":20,"authors":639,"publicationType":291,"publisherRelationship":703,"citationCount":763,"citationInfo":764,"publishDate":768,"publishYear":765,"citationAnalyzeStatus":359,"lastCitationAnalyze":769,"indexDatabases":770,"openAccess":20,"references":771,"isForceReanalyzing":362},"4feeae96-a905-4d9f-8021-d03aef3b2735","2024-01-12T00:34:16.180+00:00","2026-07-16T07:00:53.026+00:00",[],"Tracing-of-labile-zinc-in-live-fish-hepatocytes-using-FluoZin-3",{"abstract":629,"title":631,"gsPaper":633,"doi":635},{"EN":630},"Intracellular zinc levels are homeostatically regulated and although most is bound, a pool of labile Zn(II) is present in cells. We show here that the zinc probe FluoZin-3 is useful to monitor zinc fluxes during fluorescent imaging of the trout hepatic cell line D11. Nuclei and bulk cytosol appeared to lack detectable labile zinc, while the punctuate staining pattern colocalized with a lysosome-specific probe. Applying extracellular zinc alone resulted in vesicular sequestration of the metal ion. Together with Na-pyrithione a delayed and toxic rise in cellular fluorescence was triggered. When using another ionophore, 4-Br A23187, a zinc buffering effect of the vesicular pools was evident. Secondly, N-ethylmaleimide induced a homogeneous fluorescence rise, which was strongly enhanced by addition of Zn-pyrithione and disappeared after TPEN washing. This suggests the involvement of thiol residues in controlling available cytosolic zinc. Our observations have implications for the interpretation of calculated intracellular Zn2+ concentrations.",{"EN":632},"Tracing of labile zinc in live fish hepatocytes using FluoZin-3",{"VOID":634},"[\"5234189159936891393\"]",{"VOID":636},"10.1007\u002Fs10534-005-4576-y","2024-04-29T10:34:44.732+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10534-005-4576-y",[640,655,662,675,690],{"id":641,"sortIndex":21,"researcher":20,"roles":642,"affiliations":643,"properties":652},"d92c8028-72d3-4fa1-bfde-b3b408f25420",[242],[644],{"id":645,"sortIndex":21,"affiliation":646,"properties":20},"18bddb94-dd85-44ab-877f-fa9df5571e61",{"id":645,"createTime":20,"updateTime":20,"relativeEntities":647,"slug":20,"properties":648,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":651,"statistic":20},[],{"title":649},{"VI":650},"Department of Biology, University of Antwerp, Antwerp, Belgium",[],{"title":653},{"VI":654},"Frederik A. R. Muylle",{"id":656,"sortIndex":259,"researcher":20,"roles":657,"affiliations":658,"properties":659},"dcabc812-70b8-4c36-983c-0d5cd1887c8f",[242],[],{"title":660},{"VI":661},"Dirk Adriaensen",{"id":663,"sortIndex":277,"researcher":20,"roles":664,"affiliations":665,"properties":672},"117a49e4-38ca-4c23-b75a-01d2d2d20e18",[242],[666],{"id":645,"sortIndex":21,"affiliation":667,"properties":20},{"id":645,"createTime":20,"updateTime":20,"relativeEntities":668,"slug":20,"properties":669,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":671,"statistic":20},[],{"title":670},{"VI":650},[],{"title":673},{"VI":674},"Wim De Coen",{"id":676,"sortIndex":357,"researcher":20,"roles":677,"affiliations":678,"properties":687},"80805a96-2a4e-430c-9446-fd9ae7cd8d4b",[242],[679],{"id":680,"sortIndex":21,"affiliation":681,"properties":20},"21ea883b-784a-40d9-acc3-ae077e1a3638",{"id":680,"createTime":20,"updateTime":20,"relativeEntities":682,"slug":20,"properties":683,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":686,"statistic":20},[],{"title":684},{"VI":685},"Department of Biomedical Sciences, University of Antwerp, Antwerp, Belgium",[],{"title":688},{"VI":689},"Jean-Pierre Timmermans",{"id":691,"sortIndex":161,"researcher":20,"roles":692,"affiliations":693,"properties":700},"832efbe9-2005-49be-a98c-d23d4e7cb48b",[242],[694],{"id":645,"sortIndex":21,"affiliation":695,"properties":20},{"id":645,"createTime":20,"updateTime":20,"relativeEntities":696,"slug":20,"properties":697,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":699,"statistic":20},[],{"title":698},{"VI":650},[],{"title":701},{"VI":702},"Ronny Blust",{"url":638,"publisher":704,"properties":758},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":705,"slug":10,"properties":706,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":710,"manageAffiliations":727,"indexDatabases":738,"url":100,"thumbnailPath":20,"statistic":753,"gsStatistic":20,"type":211,"analyzePriority":20},[],{"issn":707,"title":708,"eissn":709},{"VOID":13},{"EN":15},{"VOID":17},[711,715,719,723],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":712,"label":713,"description":714,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":716,"label":717,"description":718,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":720,"label":721,"description":722,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":724,"label":725,"description":726,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},[728,733],{"id":49,"createTime":20,"updateTime":20,"relativeEntities":729,"slug":20,"properties":730,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":732,"statistic":20},[],{"title":731},{"EN":53},[55],{"id":57,"createTime":20,"updateTime":20,"relativeEntities":734,"slug":20,"properties":735,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":737,"statistic":20},[],{"title":736},{"EN":61},[],[739,746],{"id":65,"indexDatabase":740,"url":20,"indexYears":20,"academicFieldIds":745,"indexDatabaseRanking":20},{"id":67,"createTime":20,"updateTime":20,"relativeEntities":741,"label":742,"description":743,"key":74,"publicationTags":744,"standard":20},[],{"EN":70,"VI":70},{"EN":72,"VI":73},[76,77],[79],{"id":81,"indexDatabase":747,"url":92,"indexYears":93,"academicFieldIds":752,"indexDatabaseRanking":99},{"id":83,"createTime":20,"updateTime":20,"relativeEntities":748,"label":749,"description":750,"key":89,"publicationTags":751,"standard":20},[],{"EN":86,"VI":86},{"EN":86,"VI":88},[91],[95,96,97,98],{"impactFactor":21,"impactFactorByYear":754,"i10Index":113,"i10IndexLast5Year":114,"totalPublication":115,"totalPublicationByYear":755,"totalCitation":151,"totalCitationByYear":756,"totalCitationPerPublication":181,"totalCitationPerPublicationByYear":757,"hindexLast5Year":123,"hindex":123},{"2012":103,"2013":104,"2014":105,"2015":103,"2016":106,"2017":107,"2018":108,"2019":105,"2020":109,"2021":110,"2022":111,"2023":112},{"1988":117,"1989":118,"1990":119,"1991":120,"1992":121,"1993":122,"1994":123,"1995":124,"1996":125,"1997":126,"1998":127,"1999":128,"2000":129,"2001":130,"2002":131,"2003":132,"2004":133,"2005":134,"2006":135,"2007":136,"2008":132,"2009":137,"2010":138,"2011":139,"2012":140,"2013":141,"2014":142,"2015":143,"2016":143,"2017":144,"2018":145,"2019":146,"2020":129,"2021":147,"2022":148,"2023":149,"2024":150},{"1989":153,"1990":154,"1991":155,"1992":156,"1993":157,"1994":158,"1995":159,"1996":160,"2004":161,"2005":162,"2006":163,"2007":164,"2008":165,"2009":166,"2010":167,"2011":168,"2012":169,"2013":170,"2014":171,"2015":172,"2016":173,"2017":174,"2018":175,"2019":176,"2020":177,"2021":178,"2022":179,"2023":180},{"1989":183,"1990":184,"1991":185,"1992":186,"1993":187,"1994":188,"1995":189,"1996":190,"2004":191,"2005":192,"2006":193,"2007":194,"2008":195,"2009":196,"2010":197,"2011":198,"2012":199,"2013":200,"2014":201,"2015":202,"2016":203,"2017":204,"2018":205,"2019":206,"2020":207,"2021":208,"2022":209,"2023":210},{"pages":759,"volume":761},{"VOID":760},"437-450",{"VOID":762},"19",36,{"total":763,"publishYear":765,"statisticByYear":766},2006,{"2007":259,"2008":277,"2009":767,"2010":277,"2011":357,"2012":259,"2013":277,"2014":356,"2015":277,"2016":357,"2017":259,"2018":277,"2022":277,"2023":277,"2024":277},6,"2006-08-01","2026-07-16T07:00:53.025+00:00",[76,99],[772,775,779,785,790,795,799,803,806,811,816,819,824,830,835,841,844,847,852,855,860,865,868,872,878,883,886,891,896,901,904,907,912,917,920,925,930,934,937,941,946,950,954,959,965,968,971],{"id":20,"text":773,"url":20,"identifiers":774},"W Ahne (1985) ArticleTitleStudies on the use of fish tissue-cultures for toxicity tests in order to reduce and replace the fish tests Zentralbl Bakteriol Mikrobiol Hyg B 180 480–504 Occurrence Handle4024776 Occurrence Handle1:CAS:528:DyaL2MXltFOlsrY%3D",{},{"id":20,"text":776,"url":20,"identifiers":777},"DH Alsop CM Wood (2000) ArticleTitleKinetic analysis of zinc accumulation in the gills of juvenile rainbow trout: effects of zinc acclimation and implications for biotic ligand modeling Environ Toxicol Chem 19 1911–1918 Occurrence Handle1:CAS:528:DC%2BD3cXkt1agsr0%3D Occurrence Handle10.1897\u002F1551-5028(2000)019\u003C1911:KAOZAI>2.3.CO;2",{"doi":778},"10.1897\u002F1551-5028(2000)019\u003C1911:KAOZAI>2.3.CO;2",{"id":780,"text":781,"url":782,"identifiers":783},"4c68646b-0035-4279-8000-0006b275d4fa","P Arslan F Divirgilio M Beltrame RY Tsien T Pozzan (1985) ArticleTitleCytosolic Ca-2+ homeostasis in Ehrlich and Yoshida carcinomas – A new, membrane-permeant chelator of heavy metals reveals that these ascites tumor cell lines have normal cytosolic free Ca2+ J Biol Chem 260 2719–2727 Occurrence Handle3919006 Occurrence Handle1:CAS:528:DyaL2MXhsVKqs78%3D","https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10440-022-00541-7",{"doi":784},"10.1007\u002Fs10440-022-00541-7",{"id":20,"text":786,"url":787,"identifiers":788},"NA Begum M Kobayashi Y Moriwaki et al. (2002) ArticleTitleMycobacterium bovis BCG cell wall and lipopolysaccharide induce a novel gene, BIGM103, encoding a 7-TM protein: Identification of a new protein family having Zn-transporter and Zn-metalloprotease signatures Genomics 80 630–645 Occurrence Handle12504855 Occurrence Handle1:CAS:528:DC%2BD38Xps1Ons7o%3D Occurrence Handle10.1006\u002Fgeno.2002.7000","http:\u002F\u002Fdx.doi.org\u002F10.1006\u002Fgeno.2002.7000",{"doi":789},"10.1006\u002Fgeno.2002.7000",{"id":20,"text":791,"url":792,"identifiers":793},"IA Brand J Kleineke (1996) ArticleTitleIntracellular zinc movement and its effect on the carbohydrate metabolism of isolated rat hepatocytes J Biol Chem 271 1941–1949 Occurrence Handle8567642 Occurrence Handle1:CAS:528:DyaK28XnsF2lsA%3D%3D Occurrence Handle10.1074\u002Fjbc.271.4.1941","http:\u002F\u002Fdx.doi.org\u002F10.1074\u002Fjbc.271.4.1941",{"doi":794},"10.1074\u002Fjbc.271.4.1941",{"id":20,"text":796,"url":20,"identifiers":797},"SC Burdette GK Walkup B Spingler RY Tsien SJ Lippard (2001) ArticleTitleFluorescent sensors for Zn2+ based on a fluorescein platform: Synthesis, properties and intracellular distribution J Am Chem Soc 123 7831–7841 Occurrence Handle11493056 Occurrence Handle1:CAS:528:DC%2BD3MXltlSntrw%3D Occurrence Handle10.1021\u002Fja010059l",{"doi":798},"10.1021\u002Fja010059l",{"id":20,"text":800,"url":20,"identifiers":801},"NR Bury PA Walker CN Glover (2003) ArticleTitleNutritive metal uptake in teleost fish J Exp Biol 206 11–23 Occurrence Handle12456693 Occurrence Handle1:CAS:528:DC%2BD3sXhtVWgsrk%3D Occurrence Handle10.1242\u002Fjeb.00068",{"doi":802},"10.1242\u002Fjeb.00068",{"id":780,"text":804,"url":782,"identifiers":805},"LMT Canzoniero DM Turetsky DW Choi (1999) ArticleTitleMeasurement of intracellular free zinc concentrations accompanying zinc-induced neuronal death J Neurosci 19 RC31 Occurrence Handle10493776 Occurrence Handle1:STN:280:DC%2BD3c3ns1enuw%3D%3D",{"doi":784},{"id":20,"text":807,"url":808,"identifiers":809},"CJ Chang J Jaworski EM Nolan M Sheng SJ Lippard (2004) ArticleTitleA tautomeric zinc sensor for ratiometric fluorescence imaging: Application to nitric oxide-induced release of intracellular zinc Proc Natl Acad Sci USA 101 1129–1134 Occurrence Handle14734801 Occurrence Handle1:CAS:528:DC%2BD2cXhtlWjsbY%3D Occurrence Handle10.1073\u002Fpnas.0308079100","http:\u002F\u002Fdx.doi.org\u002F10.1073\u002Fpnas.0308079100",{"doi":810},"10.1073\u002Fpnas.0308079100",{"id":20,"text":812,"url":813,"identifiers":814},"RA Colvin CP Fontaine M Laskowski D Thomas (2003) ArticleTitleZn2+ transporters and Zn2+ homeostasis in neurons Eur J Pharmacol 479 171–185 Occurrence Handle14612148 Occurrence Handle1:CAS:528:DC%2BD3sXovVGntb0%3D Occurrence Handle10.1016\u002Fj.ejphar.2003.08.067","http:\u002F\u002Fdx.doi.org\u002F10.1016\u002Fj.ejphar.2003.08.067",{"doi":815},"10.1016\u002Fj.ejphar.2003.08.067",{"id":20,"text":817,"url":20,"identifiers":818},"P Coyle PD Zalewski JC Philcox et al. (1994) ArticleTitleMeasurement of zinc in hepatocytes by using a fluorescent probe, Zinquin: Relationship to metallothionein and intracellular zinc Biochem J 303 781–786 Occurrence Handle7980447 Occurrence Handle1:CAS:528:DyaK2cXmsFShsbk%3D",{},{"id":20,"text":820,"url":821,"identifiers":822},"KE Dineley LM Malaiyandi IJ Reynolds (2002) ArticleTitleA reevaluation of neuronal zinc measurements: Artifacts associated with high intracellular dye concentration Mol Pharmacol 62 618–627 Occurrence Handle12181438 Occurrence Handle1:CAS:528:DC%2BD38XmsVKmurs%3D Occurrence Handle10.1124\u002Fmol.62.3.618","http:\u002F\u002Fdx.doi.org\u002F10.1124\u002Fmol.62.3.618",{"doi":823},"10.1124\u002Fmol.62.3.618",{"id":825,"text":826,"url":827,"identifiers":828},"b9624ef6-9005-4219-bb59-05e2126a7a21","CJ Frederickson EJ Kasarskis D Ringo RE Frederickson (1987) ArticleTitleA quinoline fluorescence method for visualizing and assaying the histochemically reactive zinc (bouton zinc) in the brain J Neurosci Methods 20 91–103 Occurrence Handle3600033 Occurrence Handle1:CAS:528:DyaL2sXkslels70%3D Occurrence Handle10.1016\u002F0165-0270(87)90042-2","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002F0165027087900422",{"doi":829},"10.1016\u002F0165-0270(87)90042-2",{"id":20,"text":831,"url":832,"identifiers":833},"F Gagné C Blaise (1996) ArticleTitleAvailable intracellular Zn as a potential indicator of heavy metal exposure in rainbow trout hepatocytes Environ Toxicol Water Qual 11 319–325 Occurrence Handle10.1002\u002F(SICI)1098-2256(1996)11:4\u003C319::AID-TOX6>3.0.CO;2-C","http:\u002F\u002Fdx.doi.org\u002F10.1002\u002F(sici)1098-2256(1996)11:4\u003C319::aid-tox6>3.0.co;2-c",{"doi":834},"10.1002\u002F(sici)1098-2256(1996)11:4\u003C319::aid-tox6>3.0.co;2-c",{"id":836,"text":837,"url":838,"identifiers":839},"993598af-42bc-420f-ae1e-1a745ee53500","LA Gaither DJ Eide (2001) ArticleTitleEukaryotic zinc transporters and their regulation Biometals 14 251–270 Occurrence Handle11831460 Occurrence Handle1:CAS:528:DC%2BD38XpsFWrtw%3D%3D Occurrence Handle10.1023\u002FA:1012988914300","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1023\u002FA:1012988914300",{"doi":840},"10.1023\u002FA:1012988914300",{"id":780,"text":842,"url":782,"identifiers":843},"CN Glover C Hogstrand (2002) ArticleTitleIn vivo characterisation of intestinal zinc uptake in freshwater rainbow trout J Exp Biol 205 141–150 Occurrence Handle11818420 Occurrence Handle1:CAS:528:DC%2BD38XhtlGluro%3D",{"doi":784},{"id":780,"text":845,"url":782,"identifiers":846},"G Grynkiewicz M Poenie RY Tsien (1985) ArticleTitleA new generation of Ca2+ indicators with greatly improved fluorescence properties J Biol Chem 260 3440–3450 Occurrence Handle3838314 Occurrence Handle1:CAS:528:DyaL2MXitVSmu7s%3D",{"doi":784},{"id":20,"text":848,"url":849,"identifiers":850},"H Haase D Beyersmann (2002) ArticleTitleIntracellular zinc distribution and transport in C6 rat glioma cells Biochem Biophys Res Commun 296 923–928 Occurrence Handle12200136 Occurrence Handle1:CAS:528:DC%2BD38XmsV2rsrw%3D Occurrence Handle10.1016\u002FS0006-291X(02)02017-X","http:\u002F\u002Fdx.doi.org\u002F10.1016\u002Fs0006-291x(02)02017-x",{"doi":851},"10.1016\u002Fs0006-291x(02)02017-x",{"id":20,"text":853,"url":20,"identifiers":854},"R Haugland (2002) Handbook of Fluorescent Probes and Research Products Molecular Probes La Jolla",{},{"id":20,"text":856,"url":857,"identifiers":858},"LH Ho RN Ratnaike PD Zalewski (2000) ArticleTitleInvolvement of intracellular labile zinc in suppression of DEVD-caspase activity in human neuroblastoma cells Biochem Biophys Res Commun 268 148–154 Occurrence Handle10652229 Occurrence Handle1:CAS:528:DC%2BD3cXnsVWhsw%3D%3D Occurrence Handle10.1006\u002Fbbrc.2000.2090","http:\u002F\u002Fdx.doi.org\u002F10.1006\u002Fbbrc.2000.2090",{"doi":859},"10.1006\u002Fbbrc.2000.2090",{"id":20,"text":861,"url":862,"identifiers":863},"C Hogstrand CM Wood (1995) ArticleTitleMechanisms for zinc acclimation in fresh-water rainbow-trout Mar Environ Res 39 131–135 Occurrence Handle1:CAS:528:DyaK2MXkvFehsbc%3D Occurrence Handle10.1016\u002F0141-1136(94)00040-V","http:\u002F\u002Fdx.doi.org\u002F10.1016\u002F0141-1136(94)00040-v",{"doi":864},"10.1016\u002F0141-1136(94)00040-v",{"id":780,"text":866,"url":782,"identifiers":867},"C Hogstrand CM Wood (1996) The physiology and toxicology of zinc in fish EW Tayler (Eds) Toxicology of Aquatic Pollution: Physiological, Cellular and Molecular Approaches Cambridge University Press Cambridge 61–84",{"doi":784},{"id":20,"text":869,"url":20,"identifiers":870},"JHR Kägi (1991) ArticleTitleOverview of metallothionein Methods Enzymol 205 613–626 Occurrence Handle1779825 Occurrence Handle10.1016\u002F0076-6879(91)05145-L",{"doi":871},"10.1016\u002F0076-6879(91)05145-L",{"id":873,"text":874,"url":875,"identifiers":876},"5c68c125-62a1-4351-a039-f8664c67a472","T Kambe Y Yamaguchi-Iwai R Sasaki M Nagao (2004) ArticleTitleOverview of mammalian zinc transporters Cell Mol Life Sci 61 49–68 Occurrence Handle14704853 Occurrence Handle1:CAS:528:DC%2BD2cXjt1yhur4%3D Occurrence Handle10.1007\u002Fs00018-003-3148-y","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs00018-003-3148-y",{"doi":877},"10.1007\u002Fs00018-003-3148-y",{"id":20,"text":879,"url":880,"identifiers":881},"JW Kleineke IA Brand (1997) ArticleTitleRapid changes in intracellular Zn2+ in rat hepatocytes J Pharmacol Toxicol Methods 38 181–187 Occurrence Handle9566441 Occurrence Handle1:CAS:528:DyaK1cXisVKgt7s%3D Occurrence Handle10.1016\u002FS1056-8719(97)00094-4","http:\u002F\u002Fdx.doi.org\u002F10.1016\u002Fs1056-8719(97)00094-4",{"doi":882},"10.1016\u002Fs1056-8719(97)00094-4",{"id":780,"text":884,"url":782,"identifiers":885},"Krezel A, Wojcik J, Maciejczyk M, Bal W. 2003 May GSH and L-His contribute to intracellular binding of zinc? Thermodynamic and solution structural study of a ternary complex. Chem Commun, 704–705",{"doi":784},{"id":20,"text":887,"url":888,"identifiers":889},"HL Ley ML Failla DS Cherry (1983) ArticleTitleIsolation and characterization of hepatic metallothionein from rainbow trout (Salmo gairdneri) Comp Biochem Physiol B 74 507–513 Occurrence Handle6839717 Occurrence Handle10.1016\u002F0305-0491(83)90219-5","http:\u002F\u002Fdx.doi.org\u002F10.1016\u002F0305-0491(83)90219-5",{"doi":890},"10.1016\u002F0305-0491(83)90219-5",{"id":20,"text":892,"url":893,"identifiers":894},"C Lopez-Garcia E Varea JJ Palop et al. (2002) ArticleTitleCytochemical techniques for zinc and heavy metals localization in nerve cells Microsc Res Tech 56 318–331 Occurrence Handle11877810 Occurrence Handle1:CAS:528:DC%2BD38Xit1entbc%3D Occurrence Handle10.1002\u002Fjemt.10037","http:\u002F\u002Fdx.doi.org\u002F10.1002\u002Fjemt.10037",{"doi":895},"10.1002\u002Fjemt.10037",{"id":20,"text":897,"url":898,"identifiers":899},"M Maracine H Segner (1998) ArticleTitleCytotoxicity of metals in isolated fish cells: Importance of the cellular glutathione status Comp Biochem Physiol A 120 83–88 Occurrence Handle10.1016\u002FS1095-6433(98)10013-2","http:\u002F\u002Fdx.doi.org\u002F10.1016\u002Fs1095-6433(98)10013-2",{"doi":900},"10.1016\u002Fs1095-6433(98)10013-2",{"id":20,"text":902,"url":20,"identifiers":903},"W Maret (2003) ArticleTitleCellular zinc and redox states converge in the metallothionein\u002Fthionein pair J Nutr 133 1460S–1462S Occurrence Handle12730443 Occurrence Handle1:CAS:528:DC%2BD3sXjs1Oqsr0%3D",{},{"id":780,"text":905,"url":782,"identifiers":906},"AA Michalczyk J Allen RC Blomeley ML Ackland (2002) ArticleTitleConstitutive expression of hZnT4 zinc transporter in human breast epithelial cells Biochemical J 364 105–113 Occurrence Handle1:CAS:528:DC%2BD38XktFWiu7g%3D",{"doi":784},{"id":20,"text":908,"url":909,"identifiers":910},"MS Nasir CJ Fahrni DA Suhy et al. (1999) ArticleTitleThe chemical cell biology of zinc: structure and intracellular fluorescence of a zinc-quinolinesulfonamide complex J Biol Inorg Chem 4 775–783 Occurrence Handle10631609 Occurrence Handle1:CAS:528:DC%2BD3cXhslWnsQ%3D%3D Occurrence Handle10.1007\u002Fs007750050350","http:\u002F\u002Fdx.doi.org\u002F10.1007\u002Fs007750050350",{"doi":911},"10.1007\u002Fs007750050350",{"id":20,"text":913,"url":914,"identifiers":915},"CE Outten TV O’Halloran (2001) ArticleTitleFemtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis Science 292 2488–2492 Occurrence Handle11397910 Occurrence Handle1:CAS:528:DC%2BD3MXkvFWlsrk%3D Occurrence Handle10.1126\u002Fscience.1060331","http:\u002F\u002Fdx.doi.org\u002F10.1126\u002Fscience.1060331",{"doi":916},"10.1126\u002Fscience.1060331",{"id":780,"text":918,"url":782,"identifiers":919},"RD Palmiter TB Cole SD Findley (1996a) ArticleTitleZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration Embo J 15 1784–1791 Occurrence Handle1:CAS:528:DyaK28XivVant7s%3D",{"doi":784},{"id":20,"text":921,"url":922,"identifiers":923},"RD Palmiter TB Cole CJ Quaife SD Findley (1996b) ArticleTitleZnT-3, a putative transporter of zinc into synaptic vesicles Proc Natl Acad Sci USA 93 14934–14939 Occurrence Handle1:CAS:528:DyaK28XnsVOrsrw%3D Occurrence Handle10.1073\u002Fpnas.93.25.14934","http:\u002F\u002Fdx.doi.org\u002F10.1073\u002Fpnas.93.25.14934",{"doi":924},"10.1073\u002Fpnas.93.25.14934",{"id":20,"text":926,"url":927,"identifiers":928},"KB Pierson (1985) ArticleTitleOccurrence and synthesis of a non-thionein, zinc-binding protein in the rainbow-trout (Salmo gairdneri) Comp Biochem Physiol C 81 71–75 Occurrence Handle2861061 Occurrence Handle1:STN:280:BiqB38bjvFc%3D Occurrence Handle10.1016\u002F0742-8413(85)90093-3","http:\u002F\u002Fdx.doi.org\u002F10.1016\u002F0742-8413(85)90093-3",{"doi":929},"10.1016\u002F0742-8413(85)90093-3",{"id":20,"text":931,"url":20,"identifiers":932},"A Qiu M Shayeghi C Hogstrand (2005) ArticleTitleMolecular cloning and␣functional characterization of a high-affinity zinc importer (DrZIP1) from zebrafish (Danio rerio) Biochem J 388 745–754 Occurrence Handle15683366 Occurrence Handle1:CAS:528:DC%2BD2MXkvVGhtrk%3D Occurrence Handle10.1042\u002FBJ20041807",{"doi":933},"10.1042\u002FBJ20041807",{"id":780,"text":935,"url":782,"identifiers":936},"G Ranaldi G Perozzi A Truong-Tran P Zalewski C Murgia (2002) ArticleTitleIntracellular distribution of labile Zn(II) and zinc transporter expression in kidney and MDCK cells Am J Physiol 283 F1365–F1375 Occurrence Handle1:CAS:528:DC%2BD38XpvVWit7o%3D",{"doi":784},{"id":20,"text":938,"url":20,"identifiers":939},"MJ Salguiero M Zubillaga A Lysionek et al. (2000) ArticleTitleZinc as an essential micronutrient: A review Nutr Res 20 737–755 Occurrence Handle10.1016\u002FS0271-5317(00)00163-9",{"doi":940},"10.1016\u002FS0271-5317(00)00163-9",{"id":20,"text":942,"url":943,"identifiers":944},"GR Sauer N Watabe (1989) ArticleTitleUltrastructural and histochemical aspects of zinc accumulation by fish scales Tissue & Cell 21 935–943 Occurrence Handle1:CAS:528:DyaK3cXhvFegt7c%3D Occurrence Handle10.1016\u002F0040-8166(89)90044-X","http:\u002F\u002Fdx.doi.org\u002F10.1016\u002F0040-8166(89)90044-x",{"doi":945},"10.1016\u002F0040-8166(89)90044-x",{"id":20,"text":947,"url":20,"identifiers":948},"SL Sensi D Ton-That PG Sullivan et al. (2003a) ArticleTitleModulation of mitochondrial function by endogenous Zn2+ pools Proc Natl Acad Sci USA 100 6157–6162 Occurrence Handle1:CAS:528:DC%2BD3sXjvFOlurw%3D Occurrence Handle10.1073\u002Fpnas.1031598100",{"doi":949},"10.1073\u002Fpnas.1031598100",{"id":20,"text":951,"url":20,"identifiers":952},"SL Sensi D Ton-That JH Weiss A Rothe KR Gee (2003b) ArticleTitleA new mitochondrial fluorescent zinc sensor Cell Calcium 34 281–284 Occurrence Handle1:CAS:528:DC%2BD3sXlvVCrtrY%3D Occurrence Handle10.1016\u002FS0143-4160(03)00122-2",{"doi":953},"10.1016\u002FS0143-4160(03)00122-2",{"id":20,"text":955,"url":956,"identifiers":957},"CF Shaw LB He A Munoz et al. (1997) ArticleTitleKinetics of reversible N-ethylmaleimide alkylation of metallothionein and the subsequent metal release J Biol Inorg Chem 2 65–73 Occurrence Handle1:CAS:528:DyaK2sXhvVGku7s%3D Occurrence Handle10.1007\u002Fs007750050107","http:\u002F\u002Fdx.doi.org\u002F10.1007\u002Fs007750050107",{"doi":958},"10.1007\u002Fs007750050107",{"id":960,"text":961,"url":962,"identifiers":963},"9768fbfa-6477-4549-a80f-30c6899f26f2","ZL Tang KJ Wasserloos XH Liu et al. (2002) ArticleTitleNitric oxide decreases the sensitivity of pulmonary endothelial cells to LPS-induced apoptosis in a zinc-dependent fashion Mol Cell Biochem 234 211–217 Occurrence Handle12162436 Occurrence Handle10.1023\u002FA:1015930927407","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1023\u002FA:1015930927407",{"doi":964},"10.1023\u002FA:1015930927407",{"id":780,"text":966,"url":782,"identifiers":967},"B Turan H Fliss M Desilets (1997) ArticleTitleOxidants increase intracellular free Zn2+ concentration in rabbit ventricular myocytes Am J Physiol 41 H2095–H2106",{"doi":784},{"id":20,"text":969,"url":20,"identifiers":970},"BL Vallee KH Falchuk (1993) ArticleTitleThe biochemical basis of zinc physiology Physiol Rev 73 79–118 Occurrence Handle8419966 Occurrence Handle1:CAS:528:DyaK3sXhvVyhtrY%3D",{},{"id":780,"text":972,"url":782,"identifiers":973},"PD Zalewski IJ Forbes WH Betts (1993) ArticleTitleCorrelation of apoptosis with change in intracellular labile Zn(II) using Zinquin [(2-methyl-8-P-toluenesulphonamido-6-quinolyloxy)acetic acid], a new specific fluorescent-probe for Zn(II) Biochem J 296 403–408 Occurrence Handle8257431 Occurrence Handle1:CAS:528:DyaK2cXjvVer",{"doi":784},{"id":975,"createTime":976,"updateTime":977,"relativeEntities":978,"slug":979,"properties":980,"entityType":233,"verifyStatus":234,"verifyTime":991,"verifyNote":236,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":992,"fullTextUrl":20,"authors":993,"publicationType":291,"publisherRelationship":1056,"citationCount":154,"citationInfo":1115,"publishDate":1118,"publishYear":1116,"citationAnalyzeStatus":359,"lastCitationAnalyze":1119,"indexDatabases":1120,"openAccess":20,"references":20,"isForceReanalyzing":362},"6987aec3-4edb-4ffa-80fb-df94d2b9d888","2023-12-27T16:22:01.624+00:00","2026-07-15T11:50:29.085+00:00",[],"Supplementation-of-zinc-mitigates-the-altered-uptake-and-turnover-of-65Zn-in-liver-and-whole-body-of-diabetic-rats",{"abstract":981,"title":983,"gsPaper":985,"references":987,"doi":989},{"EN":982},"Diabetes is a life threatening disease and its onset is linked with both environmental and genetic factors. Zinc metabolism gets altered during diabetes and results in many complications. The present study was designed to elucidate the effects of zinc supplementation on the biokinetics of 65Zn in whole body, liver and its biodistribution in diabetic rats. The animals were divided into four groups viz; normal control; diabetic (single intraperitoneal injection of alloxan 150 mg\u002Fkg body weight); zinc treated (227 mg\u002Fl in drinking water); and diabetic + zinc treated. To carry out biokinetics study, each rat was injected intraperitoneally with 0.74 MBq radioactivity of 65Zn following 4 weeks of different treatments and the radioactivity was determined by using a suitably shielded scintillation counter. Alloxan induced diabetic rats showed a significant decrease in both the fast (Tb1) and slow (Tb2) components of biological half-life of 65Zn which, however, were normalized in whole body (P > 0.05) following zinc supplementation. In case of liver, Tb2 component was brought back to the normal but Tb1 component was not increased significantly. The present study indicates that the paucity of zinc in the tissues of the diabetic animals was due to decreased retention of tissue zinc as evidenced by increased serum Zn, hyperzincuria and increased rate of uptake of 65Zn by the liver. Zinc supplementation caused a significant improvement in the retention of zinc in the tissues and is therefore likely to be of benefit in the treatment of diabetes.",{"EN":984},"Supplementation of zinc mitigates the altered uptake and turnover of 65Zn in liver and whole body of diabetic rats",{"VOID":986},"[\"5968841241208325672\"]",{"VOID":988},"Ackland ML, Michalczyk A (2006) Zinc deficiency and its inherited disorders: a review. Genes Nut 1:41\nAdachi Y, Yoshida J, Kodera Y, Kiss T, Jakusch T, Enyedy EA, Yoshikawa Y, Sakurai H (2006) Oral administration of a zinc complex improves type diabetes and metabolic syndromes. Biochem Biophys Res Commun 351:165–170\nAl-Maroof RA, Al-Sharbatti SS (2006) Serum zinc levels in diabetic patients and effect of zinc supplementation on glycemic control of type 2 diabetes. Saudi Med J 27:344–350\nAtsushi T, K Kazuhiko G, Tetsu S et al (1998) Zinc-specific response in metallothionein induction in liver of tumor-bearing mice. J Trace Elem Exp Med 10:243–248\nBatista MN, Cuppari L, de Fatima C, Pedrosa L, Almeida MG, de Almeida JB, de Medeiros AC, Canziani ME (2006) Effect of end-stage renal disease and diabetes on zinc and copper status. Biol Trace Elem Res 112:1–12\nCai Lu (2004) Metallothionein as an adaptive protein prevents diabetes and its toxicity. Nonlinearity Biol Toxicol Med 2:89–103\nChaira D, Peter ZD, Giuditta P et al (2007) Zinc fluxes and zinc transporters genes in chronic diseases. Mutat Res 622:84–93\nChausmer AB (1998) Zinc insulin and diabetes. J Am Coll Nutr 17:109–115\nColeman JE (1992) Zinc proteins: enzymes, storage proteins, transcription factors, and replication proteins. Annu Rev Biochem 61:897–946\nCousins RJ (1986) Toward a molecular understanding of zinc metabolism. Clin Physiol Biochem 4:20–30\nDhawan DK, Goel A (1994) Protective role of zinc on rat liver function in long term toxicity induced by carbon tetrachloride. J Trace Elem Exp Med 7:1–9\nEide DJ (2000) Metal ion transport in eukaryotic microorganisms insights from Saccharomyces cerevisiae. Adv Microb Physio 43:1–38\nHenkin RI, Foster DM, Aamodt RL, Berman M (1984) Zinc metabolism in adrenal cortical insufficiency: effects of carbohydrate-active steroids. Metabolism 33:491\nHui S, Haihong Q, Junsheng G (2008) Cooperation of metallotheionein and zinc transporters for regulating zinc homeostasis in human intestinal Caco-2 cells. Nutr Res 28:406–413\nJansen J, Karges W, Rink L (2009) Zinc and diabetes—clinical links and molecular mechanisms. J Nutr Biochem 20:399–417\nKambe T, Narita H, Yamaguchi-Iwai Y et al (2002) Cloning and characterization of a novel mammalian zinc transporter, zinctransporter5, abundantly expressed in pancreatic cells. J Biol Chem 277(21):19049–19055\nKing JC, Shames DM, Woodhouse LR (2000) Zinc homeostasis in humans. J Nutr 130:1360S\nLevine AS, McClain CJ, Handwerger BS, Brown DM, Morley JE (1983) Tissue zinc status of genetically induced diabetic and streptozotocin-induced diabetic mice. Am J Clin Nutr 37:382–386\nLiuzzi JP, Cousins RJ (2004) Mammalian zinc transporters. Annu Rev Nutr 24:151–172\nLowe NM, Bremnr I, Jackson MJ (1991) Plasma 65Zn kinetics in the rat. Br J Nutr 64:445\nMateo MC, Bustamante JB, Cantalapiedra MA (1978) Serum, zinc, copper and insulin in diabetes mellitus. Biomedicine 29(2):56–58\nOhly P, Wang Z, Abel J, Gleichmann H (1998) Zinc sulphate induced metallothionein in pancreatic islets and protected against the diabetogenic toxin streptozotocin. Talanta 46:355–359\nParker MM, Humoller FL, Mahler DJ (1967) Determination of copper and zinc in biological samples. Clin Chem 13:40\nPathak A, Mahmood A, Pathak R, Dhawan D (2008) Effects of zinc on hepatic drug metabolism under ethanol toxicity. Drug Chem Toxicol 31:163–168\nQuarishi I, Collins S, Pestaner JP et al (2005) Role of zinc and zinc transporters in the molecular pathogenesis of diabetes mellitus. Med Hypothesis 65:887–892\nReeves PG, Rossow KL, Bobilya DJ (1994) Zinc-induced metallothionein and copper metabolism in intestinal mucosa, liver, and kidney of rats. Nutr Res 14:897–908\nRungby J (2010) Zinc, zinc transporters and diabetes. Diabetologia 53:1549–1551\nSalgueiro MJ, Zubillaga M, Lysionek A et al (2000) Zinc as an essential micronutrient: a review. Nutr Res 20:737\nSalgueiro MJ, Krebs N, Zubillaga MB, Weill R, Postaire E, Lysionek AE, Caro RA (2001) Diabetes zinc mellitus: is there a need of zinc supplementation in diabetes mellitus patients? Biol Trace Elem Res 81:215–228\nShahidul MI, Loots DT (2007) Diabetes, metallothionein and zinc interactions: a review. Biofactors 29:203–212\nSharma R, Dhawan D, Sharma RR, Dash RJ (1985) Effects of alloxan induced diabetes mellitus on uptake and biological half-life of I-131 in rat thyroid. IRCS Med Sci 13:90\nShiroi A, Yoshikawa M, Yokota H, Fukui H, Ishizaka S, Tatsumi K et al (2002) Identification of insulin-producing cells derived from embryonic stem cells by zinc-chelating dithizone. Stem Cells 20(4):284–292\nSidhu P, Garg ML, Dhawan DK (2004) Effect of zinc on biological half-lives of 65Zn in whole body and liver and on distribution of 65Zn in different organs of rats following nickel toxicity. Biol Trace Elem Res 102:173–188\nSondergaard LG, Stoltenberg M, Flyvbjerg A et al (2003) Zinc ions in b-cells of obese, insulin-resistant, and type2 diabetic rats traced by autometallography. APMIS 111(12):1147–1154\nTudor R, Zalewski PD, Ratnaike RN (2005) Zinc in health and chronic disease. J Nutr Health Aging 9:45–51\nVallee BL, Falchuk KH (1993) The biochemical basis of zinc physiology. Physio Rev 73:79\nWastney ME, House WA, Barnes RM et al (2000) Kinetic of zinc metabolism: variation with diet, genetics and disease. J Nutr 130:1355S",{"VOID":990},"10.1007\u002Fs10534-011-9461-2","2024-05-14T06:28:11.592+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10534-011-9461-2",[994,1011,1026,1041],{"id":995,"sortIndex":21,"researcher":20,"roles":996,"affiliations":997,"properties":1006},"c24bbc34-78d2-4bdd-9562-bcf6c9c7e25f",[242],[998],{"id":999,"sortIndex":21,"affiliation":1000,"properties":20},"3486ca39-f3ee-454c-ac4a-87db89bd11f5",{"id":999,"createTime":20,"updateTime":20,"relativeEntities":1001,"slug":20,"properties":1002,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1005,"statistic":20},[],{"title":1003},{"VI":1004},"Department of Biotechnology, GGDSD College, Sector-32, Chandigarh, India",[],{"title":1007,"gsAuthor":1009},{"VI":1008},"Ashima Pathak",{"VOID":1010},"[\"AFkFEMEAAAAJ\"]",{"id":1012,"sortIndex":259,"researcher":20,"roles":1013,"affiliations":1014,"properties":1023},"1f292009-da65-4442-8a09-2a5d96415b9d",[242],[1015],{"id":1016,"sortIndex":21,"affiliation":1017,"properties":20},"2426adbf-69ac-4487-8331-f49dfe933011",{"id":1016,"createTime":20,"updateTime":20,"relativeEntities":1018,"slug":20,"properties":1019,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1022,"statistic":20},[],{"title":1020},{"VI":1021},"Department of Biophysics, Panjab University, Chandigarh, India",[],{"title":1024},{"VI":1025},"Vishawjyoti Sharma",{"id":1027,"sortIndex":277,"researcher":20,"roles":1028,"affiliations":1029,"properties":1036},"8a20cc1c-bbaf-40d6-b8d1-185ddc6d565e",[242],[1030],{"id":1016,"sortIndex":21,"affiliation":1031,"properties":20},{"id":1016,"createTime":20,"updateTime":20,"relativeEntities":1032,"slug":20,"properties":1033,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1035,"statistic":20},[],{"title":1034},{"VI":1021},[],{"title":1037,"gsAuthor":1039},{"VI":1038},"Sanjeev Kumar",{"VOID":1040},"[\"B-39HpoAAAAJ\"]",{"id":1042,"sortIndex":357,"researcher":20,"roles":1043,"affiliations":1044,"properties":1051},"33d65f51-d2f0-4243-ab15-f8760a752e92",[242],[1045],{"id":1016,"sortIndex":21,"affiliation":1046,"properties":20},{"id":1016,"createTime":20,"updateTime":20,"relativeEntities":1047,"slug":20,"properties":1048,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1050,"statistic":20},[],{"title":1049},{"VI":1021},[],{"title":1052,"gsAuthor":1054},{"VI":1053},"D. K. Dhawan",{"VOID":1055},"[\"vDdmLewAAAAJ\"]",{"url":992,"publisher":1057,"properties":1111},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1058,"slug":10,"properties":1059,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":1063,"manageAffiliations":1080,"indexDatabases":1091,"url":100,"thumbnailPath":20,"statistic":1106,"gsStatistic":20,"type":211,"analyzePriority":20},[],{"issn":1060,"title":1061,"eissn":1062},{"VOID":13},{"EN":15},{"VOID":17},[1064,1068,1072,1076],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":1065,"label":1066,"description":1067,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":1069,"label":1070,"description":1071,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":1073,"label":1074,"description":1075,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":1077,"label":1078,"description":1079,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},[1081,1086],{"id":49,"createTime":20,"updateTime":20,"relativeEntities":1082,"slug":20,"properties":1083,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1085,"statistic":20},[],{"title":1084},{"EN":53},[55],{"id":57,"createTime":20,"updateTime":20,"relativeEntities":1087,"slug":20,"properties":1088,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1090,"statistic":20},[],{"title":1089},{"EN":61},[],[1092,1099],{"id":65,"indexDatabase":1093,"url":20,"indexYears":20,"academicFieldIds":1098,"indexDatabaseRanking":20},{"id":67,"createTime":20,"updateTime":20,"relativeEntities":1094,"label":1095,"description":1096,"key":74,"publicationTags":1097,"standard":20},[],{"EN":70,"VI":70},{"EN":72,"VI":73},[76,77],[79],{"id":81,"indexDatabase":1100,"url":92,"indexYears":93,"academicFieldIds":1105,"indexDatabaseRanking":99},{"id":83,"createTime":20,"updateTime":20,"relativeEntities":1101,"label":1102,"description":1103,"key":89,"publicationTags":1104,"standard":20},[],{"EN":86,"VI":86},{"EN":86,"VI":88},[91],[95,96,97,98],{"impactFactor":21,"impactFactorByYear":1107,"i10Index":113,"i10IndexLast5Year":114,"totalPublication":115,"totalPublicationByYear":1108,"totalCitation":151,"totalCitationByYear":1109,"totalCitationPerPublication":181,"totalCitationPerPublicationByYear":1110,"hindexLast5Year":123,"hindex":123},{"2012":103,"2013":104,"2014":105,"2015":103,"2016":106,"2017":107,"2018":108,"2019":105,"2020":109,"2021":110,"2022":111,"2023":112},{"1988":117,"1989":118,"1990":119,"1991":120,"1992":121,"1993":122,"1994":123,"1995":124,"1996":125,"1997":126,"1998":127,"1999":128,"2000":129,"2001":130,"2002":131,"2003":132,"2004":133,"2005":134,"2006":135,"2007":136,"2008":132,"2009":137,"2010":138,"2011":139,"2012":140,"2013":141,"2014":142,"2015":143,"2016":143,"2017":144,"2018":145,"2019":146,"2020":129,"2021":147,"2022":148,"2023":149,"2024":150},{"1989":153,"1990":154,"1991":155,"1992":156,"1993":157,"1994":158,"1995":159,"1996":160,"2004":161,"2005":162,"2006":163,"2007":164,"2008":165,"2009":166,"2010":167,"2011":168,"2012":169,"2013":170,"2014":171,"2015":172,"2016":173,"2017":174,"2018":175,"2019":176,"2020":177,"2021":178,"2022":179,"2023":180},{"1989":183,"1990":184,"1991":185,"1992":186,"1993":187,"1994":188,"1995":189,"1996":190,"2004":191,"2005":192,"2006":193,"2007":194,"2008":195,"2009":196,"2010":197,"2011":198,"2012":199,"2013":200,"2014":201,"2015":202,"2016":203,"2017":204,"2018":205,"2019":206,"2020":207,"2021":208,"2022":209,"2023":210},{"pages":1112,"volume":1114},{"VOID":1113},"1027-1034",{"VOID":459},{"total":154,"publishYear":1116,"statisticByYear":1117},2011,{"2012":277,"2013":277,"2014":356,"2015":259,"2016":357,"2017":259,"2019":259,"2020":259,"2021":259,"2023":259},"2011-05-17","2026-07-15T11:50:29.084+00:00",[76,99],{"id":1122,"createTime":1123,"updateTime":1124,"relativeEntities":1125,"slug":1126,"properties":1127,"entityType":233,"verifyStatus":234,"verifyTime":1138,"verifyNote":236,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1139,"fullTextUrl":20,"authors":1140,"publicationType":291,"publisherRelationship":1156,"citationCount":20,"citationInfo":20,"publishDate":1216,"publishYear":1217,"citationAnalyzeStatus":1218,"lastCitationAnalyze":1219,"indexDatabases":1220,"openAccess":20,"references":20,"isForceReanalyzing":362},"ab26b4c0-fe68-494e-814a-0336f9ae4561","2024-02-12T02:49:28.230+00:00","2026-07-14T20:02:25.395+00:00",[],"Biological-activity-of-organometallic-bismuth-compounds",{"abstract":1128,"title":1130,"gsPaper":1132,"references":1134,"doi":1136},{"EN":1129},"The chemical aspects of organometallic bismuth(Ill) compounds are discussed with respect to the stability of the metal-carbon σ bond, their low dipole moments, and the limited solubility of these complexes in hydrophilic solvents. A new Bi heterocycle, which is of potential interest in terms of stability and solution behaviour, was shown to exist as an intermediate under the conditions in the mass spectrometer. Although generally bismuth organic compounds are extremely toxic, in the 1970s they became important as biocides and this is still being investigated. They have also been discussed as irritation causing chemical warfare agents. While their application in chemotherapy never became very widespread because antibiotics were discovered, in the last few years the antitumor activity of some derivatives has been reported.",{"EN":1131},"Biological activity of organometallic bismuth compounds",{"VOID":1133},"[]",{"VOID":1135},"American Cyanamid Co. (1965) Br. P. 1.003.685\nAmerican Cyanamid Co. (1964\u002F1968) U.S.P. 3.395.212\nAmmedick E (1980) Bausteine der Chemie. Militärchemie — eine Einführung. VEB Deutscher Verlag Grundstoffindustrie, Leipzig\nBagramyan SB, Babayan EA, Dartyan RM (1975) Long-term effects of single-dose and chronic administration of copper and bismuth on laboratory animals. Biol Zh Arm 28:56–62\nCoates GE, Green MLH, Wade K (1967) Organometallic compounds, vol 1, chapt 5. Methuen, London\nDelmas-Marsalet P, Arné B (1949) A case of bismuth poisoning. J Med Bord Sud-Quest 126:76\nDub M (1968) Organometallic compounds: methods of synthesis, physical constants and chemical reactions; compounds of arsenic, antimony and bismuth, vol 3. Springer, Berlin Heidelberg New York\nDyson GM (1928) Bismuth in pharmacy and chemistry. Pharm J 120:242–244\nEhrlich P (1910) Vorträge über die Behandlung der Syphilis mit dem Ehrlichschen Präparat 606. Berl Klin Wochenschr 47:1996\nElschenbroich C, Salzen A (1986) Organometallchemie. Teubner, Stuttgart\nGiemsa G (1924) Über die chemotherapeutische Wirkung des Arsens, Antimons und Wismuths. Z Angew Chem37:765–788\nGross FJ (American Cyanamid Co.) (1962\u002F1965) U.S.P. 3.197.314\nGross FJ (American Cyanamid Co.) (1964\u002F1968) U.S.P. 3.395.212\nGross R, Schölmerich P (1973) Lehrbuch der Inneren Medizin. Schattauer, Stuttgart\nHaiduc I, Zuckerman JJ (1985) Basic organometallic chemistry. de Gruyter, Berlin New York\nKlapötke T (1987a) Synthese, spektroskopische Charakterisierung und bakterizide Wirksamkeit neuer Organylbis(thiophenolato)bismut(III)-Komplexe. J Organomet Chem331:299–307\nKlapötke T (1987b) Synthesis and characterization of novel chalcogen and pnictogen coordinated Bi(III) complexes — the first Se,Se′ coordinated Bi metallacycle. Polyhedron 6:1593–1597\nKlapötke T (1987c) Biological activity of novel bismuth chalcogenolate complexes (seminar). Maritime Inorganic Discussion Weekend, Sackville, New Brunswick, Canada\nKlapötke T (1987d) Biologische Aktivität neuer Bismut(III)organylchalkogenolat-Komplexe (Poster). 21. GDCh-Hauptversammlung, Berlin\nKlapötke T (1988) Methylbis(thiomethanolato)bismut(III) —Synthese, Charakterisierung und mikrobiologische Aktivität. Monatsh Chem (in press)\nKlapötke T, Gowik P (1987) Methylbis(2,6-dichlorthiophenolato)bismut(III) — Synthese, fungizide und bakterizide Aktivität. Z Naturforsch 42b:940–942\nKöpf H, Klapötke T, Köpf-Maier P (1986) Titanocene mercaptoanilinium derivatives as new antitumor agents (seminar). INOR 132, ACS National Meeting, Anaheim, Calif\nKöpf-Maier P (1987) Cytostatische nicht-Platinmetall-Komplexe: neue Perspektiven für die Krebsbehandlung? Naturwissenschaften 74:374–382\nKöpf-Maier P, Klapötke T (1988) Antitumor activity of some organometallic bismuth(III)thiolates. Inorg Chim Acta152 No. 1; 49–52\nKooistra JA (Procter and Gamble Co.) (1970\u002F74) U.S.P. 3.852.441\nKuschinsky G, Lüllmann H (1974) Lehrbuch der Pharmakologie. Thieme, Stuttgart\nLanger HG (Dow Chemical Co.) (1964\u002F69) U.S.P. 3.442.922\nLecoq H (1937) Role des arsines, stibines et bismuthines en toxicologie. J Pharm. Belg 19:173–181\nLeebrick JR (M&T Chemicals, Inc.) (1962\u002F65) U.S.P. 3.239.411\nLeebrick JR (M&T Chemicals, Inc.) (1962\u002F66) U.S.P. 3.247.050\nMcCombie H, Saunders BC (1947) Toxic organo-lead compounds. Nature 159:491–494\nMeyer RJ, Pietsch EHE (1952) Arsen. Gmelin Handbuch der anorganischen Chemie, vol 17. Springer, Berlin Heidelberg New York\nM&T Chemicals, Inc. (1964a) Neth. Appl. 6.405.308\nM&T Chemicals, Inc. (1964b) Neth. Appl. 6.405.309\nPschyrembel (1982) Klinisches Wörterbuch. de Gruyter, Berlin New York\nPyman FL (1935) Some lines of chemotherapeutic research. Chem Ind: 580–585\nRaiziss GW, Severac M, Moetsch JC (1934) Toxicity of various compounds of bismuth used in the therapy of syphilis. J Chemother 10:77–87\nRosenberg B, Camp Lvan, Krigas T (1965) Inhibition of cell division inEscherichia coli by electrolysis products from a platinum electrode. Nature 205:698\nRosenberg B, Camp Lvan, Grimley EB, Thomson AJ (1967a) The inhibition of growth or cell division inEscherichia coli by different ionic species of platinum(IV) complexes. J Biol Chem 242:1347\nRosenberg B, Renshaw E, Camp Lvan, Hartwick J, Drobuik J (1967b) Platinum-induced filamentous growth inEscherichia coli. J Bacteriol 93:716\nRosenberg B, Camp Lvan, Trosko JE, Mansour VH (1969) Platinum compounds: a new class of potent antitumor agents. Nature 222:385–386\nRosenberg B (1985) Fundamental studies with cisplatin. Cancer 55:2303\nSaggers DT (Fisons Ltd) (1970) D.P. 2.005.409\nSmith JD (1973) Arsenic, antimony and bismuth. In: Bailar JC, Emeléus HJ, Nyholm Sir R, Trotman-Dickenson AF (eds) Comprehensive inorganic chemistry, vol 2. Pergamon Press, Oxford, pp 622–671\nSollmann T, Seifter J (1939) Pharmacology of trimethylbismuth. J Pharmacol 67:17–49\nStöhr R (1985) Chemische Kampfstoffe und Schutz vor chemischen Kampfstoffen. Militärverlag der DDR, Berlin\nStrube I, Stolz R, Remane H (1986) Geschichte der Chemie. VEB Deutscher Verlag der Wissenschaften, Berlin\nWallhäuser KH (1984) Praxis der Sterilisation — Desinfektion — Konservierung. Thieme, Stuttgart\nWieber M (1977) Bismut-Organische Verbindungen. Gmelin Handbuch der anorganischen Chemie, vol 47. Springer, Berlin Heidelberg New York",{"VOID":1137},"10.1007\u002FBF01138064","2024-06-26T04:14:45.978+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF01138064",[1141],{"id":1142,"sortIndex":21,"researcher":20,"roles":1143,"affiliations":1144,"properties":1153},"e19ebbf0-fca9-42df-86a0-18b700404257",[242],[1145],{"id":1146,"sortIndex":21,"affiliation":1147,"properties":20},"186620b5-b5d9-431f-9204-dfa7672e4d51",{"id":1146,"createTime":20,"updateTime":20,"relativeEntities":1148,"slug":20,"properties":1149,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1152,"statistic":20},[],{"title":1150},{"EN":1151},"Department of Chemistry, University of New Brunswick, Fredericton, Canada",[],{"title":1154},{"VI":1155},"Thomas Klapötke",{"url":1139,"publisher":1157,"properties":1211},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1158,"slug":10,"properties":1159,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":1163,"manageAffiliations":1180,"indexDatabases":1191,"url":100,"thumbnailPath":20,"statistic":1206,"gsStatistic":20,"type":211,"analyzePriority":20},[],{"issn":1160,"title":1161,"eissn":1162},{"VOID":13},{"EN":15},{"VOID":17},[1164,1168,1172,1176],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":1165,"label":1166,"description":1167,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":1169,"label":1170,"description":1171,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":1173,"label":1174,"description":1175,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":1177,"label":1178,"description":1179,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},[1181,1186],{"id":49,"createTime":20,"updateTime":20,"relativeEntities":1182,"slug":20,"properties":1183,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1185,"statistic":20},[],{"title":1184},{"EN":53},[55],{"id":57,"createTime":20,"updateTime":20,"relativeEntities":1187,"slug":20,"properties":1188,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1190,"statistic":20},[],{"title":1189},{"EN":61},[],[1192,1199],{"id":65,"indexDatabase":1193,"url":20,"indexYears":20,"academicFieldIds":1198,"indexDatabaseRanking":20},{"id":67,"createTime":20,"updateTime":20,"relativeEntities":1194,"label":1195,"description":1196,"key":74,"publicationTags":1197,"standard":20},[],{"EN":70,"VI":70},{"EN":72,"VI":73},[76,77],[79],{"id":81,"indexDatabase":1200,"url":92,"indexYears":93,"academicFieldIds":1205,"indexDatabaseRanking":99},{"id":83,"createTime":20,"updateTime":20,"relativeEntities":1201,"label":1202,"description":1203,"key":89,"publicationTags":1204,"standard":20},[],{"EN":86,"VI":86},{"EN":86,"VI":88},[91],[95,96,97,98],{"impactFactor":21,"impactFactorByYear":1207,"i10Index":113,"i10IndexLast5Year":114,"totalPublication":115,"totalPublicationByYear":1208,"totalCitation":151,"totalCitationByYear":1209,"totalCitationPerPublication":181,"totalCitationPerPublicationByYear":1210,"hindexLast5Year":123,"hindex":123},{"2012":103,"2013":104,"2014":105,"2015":103,"2016":106,"2017":107,"2018":108,"2019":105,"2020":109,"2021":110,"2022":111,"2023":112},{"1988":117,"1989":118,"1990":119,"1991":120,"1992":121,"1993":122,"1994":123,"1995":124,"1996":125,"1997":126,"1998":127,"1999":128,"2000":129,"2001":130,"2002":131,"2003":132,"2004":133,"2005":134,"2006":135,"2007":136,"2008":132,"2009":137,"2010":138,"2011":139,"2012":140,"2013":141,"2014":142,"2015":143,"2016":143,"2017":144,"2018":145,"2019":146,"2020":129,"2021":147,"2022":148,"2023":149,"2024":150},{"1989":153,"1990":154,"1991":155,"1992":156,"1993":157,"1994":158,"1995":159,"1996":160,"2004":161,"2005":162,"2006":163,"2007":164,"2008":165,"2009":166,"2010":167,"2011":168,"2012":169,"2013":170,"2014":171,"2015":172,"2016":173,"2017":174,"2018":175,"2019":176,"2020":177,"2021":178,"2022":179,"2023":180},{"1989":183,"1990":184,"1991":185,"1992":186,"1993":187,"1994":188,"1995":189,"1996":190,"2004":191,"2005":192,"2006":193,"2007":194,"2008":195,"2009":196,"2010":197,"2011":198,"2012":199,"2013":200,"2014":201,"2015":202,"2016":203,"2017":204,"2018":205,"2019":206,"2020":207,"2021":208,"2022":209,"2023":210},{"pages":1212,"volume":1214},{"VOID":1213},"69-76",{"VOID":1215},"1","1988-09-01",1988,"ERROR_IN_GET_PLATFORM_ID","2026-07-14T20:02:25.394+00:00",[76],{"id":1222,"createTime":1223,"updateTime":1224,"relativeEntities":1225,"slug":1226,"properties":1227,"entityType":233,"verifyStatus":234,"verifyTime":1238,"verifyNote":236,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1239,"fullTextUrl":20,"authors":1240,"publicationType":291,"publisherRelationship":1323,"citationCount":21,"citationInfo":1383,"publishDate":1386,"publishYear":1384,"citationAnalyzeStatus":19,"lastCitationAnalyze":1387,"indexDatabases":1388,"openAccess":20,"references":20,"isForceReanalyzing":362},"dfa7676c-a85d-4738-8094-68f8866e3482","2024-01-16T16:39:51.574+00:00","2026-07-14T06:57:12.130+00:00",[],"Iron-status-and-lipopolysaccharide-regulate-Ndfip1-by-activation-of-nuclear-factor-kappa-B",{"abstract":1228,"title":1230,"gsPaper":1232,"references":1234,"doi":1236},{"EN":1229},"Nedd4 family interacting protein 1 (Ndfip1) is an adaptor protein for the Nedd4 family of ubiquitin ligases that target proteins for degradation. Recent studies confirmed the role of Ndfip1 as a regulator of iron metabolism and pointed out that Ndfip1 was involved in iron homeostasis by regulating the degradation of iron importer divalent metal transporter 1 (DMT1). However, little is known about how Ndfip1 is regulated. The aim of this article was to investigate the regulation of Ndfip1 levels and the possible mechanisms. In this study, we investigated the effect of various stimuli, including iron status and lipopolysaccharide (LPS) on Ndfip1 expression in MES23.5 dopaminergic cell lines. Results showed that Ndfip1 expression in these cells was enhanced by ferrous iron overload, but not ferric iron overload, and decreased after iron deprivation by deferoxamine. In addition, LPS could significantly increase the expression of Ndfip1. Furthermore, we demonstrated that the regulation of Ndfip1 expression by these various stimuli was achieving by activation of nuclear factor-kappa B. We speculate that iron status and LPS may contribute to the changes of Ndfip1 expression by activation of nuclear factor-kappa B.",{"EN":1231},"Iron status and lipopolysaccharide regulate Ndfip1 by activation of nuclear factor-kappa B",{"VOID":1233},"[\"15934937348145981089\"]",{"VOID":1235},"Anderson CP, Shen M, Eisenstein RS, Leibold EA (2012) Mammalian iron metabolism and its control by iron regulatory proteins. Biochim Biophys Acta 1823(9):1468–1483. doi:10.1016\u002Fj.bbamcr.2012.05.010\nBarton JC, Bertoli LF (2010) Pica associated with iron deficiency or depletion: clinical and laboratory correlates in 262 non-pregnant adult outpatients. BMC Blood Disord 10:9. doi:10.1186\u002F1471-2326-10-9\nBeard J (2003) Iron deficiency alters brain development and functioning. J Nutr 133(5 Suppl 1):1468S–1472S\nBoelmans K, Holst B, Hackius M, Finsterbusch J, Gerloff C, Fiehler J, Munchau A (2012) Brain iron deposition fingerprints in Parkinson’s disease and progressive supranuclear palsy. Mov Disord 27(3):421–427. doi:10.1002\u002Fmds.24926\nChen LC, Hsu C, Chiueh CC, Lee WS (2012) Ferrous citrate up-regulates the NOS2 through nuclear translocation of NFkappaB induced by free radicals generation in mouse cerebral endothelial cells. PLoS ONE 7(9):e46239. doi:10.1371\u002Fjournal.pone.0046239\nCrawford GD Jr, Le WD, Smith RG, Xie WJ, Stefani E, Appel SH (1992) A novel N18TG2 x mesencephalon cell hybrid expresses properties that suggest a dopaminergic cell line of substantia nigra origin. J Neurosci 12(9):3392–3398\nDing H, Yan CZ, Shi H, Zhao YS, Chang SY, Yu P, Wu WS, Zhao CY, Chang YZ, Duan XL (2011) Hepcidin is involved in iron regulation in the ischemic brain. PLoS ONE 6(9):e25324. doi:10.1371\u002Fjournal.pone.0025324\nEisenstein RS (2000) Iron regulatory proteins and the molecular control of mammalian iron metabolism. Annu Rev Nutr 20:627–662. doi:10.1146\u002Fannurev.nutr.20.1.627\nFoot NJ, Dalton HE, Shearwin-Whyatt LM, Dorstyn L, Tan SS, Yang B, Kumar S (2008) Regulation of the divalent metal ion transporter DMT1 and iron homeostasis by a ubiquitin-dependent mechanism involving Ndfips and WWP2. Blood 112(10):4268–4275. doi:10.1182\u002Fblood-2008-04-150953\nFoot NJ, Leong YA, Dorstyn LE, Dalton HE, Ho K, Zhao L, Garrick MD, Yang B, Hiwase D, Kumar S (2011) Ndfip1-deficient mice have impaired DMT1 regulation and iron homeostasis. Blood 117(2):638–646. doi:10.1182\u002Fblood-2010-07-295287\nGarrick MD, Zhao L, Roth JA, Jiang H, Feng J, Foot NJ, Dalton H, Kumar S, Garrick LM (2012) Isoform specific regulation of divalent metal (ion) transporter (DMT1) by proteasomal degradation. Biometals 25(4):787–793. doi:10.1007\u002Fs10534-012-9522-1\nGuo F, Lou Y, Feng N, Li G, Xie A, Huang X, Wang Y (2010) Exposure to lanthanum compound diminishes LPS-induced inflammation-associated gene expression: involvements of PKC and NF-kappaB signaling pathways. Biometals 23(4):669–680. doi:10.1007\u002Fs10534-010-9327-z\nHarvey KF, Shearwin-Whyatt LM, Fotia A, Parton RG, Kumar S (2002) N4WBP5, a potential target for ubiquitination by the Nedd4 family of proteins, is a novel Golgi-associated protein. J Biol Chem 277(11):9307–9317. doi:10.1074\u002Fjbc.M110443200\nHowitt J, Putz U, Lackovic J, Doan A, Dorstyn L, Cheng H, Yang B, Chan-Ling T, Silke J, Kumar S, Tan SS (2009) Divalent metal transporter 1 (DMT1) regulation by Ndfip1 prevents metal toxicity in human neurons. Proc Natl Acad Sci USA 106(36):15489–15494\nHsieh CH, Jeng SF, Hsieh MW, Chen YC, Rau CS, Lu TH, Chen SS (2008) Statin-induced heme oxygenase-1 increases NF-kappaB activation and oxygen radical production in cultured neuronal cells exposed to lipopolysaccharide. Toxicol Sci 102(1):150–159. doi:10.1093\u002Ftoxsci\u002Fkfm298\nHubert N, Hentze MW (2002) Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function. Proc Natl Acad Sci USA 99(19):12345–12350\nIngrassia R, Lanzillotta A, Sarnico I, Benarese M, Blasi F, Borgese L, Bilo F, Depero L, Chiarugi A, Spano PF, Pizzi M (2012) 1B\u002F(-)IRE DMT1 expression during brain ischemia contributes to cell death mediated by NF-kappaB\u002FRelA acetylation at Lys310. PLoS ONE 7(5):e38019. doi:10.1371\u002Fjournal.pone.0038019\nJin L, Wang J, Jin H, Fei G, Zhang Y, Chen W, Zhao L, Zhao N, Sun X, Zeng M, Zhong C (2012) Nigral iron deposition occurs across motor phenotypes of Parkinson’s disease. Eur J Neurol 19(7):969–976. doi:10.1111\u002Fj.1468-1331.2011.03658.x\nKooncumchoo P, Sharma S, Porter J, Govitrapong P, Ebadi M (2006) Coenzyme Q(10) provides neuroprotection in iron-induced apoptosis in dopaminergic neurons. J Mol Neurosci 28(2):125–141\nKristinsson J, Snaedal J, Torsdottir G, Johannesson T (2012) Ceruloplasmin and iron in Alzheimer’s disease and Parkinson’s disease: a synopsis of recent studies. Neuropsychiatr Dis Treat 8:515–521. doi:10.2147\u002FNDT.S34729\nLevenson CW, Tassabehji NM (2004) Iron and ageing: an introduction to iron regulatory mechanisms. Ageing Res Rev 3(3):251–263. doi:10.1016\u002Fj.arr.2004.03.001\nLiu L, Xu H, Jiang H, Wang J, Song N, Xie J (2010) Ghrelin prevents 1-methyl-4-phenylpyridinium ion-induced cytotoxicity through antioxidation and NF-kappaB modulation in MES23.5 cells. Exp Neurol 222(1):25–29. doi:10.1016\u002Fj.expneurol.2009.11.009\nMeans RT Jr (2013) Hepcidin and iron regulation in health and disease. Am J Med Sci 345(1):57–60. doi:10.1097\u002FMAJ.0b013e318253caf1\nMochizuki H, Yasuda T (2012) Iron accumulation in Parkinson’s disease. J Neural Transm 119(12):1511–1514. doi:10.1007\u002Fs00702-012-0905-9\nOliver PM, Cao X, Worthen GS, Shi P, Briones N, MacLeod M, White J, Kirby P, Kappler J, Marrack P, Yang B (2006) Ndfip1 protein promotes the function of itch ubiquitin ligase to prevent T cell activation and T helper 2 cell-mediated inflammations. Immunity 25(6):929–940\nParadkar PN, Roth JA (2006a) Nitric oxide transcriptionally down-regulates specific isoforms of divalent metal transporter (DMT1) via NF-kappaB. J Neurochem 96(6):1768–1777\nParadkar PN, Roth JA (2006b) Post-translational and transcriptional regulation of DMT1 during P19 embryonic carcinoma cell differentiation by retinoic acid. Biochem J 394(Pt 1):173–183\nPerez CA, Tong Y, Guo M (2008) Iron chelators as potential therapeutic agents for Parkinson’s disease. Curr Bioact Compd 4(3):150–158. doi:10.2174\u002F157340708786305952\nPutz U, Howitt J, Lackovic J, Foot N, Kumar S, Silke J, Tan SS (2008) Nedd4 family-interacting protein 1 (Ndfip1) is required for the exosomal secretion of Nedd4 family proteins. J Biol Chem 283(47):32621–32627. doi:10.1074\u002Fjbc.M804120200\nSalvador GA (2010) Iron in neuronal function and dysfunction. BioFactors 36(2):103–110. doi:10.1002\u002Fbiof.80\nSang Q, Kim MH, Kumar S, Bye N, Morganti-Kossman MC, Gunnersen J, Fuller S, Howitt J, Hyde L, Beissbarth T, Scott HS, Silke J, Tan SS (2006) Nedd4-WW domain-binding protein 5 (Ndfip1) is associated with neuronal survival after acute cortical brain injury. J Neurosci 26(27):7234–7244. doi:10.1523\u002FJNEUROSCI.1398-06.2006\nSchipper HM (2004) Brain iron deposition and the free radical-mitochondrial theory of ageing. Ageing Res Rev 3(3):265–301. doi:10.1016\u002Fj.arr.2004.02.001\nToyokuni S (2009) Role of iron in carcinogenesis: cancer as a ferrotoxic disease. Cancer Sci 100(1):9–16\nWang J, Du XX, Jiang H, Xie JX (2009) Curcumin attenuates 6-hydroxydopamine-induced cytotoxicity by anti-oxidation and nuclear factor-kappa B modulation in MES23.5 cells. Biochem Pharmacol 78(2):178–183. doi:10.1016\u002Fj.bcp.2009.03.031\nWeinberg ED (2009) Iron availability and infection. Biochim Biophys Acta 1790(7):600–605. doi:10.1016\u002Fj.bbagen.2008.07.002\nWu S, Zhang K, Lv C, Wang H, Cheng B, Jin Y, Chen Q, Lian Q, Fang X (2012) Nuclear factor-kappaB mediated lipopolysaccharide-induced mRNA expression of hepcidin in human peripheral blood leukocytes. Innate Immun 18(2):318–324. doi:10.1177\u002F1753425911405087\nXu H, Jiang H, Wang J, Xie J (2010) Rg1 protects iron-induced neurotoxicity through antioxidant and iron regulatory proteins in 6-OHDA-treated MES23.5 cells. J Cell Biochem 111(6):1537–1545. doi:10.1002\u002Fjcb.22885\nZecca L, Youdim MB, Riederer P, Connor JR, Crichton RR (2004) Iron, brain ageing and neurodegenerative disorders. Nat Rev Neurosci 5(11):863–873. doi:10.1038\u002Fnrn1537\nZhang Z, Zhang K, Du X, Li Y (2012) Neuroprotection of desferrioxamine in lipopolysaccharide-induced nigrostriatal dopamine neuron degeneration. Mol Med Rep 5(2):562–566. doi:10.3892\u002Fmmr.2011.671\nZhang HY, Wang ND, Song N, Xu HM, Shi LM, Jiang H, Xie JX (2013) 6-Hydroxydopamine promotes iron traffic in primary cultured astrocytes. Biometals. doi:10.1007\u002Fs10534-013-9647-x\nZhao N, Zhang AS, Enns CA (2013) Iron regulation by hepcidin. J Clin Invest 123(6):2337–2343. doi:10.1172\u002FJCI67225",{"VOID":1237},"10.1007\u002Fs10534-013-9674-7","2024-05-09T18:11:19.932+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10534-013-9674-7",[1241,1256,1271,1284,1297,1310],{"id":1242,"sortIndex":21,"researcher":20,"roles":1243,"affiliations":1244,"properties":1253},"5c0680e9-aa6a-4a96-bf57-594e6d223fe6",[242],[1245],{"id":1246,"sortIndex":21,"affiliation":1247,"properties":20},"bfca6846-d984-47ef-ab53-763404231d07",{"id":1246,"createTime":20,"updateTime":20,"relativeEntities":1248,"slug":20,"properties":1249,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1252,"statistic":20},[],{"title":1250},{"VI":1251},"Department of Physiology, Shandong Provincial Key Laboratory of Pathogenesis and Prevention of Neurological Disorders and State Key Disciplines: Physiology, Medical College of Qingdao University, Qingdao, China",[],{"title":1254},{"VI":1255},"Huamin Xu",{"id":1257,"sortIndex":259,"researcher":20,"roles":1258,"affiliations":1259,"properties":1268},"917b095b-ff83-4820-b431-cc3d3d7e907d",[242],[1260],{"id":1261,"sortIndex":21,"affiliation":1262,"properties":20},"30c569c3-c681-47a0-80a0-ca80579469f7",{"id":1261,"createTime":20,"updateTime":20,"relativeEntities":1263,"slug":20,"properties":1264,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1267,"statistic":20},[],{"title":1265},{"VI":1266},"Department of Neurosurgery, the Affiliated Hospital of Medical College, Qingdao University, Qingdao, China",[],{"title":1269},{"VI":1270},"Qing Chang",{"id":1272,"sortIndex":277,"researcher":20,"roles":1273,"affiliations":1274,"properties":1281},"a0dbeab4-bdfe-4287-84bc-61386fb367eb",[242],[1275],{"id":1246,"sortIndex":21,"affiliation":1276,"properties":20},{"id":1246,"createTime":20,"updateTime":20,"relativeEntities":1277,"slug":20,"properties":1278,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1280,"statistic":20},[],{"title":1279},{"VI":1251},[],{"title":1282},{"VI":1283},"Wenting Jia",{"id":1285,"sortIndex":357,"researcher":20,"roles":1286,"affiliations":1287,"properties":1294},"aa03ac8e-23f3-4c48-8e75-83e3dd8c4e33",[242],[1288],{"id":1246,"sortIndex":21,"affiliation":1289,"properties":20},{"id":1246,"createTime":20,"updateTime":20,"relativeEntities":1290,"slug":20,"properties":1291,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1293,"statistic":20},[],{"title":1292},{"VI":1251},[],{"title":1295},{"VI":1296},"Hong Jiang",{"id":1298,"sortIndex":161,"researcher":20,"roles":1299,"affiliations":1300,"properties":1307},"d0b98ffe-1e46-46df-8957-e0e4d4257f58",[242],[1301],{"id":1261,"sortIndex":21,"affiliation":1302,"properties":20},{"id":1261,"createTime":20,"updateTime":20,"relativeEntities":1303,"slug":20,"properties":1304,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1306,"statistic":20},[],{"title":1305},{"VI":1266},[],{"title":1308},{"VI":1309},"Peng Sun",{"id":1311,"sortIndex":356,"researcher":20,"roles":1312,"affiliations":1313,"properties":1320},"30b42c32-3c3f-40e8-af3d-b6abf6763ebb",[242],[1314],{"id":1246,"sortIndex":21,"affiliation":1315,"properties":20},{"id":1246,"createTime":20,"updateTime":20,"relativeEntities":1316,"slug":20,"properties":1317,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1319,"statistic":20},[],{"title":1318},{"VI":1251},[],{"title":1321},{"VI":1322},"Junxia Xie",{"url":1239,"publisher":1324,"properties":1378},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1325,"slug":10,"properties":1326,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":1330,"manageAffiliations":1347,"indexDatabases":1358,"url":100,"thumbnailPath":20,"statistic":1373,"gsStatistic":20,"type":211,"analyzePriority":20},[],{"issn":1327,"title":1328,"eissn":1329},{"VOID":13},{"EN":15},{"VOID":17},[1331,1335,1339,1343],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":1332,"label":1333,"description":1334,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":1336,"label":1337,"description":1338,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":1340,"label":1341,"description":1342,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":1344,"label":1345,"description":1346,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},[1348,1353],{"id":49,"createTime":20,"updateTime":20,"relativeEntities":1349,"slug":20,"properties":1350,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1352,"statistic":20},[],{"title":1351},{"EN":53},[55],{"id":57,"createTime":20,"updateTime":20,"relativeEntities":1354,"slug":20,"properties":1355,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1357,"statistic":20},[],{"title":1356},{"EN":61},[],[1359,1366],{"id":65,"indexDatabase":1360,"url":20,"indexYears":20,"academicFieldIds":1365,"indexDatabaseRanking":20},{"id":67,"createTime":20,"updateTime":20,"relativeEntities":1361,"label":1362,"description":1363,"key":74,"publicationTags":1364,"standard":20},[],{"EN":70,"VI":70},{"EN":72,"VI":73},[76,77],[79],{"id":81,"indexDatabase":1367,"url":92,"indexYears":93,"academicFieldIds":1372,"indexDatabaseRanking":99},{"id":83,"createTime":20,"updateTime":20,"relativeEntities":1368,"label":1369,"description":1370,"key":89,"publicationTags":1371,"standard":20},[],{"EN":86,"VI":86},{"EN":86,"VI":88},[91],[95,96,97,98],{"impactFactor":21,"impactFactorByYear":1374,"i10Index":113,"i10IndexLast5Year":114,"totalPublication":115,"totalPublicationByYear":1375,"totalCitation":151,"totalCitationByYear":1376,"totalCitationPerPublication":181,"totalCitationPerPublicationByYear":1377,"hindexLast5Year":123,"hindex":123},{"2012":103,"2013":104,"2014":105,"2015":103,"2016":106,"2017":107,"2018":108,"2019":105,"2020":109,"2021":110,"2022":111,"2023":112},{"1988":117,"1989":118,"1990":119,"1991":120,"1992":121,"1993":122,"1994":123,"1995":124,"1996":125,"1997":126,"1998":127,"1999":128,"2000":129,"2001":130,"2002":131,"2003":132,"2004":133,"2005":134,"2006":135,"2007":136,"2008":132,"2009":137,"2010":138,"2011":139,"2012":140,"2013":141,"2014":142,"2015":143,"2016":143,"2017":144,"2018":145,"2019":146,"2020":129,"2021":147,"2022":148,"2023":149,"2024":150},{"1989":153,"1990":154,"1991":155,"1992":156,"1993":157,"1994":158,"1995":159,"1996":160,"2004":161,"2005":162,"2006":163,"2007":164,"2008":165,"2009":166,"2010":167,"2011":168,"2012":169,"2013":170,"2014":171,"2015":172,"2016":173,"2017":174,"2018":175,"2019":176,"2020":177,"2021":178,"2022":179,"2023":180},{"1989":183,"1990":184,"1991":185,"1992":186,"1993":187,"1994":188,"1995":189,"1996":190,"2004":191,"2005":192,"2006":193,"2007":194,"2008":195,"2009":196,"2010":197,"2011":198,"2012":199,"2013":200,"2014":201,"2015":202,"2016":203,"2017":204,"2018":205,"2019":206,"2020":207,"2021":208,"2022":209,"2023":210},{"pages":1379,"volume":1381},{"VOID":1380},"981-988",{"VOID":1382},"26",{"total":21,"publishYear":1384,"statisticByYear":1385},2013,{},"2013-09-18","2026-07-14T06:57:12.129+00:00",[76,99],{"id":1390,"createTime":1391,"updateTime":1392,"relativeEntities":1393,"slug":1394,"properties":1395,"entityType":233,"verifyStatus":234,"verifyTime":1404,"verifyNote":236,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1405,"fullTextUrl":20,"authors":1406,"publicationType":291,"publisherRelationship":1476,"citationCount":21,"citationInfo":1536,"publishDate":1539,"publishYear":1537,"citationAnalyzeStatus":19,"lastCitationAnalyze":1540,"indexDatabases":1541,"openAccess":20,"references":1542,"isForceReanalyzing":362},"a90d7032-37ed-43b2-803c-a435a3b8f04e","2023-12-30T21:56:15.483+00:00","2026-07-10T20:08:22.816+00:00",[],"TPEN-exerts-selective-anti-leukemic-efficacy-in-ex-vivo-drug-resistant-childhood-acute-leukemia",{"abstract":1396,"title":1398,"gsPaper":1400,"doi":1402},{"EN":1397},"Despite some advances in the treatment of acute lymphoblastic (ALL) and myeloid leukemia (AML) in recent years, there is still a prominent percentage of pediatric patients with a reduced overall prognosis. Therefore, other therapeutic approaches are needed to treat those patients. In the present study, we report that the metal chelator TPEN affected ΔΨm and DNA content in isolated CD34+ refractory cells from bone marrow ALL (n = 7; B-cell, n = 4; T-cell, n = 3) and AML (n = 3) pediatric patients. Furthermore, TPEN induced oxidation of hydrogen peroxide (H2O2) sensor protein DJ-1, induced up-regulation of BH3-only pro-apoptotic protein PUMA, transcription factor p53 and activated the executor protease CASPASE-3 as apoptosis markers, and reduced the reactivity of the cellular proliferating marker Ki-67 in all acute leukemic groups, and reduced the phosphorylation of c-ABL protein signal in an AML case. Remarkably, bone marrow cells from non-leukemic patients’ cells (n = 2) displayed neither loss of ΔΨm nor loss of DNA content when exposed to TPEN. We conclude that TPEN selectively induces apoptosis in acute leukemic cells via reactive oxygen species (ROS) signaling mechanism. Understanding the pathways of TPEN-induced cell death may provide insight into more effective therapeutic ROS-inducing anticancer agents.",{"EN":1399},"TPEN exerts selective anti-leukemic efficacy in ex vivo drug-resistant childhood acute leukemia",{"VOID":1401},"[\"8007357459348491099\"]",{"VOID":1403},"10.1007\u002Fs10534-020-00262-0","2024-05-01T13:28:47.175+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10534-020-00262-0",[1407,1422,1435,1450,1463],{"id":1408,"sortIndex":21,"researcher":20,"roles":1409,"affiliations":1410,"properties":1419},"91b84f57-902b-4dde-836e-645f03ad33fb",[242],[1411],{"id":1412,"sortIndex":21,"affiliation":1413,"properties":20},"4ce451cf-2655-4a4d-a957-e3da5e8baa28",{"id":1412,"createTime":20,"updateTime":20,"relativeEntities":1414,"slug":20,"properties":1415,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1418,"statistic":20},[],{"title":1416},{"VI":1417},"Neuroscience Research Group, Faculty of Medicine, Medical Research Institute, University of Antioquia (UdeA), SIU Medellin, Medellin, Colombia",[],{"title":1420},{"VI":1421},"Miguel Mendivil-Perez",{"id":1423,"sortIndex":259,"researcher":20,"roles":1424,"affiliations":1425,"properties":1432},"387c7940-8776-4dd4-925c-6a0fd23446f2",[242],[1426],{"id":1412,"sortIndex":21,"affiliation":1427,"properties":20},{"id":1412,"createTime":20,"updateTime":20,"relativeEntities":1428,"slug":20,"properties":1429,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1431,"statistic":20},[],{"title":1430},{"VI":1417},[],{"title":1433},{"VI":1434},"Carlos Velez-Pardo",{"id":1436,"sortIndex":277,"researcher":20,"roles":1437,"affiliations":1438,"properties":1447},"0753fb48-b773-4d29-a0f5-650f45aee45d",[242],[1439],{"id":1440,"sortIndex":21,"affiliation":1441,"properties":20},"7544b9d6-0ff0-4887-819d-6c9a9c39f9ae",{"id":1440,"createTime":20,"updateTime":20,"relativeEntities":1442,"slug":20,"properties":1443,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1446,"statistic":20},[],{"title":1444},{"VI":1445},"Children’s Hospital San Vicente Foundation, Pediatric Hemato-Oncology Unit, Medellin, Colombia",[],{"title":1448},{"VI":1449},"Gloria E. David-Yepes",{"id":1451,"sortIndex":357,"researcher":20,"roles":1452,"affiliations":1453,"properties":1460},"e707e29d-0700-4c55-b402-1ef9e9a13185",[242],[1454],{"id":1440,"sortIndex":21,"affiliation":1455,"properties":20},{"id":1440,"createTime":20,"updateTime":20,"relativeEntities":1456,"slug":20,"properties":1457,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1459,"statistic":20},[],{"title":1458},{"VI":1445},[],{"title":1461},{"VI":1462},"Javier E. Fox",{"id":1464,"sortIndex":161,"researcher":20,"roles":1465,"affiliations":1466,"properties":1473},"23b51a82-f7d1-423e-b4db-828419067d5a",[242],[1467],{"id":1412,"sortIndex":21,"affiliation":1468,"properties":20},{"id":1412,"createTime":20,"updateTime":20,"relativeEntities":1469,"slug":20,"properties":1470,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1472,"statistic":20},[],{"title":1471},{"VI":1417},[],{"title":1474},{"VI":1475},"Marlene Jimenez-Del-Rio",{"url":1405,"publisher":1477,"properties":1531},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1478,"slug":10,"properties":1479,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":1483,"manageAffiliations":1500,"indexDatabases":1511,"url":100,"thumbnailPath":20,"statistic":1526,"gsStatistic":20,"type":211,"analyzePriority":20},[],{"issn":1480,"title":1481,"eissn":1482},{"VOID":13},{"EN":15},{"VOID":17},[1484,1488,1492,1496],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":1485,"label":1486,"description":1487,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":1489,"label":1490,"description":1491,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":1493,"label":1494,"description":1495,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":1497,"label":1498,"description":1499,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},[1501,1506],{"id":49,"createTime":20,"updateTime":20,"relativeEntities":1502,"slug":20,"properties":1503,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1505,"statistic":20},[],{"title":1504},{"EN":53},[55],{"id":57,"createTime":20,"updateTime":20,"relativeEntities":1507,"slug":20,"properties":1508,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1510,"statistic":20},[],{"title":1509},{"EN":61},[],[1512,1519],{"id":65,"indexDatabase":1513,"url":20,"indexYears":20,"academicFieldIds":1518,"indexDatabaseRanking":20},{"id":67,"createTime":20,"updateTime":20,"relativeEntities":1514,"label":1515,"description":1516,"key":74,"publicationTags":1517,"standard":20},[],{"EN":70,"VI":70},{"EN":72,"VI":73},[76,77],[79],{"id":81,"indexDatabase":1520,"url":92,"indexYears":93,"academicFieldIds":1525,"indexDatabaseRanking":99},{"id":83,"createTime":20,"updateTime":20,"relativeEntities":1521,"label":1522,"description":1523,"key":89,"publicationTags":1524,"standard":20},[],{"EN":86,"VI":86},{"EN":86,"VI":88},[91],[95,96,97,98],{"impactFactor":21,"impactFactorByYear":1527,"i10Index":113,"i10IndexLast5Year":114,"totalPublication":115,"totalPublicationByYear":1528,"totalCitation":151,"totalCitationByYear":1529,"totalCitationPerPublication":181,"totalCitationPerPublicationByYear":1530,"hindexLast5Year":123,"hindex":123},{"2012":103,"2013":104,"2014":105,"2015":103,"2016":106,"2017":107,"2018":108,"2019":105,"2020":109,"2021":110,"2022":111,"2023":112},{"1988":117,"1989":118,"1990":119,"1991":120,"1992":121,"1993":122,"1994":123,"1995":124,"1996":125,"1997":126,"1998":127,"1999":128,"2000":129,"2001":130,"2002":131,"2003":132,"2004":133,"2005":134,"2006":135,"2007":136,"2008":132,"2009":137,"2010":138,"2011":139,"2012":140,"2013":141,"2014":142,"2015":143,"2016":143,"2017":144,"2018":145,"2019":146,"2020":129,"2021":147,"2022":148,"2023":149,"2024":150},{"1989":153,"1990":154,"1991":155,"1992":156,"1993":157,"1994":158,"1995":159,"1996":160,"2004":161,"2005":162,"2006":163,"2007":164,"2008":165,"2009":166,"2010":167,"2011":168,"2012":169,"2013":170,"2014":171,"2015":172,"2016":173,"2017":174,"2018":175,"2019":176,"2020":177,"2021":178,"2022":179,"2023":180},{"1989":183,"1990":184,"1991":185,"1992":186,"1993":187,"1994":188,"1995":189,"1996":190,"2004":191,"2005":192,"2006":193,"2007":194,"2008":195,"2009":196,"2010":197,"2011":198,"2012":199,"2013":200,"2014":201,"2015":202,"2016":203,"2017":204,"2018":205,"2019":206,"2020":207,"2021":208,"2022":209,"2023":210},{"pages":1532,"volume":1534},{"VOID":1533},"49-66",{"VOID":1535},"34",{"total":21,"publishYear":1537,"statisticByYear":1538},2020,{},"2020-10-24","2026-07-10T20:08:22.815+00:00",[76,99],[1543,1552,1561,1567,1575,1583,1591,1597,1604,1613,1621,1630,1638,1647,1655,1661,1667,1673,1681,1684,1693,1701,1709,1714,1723,1731,1737,1743,1752,1761,1769,1777,1780,1786,1795,1803,1812,1821,1830,1839,1845,1851,1860,1869,1878,1887,1896,1905,1911,1917,1923,1929,1938,1946,1955,1960,1969,1978,1987,1995,2001,2010,2016,2019,2027,2034],{"id":20,"text":1544,"url":1545,"identifiers":1546},"Bahat A, Gross A (2019) Mitochondrial plasticity in cell fate regulation. J Biol Chem 294:13852–13863. https:\u002F\u002Fdoi.org\u002F10.1074\u002Fjbc.REV118.000828","https:\u002F\u002Fdoi.org\u002F10.1074\u002Fjbc.rev118.000828",{"mag":1547,"pmc":1548,"openalex":1549,"pm":1550,"doi":1551},"2966274874","6755789","W2966274874","31383739","10.1074\u002Fjbc.rev118.000828",{"id":20,"text":1553,"url":1554,"identifiers":1555},"Bonilla-Porras AR, Jimenez-Del-Rio M, Velez-Pardo C (2011) Vitamin K3 and vitamin C alone or in combination induced apoptosis in leukemia cells by a similar oxidative stress signalling mechanism. Cancer Cell Int 11:19. https:\u002F\u002Fdoi.org\u002F10.1186\u002F1475-2867-11-19","https:\u002F\u002Fdoi.org\u002F10.1186\u002F1475-2867-11-19",{"mag":1556,"pmc":1557,"openalex":1558,"pm":1559,"doi":1560},"2150886441","3127817","W2150886441","21663679","10.1186\u002F1475-2867-11-19",{"id":1562,"text":1563,"url":1564,"identifiers":1565},"298bb471-9bbb-4658-b0d5-5527eed120c8","Carter BZ, Mak DH, Cortes J, Andreeff M (2010) The elusive chronic myeloid leukemia stem cell: does it matter and how do we eliminate it? Semin Hematol 47:362–370. https:\u002F\u002Fdoi.org\u002F10.1053\u002Fj.seminhematol.2010.06.006","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0037196310000806",{"doi":1566},"10.1053\u002Fj.seminhematol.2010.06.006",{"id":20,"text":1568,"url":1569,"identifiers":1570},"Chandel NS (2015) Evolution of mitochondria as signaling organelles. Cell Metab 22:204–206. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.cmet.2015.05.013","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.cmet.2015.05.013",{"mag":1571,"openalex":1572,"pm":1573,"doi":1574},"1938258474","W1938258474","26073494","10.1016\u002Fj.cmet.2015.05.013",{"id":20,"text":1576,"url":1577,"identifiers":1578},"Cho E, Hwang JJ, Han SH, Chung SJ, Koh JY, Lee JY (2010) Endogenous zinc mediates apoptotic programmed cell death in the developing brain. Neurotox Res 17:156–166. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs12640-009-9085-2","https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs12640-009-9085-2",{"mag":1579,"openalex":1580,"pm":1581,"doi":1582},"2037298288","W2037298288","19609831","10.1007\u002Fs12640-009-9085-2",{"id":20,"text":1584,"url":1585,"identifiers":1586},"Demidowicz E et al (2019) Outcome of pediatric acute lymphoblastic leukemia: sixty years of progress. Anticancer Res 39:5203–5207. https:\u002F\u002Fdoi.org\u002F10.21873\u002Fanticanres.13717","https:\u002F\u002Fdoi.org\u002F10.21873\u002Fanticanres.13717",{"mag":1587,"openalex":1588,"pm":1589,"doi":1590},"2972946642","W2972946642","31519634","10.21873\u002Fanticanres.13717",{"id":1592,"text":1593,"url":1594,"identifiers":1595},"6bae7c92-1bfa-4ea6-80ae-505a12603e41","Dickens E, Ahmed S (2018) Principles of cancer treatment by chemotherapy. Surgery 36:134–138. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.mpsur.2017.12.002","https:\u002F\u002Flinkinghub.elsevier.com\u002Fretrieve\u002Fpii\u002FS026393190670182X",{"doi":1596},"10.1383\u002Fsurg.2006.24.2.66",{"id":20,"text":1598,"url":1599,"identifiers":1600},"Dohner H, Weisdorf DJ, Bloomfield CD (2015) Acute myeloid leukemia. N Engl J Med 373:1136–1152. https:\u002F\u002Fdoi.org\u002F10.1056\u002FNEJMra1406184","https:\u002F\u002Fdoi.org\u002F10.1056\u002Fnejmra1406184",{"openalex":1601,"pm":1602,"doi":1603},"W4231346141","26376137","10.1056\u002Fnejmra1406184",{"id":20,"text":1605,"url":1606,"identifiers":1607},"Dorstyn L, Akey CW, Kumar S (2018) New insights into apoptosome structure and function. Cell Death Differ 25:1194–1208. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41418-017-0025-z","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41418-017-0025-z",{"mag":1608,"pmc":1609,"openalex":1610,"pm":1611,"doi":1612},"2803563276","6030056","W2803563276","29765111","10.1038\u002Fs41418-017-0025-z",{"id":20,"text":1614,"url":1615,"identifiers":1616},"Estey E, Levine RL, Lowenberg B (2015) Current challenges in clinical development of “targeted therapies”: the case of acute myeloid leukemia. Blood 125:2461–2466. https:\u002F\u002Fdoi.org\u002F10.1182\u002Fblood-2015-01-561373","https:\u002F\u002Fdoi.org\u002F10.1182\u002Fblood-2015-01-561373",{"mag":1617,"openalex":1618,"pm":1619,"doi":1620},"2018326038","W2018326038","25762181","10.1182\u002Fblood-2015-01-561373",{"id":20,"text":1622,"url":1623,"identifiers":1624},"Fatfat M et al (2014) Copper chelation selectively kills colon cancer cells through redox cycling and generation of reactive oxygen species. BMC Cancer 14:527. https:\u002F\u002Fdoi.org\u002F10.1186\u002F1471-2407-14-527","https:\u002F\u002Fdoi.org\u002F10.1186\u002F1471-2407-14-527",{"mag":1625,"pmc":1626,"openalex":1627,"pm":1628,"doi":1629},"2069748048","4223620","W2069748048","25047035","10.1186\u002F1471-2407-14-527",{"id":20,"text":1631,"url":1632,"identifiers":1633},"Galadari S, Rahman A, Pallichankandy S, Thayyullathil F (2017) Reactive oxygen species and cancer paradox: to promote or to suppress? Free Radic Biol Med 104:144–164. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.freeradbiomed.2017.01.004","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.freeradbiomed.2017.01.004",{"mag":1634,"openalex":1635,"pm":1636,"doi":1637},"2575532686","W2575532686","28088622","10.1016\u002Fj.freeradbiomed.2017.01.004",{"id":20,"text":1639,"url":1640,"identifiers":1641},"Galluzzi L et al (2018) (2018) Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death. Cell Death Differ 25:486–541. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41418-017-0012-4","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41418-017-0012-4",{"mag":1642,"pmc":1643,"openalex":1644,"pm":1645,"doi":1646},"2788640168","5864239","W2788640168","29362479","10.1038\u002Fs41418-017-0012-4",{"id":20,"text":1648,"url":1649,"identifiers":1650},"Hashemi M, Ghavami S, Eshraghi M, Booy EP, Los M (2007) Cytotoxic effects of intra and extracellular zinc chelation on human breast cancer cells. Eur J Pharmacol 557:9–19. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.ejphar.2006.11.010","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.ejphar.2006.11.010",{"mag":1651,"openalex":1652,"pm":1653,"doi":1654},"2169527889","W2169527889","17169355","10.1016\u002Fj.ejphar.2006.11.010",{"id":1656,"text":1657,"url":1658,"identifiers":1659},"155b0f83-0b2d-4f97-a111-59a60ee418cf","Hochhaus A et al (1996) A novel BCR-ABL fusion gene (e6a2) in a patient with Philadelphia chromosome-negative chronic myelogenous leukemia. Blood 88:2236–2240","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0006497120624247",{"doi":1660},"10.1182\u002Fblood.v88.6.2236.bloodjournal8862236",{"id":1662,"text":1663,"url":1664,"identifiers":1665},"d8b5e50f-2362-4673-90fb-21661a6962d6","Hunger SP, Mullighan CG (2015) Acute lymphoblastic leukemia in children. N Engl J Med 373:1541–1552. https:\u002F\u002Fdoi.org\u002F10.1056\u002FNEJMra1400972","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10269-006-0449-4",{"doi":1666},"10.1007\u002Fs10269-006-0449-4",{"id":1668,"text":1669,"url":1670,"identifiers":1671},"2d3eb999-c622-458e-b7e3-97cc3a675256","Inaba H, Greaves M, Mullighan CG (2013) Acute lymphoblastic leukaemia Lancet 381:1943–1955. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fs0140-6736(12)62187-4","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0140673612621874",{"doi":1672},"10.1016\u002Fs0140-6736(12)62187-4",{"id":20,"text":1674,"url":1675,"identifiers":1676},"Jabbour E, O’Brien S, Konopleva M, Kantarjian H (2015) New insights into the pathophysiology and therapy of adult acute lymphoblastic leukemia. Cancer 121:2517–2528. https:\u002F\u002Fdoi.org\u002F10.1002\u002Fcncr.29383","https:\u002F\u002Fdoi.org\u002F10.1002\u002Fcncr.29383",{"mag":1677,"openalex":1678,"pm":1679,"doi":1680},"1879221139","W1879221139","25891003","10.1002\u002Fcncr.29383",{"id":780,"text":1682,"url":782,"identifiers":1683},"Janicke RU, Sprengart ML, Wati MR, Porter AG (1998) Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. J Biol Chem 273:9357–9360",{"doi":784},{"id":20,"text":1685,"url":1686,"identifiers":1687},"Kalkavan H, Green DR (2018) MOMP, cell suicide as a BCL-2 family business. Cell Death Differ 25:46–55. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fcdd.2017.179","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fcdd.2017.179",{"mag":1688,"pmc":1689,"openalex":1690,"pm":1691,"doi":1692},"2766197806","5729535","W2766197806","31745309","10.1038\u002Fcdd.2017.179",{"id":20,"text":1694,"url":1695,"identifiers":1696},"Kinumi T, Kimata J, Taira T, Ariga H, Niki E (2004) Cysteine-106 of DJ-1 is the most sensitive cysteine residue to hydrogen peroxide-mediated oxidation in vivo in human umbilical vein endothelial cells. Biochem Biophys Res Commun 317:722–728. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.bbrc.2004.03.110","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.bbrc.2004.03.110",{"mag":1697,"openalex":1698,"pm":1699,"doi":1700},"1976393002","W1976393002","15081400","10.1016\u002Fj.bbrc.2004.03.110",{"id":20,"text":1702,"url":1703,"identifiers":1704},"Lee H, Lee HJ, Seo J, Kim HE, Shin YK, Kim JH, Lee C (2016) Activation of oxygen and hydrogen peroxide by copper(II) Coupled with hydroxylamine for oxidation of organic. Contaminants Environ Sci Technol 50:8231–8238. https:\u002F\u002Fdoi.org\u002F10.1021\u002Facs.est.6b02067","https:\u002F\u002Fdoi.org\u002F10.1021\u002Facs.est.6b02067",{"mag":1705,"openalex":1706,"pm":1707,"doi":1708},"2471389182","W2471389182","27387011","10.1021\u002Facs.est.6b02067",{"id":20,"text":1710,"url":1711,"identifiers":1712},"Linabery AM, Ross JA (2008) Trends in childhood cancer incidence in the U.S. (1992–2004). Cancer 112:416–432. https:\u002F\u002Fdoi.org\u002F10.1002\u002Fcncr.23169","https:\u002F\u002Fdoi.org\u002F10.1002\u002Fcncr.23169",{"doi":1713},"10.1002\u002Fcncr.23169",{"id":20,"text":1715,"url":1716,"identifiers":1717},"Liu J, Wang Z (2015) Increased oxidative stress as a selective anticancer therapy. Oxid Med Cell Longev 2015:294303. https:\u002F\u002Fdoi.org\u002F10.1155\u002F2015\u002F294303","https:\u002F\u002Fdoi.org\u002F10.1155\u002F2015\u002F294303",{"mag":1718,"pmc":1719,"openalex":1720,"pm":1721,"doi":1722},"1536274572","4529973","W1536274572","26273420","10.1155\u002F2015\u002F294303",{"id":20,"text":1724,"url":1725,"identifiers":1726},"Locatelli F, Schrappe M, Bernardo ME, Rutella S (2012) How I treat relapsed childhood acute lymphoblastic leukemia. Blood 120:2807–2816. https:\u002F\u002Fdoi.org\u002F10.1182\u002Fblood-2012-02-265884","https:\u002F\u002Fdoi.org\u002F10.1182\u002Fblood-2012-02-265884",{"mag":1727,"openalex":1728,"pm":1729,"doi":1730},"2051646706","W2051646706","22896001","10.1182\u002Fblood-2012-02-265884",{"id":1732,"text":1733,"url":1734,"identifiers":1735},"979ad476-ed55-4093-a9bf-ebae340c650b","Malouf C, Ottersbach K (2018) Molecular processes involved in B cell acute lymphoblastic leukaemia. Cell Mol Life Sci 75:417–446. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs00018-017-2620-z","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs00018-017-2620-z",{"doi":1736},"10.1007\u002Fs00018-017-2620-z",{"id":1738,"text":1739,"url":1740,"identifiers":1741},"6104bc2d-2744-463d-ba53-b83c3733ada8","Mastrangelo D et al (2015) Cytotoxic effects of high concentrations of sodium ascorbate on human myeloid cell lines. Ann Hematol 94:1807–1816. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs00277-015-2464-2","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs00277-015-2464-2",{"doi":1742},"10.1007\u002Fs00277-015-2464-2",{"id":20,"text":1744,"url":1745,"identifiers":1746},"McNeer NA et al (2019) Genetic mechanisms of primary chemotherapy resistance in pediatric acute myeloid leukemia. Leukemia. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41375-019-0402-3","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41375-019-0402-3",{"mag":1747,"pmc":1748,"openalex":1749,"pm":1750,"doi":1751},"2913532930","6687545","W2913532930","30760869","10.1038\u002Fs41375-019-0402-3",{"id":20,"text":1753,"url":1754,"identifiers":1755},"Mendivil-Perez M, Velez-Pardo C, Jimenez-Del-Rio M (2012) TPEN induces apoptosis independently of zinc chelator activity in a model of acute lymphoblastic leukemia and ex vivo acute leukemia cells through oxidative stress and mitochondria caspase-3- and AIF-dependent pathways. Oxid Med Cell Longev 2012:313275. https:\u002F\u002Fdoi.org\u002F10.1155\u002F2012\u002F313275","https:\u002F\u002Fdoi.org\u002F10.1155\u002F2012\u002F313275",{"mag":1756,"pmc":1757,"openalex":1758,"pm":1759,"doi":1760},"1988875965","3540963","W1988875965","23320127","10.1155\u002F2012\u002F313275",{"id":20,"text":1762,"url":1763,"identifiers":1764},"Mendivil-Perez M, Velez-Pardo C, Jimenez-Del-Rio M (2015) Doxorubicin induces apoptosis in Jurkat cells by mitochondria-dependent and mitochondria-independent mechanisms under normoxic and hypoxic conditions. Anticancer Drugs 26:583–598. https:\u002F\u002Fdoi.org\u002F10.1097\u002Fcad.0000000000000223","https:\u002F\u002Fdoi.org\u002F10.1097\u002Fcad.0000000000000223",{"mag":1765,"openalex":1766,"pm":1767,"doi":1768},"2332756390","W2332756390","25734830","10.1097\u002Fcad.0000000000000223",{"id":20,"text":1770,"url":1771,"identifiers":1772},"Messinger Y et al (2017) Combination of clofarabine, cyclophosphamide, and etoposide for relapsed or refractory childhood and adolescent acute myeloid leukemia. Pediatr Hematol Oncol 34:187–198. https:\u002F\u002Fdoi.org\u002F10.1080\u002F08880018.2017.1360970","https:\u002F\u002Fdoi.org\u002F10.1080\u002F08880018.2017.1360970",{"mag":1773,"openalex":1774,"pm":1775,"doi":1776},"2766936842","W2766936842","29039989","10.1080\u002F08880018.2017.1360970",{"id":780,"text":1778,"url":782,"identifiers":1779},"Nakano K, Vousden KH (2001) PUMA, a novel proapoptotic gene, is induced by p53. Mol Cell 7:683–694",{"doi":784},{"id":1781,"text":1782,"url":1783,"identifiers":1784},"a4548eb1-49d2-4605-a3b7-5a9949374767","Neuzil J, Dong LF, Rohlena J, Truksa J, Ralph SJ (2013) Classification of mitocans, anti-cancer drugs acting on mitochondria. Mitochondrion 13:199–208. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.mito.2012.07.112","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1567724912002000",{"doi":1785},"10.1016\u002Fj.mito.2012.07.112",{"id":20,"text":1787,"url":1788,"identifiers":1789},"Noguera NI et al (2017) High-dose ascorbate and arsenic trioxide selectively kill acute myeloid leukemia and acute promyelocytic leukemia blasts in vitro. Oncotarget 8:32550–32565. https:\u002F\u002Fdoi.org\u002F10.18632\u002Foncotarget.15925","https:\u002F\u002Fdoi.org\u002F10.18632\u002Foncotarget.15925",{"mag":1790,"pmc":1791,"openalex":1792,"pm":1793,"doi":1794},"2593214939","5464808","W2593214939","28427227","10.18632\u002Foncotarget.15925",{"id":20,"text":1796,"url":1797,"identifiers":1798},"Olivas-Aguirre M, Pottosin I, Dobrovinskaya O (2019) Mitochondria as emerging targets for therapies against T cell acute lymphoblastic leukemia. J Leukoc Biol 105:935–946. https:\u002F\u002Fdoi.org\u002F10.1002\u002Fjlb.5vmr0818-330rr","https:\u002F\u002Fdoi.org\u002F10.1002\u002Fjlb.5vmr0818-330rr",{"mag":1799,"openalex":1800,"pm":1801,"doi":1802},"2912582797","W2912582797","30698851","10.1002\u002Fjlb.5vmr0818-330rr",{"id":20,"text":1804,"url":1805,"identifiers":1806},"Piedimonte M et al (2019) A rare BCR-ABL1 transcript in Philadelphia-positive acute myeloid leukemia: case report and literature review. BMC Cancer. https:\u002F\u002Fdoi.org\u002F10.1186\u002Fs12885-019-5265-5","https:\u002F\u002Fdoi.org\u002F10.1186\u002Fs12885-019-5265-5",{"mag":1807,"pmc":1808,"openalex":1809,"pm":1810,"doi":1811},"2917419663","6329120","W2917419663","30630459","10.1186\u002Fs12885-019-5265-5",{"id":20,"text":1813,"url":1814,"identifiers":1815},"Prieto-Bermejo R, Romo-Gonzalez M, Perez-Fernandez A, Ijurko C, Hernandez-Hernandez A (2018) Reactive oxygen species in haematopoiesis: leukaemic cells take a walk on the wild side. J Exp Clin Cancer Res 37:125. https:\u002F\u002Fdoi.org\u002F10.1186\u002Fs13046-018-0797-0","https:\u002F\u002Fdoi.org\u002F10.1186\u002Fs13046-018-0797-0",{"mag":1816,"pmc":1817,"openalex":1818,"pm":1819,"doi":1820},"2809886836","6019308","W2809886836","29940987","10.1186\u002Fs13046-018-0797-0",{"id":20,"text":1822,"url":1823,"identifiers":1824},"Pui CH et al (2009) Treating childhood acute lymphoblastic leukemia without cranial irradiation. N Engl J Med 360:2730–2741. https:\u002F\u002Fdoi.org\u002F10.1056\u002FNEJMoa0900386","https:\u002F\u002Fdoi.org\u002F10.1056\u002Fnejmoa0900386",{"mag":1825,"pmc":1826,"openalex":1827,"pm":1828,"doi":1829},"2059999488","2754320","W2059999488","19553647","10.1056\u002Fnejmoa0900386",{"id":20,"text":1831,"url":1832,"identifiers":1833},"Pui CH, Carroll WL, Meshinchi S, Arceci RJ (2011) Biology, risk stratification, and therapy of pediatric acute leukemias: an update. J Clin Oncol 29:551–565. https:\u002F\u002Fdoi.org\u002F10.1200\u002Fjco.2010.30.7405","https:\u002F\u002Fdoi.org\u002F10.1200\u002Fjco.2010.30.7405",{"mag":1834,"pmc":1835,"openalex":1836,"pm":1837,"doi":1838},"2141869972","3071256","W2141869972","21220611","10.1200\u002Fjco.2010.30.7405",{"id":1840,"text":1841,"url":1842,"identifiers":1843},"61355fec-979d-4198-ac6a-729df0c22ce7","Pui CH, Howard SC (2008) Current management and challenges of malignant disease in the CNS in paediatric leukaemia. Lancet Oncol 9:257–268. https:\u002F\u002Fdoi.org\u002F10.1016\u002FS1470-2045(08)70070-6","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1470204508700706",{"doi":1844},"10.1016\u002Fs1470-2045(08)70070-6",{"id":1846,"text":1847,"url":1848,"identifiers":1849},"87bf70fe-e990-4b59-ab76-1efe0cfa688a","Pui CH, Mullighan CG, Evans WE, Relling MV (2012) Pediatric acute lymphoblastic leukemia: where are we going and how do we get there? Blood 120:1165–1174. https:\u002F\u002Fdoi.org\u002F10.1182\u002Fblood-2012-05-378943","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0006497120465176",{"doi":1850},"10.1182\u002Fblood-2012-05-378943",{"id":20,"text":1852,"url":1853,"identifiers":1854},"Pui CH et al (2015) Childhood acute lymphoblastic leukemia: progress through collaboration. J Clin Oncol 33:2938–2948. https:\u002F\u002Fdoi.org\u002F10.1200\u002Fjco.2014.59.1636","https:\u002F\u002Fdoi.org\u002F10.1200\u002Fjco.2014.59.1636",{"mag":1855,"pmc":1856,"openalex":1857,"pm":1858,"doi":1859},"2125277492","4567699","W2125277492","26304874","10.1200\u002Fjco.2014.59.1636",{"id":20,"text":1861,"url":1862,"identifiers":1863},"Puumala SE, Ross JA, Aplenc R, Spector LG (2013) Epidemiology of childhood acute myeloid leukemia. Pediatr Blood Cancer 60:728–733. https:\u002F\u002Fdoi.org\u002F10.1002\u002Fpbc.24464","https:\u002F\u002Fdoi.org\u002F10.1002\u002Fpbc.24464",{"mag":1864,"pmc":1865,"openalex":1866,"pm":1867,"doi":1868},"2046842883","3664189","W2046842883","23303597","10.1002\u002Fpbc.24464",{"id":20,"text":1870,"url":1871,"identifiers":1872},"Rahal ON, Fatfat M, Hankache C, Osman B, Khalife H, Machaca K, Muhtasib HG (2016) Chk1 and DNA-PK mediate TPEN-induced DNA damage in a ROS dependent manner in human colon cancer cells. Cancer Biol Ther 17:1139–1148. https:\u002F\u002Fdoi.org\u002F10.1080\u002F15384047.2016.1235658","https:\u002F\u002Fdoi.org\u002F10.1080\u002F15384047.2016.1235658",{"mag":1873,"pmc":1874,"openalex":1875,"pm":1876,"doi":1877},"2529289268","5137490","W2529289268","27690730","10.1080\u002F15384047.2016.1235658",{"id":20,"text":1879,"url":1880,"identifiers":1881},"Ramos NR, Mo CC, Karp JE, Hourigan CS (2015) Current approaches in the treatment of relapsed and refractory acute myeloid leukemia J. Clin Med 4:665–695. https:\u002F\u002Fdoi.org\u002F10.3390\u002Fjcm4040665","https:\u002F\u002Fdoi.org\u002F10.3390\u002Fjcm4040665",{"mag":1882,"pmc":1883,"openalex":1884,"pm":1885,"doi":1886},"2003424912","4412468","W2003424912","25932335","10.3390\u002Fjcm4040665",{"id":20,"text":1888,"url":1889,"identifiers":1890},"Rasche M et al (2018) Successes and challenges in the treatment of pediatric acute myeloid leukemia: a retrospective analysis of the AML-BFM trials from 1987 to 2012. Leukemia 32:2167–2177. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41375-018-0071-7","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41375-018-0071-7",{"mag":1891,"pmc":1892,"openalex":1893,"pm":1894,"doi":1895},"2793614832","6170392","W2793614832","29550834","10.1038\u002Fs41375-018-0071-7",{"id":20,"text":1897,"url":1898,"identifiers":1899},"Reczek CR, Chandel NS (2015) ROS-dependent signal transduction. Curr Opin Cell Biol 33:8–13. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.ceb.2014.09.010","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.ceb.2014.09.010",{"mag":1900,"pmc":1901,"openalex":1902,"pm":1903,"doi":1904},"1994133951","4380867","W1994133951","25305438","10.1016\u002Fj.ceb.2014.09.010",{"id":1906,"text":1907,"url":1908,"identifiers":1909},"a243a452-7303-4058-9ca8-3786c5669c7e","Rojas-Valencia L, Velez-Pardo C, Jimenez-Del-Rio M (2017) Metal chelator TPEN selectively induces apoptosis in K562 cells through reactive oxygen species signaling mechanism: implications for chronic myeloid leukemia. Biometals. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs10534-017-0015-0","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10534-017-0015-0",{"doi":1910},"10.1007\u002Fs10534-017-0015-0",{"id":1912,"text":1913,"url":1914,"identifiers":1915},"0b3089c6-8f94-4f6e-8513-b9d448d63305","Rubnitz JE (2017) Current management of childhood acute myeloid leukemia. Paediatr Drugs 19:1–10. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs40272-016-0200-6","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs40272-016-0200-6",{"doi":1916},"10.1007\u002Fs40272-016-0200-6",{"id":1918,"text":1919,"url":1920,"identifiers":1921},"f6a70e18-e356-42e3-8016-5a9929b4f90e","Ruiz-Moreno C, Jimenez-Del-Rio M, Sierra-Garcia L, Lopez-Osorio B, Velez-Pardo C (2016) Vitamin E synthetic derivate-TPGS-selectively induces apoptosis in jurkat t cells via oxidative stress signaling pathways: implications for acute lymphoblastic leukemia. Apoptosis 21:1019–1032. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs10495-016-1266-x","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10495-016-1266-x",{"doi":1922},"10.1007\u002Fs10495-016-1266-x",{"id":1924,"text":1925,"url":1926,"identifiers":1927},"4b1e6fc0-b7d9-4195-9da2-c6a1048676cd","Ruiz-Moreno C, Velez-Pardo C, Jimenez-Del-Rio M (2018) Minocycline induces apoptosis in acute lymphoblastic leukemia Jurkat cells. Toxicol In Vitro 50:336–346. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.tiv.2018.03.012","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS088723331830105X",{"doi":1928},"10.1016\u002Fj.tiv.2018.03.012",{"id":20,"text":1930,"url":1931,"identifiers":1932},"Salimi A, Roudkenar MH, Sadeghi L, Mohseni A, Seydi E, Pirahmadi N, Pourahmad J (2015) Ellagic acid, a polyphenolic compound, selectively induces ROS-mediated apoptosis in cancerous B-lymphocytes of CLL patients by directly targeting mitochondria. Redox Biol 6:461–471. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.redox.2015.08.021.","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.redox.2015.08.021",{"mag":1933,"pmc":1934,"openalex":1935,"pm":1936,"doi":1937},"2214870473","4588415","W2214870473","26418626","10.1016\u002Fj.redox.2015.08.021",{"id":20,"text":1939,"url":1940,"identifiers":1941},"Scholzen T, Gerdes J (2000) The Ki-67 protein: from the known and the unknown. J Cell Physiol 182:311–322. doi:https:\u002F\u002Fdoi.org\u002F10.1002\u002F(sici)1097-4652(200003)182:3\u003C311::aid-jcp1>3.0.co;2-9","https:\u002F\u002Fdoi.org\u002F10.1002\u002F(sici)1097-4652(200003)182:3\u003C311::aid-jcp1>3.0.co;2-9",{"mag":1942,"openalex":1943,"pm":1944,"doi":1945},"1974208182","W1974208182","10653597","10.1002\u002F(sici)1097-4652(200003)182:3",{"id":20,"text":1947,"url":1948,"identifiers":1949},"Schrappe M et al (2012) Outcomes after induction failure in childhood acute lymphoblastic leukemia. N Engl J Med 366:1371–1381. https:\u002F\u002Fdoi.org\u002F10.1056\u002FNEJMoa1110169","https:\u002F\u002Fdoi.org\u002F10.1056\u002Fnejmoa1110169",{"mag":1950,"pmc":1951,"openalex":1952,"pm":1953,"doi":1954},"2113030986","3374496","W2113030986","22494120","10.1056\u002Fnejmoa1110169",{"id":20,"text":1956,"url":1957,"identifiers":1958},"Soto-Mercado V, Mendivil-Perez M, Uruena-Pinzon C, Fiorentino S, Velez-Pardo C, Jimenez-Del-Rio M (2018) TPEN exerts antitumor efficacy in murine mammary adenocarcinoma through an H2O2 signaling mechanism dependent on caspase-3 anticancer agents. Med Chem 18:1617–1628. https:\u002F\u002Fdoi.org\u002F10.2174\u002F1871520618666180426111520","https:\u002F\u002Fdoi.org\u002F10.2174\u002F1871520618666180426111520",{"doi":1959},"10.2174\u002F1871520618666180426111520",{"id":20,"text":1961,"url":1962,"identifiers":1963},"Stuart CH, Singh R, Smith TL, D’Agostino R Jr, Caudell D, Balaji KC, Gmeiner WH (2016) Prostate-specific membrane antigen-targeted liposomes specifically deliver the Zn(2+) chelator TPEN inducing oxidative stress in prostate cancer cells. Nanomedicine (Lond) 11:1207–1222. https:\u002F\u002Fdoi.org\u002F10.2217\u002Fnnm-2015-0017","https:\u002F\u002Fdoi.org\u002F10.2217\u002Fnnm-2015-0017",{"mag":1964,"pmc":1965,"openalex":1966,"pm":1967,"doi":1968},"2341321748","4910947","W2341321748","27077564","10.2217\u002Fnnm-2015-0017",{"id":20,"text":1970,"url":1971,"identifiers":1972},"Sun W et al (2018) Outcome of children with multiply relapsed B-cell acute lymphoblastic leukemia: a therapeutic advances in childhood leukemia & lymphoma study. Leukemia 32:2316–2325. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41375-018-0094-0","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41375-018-0094-0",{"mag":1973,"pmc":1974,"openalex":1975,"pm":1976,"doi":1977},"2792798899","6224404","W2792798899","29728694","10.1038\u002Fs41375-018-0094-0",{"id":20,"text":1979,"url":1980,"identifiers":1981},"Sung YJ et al (2018) Mitochondrial Lon sequesters and stabilizes p53 in the matrix to restrain apoptosis under oxidative stress via its chaperone activity. Cell Death Dis 9:697. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41419-018-0730-7","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41419-018-0730-7",{"mag":1982,"pmc":1983,"openalex":1984,"pm":1985,"doi":1986},"2807957376","5998145","W2807957376","29899330","10.1038\u002Fs41419-018-0730-7",{"id":20,"text":1988,"url":1989,"identifiers":1990},"Taga T, Tomizawa D, Takahashi H, Adachi S (2016) Acute myeloid leukemia in children: current status and future directions. Pediatr Int 58:71–80. https:\u002F\u002Fdoi.org\u002F10.1111\u002Fped.12865","https:\u002F\u002Fdoi.org\u002F10.1111\u002Fped.12865",{"mag":1991,"openalex":1992,"pm":1993,"doi":1994},"2193293559","W2193293559","26645706","10.1111\u002Fped.12865",{"id":1996,"text":1997,"url":1998,"identifiers":1999},"8bbb0351-e34d-4714-a3af-52204f50192f","Teachey DT, Pui CH (2019) Comparative features and outcomes between paediatric T-cell and B-cell acute lymphoblastic leukaemia. Lancet Oncol 20:e142–e154. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fs1470-2045(19)30031-2","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1470204519300312",{"doi":2000},"10.1016\u002Fs1470-2045(19)30031-2",{"id":20,"text":2002,"url":2003,"identifiers":2004},"Wang JY (2014) The capable ABL: what is its biological function? Mol Cell Biol 34:1188–1197. https:\u002F\u002Fdoi.org\u002F10.1128\u002Fmcb.01454-13","https:\u002F\u002Fdoi.org\u002F10.1128\u002Fmcb.01454-13",{"mag":2005,"pmc":2006,"openalex":2007,"pm":2008,"doi":2009},"2133900563","3993570","W2133900563","24421390","10.1128\u002Fmcb.01454-13",{"id":2011,"text":2012,"url":2013,"identifiers":2014},"77987fec-0882-4aae-badb-3b4bd4cab715","Wax PM (2013) Current use of chelation in American health care. J Med Toxicol 9:303–307. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs13181-013-0347-2","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs13181-013-0347-2",{"doi":2015},"10.1007\u002Fs13181-013-0347-2",{"id":780,"text":2017,"url":782,"identifiers":2018},"Yu J, Zhang L, Hwang PM, Kinzler KW, Vogelstein B (2001) PUMA induces the rapid apoptosis of colorectal cancer cells. Mol Cell 7:673–682",{"doi":784},{"id":20,"text":2020,"url":2021,"identifiers":2022},"Zhao Y et al (2014) Chelating intracellularly accumulated zinc decreased ischemic brain injury through reducing neuronal apoptotic death. Stroke 45:1139–1147. https:\u002F\u002Fdoi.org\u002F10.1161\u002FSTROKEAHA.113.004296","https:\u002F\u002Fdoi.org\u002F10.1161\u002Fstrokeaha.113.004296",{"mag":2023,"openalex":2024,"pm":2025,"doi":2026},"2170743106","W2170743106","24643405","10.1161\u002Fstrokeaha.113.004296",{"id":20,"text":2028,"url":2029,"identifiers":2030},"Zhou P, Zhang J, Zhang Y, Liu Y, Liang J, Liu B, Zhang W (2016) Generation of hydrogen peroxide and hydroxyl radical resulting from oxygen-dependent oxidation of L-ascorbic acid via copper redox-catalyzed reactions. RSC Adv 6:38541–38547. https:\u002F\u002Fdoi.org\u002F10.1039\u002FC6RA02843H","https:\u002F\u002Fdoi.org\u002F10.1039\u002Fc6ra02843h",{"mag":2031,"openalex":2032,"doi":2033},"2322873345","W2322873345","10.1039\u002Fc6ra02843h",{"id":20,"text":2035,"url":2036,"identifiers":2037},"Zhu B et al (2017) Zinc depletion by TPEN induces apoptosis in human acute promyelocytic NB4 Cells. Cell Physiol Biochem 42:1822–1836. https:\u002F\u002Fdoi.org\u002F10.1159\u002F000479539","https:\u002F\u002Fdoi.org\u002F10.1159\u002F000479539",{"mag":2038,"openalex":2039,"pm":2040,"doi":2041},"2739819674","W2739819674","28750402","10.1159\u002F000479539",{"id":2043,"createTime":2044,"updateTime":2045,"relativeEntities":2046,"slug":2047,"properties":2048,"entityType":233,"verifyStatus":234,"verifyTime":2057,"verifyNote":236,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":2058,"fullTextUrl":20,"authors":2059,"publicationType":291,"publisherRelationship":2142,"citationCount":2202,"citationInfo":2203,"publishDate":2206,"publishYear":2204,"citationAnalyzeStatus":19,"lastCitationAnalyze":2207,"indexDatabases":2208,"openAccess":20,"references":2209,"isForceReanalyzing":362},"a2bc3252-1f29-453b-8015-6d64f3401d02","2024-01-05T20:37:16.730+00:00","2026-05-21T11:24:35.135+00:00",[],"Hepatic-distribution-of-iron-copper-zinc-and-cadmium-containing-proteins-in-normal-and-iron-overload-mice",{"abstract":2049,"title":2051,"gsPaper":2053,"doi":2055},{"EN":2050},"Subcellular distribution of metal-containing proteins of Fe, Cu, Zn and Cd were determined in the liver samples of iron overload mice by size exclusion high performance liquid chromatography with on-line coupling to UV and inductively coupled plasma mass spectrometry. Collision cell techniques was used to remove polyatomic interferences for some elements, such as Fe. Comparative molecular weight (MW) information of the elemental fraction was obtained within a retention time of 40 min. Fe was present only in high-MW (HMW) protein; Cu, Zn and Cd were found in different MW proteins. It was also observed that these four elements studied showed predominant association with HMW fractions. Moreover, compared with the normal group, we found that the contents of these elements except Cu significantly increased and the distribution of some elements like Cd changed in iron overload mouse liver. It means that excessive iron accumulation in vivo may affect the metabolism of other element such as Zn and Cd.",{"EN":2052},"Hepatic distribution of iron, copper, zinc and cadmium-containing proteins in normal and iron overload mice",{"VOID":2054},"[\"879067256308052811\"]",{"VOID":2056},"10.1007\u002Fs10534-008-9161-8","2024-04-29T00:43:04.585+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10534-008-9161-8",[2060,2084,2097,2120],{"id":2061,"sortIndex":21,"researcher":20,"roles":2062,"affiliations":2063,"properties":2081},"010c338e-1f82-4b2d-8f82-5592ddc5e6fe",[242],[2064,2072],{"id":2065,"sortIndex":21,"affiliation":2066,"properties":20},"85b53755-7478-4f6d-ac1d-9dc07608df96",{"id":2065,"createTime":20,"updateTime":20,"relativeEntities":2067,"slug":20,"properties":2068,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2071,"statistic":20},[],{"title":2069},{"VI":2070},"Key Laboratory of Nuclear Analytical Techniques, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing, People’s Republic of China",[],{"id":2073,"sortIndex":259,"affiliation":2074,"properties":2080},"a8bd8451-b101-4320-98e4-06f0a9899155",{"id":2073,"createTime":20,"updateTime":20,"relativeEntities":2075,"slug":20,"properties":2076,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2079,"statistic":20},[],{"title":2077},{"EN":2078},"Department of Chemistry and Chemical Engineering, Huazhong University of Science and Technology, Wuhan, People’s Republic of China",[],{},{"title":2082},{"VI":2083},"Yan Zhang",{"id":2085,"sortIndex":259,"researcher":20,"roles":2086,"affiliations":2087,"properties":2094},"05139cc5-0db4-48de-84c5-9d0246675b31",[242],[2088],{"id":2065,"sortIndex":21,"affiliation":2089,"properties":20},{"id":2065,"createTime":20,"updateTime":20,"relativeEntities":2090,"slug":20,"properties":2091,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2093,"statistic":20},[],{"title":2092},{"VI":2070},[],{"title":2095},{"VI":2096},"Bai Li",{"id":2098,"sortIndex":277,"researcher":20,"roles":2099,"affiliations":2100,"properties":2115},"e94f1a59-8caa-4e00-b014-52179af0fa83",[242],[2101,2107],{"id":2065,"sortIndex":21,"affiliation":2102,"properties":20},{"id":2065,"createTime":20,"updateTime":20,"relativeEntities":2103,"slug":20,"properties":2104,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2106,"statistic":20},[],{"title":2105},{"VI":2070},[],{"id":2108,"sortIndex":259,"affiliation":2109,"properties":20},"9c5ae29c-ea95-4454-85f4-58f5073f1d71",{"id":2108,"createTime":20,"updateTime":20,"relativeEntities":2110,"slug":20,"properties":2111,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2114,"statistic":20},[],{"title":2112},{"VI":2113},"National Center for Nanoscience and Technology, Beijing, People’s Republic of China",[],{"title":2116,"gsAuthor":2118},{"VI":2117},"Chunying Chen",{"VOID":2119},"[\"8FUTiREAAAAJ\"]",{"id":2121,"sortIndex":357,"researcher":20,"roles":2122,"affiliations":2123,"properties":2139},"330bb160-6490-447e-ab7d-81b1f0b0b242",[242],[2124,2130],{"id":2073,"sortIndex":21,"affiliation":2125,"properties":20},{"id":2073,"createTime":20,"updateTime":20,"relativeEntities":2126,"slug":20,"properties":2127,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2129,"statistic":20},[],{"title":2128},{"EN":2078},[],{"id":2131,"sortIndex":259,"affiliation":2132,"properties":2138},"da3e350d-3a07-45e3-9833-83e1c91c8ffc",{"id":2131,"createTime":20,"updateTime":20,"relativeEntities":2133,"slug":20,"properties":2134,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2137,"statistic":20},[],{"title":2135},{"VI":2136},"Division of Nitric Oxide and Inflammatory Medicine, E-Institutes of Shanghai Universities, Shanghai, People’s Republic of China",[],{},{"title":2140},{"VI":2141},"Zhonghong Gao",{"url":2058,"publisher":2143,"properties":2197},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":2144,"slug":10,"properties":2145,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":2149,"manageAffiliations":2166,"indexDatabases":2177,"url":100,"thumbnailPath":20,"statistic":2192,"gsStatistic":20,"type":211,"analyzePriority":20},[],{"issn":2146,"title":2147,"eissn":2148},{"VOID":13},{"EN":15},{"VOID":17},[2150,2154,2158,2162],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":2151,"label":2152,"description":2153,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":2155,"label":2156,"description":2157,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":2159,"label":2160,"description":2161,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":2163,"label":2164,"description":2165,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},[2167,2172],{"id":49,"createTime":20,"updateTime":20,"relativeEntities":2168,"slug":20,"properties":2169,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2171,"statistic":20},[],{"title":2170},{"EN":53},[55],{"id":57,"createTime":20,"updateTime":20,"relativeEntities":2173,"slug":20,"properties":2174,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2176,"statistic":20},[],{"title":2175},{"EN":61},[],[2178,2185],{"id":65,"indexDatabase":2179,"url":20,"indexYears":20,"academicFieldIds":2184,"indexDatabaseRanking":20},{"id":67,"createTime":20,"updateTime":20,"relativeEntities":2180,"label":2181,"description":2182,"key":74,"publicationTags":2183,"standard":20},[],{"EN":70,"VI":70},{"EN":72,"VI":73},[76,77],[79],{"id":81,"indexDatabase":2186,"url":92,"indexYears":93,"academicFieldIds":2191,"indexDatabaseRanking":99},{"id":83,"createTime":20,"updateTime":20,"relativeEntities":2187,"label":2188,"description":2189,"key":89,"publicationTags":2190,"standard":20},[],{"EN":86,"VI":86},{"EN":86,"VI":88},[91],[95,96,97,98],{"impactFactor":21,"impactFactorByYear":2193,"i10Index":113,"i10IndexLast5Year":114,"totalPublication":115,"totalPublicationByYear":2194,"totalCitation":151,"totalCitationByYear":2195,"totalCitationPerPublication":181,"totalCitationPerPublicationByYear":2196,"hindexLast5Year":123,"hindex":123},{"2012":103,"2013":104,"2014":105,"2015":103,"2016":106,"2017":107,"2018":108,"2019":105,"2020":109,"2021":110,"2022":111,"2023":112},{"1988":117,"1989":118,"1990":119,"1991":120,"1992":121,"1993":122,"1994":123,"1995":124,"1996":125,"1997":126,"1998":127,"1999":128,"2000":129,"2001":130,"2002":131,"2003":132,"2004":133,"2005":134,"2006":135,"2007":136,"2008":132,"2009":137,"2010":138,"2011":139,"2012":140,"2013":141,"2014":142,"2015":143,"2016":143,"2017":144,"2018":145,"2019":146,"2020":129,"2021":147,"2022":148,"2023":149,"2024":150},{"1989":153,"1990":154,"1991":155,"1992":156,"1993":157,"1994":158,"1995":159,"1996":160,"2004":161,"2005":162,"2006":163,"2007":164,"2008":165,"2009":166,"2010":167,"2011":168,"2012":169,"2013":170,"2014":171,"2015":172,"2016":173,"2017":174,"2018":175,"2019":176,"2020":177,"2021":178,"2022":179,"2023":180},{"1989":183,"1990":184,"1991":185,"1992":186,"1993":187,"1994":188,"1995":189,"1996":190,"2004":191,"2005":192,"2006":193,"2007":194,"2008":195,"2009":196,"2010":197,"2011":198,"2012":199,"2013":200,"2014":201,"2015":202,"2016":203,"2017":204,"2018":205,"2019":206,"2020":207,"2021":208,"2022":209,"2023":210},{"pages":2198,"volume":2200},{"VOID":2199},"251-259",{"VOID":2201},"22",19,{"total":2202,"publishYear":2204,"statisticByYear":2205},2008,{"2009":259,"2011":161,"2012":161,"2013":259,"2014":161,"2016":259,"2018":259,"2019":259,"2024":259},"2008-09-05","2026-05-21T11:24:35.134+00:00",[76,99],[2210,2213,2216,2219,2225,2228,2231,2234,2237,2240,2243,2249,2252,2255,2261,2264,2267,2270,2276,2282,2285,2288,2291,2294,2297,2303,2306,2309,2312,2315,2318,2321],{"id":780,"text":2211,"url":782,"identifiers":2212},"Chery CC, Günther D, Cornelis R, Vanhaecke F, Moens L (2003) Detection of metals in proteins by means of polyacrylamide gel electrophoresis and laser ablation-inductively coupled plasma-mass spectrometry: application to selenium. Electrophoresis 24:3305–3313",{"doi":784},{"id":780,"text":2214,"url":782,"identifiers":2215},"De Smet H, De Wachter B, Lobinski R, Blust R (2001) Dynamics of (Cd, Zn)-metallothioneins in gills, liver and kidney of common carp Cyprinus carpio during cadmium exposure. Aquat Toxicol 52:269–281",{"doi":784},{"id":20,"text":2217,"url":20,"identifiers":2218},"Faa G, Terlizzo M, Gerosa C, Conqiu T, Anqelucci E (2002) Patterns of iron distribution in liver cells in β-thalassemia studied by X-ray microanalysis. Haematologica 87:479–484",{},{"id":2220,"text":2221,"url":2222,"identifiers":2223},"60fb2b9f-30e0-4c55-8f83-33564126b9e8","Ferrarello CN, Fernandez de la Campa MR, Sanz-Medel A (2002) Multielement trace-element speciation in metal-biomolecules by chromatography coupled with ICP-MS. Anal Bioanal Chem 373:412–421","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs00216-002-1278-y",{"doi":2224},"10.1007\u002Fs00216-002-1278-y",{"id":780,"text":2226,"url":782,"identifiers":2227},"Fleet JC, Andrews GK, McCormick CC (1990) Iron-induced metallothionein in chick liver: a rapid, route-dependent effect independent of zinc status. J Nutr 120:1214–1222",{"doi":784},{"id":20,"text":2229,"url":20,"identifiers":2230},"Jurczuk M, Brzoska MM, Galazyn-Sidorczuk M (1997) Distribution of the 59Fe radioisotope in the organism of a rat after a subacute exposure to cadmium. Pol J Environ Stud 6:74–76",{},{"id":780,"text":2232,"url":782,"identifiers":2233},"Kannamkumarath SS, Wrobel K, B’Hymer C, Caruso JA (2002) Capillary electrophoresis-inductively coupled plasma mass spectrometry: an attractive complementary technique for elemental speciation analysis. J Chromatogr A 975:245–266",{"doi":784},{"id":780,"text":2235,"url":782,"identifiers":2236},"Leber A, Hemmens B, Klosch B, GoesslerW Raber G, Mayer B, Schmidt K (1999) Characterization of recombinant human endothelial nitric-oxide synthase purified from the yeast Pichia pastoris. J Biol Chem 274:37658–37664",{"doi":784},{"id":20,"text":2238,"url":20,"identifiers":2239},"Liuzzi JP, Avdemir F, Nam H, Knutson MD, Cousins RJ (2006) Zip14 (Slc39a14) mediates non-transferrin-bound iron uptake into cells. Proc Natl Acad Sci USA 103:13612–13617",{},{"id":780,"text":2241,"url":782,"identifiers":2242},"Lobiński R, Schaumlöffel D, Szpunar J (2006) Mass spectrometry in bioinorganic analytical chemistry. Mass Spectrom Rev 25:255–289",{"doi":784},{"id":2244,"text":2245,"url":2246,"identifiers":2247},"9d1cb487-ca03-4a0b-b083-d8ea1bdb2c2f","Nordberg M (1998) Metallothioneins: historical review and state of knowledge. Talanta 46:243–254","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0039914097003457",{"doi":2248},"10.1016\u002Fs0039-9140(97)00345-7",{"id":780,"text":2250,"url":782,"identifiers":2251},"Martino FAR, Sánchez MLF, Medel AS (2002) Multi-elemental fractionation in milk whey by size exclusion chromatography coupled on line to ICP-MS. J Anal At Spectrom 17:1271",{"doi":784},{"id":780,"text":2253,"url":782,"identifiers":2254},"McCormick CC (1984) The tissue-specific accumulation of hepatic zinc metallothionein following parenteral iron loading. Proc Soc Exp Biol Med 176:393–402",{"doi":784},{"id":2256,"text":2257,"url":2258,"identifiers":2259},"0bcaa47f-0516-44c6-b267-2abab8353691","Miyazaki I, Asanuma M, Higashi Y, Sogawa CA, Tanaka K, Ogawa N (2002) Age-related changes in expression of metallothionein-III in rat brain. Neurosci Res 43:323–333","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0168010202000573",{"doi":2260},"10.1016\u002Fs0168-0102(02)00057-3",{"id":20,"text":2262,"url":20,"identifiers":2263},"Papanastasiou DA, Vayenas DV, Vassilopoulos A, Repanti M (2000) Concentration of iron and distribution of iron and transferrin after experimental iron overload in rat tissues in vivo: study of the liver, the spleen, the central nervous system and other organs. Pathol Res Pract 196:47–54",{},{"id":780,"text":2265,"url":782,"identifiers":2266},"Parkes JG, Templeton DM (1994) Iron transport and subcellular distribution in Hep G2 hepatocarcinoma cells. Ann Clin Lab Sci 24:509–520",{"doi":784},{"id":780,"text":2268,"url":782,"identifiers":2269},"Peterson GL (1977) A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem 83:346–350",{"doi":784},{"id":2271,"text":2272,"url":2273,"identifiers":2274},"40015cc8-d39a-43c1-9aca-2ef3849de614","Raja KB, Jafri SE, Peters TJ, Simpson RJ (2006) Iron and cadmium uptake by duodenum of hypotransferrinaemic mice. Biometals 19:547–553","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10534-005-5919-4",{"doi":2275},"10.1007\u002Fs10534-005-5919-4",{"id":2277,"text":2278,"url":2279,"identifiers":2280},"e84183a6-e5c5-4a7e-9448-519c6f4b249f","Richarz AN, Bratter P (2002) Speciation analysis of trace elements in the brains of individuals with Alzheimer’s disease with special emphasis on metallothioneins. Anal Bioanal Chem 372:412–417","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs00216-001-1187-5",{"doi":2281},"10.1007\u002Fs00216-001-1187-5",{"id":20,"text":2283,"url":20,"identifiers":2284},"Roberts HR (1981) Food safety. Wiley, New York",{},{"id":780,"text":2286,"url":782,"identifiers":2287},"Sadi BB, Wrobel K, Wrobel K, Kannamkumarath SS, Castillo JR, Caruso JA (2002) SEC-ICP-MS studies for elements binding to different molecular weight fractions of humic substances in compost extract obtained from urban solid waste. J Environ Monit 4:1010–1016",{"doi":784},{"id":780,"text":2289,"url":782,"identifiers":2290},"Stuhne-Sekalec L, Xu SX, Parkes JG, Olivieri NF, Templeton DM (1992) Speciation of tissue and cellular iron with on-line detection by inductively coupled plasma-mass spectrometry. Anal Biochem 205:278–284",{"doi":784},{"id":780,"text":2292,"url":782,"identifiers":2293},"Szpunar J (2000) Bio-inorganic speciation analysis by hyphenated techniques. Analyst 125:963–988",{"doi":784},{"id":780,"text":2295,"url":782,"identifiers":2296},"Szpunar J (2005) Advances in analytical methodology for bioinorganic speciation analysis: metallomics, metalloproteomics and heteroatom-tagged proteomics and metabolomics. Analyst 130:442–465",{"doi":784},{"id":2298,"text":2299,"url":2300,"identifiers":2301},"da1036e8-579c-4257-a591-190d26e7c5a1","Szpunar J, Lobiński R (2002) Multidimensional approaches in biochemical speciation analysis. Anal Bioanal Chem 373:404–411","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs00216-002-1282-2",{"doi":2302},"10.1007\u002Fs00216-002-1282-2",{"id":780,"text":2304,"url":782,"identifiers":2305},"Tanaka M, Yanagi M, Shirota K, Une Y, Nomure Y, Masaoka Y, Akahori F (1995) Effect of cadmium in the zinc deficient rat. Vet Hum Toxicol 37:203–208",{"doi":784},{"id":20,"text":2307,"url":20,"identifiers":2308},"Wang J, Dreessen D, Wiederin DR, Houk RS (2001) Measurement of trace elements in proteins extracted from liver by size exclusion chromatography-ICP-MS with a magnetic sector mass spectrometer. Anal Biochem 288:89–96",{},{"id":780,"text":2310,"url":782,"identifiers":2311},"Wind M, Lehmann WD (2004) Element and molecular mass spectrometry—an emerging analytical dream team in the life sciences. J Anal At Spectrom 19:20–25",{"doi":784},{"id":20,"text":2313,"url":20,"identifiers":2314},"Yeh CF, Jiang SJ (2002) Determination of monophosphate nucleotides by capillary electrophoresis ICP-MS. Analyst 127:1324–1327",{},{"id":20,"text":2316,"url":20,"identifiers":2317},"Zaidi JH, Arif M, Fatima I, Qureshi IH (2002) Radiochemical neutron activation analysis for trace elements of basic ingredients of pan. J Radioanal Nucl Chem 253:459–464",{},{"id":780,"text":2319,"url":782,"identifiers":2320},"Zhang Y, Li HL, Zhao YL, Gao ZH (2006) Dietary supplementation of baicalin and quercetin attenuates iron overload induced mouse liver injury. Eur J Pharmacol 535:263–269",{"doi":784},{"id":2322,"text":2323,"url":2324,"identifiers":2325},"f74d09b6-cc76-466f-93c3-4ffff4adf328","Zhao YL, Li HL, Gao ZH, Xu HB (2005) Effects of dietary baicalin supplementation on iron overload induced mouse liver oxidative injury. Eur J Pharmacol 509:195–200","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS001429990401372X",{"doi":2326},"10.1016\u002Fj.ejphar.2004.11.060",{"id":2328,"createTime":2329,"updateTime":2330,"relativeEntities":2331,"slug":2332,"properties":2333,"entityType":233,"verifyStatus":234,"verifyTime":2346,"verifyNote":236,"languages":2347,"translateLanguages":20,"viewCount":21,"primaryUrl":2349,"fullTextUrl":20,"authors":2350,"publicationType":291,"publisherRelationship":2457,"citationCount":21,"citationInfo":2518,"publishDate":2520,"publishYear":354,"citationAnalyzeStatus":19,"lastCitationAnalyze":2521,"indexDatabases":2522,"openAccess":20,"references":2523,"isForceReanalyzing":362},"17827f48-a2d0-46cd-80c6-f3cc9125d623","2024-04-16T19:27:55.009+00:00","2026-05-21T05:35:15.782+00:00",[],"Metal-binding-of-metallothioneins-in-human-astrocytomas-U87-MG-IPDDC-2A-",{"openalex":2334,"mag":2336,"title":2338,"gsPaper":2340,"pm":2342,"doi":2344},{"VOID":2335},"W2036350160",{"VOID":2337},"2036350160",{"EN":2339},"Metal binding of metallothioneins in human astrocytomas (U87 MG, IPDDC-2A)",{"VOID":2341},"[\"6823268090965233027\"]",{"VOID":2343},"17115260",{"VOID":2345},"10.1007\u002Fs10534-006-9041-z","2024-05-12T01:10:59.630+00:00",[2348],"EN","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10534-006-9041-z",[2351,2370,2385,2402,2421,2440],{"id":2352,"sortIndex":21,"researcher":20,"roles":2353,"affiliations":2354,"properties":2363},"19769b05-dc81-4008-ab09-ffaba518b30d",[],[2355],{"id":2356,"sortIndex":21,"affiliation":2357,"properties":20},"65184bca-8ebe-4d1f-9a46-399dfefceefd",{"id":2356,"createTime":20,"updateTime":20,"relativeEntities":2358,"slug":20,"properties":2359,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2362,"statistic":20},[],{"title":2360},{"EN":2361},"National Institute of Biology, Večna pot 111, 1000, Ljubljana, Slovenia",[],{"orcid":2364,"title":2366,"openalex":2368},{"VOID":2365},"https:\u002F\u002Forcid.org\u002F0000-0002-4349-3752",{"EN":2367},"Magda Tušek Žnidarič",{"VOID":2369},"A5007034867",{"id":2371,"sortIndex":259,"researcher":20,"roles":2372,"affiliations":2373,"properties":2380},"26b676a0-264f-4e52-9ffe-102f0f43075e",[],[2374],{"id":2356,"sortIndex":21,"affiliation":2375,"properties":20},{"id":2356,"createTime":20,"updateTime":20,"relativeEntities":2376,"slug":20,"properties":2377,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2379,"statistic":20},[],{"title":2378},{"EN":2361},[],{"title":2381,"openalex":2383},{"EN":2382},"Anja Pucer",{"VOID":2384},"A5051481695",{"id":2386,"sortIndex":277,"researcher":20,"roles":2387,"affiliations":2388,"properties":2397},"6432a476-ba7e-4b77-b8d2-b7cff43d1cb0",[],[2389],{"id":2390,"sortIndex":21,"affiliation":2391,"properties":20},"98948261-89b4-4910-84d2-19c2102c8230",{"id":2390,"createTime":20,"updateTime":20,"relativeEntities":2392,"slug":20,"properties":2393,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2396,"statistic":20},[],{"title":2394},{"VI":2395},"National Institute of Biology, Ljubljana, Slovenia",[],{"title":2398,"openalex":2400},{"EN":2399},"T Fatur",{"VOID":2401},"A5034061974",{"id":2403,"sortIndex":357,"researcher":20,"roles":2404,"affiliations":2405,"properties":2412},"354ba448-b230-4ca5-a041-61d1d3a71122",[],[2406],{"id":2390,"sortIndex":21,"affiliation":2407,"properties":20},{"id":2390,"createTime":20,"updateTime":20,"relativeEntities":2408,"slug":20,"properties":2409,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2411,"statistic":20},[],{"title":2410},{"VI":2395},[],{"orcid":2413,"title":2415,"gsAuthor":2417,"openalex":2419},{"VOID":2414},"https:\u002F\u002Forcid.org\u002F0000-0002-1437-2556",{"EN":2416},"Metka Filipič",{"VOID":2418},"[\"C0o9YQoAAAAJ\"]",{"VOID":2420},"A5001381955",{"id":2422,"sortIndex":161,"researcher":20,"roles":2423,"affiliations":2424,"properties":2433},"e792e3b9-4c1d-4d97-98db-649cbb1e1823",[],[2425],{"id":2426,"sortIndex":21,"affiliation":2427,"properties":20},"2004306a-95d7-424f-bd65-044878c84cf7",{"id":2426,"createTime":20,"updateTime":20,"relativeEntities":2428,"slug":20,"properties":2429,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2432,"statistic":20},[],{"title":2430},{"VI":2431},"Department of Environmental Sciences, J. Stefan Institute, Ljubljana, Slovenia",[],{"orcid":2434,"title":2436,"openalex":2438},{"VOID":2435},"https:\u002F\u002Forcid.org\u002F0000-0002-8018-1715",{"EN":2437},"Janez Ščančar",{"VOID":2439},"A5053771070",{"id":2441,"sortIndex":356,"researcher":20,"roles":2442,"affiliations":2443,"properties":2450},"21110f36-2b0b-49ac-a737-76eba4b47498",[],[2444],{"id":2426,"sortIndex":21,"affiliation":2445,"properties":20},{"id":2426,"createTime":20,"updateTime":20,"relativeEntities":2446,"slug":20,"properties":2447,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2449,"statistic":20},[],{"title":2448},{"VI":2431},[],{"orcid":2451,"title":2453,"openalex":2455},{"VOID":2452},"https:\u002F\u002Forcid.org\u002F0000-0001-7179-0917",{"EN":2454},"Ingrid Falnoga",{"VOID":2456},"A5013029636",{"url":20,"publisher":2458,"properties":2512},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":2459,"slug":10,"properties":2460,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":2464,"manageAffiliations":2481,"indexDatabases":2492,"url":100,"thumbnailPath":20,"statistic":2507,"gsStatistic":20,"type":211,"analyzePriority":20},[],{"issn":2461,"title":2462,"eissn":2463},{"VOID":13},{"EN":15},{"VOID":17},[2465,2469,2473,2477],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":2466,"label":2467,"description":2468,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":2470,"label":2471,"description":2472,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":2474,"label":2475,"description":2476,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":2478,"label":2479,"description":2480,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},[2482,2487],{"id":49,"createTime":20,"updateTime":20,"relativeEntities":2483,"slug":20,"properties":2484,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2486,"statistic":20},[],{"title":2485},{"EN":53},[55],{"id":57,"createTime":20,"updateTime":20,"relativeEntities":2488,"slug":20,"properties":2489,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2491,"statistic":20},[],{"title":2490},{"EN":61},[],[2493,2500],{"id":65,"indexDatabase":2494,"url":20,"indexYears":20,"academicFieldIds":2499,"indexDatabaseRanking":20},{"id":67,"createTime":20,"updateTime":20,"relativeEntities":2495,"label":2496,"description":2497,"key":74,"publicationTags":2498,"standard":20},[],{"EN":70,"VI":70},{"EN":72,"VI":73},[76,77],[79],{"id":81,"indexDatabase":2501,"url":92,"indexYears":93,"academicFieldIds":2506,"indexDatabaseRanking":99},{"id":83,"createTime":20,"updateTime":20,"relativeEntities":2502,"label":2503,"description":2504,"key":89,"publicationTags":2505,"standard":20},[],{"EN":86,"VI":86},{"EN":86,"VI":88},[91],[95,96,97,98],{"impactFactor":21,"impactFactorByYear":2508,"i10Index":113,"i10IndexLast5Year":114,"totalPublication":115,"totalPublicationByYear":2509,"totalCitation":151,"totalCitationByYear":2510,"totalCitationPerPublication":181,"totalCitationPerPublicationByYear":2511,"hindexLast5Year":123,"hindex":123},{"2012":103,"2013":104,"2014":105,"2015":103,"2016":106,"2017":107,"2018":108,"2019":105,"2020":109,"2021":110,"2022":111,"2023":112},{"1988":117,"1989":118,"1990":119,"1991":120,"1992":121,"1993":122,"1994":123,"1995":124,"1996":125,"1997":126,"1998":127,"1999":128,"2000":129,"2001":130,"2002":131,"2003":132,"2004":133,"2005":134,"2006":135,"2007":136,"2008":132,"2009":137,"2010":138,"2011":139,"2012":140,"2013":141,"2014":142,"2015":143,"2016":143,"2017":144,"2018":145,"2019":146,"2020":129,"2021":147,"2022":148,"2023":149,"2024":150},{"1989":153,"1990":154,"1991":155,"1992":156,"1993":157,"1994":158,"1995":159,"1996":160,"2004":161,"2005":162,"2006":163,"2007":164,"2008":165,"2009":166,"2010":167,"2011":168,"2012":169,"2013":170,"2014":171,"2015":172,"2016":173,"2017":174,"2018":175,"2019":176,"2020":177,"2021":178,"2022":179,"2023":180},{"1989":183,"1990":184,"1991":185,"1992":186,"1993":187,"1994":188,"1995":189,"1996":190,"2004":191,"2005":192,"2006":193,"2007":194,"2008":195,"2009":196,"2010":197,"2011":198,"2012":199,"2013":200,"2014":201,"2015":202,"2016":203,"2017":204,"2018":205,"2019":206,"2020":207,"2021":208,"2022":209,"2023":210},{"issue":2513,"pages":2515,"volume":2517},{"VOID":2514},"5",{"VOID":2516},"781-792",{"VOID":351},{"total":21,"publishYear":354,"statisticByYear":2519},{},"2007-08-27","2026-05-21T05:35:15.781+00:00",[76,99],[2524,2528,2532,2535,2539,2543,2547,2551,2555,2558,2562,2566,2570,2573,2577,2581,2585,2589,2593,2597,2600,2603,2607,2611,2615,2619,2623,2627,2631,2635,2639,2643,2647,2650,2654,2658,2662,2666,2670,2674,2678,2682,2686,2690],{"id":20,"text":2525,"url":20,"identifiers":2526},"Amoureux MC, Wurch T, Pauwels PJ, 1995 Modulation of metallothionein-III mRNA content and growth rate of rat C6-glial cells by transfection with human 5-HTID receptor genes. Biochem Biophys Res Commun 214(2):639–645",{"doi":2527},"10.1006\u002Fbbrc.1995.2334",{"id":20,"text":2529,"url":20,"identifiers":2530},"Aoki C, Nakanishi T, Sogawa N, Ishii K, Ogawa N, Takigawa M, Furuta H, 1998 Stimulatory effects of 4-methylcatechol, dopamine and levodopa on the expression of metallothionein-III (GIF) mRNA in immortalized mouse brain glial cells (VR-2g). Brain Res 792:335–339",{"doi":2531},"10.1016\u002FS0006-8993(98)00239-X",{"id":20,"text":2533,"url":20,"identifiers":2534},"Araque A, Parpura V, Sanzgiri RP, Haydon PG 1999 Tripartite synapses: glia, the uncknowledged partner. TINS 22(5):208–215",{},{"id":20,"text":2536,"url":20,"identifiers":2537},"Beattie JH, Owen HLW, Wallace SM, Arthur JR, Kwun IS, Hawksworth GM, Wallace HM, 2005 Metallothionein overexpression and resistence to toxic stress. Toxicol Lett 157:69–78",{"doi":2538},"10.1016\u002Fj.toxlet.2005.01.005",{"id":20,"text":2540,"url":20,"identifiers":2541},"Bredel M, 2001 Anticancer drug resistance in primary human brain tumors. Brain Res Rev 35:161–204",{"doi":2542},"10.1016\u002FS0165-0173(01)00045-5",{"id":20,"text":2544,"url":20,"identifiers":2545},"Bredel M, Zentner J, 2002 Brain-tumour drug resistance: the bare essentials. Lancet Oncol 3:397–406",{"doi":2546},"10.1016\u002FS1470-2045(02)00786-6",{"id":20,"text":2548,"url":20,"identifiers":2549},"Chan J, Huang Z, Merrifield ME, Salgado MT, Stilman MJ, 2002 Studies of metal binding reactions in metallothioneins by spectroscopic, molecular biology, and molecular modeling technique. Coordinat Chem Rev 233(234):319–339",{"doi":2550},"10.1016\u002FS0010-8545(02)00176-5",{"id":20,"text":2552,"url":20,"identifiers":2553},"Cherian MG, Jayasurya A, Bay BH, 2003 Metallothioneins in human tumors and potential roles in cancerogenesis. Mutation Res 533:201–209",{"doi":2554},"10.1016\u002Fj.mrfmmm.2003.07.013",{"id":20,"text":2556,"url":20,"identifiers":2557},"Chian-Feng C, Sue-Hong W, Lih-Yuan L, 1996 Identification and characterization of metallothionein III (growth inhybitory factor) from porcine brain. Comput Biochem Physiol 115B(1):27–32",{},{"id":20,"text":2559,"url":20,"identifiers":2560},"Chung RS, West AK, 2004 A role for extracellular metallothioneins in CSN in injury and repair. Neuroscience 123:595–599",{"doi":2561},"10.1016\u002Fj.neuroscience.2003.10.019",{"id":20,"text":2563,"url":20,"identifiers":2564},"Falnoga I, Tušek Žnidarič M, Horvat M, Stegnar P, 2000 Mercury, selenium, and cadmium in human autopsy samples from Idrija residents and mercury mine workers. Environ Res Sect A 84:211–218",{"doi":2565},"10.1006\u002Fenrs.2000.4116",{"id":20,"text":2567,"url":20,"identifiers":2568},"Fatur T, Tušek M, Falnoga I, ščančar J, Lah TT, Filipič M, 2002 DNA damage and metallothionein synthesis in human hepatoma cells (HepG2) exposed to cadmium. Food Chem Toxicol 40:1069–1076",{"doi":2569},"10.1016\u002FS0278-6915(02)00058-3",{"id":20,"text":2571,"url":20,"identifiers":2572},"George SG, 1983 Heavy metal detoxication in the mussel Mytilus edulis – composition of Cd-containing granules (tertiary lysosomes). Comput Biochem Physiol 76C:53–57",{},{"id":20,"text":2574,"url":20,"identifiers":2575},"Gerhardsson L, Englyst V, Lundstrom NG, Sandberg S, Nordberg G, 2002 Cadmium, copper and zinc in tissues of deceased copper smelter workers. J Trace Elem Med Biol 16:261–266",{"doi":2576},"10.1016\u002FS0946-672X(02)80055-4",{"id":20,"text":2578,"url":20,"identifiers":2579},"Gerrett SH, Park S, Sens MA, Somji S, Singh RK, Namburi VBRK, Sens DA, 2005 Expression of metallothionein isoform 3 is restricted at the post-transcriptional level in human bladder epithelial cells. Taxicol Sci 8(1):66–74",{"doi":2580},"10.1093\u002Ftoxsci\u002Fkfi231",{"id":20,"text":2582,"url":20,"identifiers":2583},"Hidalgo J, Ashner M, Zatta P, Vašak M, 2001 Roles of metallothoinein family of proteins in the central nervous system. Brain Res Bull 55:133–145",{"doi":2584},"10.1016\u002FS0361-9230(01)00452-X",{"id":20,"text":2586,"url":20,"identifiers":2587},"Hiura T, Khalid H, Yanmashita H, Tokunaga Y, Yasunaga A, Shibata S, 1998 Immunoshistochemical analysis of metallothionein in astrocytic tumors in relation to tumor grade, proliferative potential and survival. Cancer 83(11):2361–22369",{"doi":2588},"10.1002\u002F(SICI)1097-0142(19981201)83:11\u003C2361::AID-CNCR16>3.0.CO;2-N",{"id":20,"text":2590,"url":20,"identifiers":2591},"Hozumi I, Asanuma M, Yamada M, Uchida Y, 2004 Metallothioneins and neurodegenerative disease. J Health Sci 50(4):323–331",{"doi":2592},"10.1248\u002Fjhs.50.323",{"id":20,"text":2594,"url":20,"identifiers":2595},"Im JY, Paik SG, Han PL, 2006 Cadmium-induced astroglia death proceeds via glutathione depletion. J Neurosci Res 83:301–308",{"doi":2596},"10.1002\u002Fjnr.20722",{"id":20,"text":2598,"url":20,"identifiers":2599},"Kägi JHR, Kojima Y, 1987 Chemistry and biochemistry of metallothionein. Experientia Suppl 52:26–61",{},{"id":20,"text":2601,"url":20,"identifiers":2602},"Kägi JHR. 1993 Evolution, structure and chemical activity of class 1 metallothioneins: an overview. V: metallothionein III: biological roles and medical implications [Third International Conference on Metallothionein]. Suzuki KT, Imura N, Kimura M, eds., Birkhäuser; 29–56",{},{"id":20,"text":2604,"url":20,"identifiers":2605},"Kostial K, Cadmium V, 1986 Trace elements in human and animal nutrition, vol. 2. Mertz W, ed., Academid Press",{"doi":2606},"10.1016\u002FB978-0-08-092469-4.50009-1",{"id":20,"text":2608,"url":20,"identifiers":2609},"Køhler LB, Berezin V, Bock E, Penkowa M, 2003 The role of metallothion II in neuronal differentiation and survival. Brain Res 992:128–136",{"doi":2610},"10.1016\u002Fj.brainres.2003.08.049",{"id":20,"text":2612,"url":20,"identifiers":2613},"Meloni G, Knipp M, Vašak M, 2005 Detection of neuronal growth inhibitory factor (metallothionein-3 in polyacrylamide gels and by Western blot analysis. J Bichem Biophys Methods 64:76–81",{"doi":2614},"10.1016\u002Fj.jbbm.2005.05.005",{"id":20,"text":2616,"url":20,"identifiers":2617},"Miles TA, Hawksworth GM, Beattie JH, Rodilla V, 2000 Induction, regulation, degradation, and biological significance of mammalian metallothioneins. Crit Rev Biochem Mol Biol 35(1):35–70",{"doi":2618},"10.1080\u002F10409230091169168",{"id":20,"text":2620,"url":20,"identifiers":2621},"Mocchegiani E, Giacconi R, Fattoretti P, Casoli T, Cipriano C, Muti E, Malavolta M, DiStefano G, Bertoni-Freddari C, 2004 Metallothionein isoforms (I + II and III) and interleucin-6 in the hippocampus of old rats: may their conconmitant increments lead to neurodegeneration. Brain Res 63:133–142",{"doi":2622},"10.1016\u002Fj.brainresbull.2004.02.004",{"id":20,"text":2624,"url":20,"identifiers":2625},"Mosman T, 1983 Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assay. J Immunol Meth 65:55–63",{"doi":2626},"10.1016\u002F0022-1759(83)90303-4",{"id":20,"text":2628,"url":20,"identifiers":2629},"Nordberg M, 1998 Metallothioneins: historical review and state of knowledge. Talanta 46:243–254",{"doi":2630},"10.1016\u002FS0039-9140(97)00345-7",{"id":20,"text":2632,"url":20,"identifiers":2633},"Palumaa P, Tammiste I, Kruusel K, Kangur L, Jornval H, Sillard R, 2005 Metal binding of metallothionein-3 versus metallothiionein-2: lower affinity and higher plasticity. Bichim Biophys Acta 1747:205–211",{"doi":2634},"10.1016\u002Fj.bbapap.2004.11.007",{"id":20,"text":2636,"url":20,"identifiers":2637},"Pattanaik A, Shaw CF III, Petering DH, Garvey J, Kraker AJ, 1994 Basal metallothionein in tumors: widespread presence of apoprotein. J Inorg Biochem 54,(2):91–105",{"doi":2638},"10.1016\u002F0162-0134(94)80023-5",{"id":20,"text":2640,"url":20,"identifiers":2641},"Rising L, Vitarella D, Kimelberg HK, Aschner M, 1995 Cadmium chloride (CdCl2)-induced metallothionein (MT) expression in neuronal rat primary astrocyte cultures. Brain Res 678(1–2):91–98",{"doi":2642},"10.1016\u002F0006-8993(95)00170-U",{"id":20,"text":2644,"url":20,"identifiers":2645},"Romero-Isart N, Vašak M, 2002 Advances in the structure and chemistry of metallothioneins. J Inorg Biochem 88:388–396",{"doi":2646},"10.1016\u002FS0162-0134(01)00347-6",{"id":20,"text":2648,"url":20,"identifiers":2649},"Satomi K, Nakai K, Kurokawa N, Kanehisa T, Naganima A, Satoh H, 2005 Metal components analysis of metallothionein-III in the brain sections of metallothionein-I and metallothionein-II null mice exposed to mercury vapor with HPLC\u002FICP-MS. Anal Bioanal Chem 38:1514–1519",{},{"id":20,"text":2651,"url":20,"identifiers":2652},"Sawada J, Kikuchi J, Shibutani M, Mitsumori K, Inoue K, Kasahara T, 1994 Induction of metallothionein in astrocytes by cytokines and heavy metals. Bio Signals 3(3):157–168",{"doi":2653},"10.1159\u002F000109539",{"id":20,"text":2655,"url":20,"identifiers":2656},"Sens MA, Somji S, Lamm DL, Garrett SH, Slowinsky F, Todd JH, Sens DA, 2000 Metallothionein isoform 3 as a potential biomarker for human bladder cancer",{"doi":2657},"10.2307\u002F3454381",{"id":20,"text":2659,"url":20,"identifiers":2660},"Tapiero H, Tew KD, 2003 Trace elements in human physiology: zinc and metallothioneins. Biomed Pharmacoth 57:399–411",{"doi":2661},"10.1016\u002FS0753-3322(03)00081-7",{"id":20,"text":2663,"url":20,"identifiers":2664},"Tiffany-Castiglioni E, Qian Y, 2001 Stroglia as metal depots: molecular mechanisms for metal accumulation, storage and release. Neurotoxicology 22:577–592",{"doi":2665},"10.1016\u002FS0161-813X(01)00050-X",{"id":20,"text":2667,"url":20,"identifiers":2668},"Uchida Y, Takio K, Titani K, Ihara Y, Tomonaga M, 1991 The growth inhibitory factor that is deficient in Alzheimer s disease is a 68 amino acid metallothionein-like protein. Neuron 7:337–347",{"doi":2669},"10.1016\u002F0896-6273(91)90272-2",{"id":20,"text":2671,"url":20,"identifiers":2672},"Uchida Y, Gomi F, Masumizu T, Miura Y, 2002 Growth inhibitory factor prevents neurite extension and the death of cortical neurons caused by high oxygen exposure through hydroxyl radical scavenging. J Biol Chem 277(35):32353–32359",{"doi":2673},"10.1074\u002Fjbc.M111263200",{"id":20,"text":2675,"url":20,"identifiers":2676},"Vašak M, 2005 Advances in metallothionein structure and functions. J Trace Elem Med Biol 19:13–17",{"doi":2677},"10.1016\u002Fj.jtemb.2005.03.003",{"id":20,"text":2679,"url":20,"identifiers":2680},"Yasutake A, Nakano A, Hirayama K, 1998 Induction by mercury compounds of brain metallothionein in rats: Hg0 exposure induces long-lived brain metallothioneins. Arch Toxicol 72:187–191",{"doi":2681},"10.1007\u002Fs002040050486",{"id":20,"text":2683,"url":20,"identifiers":2684},"Yoshifumi I, Keung WM, 2003 Anti-amyloid B activity of metallothionein-III is different from its neuronal growth inhibitory activity: structure-activity studies. Brain Res 960:228–234",{"doi":2685},"10.1016\u002FS0006-8993(02)03891-X",{"id":20,"text":2687,"url":20,"identifiers":2688},"You HJ, Oh D, Choi CY, Lee DG, Hahm KS, Moon AR, Jeong HG, 2002 Protective effect of metallothionein-III on DNA damage in response to reactive oxygen species. Biochim Biophys Acta 1573:33–38",{"doi":2689},"10.1016\u002FS0304-4165(02)00325-2",{"id":20,"text":2691,"url":20,"identifiers":2692},"Yu H, Lukiw W, Bergeron WJ, Niznik C, Fraser HBPE, 2001 Metallothionein III is reduced in Alzheimer¨s disease. Brain Res 894:37–45",{"doi":2693},"10.1016\u002FS0006-8993(00)03196-6"]