[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"_public_publisher_byId_9c2ad4bd-0924-4534-81c3-d89f019058fb":3,"_public_publication_all{\"sortAscending\":false,\"sortField\":\"updateTime\",\"page\":0,\"size\":10,\"facet\":true,\"searchKey\":\"publisherId:9c2ad4bd-0924-4534-81c3-d89f019058fb,\"}":119},{"code":4,"data":5,"meta":18},"SUCCESS",{"id":6,"createTime":7,"updateTime":8,"relativeEntities":9,"slug":10,"properties":11,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":20,"manageAffiliations":53,"indexDatabases":76,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},"9c2ad4bd-0924-4534-81c3-d89f019058fb","2023-12-05T07:24:24.946+00:00","2025-11-21T10:06:08.515+00:00",[],"Journal-of-Photochemistry-and-Photobiology-B-Biology",{"issn":12,"title":14},{"VOID":13},"10111344",{"EN":15},"Journal of Photochemistry and Photobiology B: Biology","PUBLISHER","PENDING",null,0,[21,29,37,45],{"id":22,"createTime":23,"updateTime":24,"relativeEntities":25,"label":26,"description":28,"parentId":18,"standard":18,"scholarHubFieldId":18},"004f1a3b-9e46-4ef0-89e3-55090114af29","2023-05-29T10:24:07.417+00:00","2023-11-21T07:53:13.939+00:00",[],{"EN":27},"Radiological and Ultrasound Technology",{},{"id":30,"createTime":31,"updateTime":32,"relativeEntities":33,"label":34,"description":36,"parentId":18,"standard":18,"scholarHubFieldId":18},"a86091b2-a11b-4669-b693-653762a75923","2023-05-29T10:24:31.583+00:00","2023-11-21T08:11:28.198+00:00",[],{"EN":35},"Biophysics",{},{"id":38,"createTime":39,"updateTime":40,"relativeEntities":41,"label":42,"description":44,"parentId":18,"standard":18,"scholarHubFieldId":18},"e8fbc4e0-9522-4354-a98f-7f288efdcb2a","2023-05-29T10:24:07.493+00:00","2023-11-21T08:07:05.805+00:00",[],{"EN":43},"Radiology, Nuclear Medicine and Imaging",{},{"id":46,"createTime":47,"updateTime":48,"relativeEntities":49,"label":50,"description":52,"parentId":18,"standard":18,"scholarHubFieldId":18},"0d971a72-32b3-4406-aae7-7a4f741226dc","2023-05-29T10:25:41.509+00:00","2023-11-21T06:52:46.519+00:00",[],{"EN":51},"Radiation",{},[54,66],{"id":55,"createTime":56,"updateTime":57,"relativeEntities":58,"slug":59,"properties":60,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":64,"url":18,"parentIds":65,"statistic":18},"11dda69c-480e-41b6-a02f-059fa8a8b684","2023-05-29T12:13:01.142+00:00","2023-12-20T07:26:22.527+00:00",[],"ELSEVIER-SCIENCE-SA",{"title":61},{"EN":62},"ELSEVIER SCIENCE SA","AFFILIATION",6,[],{"id":67,"createTime":68,"updateTime":69,"relativeEntities":70,"slug":71,"properties":72,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":74,"url":18,"parentIds":75,"statistic":18},"c749757b-dddf-4e6f-9697-b9c441adc06c","2023-05-29T10:24:07.401+00:00","2025-11-21T10:06:14.206+00:00",[],"Elsevier",{"title":73},{"EN":71},11,[],[77,99],{"id":78,"indexDatabase":79,"url":91,"indexYears":92,"academicFieldIds":93,"indexDatabaseRanking":98},"5f659996-3c73-4526-b54a-9534f0ecf043",{"id":80,"createTime":81,"updateTime":82,"relativeEntities":83,"label":84,"description":86,"key":88,"publicationTags":89,"standard":18},"3c7051d4-eb7d-4c57-a56b-36fc74c5d1e9","2023-05-22T09:57:18.509+00:00","2025-11-21T10:07:52.274+00:00",[],{"EN":85,"VI":85},"Scopus - Elsevier",{"EN":85,"VI":87},"Cơ sở dữ liệu Scopus thuộc Elsevier","scopus",[90],"SCOPUS","https:\u002F\u002Fwww.scopus.com\u002Fsourceid\u002F17622","1987-2025",[94,95,96,97],"d052b227-e96b-45cf-9cc1-b77ec3409e8e","3473dbec-c53d-4463-88f5-866ed6297f33","de92cf1a-2f51-4173-92e5-47b52fde9929","a2541f09-5a54-41e7-820b-effbd7bac237","SCOPUS__Q2",{"id":100,"indexDatabase":101,"url":115,"indexYears":18,"academicFieldIds":116,"indexDatabaseRanking":18},"0a4b0433-9caa-408a-93f4-f034f6d4c3b5",{"id":102,"createTime":103,"updateTime":104,"relativeEntities":105,"label":106,"description":108,"key":111,"publicationTags":112,"standard":18},"a4921856-b128-4d9f-8f1f-e80813d3bbd4","2023-05-22T09:59:31.026+00:00","2025-11-21T10:07:52.153+00:00",[],{"EN":107,"VI":107},"ISI\u002FSCIE - Science Citation Index Expanded",{"VI":109,"EN":110},"Cơ sở dữ liệu SCIE","SCIE database","scie",[113,114],"SCIE","ISI","https:\u002F\u002Fmjl.clarivate.com\u002Fsearch-results?issn=1011-1344",[117,118],"10e9c71e-2256-419c-bdd2-a39e436e76e3","d875699a-416e-4523-bcb9-17b1b64de061",{"meta":120,"data":122},{"total":121},"2892",[123,270,421,539,623,831,1024,1164,1258,1376],{"id":124,"createTime":125,"updateTime":126,"relativeEntities":127,"slug":128,"properties":129,"entityType":136,"verifyStatus":137,"verifyTime":126,"verifyNote":138,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":139,"fullTextUrl":18,"authors":140,"publicationType":238,"publisherRelationship":239,"citationCount":18,"citationInfo":18,"publishDate":267,"publishYear":268,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":269},"05ef1c65-5aa6-4b28-81ab-4033779c780a","2024-01-09T17:21:56.560+00:00","2024-09-13T23:58:44.801+00:00",[],"Dynamic-photodamage-of-red-blood-cell-induced-by-CisDiMPyP-porphyrin",{"references":130,"title":132,"doi":134},{"VOID":131},"Sender, 2016, Revised estimates for the number of human and bacteria cells in the body, PLoS Biol., 14, 1, 10.1371\u002Fjournal.pbio.1002533\nKuhn, 2017, Red blood cell function and dysfunction: redox regulation, nitric oxide metabolism, Anemia, Antioxid. Redox Signal., 26, 718, 10.1089\u002Fars.2016.6954\nSinha, 2015, Single-cell evaluation of red blood cell bio-mechanical and nano-structural alterations upon chemically induced oxidative stress, Sci. Rep., 5, 9768, 10.1038\u002Fsrep09768\nHebbel, 1990, Oxidation-induced changes in microrheologic properties of the red blood cell membrane, Blood, 76, 1015, 10.1182\u002Fblood.V76.5.1015.1015\nTsubone, 2017, Enhanced efficiency of cell death by lysosome-specific photodamage, Sci. Rep., 7, 6734, 10.1038\u002Fs41598-017-06788-7\nSonoda, 1987, The role of singlet oxygen in the photohemolysis of red blood cells sensitized by phthalocyanine sulfonates, Photochem. Photobiol., 46, 625, 10.1111\u002Fj.1751-1097.1987.tb04823.x\nItri, 2014, Membrane changes under oxidative stress: the impact of oxidized lipids, Biophys. Rev., 6, 47, 10.1007\u002Fs12551-013-0128-9\nTsubone, 2019, Understanding membrane remodelling initiated by photosensitized lipid oxidation, Biophys. Chem., 254, 10.1016\u002Fj.bpc.2019.106263\nDavies, 2016, Protein oxidation and peroxidation, Biochem. J., 473, 805, 10.1042\u002FBJ20151227\nGracanin, 2009, Singlet-oxygen-mediated amino acid and protein oxidation: formation of tryptophan peroxides and decomposition products, Free Radic. Biol. Med., 47, 92, 10.1016\u002Fj.freeradbiomed.2009.04.015\nTsubone, 2019, Contrasting roles of oxidized lipids in modulating membrane microdomains, Biochim. Biophys. Acta Biomembr., 1861, 660, 10.1016\u002Fj.bbamem.2018.12.017\nWatabe, 2007, Oxidation decomposition of unsaturated fatty acids by singlet oxygen in phospholipid bilayer membranes, J Oleo Sci, 56, 73, 10.5650\u002Fjos.56.73\nKorytowski, 1999, Singlet oxygen adducts of cholesterol: photogeneration and reductive turnover in membrane systems, Photochem. Photobiol., 70, 484, 10.1111\u002Fj.1751-1097.1999.tb08242.x\nGirotti, 1998, Lipid hydroperoxide generation, turnover, and effector action in biological systems, J. Lipid Res., 39, 1529, 10.1016\u002FS0022-2275(20)32182-9\nBachowski, 1991, Phthalocyanine-sensitized lipid peroxidation in cell membranes: use of cholesterol and azide as probes of primary photochemistry, J. Photochem. Photobiol. B, 9, 307, 10.1016\u002F1011-1344(91)80168-H\nGirotti, 1987, Lipid peroxidation in erythrocyte membranes: cholesterol product analysis in photosensitized and xanthine oxidase-catalyzed reactions, Lipids, 22, 401, 10.1007\u002FBF02537268\nVerweij, 1981, Photodynamic protein cross-linking, Biochim. Biophys. Acta, 647, 87, 10.1016\u002F0005-2736(81)90297-2\nGirotti, 1980, Photosensitized cross-linking of erythrocyte membrane proteins. Evidence against participation of amino groups in the reaction, Biochim. Biophys. Acta, 602, 45, 10.1016\u002F0005-2736(80)90288-6\nVilsen, 1984, Reaction of phenylhydrazine with erythrocytes. Cross-linking of spectrin by disulfide exchange with oxidized hemoglobin, Biochem. Pharmacol., 33, 2739, 10.1016\u002F0006-2952(84)90690-7\nLamola, 1980, Cross-linking of membrane proteins and protoporphyrin-sensitized photohemolysis, Photochem. Photobiol., 31, 597, 10.1111\u002Fj.1751-1097.1980.tb03752.x\nBeaton, 1995, Alterations in erythrocyte band 3 organization induced by the photosensitizer, hematoporphyrin derivative, Photochem. Photobiol., 62, 353, 10.1111\u002Fj.1751-1097.1995.tb05281.x\nGirotti, 1979, Protoporphyrin-sensitized photodamage in isolated membranes of human erythrocytes, Biochemistry, 18, 4403, 10.1021\u002Fbi00587a021\nDubbelman, 1980, Protoporphyrin-induced photodynamic effects on transport processes across the membrane of human-erythrocytes, Biochim. Biophys. Acta, 595, 133, 10.1016\u002F0005-2736(80)90255-2\nDubbelman, 1977, Photodynamic effects of Protoporphyrin on red blood-cell deformability, Biochem Bioph Res Co, 77, 811, 10.1016\u002FS0006-291X(77)80050-8\nTozzi-Ciancarelli, 1989, Human erythrocyte damage at the initial stages of oxidative stress, Cell Biophys., 15, 225, 10.1007\u002FBF02989685\nSilva, 2010, Mechanisms of singlet-oxygen and superoxide-ion generation by porphyrins and bacteriochlorins and their implications in photodynamic therapy, Chemistry, 16, 9273, 10.1002\u002Fchem.201000111\nPineiro, 1998, Photoacoustic measurements of porphyrin triplet-state quantum yields and singlet-oxygen efficiencies, Chem. Eur. J., 4, 2299, 10.1002\u002F(SICI)1521-3765(19981102)4:11\u003C2299::AID-CHEM2299>3.0.CO;2-H\nTsubone, 2020, Porphyrin-loaded TyroSpheres for the intracellular delivery of drugs and Photoinduced oxidant species, Mol. Pharm., 17, 2911, 10.1021\u002Facs.molpharmaceut.0c00338\nCaetano, 2007, Photo-induced destruction of giant vesicles in methylene blue solutions, Langmuir, 23, 1307, 10.1021\u002Fla061510v\nLakowicz, 2006\nKinoshita, 2010, Long-lived, high-strength states of ICAM-1 bonds to beta(2) integrin, II: lifetimes of LFA-1 bonds under force in leukocyte signaling, Biophys. J., 98, 1467, 10.1016\u002Fj.bpj.2009.12.4316\nEvans, 2007, Using force to probe single-molecule receptor-cytoskeletal anchoring beneath the surface of a living cell, Methods Cell Biol., 83, 373, 10.1016\u002FS0091-679X(07)83016-0\nLopes, 2023, A mathematical model of fibrinogen-mediated erythrocyte-erythrocyte adhesion, Commun Biol, 6, 192, 10.1038\u002Fs42003-023-04560-4\nEvans, 1976, Elastic area compressibility Modulus of red-cell membrane, Biophys. J., 16, 585, 10.1016\u002FS0006-3495(76)85713-X\nWaugh, 1979, Thermoelasticity of red blood cell membrane, Biophys. J., 26, 115, 10.1016\u002FS0006-3495(79)85239-X\nMin, 2002, Chemistry and reaction of singlet oxygen in foods, Compr. Rev. Food Sci. Food Saf., 1, 58, 10.1111\u002Fj.1541-4337.2002.tb00007.x\nKuimova, 2009, Singlet oxygen in a cell: spatially dependent lifetimes and quenching rate constants, J. Am. Chem. Soc., 131, 332, 10.1021\u002Fja807484b\nBaier, 2005, Time-resolved investigations of singlet oxygen luminescence in water, in phosphatidylcholine, and in aqueous suspensions of phosphatidylcholine or HT29 cells, J. Phys. Chem. B, 109, 3041, 10.1021\u002Fjp0455531\nHackbarth, 2010, New insights to primary photodynamic effects – singlet oxygen kinetics in living cells, J. Photochem. Photobiol. B Biol., 98, 173, 10.1016\u002Fj.jphotobiol.2009.11.013\nLi, 2001, Quenching of singlet molecular oxygen (1O2) by azide anion in solvent mixtures, Photochem. Photobiol., 74, 760, 10.1562\u002F0031-8655(2001)074\u003C0760:QOSMOO>2.0.CO;2\nLiu, 2019, Singlet oxygen sensor green is not a suitable probe for (1)O(2) in the presence of ionizing radiation, Sci. Rep., 9, 8393, 10.1038\u002Fs41598-019-44880-2\nEvans, 1976, Membrane viscoelasticity, Biophys. J., 16, 1, 10.1016\u002FS0006-3495(76)85658-5\nRamdani, 2014, ATP, an extracellular signaling molecule in red blood cells: a messenger for malaria?, Biom. J., 37, 284\nMoller, 2023, Oxidants and antioxidants in the redox biochemistry of human red blood cells, ACS Omega, 8, 147, 10.1021\u002Facsomega.2c06768\nHochmuth, 1983, Mechanical measurement of red cell membrane thickness, Science, 220, 101, 10.1126\u002Fscience.6828875\nHimbert, 2017, The molecular structure of human red blood cell membranes from highly oriented, solid supported multi-lamellar membranes, Sci. Rep., 7, 39661, 10.1038\u002Fsrep39661\nRiske, 2009, Giant vesicles under oxidative stress induced by a membrane-anchored photosensitizer, Biophys. J., 97, 1362, 10.1016\u002Fj.bpj.2009.06.023\nWeber, 2014, Lipid oxidation induces structural changes in biomimetic membranes, Soft Matter, 10, 4241, 10.1039\u002Fc3sm52740a\nWays, 1964, Characterization and quantification of red cell lipids in normal man, J. Lipid Res., 5, 318, 10.1016\u002FS0022-2275(20)40200-7\nDodge, 1967, Composition of phospholipids and of phospholipid fatty acids and aldehydes in human red cells, J. Lipid Res., 8, 667, 10.1016\u002FS0022-2275(20)38890-8\nTimperio, 2013, Red blood cell lipidomics analysis through HPLC-ESI-qTOF: application to red blood cell storage, J. Integr. Omics A Methodolog., 3, 11\nScanavachi, 2021, Lipid hydroperoxide compromises the membrane structure organization and softens bending rigidity, Langmuir, 37, 9952, 10.1021\u002Facs.langmuir.1c00830\nLux, 2016, Anatomy of the red cell membrane skeleton: unanswered questions, Blood, 127, 187, 10.1182\u002Fblood-2014-12-512772\nSalomao, 2008, Protein 4.1R-dependent multiprotein complex: new insights into the structural organization of the red blood cell membrane, Proc. Natl. Acad. Sci. U. S. A., 105, 8026, 10.1073\u002Fpnas.0803225105\nPark, 2010, Metabolic remodeling of the human red blood cell membrane, Proc. Natl. Acad. Sci. U. S. A., 107, 1289, 10.1073\u002Fpnas.0910785107\nLi, 2016, Modeling of band-3 protein diffusion in the normal and defective red blood cell membrane, Soft Matter, 12, 3643, 10.1039\u002FC4SM02201G\nAoki, 2017, A comprehensive review of our current understanding of red blood cell (RBC) glycoproteins, Membranes (Basel), 7\nAnong, 2006, Rate of rupture and reattachment of the band 3-ankyrin bridge on the human erythrocyte membrane, J. Biol. Chem., 281, 22360, 10.1074\u002Fjbc.M513839200\nKrieger, 2011, Cysteine shotgun-mass spectrometry (CS-MS) reveals dynamic sequence of protein structure changes within mutant and stressed cells, Proc. Natl. Acad. Sci. U. S. A., 108, 8269, 10.1073\u002Fpnas.1018887108\nFerru, 2011, Regulation of membrane-cytoskeletal interactions by tyrosine phosphorylation of erythrocyte band 3, Blood, 117, 5998, 10.1182\u002Fblood-2010-11-317024\nPantaleo, 2011, Irreversible AE1 tyrosine phosphorylation leads to membrane vesiculation in G6PD deficient red cells, PLoS One, 6, 10.1371\u002Fjournal.pone.0015847\nChu, 2016, Reversible binding of hemoglobin to band 3 constitutes the molecular switch that mediates O2 regulation of erythrocyte properties, Blood, 128, 2708, 10.1182\u002Fblood-2016-01-692079\nShimo, 2015, Particle simulation of oxidation induced band 3 clustering in human erythrocytes, PLoS Comput. Biol., 11, 10.1371\u002Fjournal.pcbi.1004210\nNigg, 1980, Anchorage of a band 3 population at the erythrocyte cytoplasmic membrane surface: protein rotational diffusion measurements, Proc. Natl. Acad. Sci. U. S. A., 77, 4702, 10.1073\u002Fpnas.77.8.4702\nKodippili, 2009, Imaging of the diffusion of single band 3 molecules on normal and mutant erythrocytes, Blood, 113, 6237, 10.1182\u002Fblood-2009-02-205450\nDeziel, 1980, Photodynamic action of bilirubin on liposomes and erythrocyte membranes, J. Biol. Chem., 255, 8192, 10.1016\u002FS0021-9258(19)70629-2\nBancirova, 2011, Sodium azide as a specific quencher of singlet oxygen during chemiluminescent detection by luminol and Cypridina luciferin analogues, Luminescence, 26, 685, 10.1002\u002Fbio.1296\nSankarapandi, 1999, Evidence against the generation of free hydroxyl radicals from the interaction of copper,zinc-superoxide dismutase and hydrogen peroxide, J. Biol. Chem., 274, 34576, 10.1074\u002Fjbc.274.49.34576\nHalliwell, 1990, Role of free-radicals and catalytic metal-ions in human-disease - an overview, Methods Enzymol., 186, 1, 10.1016\u002F0076-6879(90)86093-B\nBaptista, 2017, Type I and type II photosensitized oxidation reactions: guidelines and mechanistic pathways, Photochem. Photobiol., 93, 912, 10.1111\u002Fphp.12716\nNiki, 2014, Role of vitamin E as a lipid-soluble peroxyl radical scavenger: in vitro and in vivo evidence, Free Radic. Biol. Med., 66, 3, 10.1016\u002Fj.freeradbiomed.2013.03.022\nAldini, 2018, N-acetylcysteine as an antioxidant and disulphide breaking agent: the reasons why, Free Radic. Res., 52, 751, 10.1080\u002F10715762.2018.1468564\nMorel, 1992, Antioxidant and free radical scavenging activities of the iron chelators pyoverdin and hydroxypyrid-4-ones in iron-loaded hepatocyte cultures: comparison of their mechanism of protection with that of desferrioxamine, Free Radic. Biol. Med., 13, 499, 10.1016\u002F0891-5849(92)90144-6\nFukuhara, 2023, DTPA-bound planar Catechin with potent antioxidant activity triggered by Fe(3+) coordination, Antioxidants (Basel), 12",{"EN":133},"Dynamic photodamage of red blood cell induced by CisDiMPyP porphyrin",{"VOID":135},"10.1016\u002Fj.jphotobiol.2023.112754","PUBLICATION","VERIFIED","Auto Verify","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1011134423001082",[141,171,193,206],{"id":142,"sortIndex":143,"researcher":18,"roles":144,"affiliations":146,"properties":168},"799c040c-54a7-4f78-8b3a-3602bfb8dcfb",2,[145],"AUTHOR",[147,157],{"id":18,"sortIndex":19,"affiliation":148,"properties":18},{"id":149,"createTime":150,"updateTime":151,"relativeEntities":152,"slug":153,"properties":154,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"1d47e1e7-7ea6-4f04-93e0-8c3f4a560a17","2024-04-19T16:04:07.738+00:00","2024-12-22T21:27:35.227+00:00",[],"Institute-of-Physics-University-of-S%C3%A3o-Paulo-S%C3%A3o-Paulo-Brazil",{"title":155},{"EN":156},"Institute of Physics, University of São Paulo, São Paulo, Brazil",{"id":158,"sortIndex":159,"affiliation":160,"properties":167},"57e1154e-4f4e-418f-9683-efaca3c579ed",1,{"id":161,"createTime":162,"updateTime":162,"relativeEntities":163,"slug":18,"properties":164,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"9dca1a05-7f7d-4b6f-ac79-887f64a1a0f2","2024-01-09T17:21:56.900+00:00",[],{"title":165},{"VI":166},"Institute of Chemistry, Federal University of Uberlandia, Minas Gerais, Brazil",{},{"title":169},{"VI":170},"Tayana M. Tsubone",{"id":172,"sortIndex":19,"researcher":18,"roles":173,"affiliations":174,"properties":190},"69cf5cbd-7522-42dd-a1ac-3edd1e73bb76",[145],[175,180],{"id":18,"sortIndex":19,"affiliation":176,"properties":18},{"id":149,"createTime":150,"updateTime":151,"relativeEntities":177,"slug":153,"properties":178,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":179},{"EN":156},{"id":181,"sortIndex":159,"affiliation":182,"properties":189},"7650dc92-22c5-45e4-9092-e76136002141",{"id":183,"createTime":184,"updateTime":184,"relativeEntities":185,"slug":18,"properties":186,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"8b8ee8c2-fbe9-447c-a909-6cd406e31102","2024-01-09T17:21:56.689+00:00",[],{"title":187},{"VI":188},"Department of Cell Biology, Harvard Medical School, Program in Cellular and Molecular Medicine (PCMM), Boston Children's Hospital, Boston, MA 02115, United States",{},{"title":191},{"VI":192},"Gustavo Scanavachi",{"id":194,"sortIndex":195,"researcher":18,"roles":196,"affiliations":197,"properties":203},"29e6f5fc-b6b0-4567-a545-95f978048997",3,[145],[198],{"id":18,"sortIndex":19,"affiliation":199,"properties":18},{"id":149,"createTime":150,"updateTime":151,"relativeEntities":200,"slug":153,"properties":201,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":202},{"EN":156},{"title":204},{"VI":205},"Rosangela Itri",{"id":207,"sortIndex":159,"researcher":18,"roles":208,"affiliations":209,"properties":235},"e4cc34fa-9c30-4d01-88a5-8f0a3cf30632",[145],[210,215,225],{"id":18,"sortIndex":19,"affiliation":211,"properties":18},{"id":149,"createTime":150,"updateTime":151,"relativeEntities":212,"slug":153,"properties":213,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":214},{"EN":156},{"id":216,"sortIndex":159,"affiliation":217,"properties":224},"ed95c9ce-b714-4fc4-8f36-4365145c5422",{"id":218,"createTime":219,"updateTime":219,"relativeEntities":220,"slug":18,"properties":221,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"cbaddb74-1d90-4a82-97a4-aeb11d3e69eb","2023-12-06T10:31:36.388+00:00",[],{"title":222},{"VI":223},"Department of Molecular Medicine, University of Southern Denmark, Odense, Denmark",{},{"id":226,"sortIndex":143,"affiliation":227,"properties":234},"7f616381-2fc8-4229-a14b-a7a331decbe9",{"id":228,"createTime":229,"updateTime":229,"relativeEntities":230,"slug":18,"properties":231,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"749401ac-c6ab-4526-9208-e27796e2a363","2024-01-09T17:21:56.825+00:00",[],{"title":232},{"VI":233},"Department of Biological Chemistry and Molecular Pharmacology (BCMP), Harvard Medical School, Program in Cellular and Molecular Medicine (PCMM), Boston Children's Hospital, Boston, MA 02115, United States",{},{"title":236},{"VI":237},"Koji Kinoshita","ARTICLE",{"url":139,"publisher":240,"properties":262},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":241,"slug":10,"properties":242,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":245,"manageAffiliations":246,"indexDatabases":247,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":243,"title":244},{"VOID":13},{"EN":15},[],[],[248,255],{"id":78,"indexDatabase":249,"url":91,"indexYears":92,"academicFieldIds":254,"indexDatabaseRanking":98},{"id":80,"createTime":81,"updateTime":82,"relativeEntities":250,"label":251,"description":252,"key":88,"publicationTags":253,"standard":18},[],{"EN":85,"VI":85},{"EN":85,"VI":87},[90],[94,95,96,97],{"id":100,"indexDatabase":256,"url":115,"indexYears":18,"academicFieldIds":261,"indexDatabaseRanking":18},{"id":102,"createTime":103,"updateTime":104,"relativeEntities":257,"label":258,"description":259,"key":111,"publicationTags":260,"standard":18},[],{"EN":107,"VI":107},{"VI":109,"EN":110},[113,114],[117,118],{"volume":263,"pages":265},{"VOID":264},"245",{"VOID":266},"112754","2023-08-01",2023,false,{"id":271,"createTime":272,"updateTime":272,"relativeEntities":273,"slug":18,"properties":274,"entityType":136,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":281,"fullTextUrl":18,"authors":282,"publicationType":238,"publisherRelationship":391,"citationCount":18,"citationInfo":18,"publishDate":419,"publishYear":420,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":269},"be1a4311-ecd6-4246-bdbd-94cd57857c3e","2023-12-13T23:58:17.857+00:00",[],{"references":275,"title":277,"doi":279},{"VOID":276},"Hu, 2002, The photosynthetic apparatus of purple bacteria, Q. Rev. Biophys., 35, 1, 10.1017\u002FS0033583501003754\nYoder, 2002, Structure and function in the isolated reaction center complex of Photosystem II: energy and charge transfer dynamics and mechanism, Photosynth. Res., 72, 147, 10.1023\u002FA:1016180616774\nBusch, 2011, The structure and function of eukaryotic photosystem I, Biochim. Biophys. Acta, 1807, 864, 10.1016\u002Fj.bbabio.2010.09.009\nShockley, 1961, Detailed balance limit of efficiency of p-n junction solar cells, J. Appl. Phys., 32, 510, 10.1063\u002F1.1736034\nWurfel, 2005\nCzechowski, 2014, Large plasmonic fluorescence enhancement of cyanobacterial photosystem I coupled to silver island films, Appl. Phys. Lett., 105, 043701, 10.1063\u002F1.4891856\nMaćkowski, 2016, Origin of bimodal fluorescence enhancement factors of Chlorobaculum tepidum reaction centers on silver island films, FEBS Lett., 590, 2558, 10.1002\u002F1873-3468.12292\nOleynikov, 2007, Fluorescent semiconductor nanocrystals for biology and medicine, Russ. Nanotechnol., 2, 160\nLeatherdale, 2002, On the absorption cross section of CdSe nanocrystal quantum dots, J. Phys. Chem. B, 106, 7619, 10.1021\u002Fjp025698c\nMicic, 1997, Size-dependent spectroscopy of InP quantum dots, J. Phys. Chem., B101, 4904, 10.1021\u002Fjp9704731\nGerion, 2001, Synthesis and properties of biocompatible water-soluble silica-coated CdSe\u002FZnS semiconductor quantum dots, J. Phys. Chem. B, 105, 8861, 10.1021\u002Fjp0105488\nPons, 2007, On the quenching of semiconductor quantum dot photoluminescence by proximal gold nanoparticles, Nano Lett., 7, 3157, 10.1021\u002Fnl071729+\nNabiev, 2010, Fluorescent quantum dots as artificial antennas for enhanced light harvesting and energy transfer to photosynthetic reaction centers, Angew. Chem., 49, 7217, 10.1002\u002Fanie.201003067\nMaksimov, 2010, Quantum dots and photosensitive protein phycoerythrin hybrid systems, Russ. Nanotechnol., 5, 107, 10.1134\u002FS199507801007013X\nSandermann, 1978, Regulation of membrane enzymes by lipids, Biochim. Biophys. Acta, 515, 209, 10.1016\u002F0304-4157(78)90015-1\nLatruffe, 1986, Lipid-protein interactions in biomembranes studied through the phospholipids specificity of D-beta-hydroxybutyrate dehydrogenase, Biochimie, 68, 481, 10.1016\u002FS0300-9084(86)80015-3\nNyholm, 2007, How protein transmembrane segments sense the lipid environment, Biochemistry, 46, 1457, 10.1021\u002Fbi061941c\nWood, 1965, The lipids and fatty acid metabolism of photosynthetic bacteria, Biochim. Biophys. Acta, 106, 261, 10.1016\u002F0005-2760(65)90034-2\nOnishi, 1982, Rhodopseudomonas sphaeroides membranes: alterations in phospholipid composition in aerobically and phototrophically grown cells, J. Bacteriol., 149, 831, 10.1128\u002Fjb.149.3.831-839.1982\nBenning, 2004, Membrane lipids in anoxygenic photosynthetic bacteria, vol. 6, 83, 10.1007\u002F0-306-48087-5_5\nCamara-Artigas, 2002, Interactions between lipids and bacterial reaction centers determined by protein crystallography, Proc. Natl. Acad. Sci. U. S. A., 99, 11055, 10.1073\u002Fpnas.162368399\nAgostiano, 2005, Trapping of a long-living charge separated state of photosynthetic reaction centers in proteoliposomes of negatively charged phospholipids, Photosynth. Res., 83, 53, 10.1007\u002Fs11120-004-3197-6\nMilano, 2007, Enthalpy\u002Fentropy driven activation of the first interquinone electron transfer in bacterial photosynthetic reaction centers embedded in vesicles of physiologically important phospholipids, Bioelectrochemistry, 70, 18, 10.1016\u002Fj.bioelechem.2006.03.024\nBerg, 1979, Conformational mobility and functional activity of photosynthetic reaction centers of Rhodopseudomonas sphaeroides, Mol. Biol. (Moscow), 13, 469\nKotelnikov, 1983, Molecular dynamics and electron transfer in photosynthetic reaction centers, Mol. Biol. (Moscow), 17, 846\nKononenko, 1986, Electron transfer and intramolecular dynamics of photosynthetic reaction centers, Chem. Phys. (Moscow), 5, 795\nCrowe, 1992, Anhydrobiosis, Annu. Rev. Physiol., 54, 579, 10.1146\u002Fannurev.ph.54.030192.003051\nZakharova, 2000, Methods for isolating reaction center preparations from purple photosynthetic bacteria, Biochem. Mosc., 65, 181\nBellare, 1988, Controlled environment vitrification system: an improved sample preparation technique, J. Electron Microsc. Tech., 10, 87, 10.1002\u002Fjemt.1060100111\nFrederik, 1991, Perspective and limitations of cryo-electron microscopy. From model systems to biological specimens, J. Microsc., 161, 253, 10.1111\u002Fj.1365-2818.1991.tb03088.x\nPalazzo, 2002, Electron transfer kinetics in photosynthetic reaction centers embedded in trehalose glasses: trapping of conformational substrates at room temperature, Biophys. J., 82, 558, 10.1016\u002FS0006-3495(02)75421-0\nWinston, 1960, Saturated solutions for the control of humidity in biological research, Ecology, 41, 232, 10.2307\u002F1931961\nMilano, 2009, Characterisation of RC-proteoliposomes at different RC\u002Flipid ratios, Photosynth. Res., 100, 107, 10.1007\u002Fs11120-009-9423-5\nIba, 1984, Transmembrane orientation of reaction centers in proteoliposomes from Rhodopseudomonas sphaeroides, J. Biochem., 96, 1823, 10.1093\u002Foxfordjournals.jbchem.a135016\nAl-Jamal, 2008, Functionalized-quantum-dot–liposome hybrids as multimodal nanoparticles for cancer, Small, 4, 1406, 10.1002\u002Fsmll.200701043\nGeneralov, 2011, Entrapment in phospholipid vesicles quenches photoactivity of quantum dots, Int. J. Nanomedicine, 6, 1875\nOkamura, 1992, Proton transfer in reaction centers from photosynthetic bacteria, Annu. Rev. Biochem., 61, 861, 10.1146\u002Fannurev.bi.61.070192.004241\nLancaster, 1996, Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopseudomonas viridis, Biophys. J., 70, 2469, 10.1016\u002FS0006-3495(96)79820-X\nMiksovska, 1996, Distant electrostatic interactions modulate the free energy level of QA− in the photosynthetic reaction center, Biochemistry, 35, 15411, 10.1021\u002Fbi961299u\nLakowicz, 1999\nKrasilnikov, 2000, Reaction of charge recombination between photooxidized bacteriochlorophyll and reduced primary quinone in Rb. sphaeroides reaction centers is accelerated under temperatures above 300K, Dokl. Biochem. Biophys., 375, 828\nKrasilnikov, 2007, The influence of hydrogen bonds on electron transfer rate in photosynthetic RCs, Biochim. Biophys. Acta, 1767, 541, 10.1016\u002Fj.bbabio.2007.02.024\nKrasilnikov, 2009, Relaxation mechanism of molecular systems containing hydrogen bonds and free energy temperature dependence of reaction of charges recombination within Rhodobacter sphaeroides RC, Photochem. Photobiol. Sci., 8, 181, 10.1039\u002Fb811014j\nKnox, 1979, Functional activity in photosynthetic reaction centers from Rhodopseudomonas sphaeroides at fixed hydration levels of the preparations, Bioorg. Chem. (USSR), 5, 879\nClayton, 1978, Effects of dehydration on reaction centers from Rps. sphaeroides, Biochim. Biophys. Acta, 504, 255, 10.1016\u002F0005-2728(78)90174-3\nMcMahon, 1998, Electron transfer and protein dynamics in the photosynthetic reaction center, Biophys. J., 74, 2567, 10.1016\u002FS0006-3495(98)77964-0\nOkamura, 2000, Proton and electron transfer in bacterial reaction centers, Biochim. Biophys. Acta, 1458, 148, 10.1016\u002FS0005-2728(00)00065-7\nAmbrosone, 2002, Effect of heterogeneity in the distribution of ligands and proteins among disconnected particles: the binding of ubiquinone to the bacterial reaction center, Phys. Chem. Chem. Phys., 4, 3071, 10.1039\u002Fb109809h\nCarpenter, 1989, An infrared spectroscopic study of the interaction of carbohydrates with dried proteins, Biochemistry, 28, 3916, 10.1021\u002Fbi00435a044\nBelton, 1994, IR and Raman spectroscopic studies of the interaction of trehalose with hen egg white lisozyme, Biopolymers, 34, 957, 10.1002\u002Fbip.360340713\nSubrata, 2015, Molecular insights into the role of aqueous trehalose solution on temperature-induced protein denaturation, J. Phys. Chem. B, 119, 1598, 10.1021\u002Fjp510423n",{"EN":278},"Purple-bacterial photosynthetic reaction centers and quantum‐dot hybrid‐assemblies in lecithin liposomes and thin films",{"VOID":280},"10.1016\u002Fj.jphotobiol.2016.09.009","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1011134416304705",[283,299,314,329,341,353,365,378],{"id":284,"sortIndex":285,"researcher":18,"roles":286,"affiliations":287,"properties":296},"07ea1498-375c-44e6-a0c7-2df3280870be",5,[145],[288],{"id":18,"sortIndex":19,"affiliation":289,"properties":18},{"id":290,"createTime":291,"updateTime":291,"relativeEntities":292,"slug":18,"properties":293,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"d1ecdf14-34ab-4112-b370-62450cbc4b54","2023-12-13T23:58:17.972+00:00",[],{"title":294},{"VI":295},"Institut für Optik und Atomare Physik, Technische Universität Berlin, Strasse des 17 Juni 135, ER 1-1, D-10623 Berlin, Germany",{"title":297},{"VI":298},"Maria Krikunova",{"id":300,"sortIndex":195,"researcher":18,"roles":301,"affiliations":302,"properties":311},"e1fc58f9-4a3d-4b3f-8edf-7edc280ee3ae",[145],[303],{"id":18,"sortIndex":19,"affiliation":304,"properties":18},{"id":305,"createTime":306,"updateTime":306,"relativeEntities":307,"slug":18,"properties":308,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"2854e878-5b02-466a-ad19-36b71ca080e0","2023-12-13T23:57:59.975+00:00",[],{"title":309},{"VI":310},"Biology Faculty, Lomonosov Moscow State University, 119991 Moscow, Russia",{"title":312},{"VI":313},"Nadezda P. Grishanova",{"id":315,"sortIndex":64,"researcher":18,"roles":316,"affiliations":317,"properties":326},"d66181f5-a298-4bd5-8150-d65e33338383",[145],[318],{"id":18,"sortIndex":19,"affiliation":319,"properties":18},{"id":320,"createTime":321,"updateTime":321,"relativeEntities":322,"slug":18,"properties":323,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"3c8a9eeb-5ab7-4c41-98d3-c7d20b6ce50c","2023-12-13T23:58:17.986+00:00",[],{"title":324},{"VI":325},"Charles University, Department of Chemical Physics and Optics, Ke Karlovu 3, 121 16 Prague, Czech Republic",{"title":327},{"VI":328},"Heiko Lokstein",{"id":330,"sortIndex":159,"researcher":18,"roles":331,"affiliations":332,"properties":338},"2b342757-bc93-4a36-9635-0468350daed0",[145],[333],{"id":18,"sortIndex":19,"affiliation":334,"properties":18},{"id":305,"createTime":306,"updateTime":306,"relativeEntities":335,"slug":18,"properties":336,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":337},{"VI":310},{"title":339},{"VI":340},"Petr P. Knox",{"id":342,"sortIndex":19,"researcher":18,"roles":343,"affiliations":344,"properties":350},"5260b6ce-aa3b-4d5e-ba28-0dfdcfd8c65b",[145],[345],{"id":18,"sortIndex":19,"affiliation":346,"properties":18},{"id":305,"createTime":306,"updateTime":306,"relativeEntities":347,"slug":18,"properties":348,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":349},{"VI":310},{"title":351},{"VI":352},"Eugeny P. Lukashev",{"id":354,"sortIndex":143,"researcher":18,"roles":355,"affiliations":356,"properties":362},"d0caa3f8-abe1-47f8-998d-6c97ff1ff6e6",[145],[357],{"id":18,"sortIndex":19,"affiliation":358,"properties":18},{"id":305,"createTime":306,"updateTime":306,"relativeEntities":359,"slug":18,"properties":360,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":361},{"VI":310},{"title":363},{"VI":364},"Vladimir V. Gorokhov",{"id":366,"sortIndex":367,"researcher":18,"roles":368,"affiliations":369,"properties":375},"ba075853-e9bf-492b-bc17-3367c70f3db7",4,[145],[370],{"id":18,"sortIndex":19,"affiliation":371,"properties":18},{"id":305,"createTime":306,"updateTime":306,"relativeEntities":372,"slug":18,"properties":373,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":374},{"VI":310},{"title":376},{"VI":377},"Nuranija Kh. Seifullina",{"id":379,"sortIndex":380,"researcher":18,"roles":381,"affiliations":382,"properties":388},"b33604bc-0ccf-4c93-b9bd-cb0ef1166240",7,[145],[383],{"id":18,"sortIndex":19,"affiliation":384,"properties":18},{"id":305,"createTime":306,"updateTime":306,"relativeEntities":385,"slug":18,"properties":386,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":387},{"VI":310},{"title":389},{"VI":390},"Vladimir Z. Paschenko",{"url":281,"publisher":392,"properties":414},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":393,"slug":10,"properties":394,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":397,"manageAffiliations":398,"indexDatabases":399,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":395,"title":396},{"VOID":13},{"EN":15},[],[],[400,407],{"id":78,"indexDatabase":401,"url":91,"indexYears":92,"academicFieldIds":406,"indexDatabaseRanking":98},{"id":80,"createTime":81,"updateTime":82,"relativeEntities":402,"label":403,"description":404,"key":88,"publicationTags":405,"standard":18},[],{"EN":85,"VI":85},{"EN":85,"VI":87},[90],[94,95,96,97],{"id":100,"indexDatabase":408,"url":115,"indexYears":18,"academicFieldIds":413,"indexDatabaseRanking":18},{"id":102,"createTime":103,"updateTime":104,"relativeEntities":409,"label":410,"description":411,"key":111,"publicationTags":412,"standard":18},[],{"EN":107,"VI":107},{"VI":109,"EN":110},[113,114],[117,118],{"volume":415,"pages":417},{"VOID":416},"164",{"VOID":418},"73-82","2016-11-01",2016,{"id":422,"createTime":423,"updateTime":424,"relativeEntities":425,"slug":426,"properties":427,"entityType":136,"verifyStatus":137,"verifyTime":424,"verifyNote":138,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":434,"fullTextUrl":18,"authors":435,"publicationType":238,"publisherRelationship":510,"citationCount":18,"citationInfo":18,"publishDate":538,"publishYear":420,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":269},"02c27bac-bfe0-4822-b545-8c5c54fd7217","2024-01-05T01:21:23.705+00:00","2025-02-26T23:55:33.950+00:00",[],"Calculation-of-the-sun-protection-factor-of-sunscreens-with-different-vehicles-using-measured-film-thickness-distribution-Comparison-with-the-SPF-in-vitro",{"references":428,"title":430,"doi":432},{"VOID":429},"Diffey, 2009, Reported sun exposure, attitudes to sun protection and perceptions of skin cancer risk: a survey of visitors to Cancer Research UK's SunSmart campaign website, Br. J. Dermatol., 160, 1292, 10.1111\u002Fj.1365-2133.2009.09149.x\nMoyal, 2008, Broad-spectrum sunscreens provide better protection from solar ultraviolet-simulated radiation and natural sunlight-induced immunosuppression in human beings, J. Am. Acad. Dermatol., 58, 149, 10.1016\u002Fj.jaad.2007.04.035\nSeité, 2010, Photodamage to human skin by suberythemal exposure to solar ultraviolet radiation can be attenuated by sunscreens: a review, Br. J. Dermatol., 163, 903, 10.1111\u002Fj.1365-2133.2010.10018.x\nGreen, 2011, Reduced melanoma after regular sunscreen use: randomized trial follow-up, J. Clin. Oncol., 29, 257, 10.1200\u002FJCO.2010.28.7078\nGreen, 1999, Daily sunscreen application and betacarotene supplementation in prevention of basal-cell and squamous-cell carcinomas of the skin: a randomised controlled trial, Lancet, 354, 723, 10.1016\u002FS0140-6736(98)12168-2\nISO 24444\nRohr, 2010, In vitro sun protection factor: still a challenge with no final answer, Skin Pharmacol. Physiol., 23, 201, 10.1159\u002F000292777\nMarguerie, 2012, A new chemical approach to optimize the in vitro SPF method on the HD6 PMMA plate, J. Cosmet. Sci., 63, 243\nPissavini, 2009, Characterizing roughness: a new substrate to measure SPF, Cosmet. Toiletries, 124, 56\nMiura, 2012, Influence of application amount on sunscreen photodegradation in in vitro sun protection factor evaluation: proposal of a skin-mimicking substrate, Photochem. Photobiol., 88, 475, 10.1111\u002Fj.1751-1097.2011.01042.x\nMiksa, 2013, Adjusting substrate\u002Fproduct interfacial properties to improve in vivo\u002Fin vitro SPF correlation, Cosmet. Toiletries, 128, 170\nRhodes, 1997, Fluorescence spectroscopy: a rapid, noninvasive method for measurement of skin surface thickness of topical agents, Br. J. Dermatol., 136, 12, 10.1111\u002Fj.1365-2133.1997.tb08739.x\nFageon, 2009, Importance of sunscreen products spreading protocol and substrate roughness for in vitro sun protection factor assessment, Int. J. Cosmet. Sci., 31, 405, 10.1111\u002Fj.1468-2494.2009.00524.x\nFerrero, 2003, Efficiency of a continuous height distribution model of sunscreen film geometry to predict a realistic sun protection factor, J. Cosmet. Sci., 54, 463\nHerzog, 2009, Models for simulation of sun protection factors and indices characterizing the UVA protection of sunscreens: principles and applications\nO'Neill, 1984, Effect of film irregularities on sunscreen efficacy, J. Pharm. Sci., 73, 888, 10.1002\u002Fjps.2600730707\nLademann, 2004, Influence of nonhomogeneous distribution of topically applied UV filters on sun protection factors, J. Biomed. Opt., 9, 1358, 10.1117\u002F1.1805557\nPissavini, 2013, The likelihood of sunburn in sunscreen users is disproportionate to the SPF, Photodermatol. Photoimmunol. Photomed., 29, 111, 10.1111\u002Fphpp.12033\nVergou, 2013, Methods for the evaluation of the protective efficacy of sunscreen products, Skin Pharmacol. Physiol., 26, 30, 10.1159\u002F000343576\nFerrero, 2010, How a calculated model of sunscreen film geometry can explain in vitro and in vivo SPF variation, Photochem. Photobiol. Sci., 9, 540, 10.1039\u002Fb9pp00183b\nSohn, 2015, Porcine ear skin as a biological substrate for in vitro testing of sunscreen performance, Skin Pharmacol. Physiol., 28, 31, 10.1159\u002F000358273\nSohn, 2014, Film thickness frequency distribution of different vehicles determines sunscreen efficacy, J. Biomed. Opt., 19, 115005, 10.1117\u002F1.JBO.19.11.115005\nISO 25178-602\nHerzog, 2004, Prediction of sun protection factors and UVA parameters of sunscreens by using a calibrated step film model, J. Pharm. Sci., 93, 1780, 10.1002\u002Fjps.20089\nHerzog, 2010, Models for the calculation of sun protection factors and parameters characterizing the UVA protection ability of cosmetic sunscreens, 275\nSayre, 1979, A comparison of in vivo and in vitro testing of sunscreening formulas, Photochem. Photobiol., 29, 559, 10.1111\u002Fj.1751-1097.1979.tb07090.x\nISO 24443\nHerzog, 2002, Prediction of sun protection factors by calculation of transmissions with a calibrated step film model, J. Cosmet. Sci., 53, 11\nBASF, BASF sunscreen simulator, https:\u002F\u002Fwww.sunscreensimulator.basf.com\u002F(accessed 9 July 2015).\nFerrero, 2006, Importance of substrate roughness for in vitro sun protection assessment, IFSCC Mag., 9, 97\nHerzog, 2015, Simulation of sunscreen performance, Pure Appl. Chem., 87, 937, 10.1515\u002Fpac-2015-0401\nSchittkowski, 2003, Numerical data fitting in dynamical systems — a practical introduction with applications and software",{"EN":431},"Calculation of the sun protection factor of sunscreens with different vehicles using measured film thickness distribution — Comparison with the SPF in vitro",{"VOID":433},"10.1016\u002Fj.jphotobiol.2016.02.038","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1011134415300622",[436,461,476,491],{"id":437,"sortIndex":19,"researcher":18,"roles":438,"affiliations":439,"properties":458},"07facac1-af73-4f06-ac33-3e6f88970c38",[145],[440,448],{"id":18,"sortIndex":19,"affiliation":441,"properties":18},{"id":442,"createTime":443,"updateTime":443,"relativeEntities":444,"slug":18,"properties":445,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"a44c358e-0522-4663-9bed-7006f6c04507","2024-01-05T01:21:23.755+00:00",[],{"title":446},{"VI":447},"University of Applied Sciences and Arts Northwestern Switzerland, School of Life Sciences, Muttenz\u002FBasel, Switzerland",{"id":449,"sortIndex":159,"affiliation":450,"properties":457},"7b11794f-571a-44a3-9bf2-37d62fcefd13",{"id":451,"createTime":452,"updateTime":452,"relativeEntities":453,"slug":18,"properties":454,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"83a8b0cc-fa3c-4980-869e-42e524eecb70","2024-01-05T01:21:23.759+00:00",[],{"title":455},{"VI":456},"University of Basel, Department of Pharmaceutical Sciences, Basel, Switzerland",{},{"title":459},{"VI":460},"Myriam Sohn",{"id":462,"sortIndex":159,"researcher":18,"roles":463,"affiliations":464,"properties":473},"2be91fe2-c8a7-488d-9f01-1e4644346710",[145],[465],{"id":18,"sortIndex":19,"affiliation":466,"properties":18},{"id":467,"createTime":468,"updateTime":468,"relativeEntities":469,"slug":18,"properties":470,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"b98bb2b2-793c-43e8-a6a2-d934d9c49d0d","2024-01-05T01:21:23.736+00:00",[],{"title":471},{"VI":472},"BASF Grenzach GmbH, Grenzach-Whylen, Germany",{"title":474},{"VI":475},"Bernd Herzog",{"id":477,"sortIndex":143,"researcher":18,"roles":478,"affiliations":479,"properties":488},"55cad775-9b99-44b6-a9ee-a2bed4a6dbcb",[145],[480],{"id":18,"sortIndex":19,"affiliation":481,"properties":18},{"id":482,"createTime":483,"updateTime":483,"relativeEntities":484,"slug":18,"properties":485,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"562a3c7d-c6c5-4aeb-9435-bb55faf4eac0","2024-01-05T01:21:23.746+00:00",[],{"title":486},{"VI":487},"BASF Personal Care Nutrition GmbH, Monheim, Germany",{"title":489},{"VI":490},"Uli Osterwalder",{"id":492,"sortIndex":195,"researcher":18,"roles":493,"affiliations":494,"properties":507},"57972eab-e923-447e-8466-54bb8025ef57",[145],[495,500],{"id":18,"sortIndex":19,"affiliation":496,"properties":18},{"id":442,"createTime":443,"updateTime":443,"relativeEntities":497,"slug":18,"properties":498,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":499},{"VI":447},{"id":501,"sortIndex":159,"affiliation":502,"properties":506},"6bbd7dfc-e45f-4ba0-9a5c-42824ae7a4cf",{"id":451,"createTime":452,"updateTime":452,"relativeEntities":503,"slug":18,"properties":504,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":505},{"VI":456},{},{"title":508},{"VI":509},"Georgios Imanidis",{"url":434,"publisher":511,"properties":533},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":512,"slug":10,"properties":513,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":516,"manageAffiliations":517,"indexDatabases":518,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":514,"title":515},{"VOID":13},{"EN":15},[],[],[519,526],{"id":78,"indexDatabase":520,"url":91,"indexYears":92,"academicFieldIds":525,"indexDatabaseRanking":98},{"id":80,"createTime":81,"updateTime":82,"relativeEntities":521,"label":522,"description":523,"key":88,"publicationTags":524,"standard":18},[],{"EN":85,"VI":85},{"EN":85,"VI":87},[90],[94,95,96,97],{"id":100,"indexDatabase":527,"url":115,"indexYears":18,"academicFieldIds":532,"indexDatabaseRanking":18},{"id":102,"createTime":103,"updateTime":104,"relativeEntities":528,"label":529,"description":530,"key":111,"publicationTags":531,"standard":18},[],{"EN":107,"VI":107},{"VI":109,"EN":110},[113,114],[117,118],{"volume":534,"pages":536},{"VOID":535},"159",{"VOID":537},"74-81","2016-06-01",{"id":540,"createTime":541,"updateTime":542,"relativeEntities":543,"slug":544,"properties":545,"entityType":136,"verifyStatus":137,"verifyTime":542,"verifyNote":138,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":552,"fullTextUrl":18,"authors":553,"publicationType":238,"publisherRelationship":593,"citationCount":18,"citationInfo":18,"publishDate":621,"publishYear":622,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":269},"6f983746-cb15-4a41-9026-b5bf851cb63b","2024-01-02T05:42:00.454+00:00","2024-12-26T23:55:06.251+00:00",[],"Vesicular-effect-on-the-reactivity-of-anthracene-derivatives-towards-singlet-molecular-oxygen",{"references":546,"title":548,"doi":550},{"VOID":547},"Fendler, 1982, 113\nKrinsky, 1979, Biological roles of singlet oxygen, 597\nFoote, 1976, Photosensitized oxidation and singlet oxygen: consequence in biological systems, II, 85\nDurán, 1982, Singlet oxygen in biological processes, 345\nDearden, 1986, Kinetics of O2(1Δg) photo-oxidation reactions in egg yolk lecithin vesicles, J. Chem. Soc., Faraday Trans. I, 82, 1627, 10.1039\u002Ff19868201627\nDearden, 1985, Fatty acid analysis as a function of photo-oxidation in egg yolk lecithin vesicles, Photochem. Photobiol., 41, 213, 10.1111\u002Fj.1751-1097.1985.tb03474.x\nRodgers, 1982, A laser flash kinetic spectrophotometric examination of the dynamics of singlet oxygen in unilammellar vesicles, Photochem. Photobiol., 35, 473, 10.1111\u002Fj.1751-1097.1982.tb02596.x\nCuccovia, 1979, Effect of dialkyldimethylammonium vesicles on the thiolysis of p-nitrophenyl acetate, Tetrahedron Lett., 33, 3065, 10.1016\u002FS0040-4039(01)95320-1\nMiola, 1983, Models for specific counter ion effects on the incorporation of charged amphiphilic substrates into like-charged ionic micelles, J. Phys. Chem., 87, 4417, 10.1021\u002Fj100245a020\nRibeiro, 1983, Preparation and characterization of large dioctadecyldimethylammonium chloride liposomes and comparison with small sonicated vesicles, Biochim. Biophys. Acta, 733, 172, 10.1016\u002F0005-2736(83)90103-7\nMoss, 1984, Trans membrane transport of 1-anilino-8-naphthalenesulfonate in simple cationic surfactant vesicles, Tetrahedron Lett., 25, 4063, 10.1016\u002FS0040-4039(01)90182-0\nKano, 1979, Turbidity, viscosity, fluorescence polarization of 2-methylanthracene and positron annihilation in sonicated dioctadecyldimethylammonium chloride, J. Am. Chem. Soc., 101, 4030, 10.1021\u002Fja00509a002\nCorey, A study of the photo-oxidation of organic compounds by externally generated singlet oxygen molecules, J. Am. Chem. Soc., 86, 3881, 10.1021\u002Fja01072a062\nLee, 1983, Singlet oxygen in micellar systems. Distribution equilibria between hydrophobic and hydrophilic compartments, J. Phys. Chem., 87, 4894, 10.1021\u002Fj150642a027\nAbuin, 1984, Solubilization of naphthalene derivatives in micellar assemblies, J. Colloid Interface Sci., 98, 152, 10.1016\u002F0021-9797(84)90489-2\nRicchelli, 1986, Distribution of porphyrins in the various compartments of unilamellar liposomes of dipalmitoylphosphatidylcholine as probed by fluorescence spectroscopy, Photochem. Photobiol., 44, 151, 10.1111\u002Fj.1751-1097.1986.tb03579.x\nStelzer, 1985, Interactions of pyrethroids with phosphatidylcholine bilayers: comparisons in liposomal systems exhibiting large or small radii of curvature, Chem. Biol. Interact., 54, 105, 10.1016\u002FS0009-2797(85)80156-3\nKaneshina, 1983, Thermodynamic of pressure—anesthetic antagonism on the phase transition of lipid membranes: comparisons in liposomal systems exhibiting large or small radii of curvature, J. Colloid Interface Sci., 93, 215, 10.1016\u002F0021-9797(83)90399-5\nAbuin, 1988, Fluorescence probe study of the effect of size on the properties of dioctadecyldimethylammonium chloride vesicles, J. Colloid Interface Sci., 122, 201, 10.1016\u002F0021-9797(88)90303-7\nAravena, 1985, Reactivity of ozone towards micelle incorporated unsaturated compounds, J. Free Radicals Biol. Med., 1, 327, 10.1016\u002F0748-5514(85)90139-4\nMatheson, 1978, Solubility of gases in micellar solutions, J. Colloid Interface Sci., 66, 464, 10.1016\u002F0021-9797(78)90066-8\nRubio, 1985, O2(3Σ) and O2(1Δg) processes in microheterogeneous systems, An. Asoc. Quím. Argent., 73, 301\nCazing, 1986, Is water the best or the worst solvent for [2 + 4] cycloadditions of singlet oxygen to aromatic compounds?, J. Chem. Soc., Chem. Commun., 952, 10.1039\u002Fc39860000952",{"EN":549},"Vesicular effect on the reactivity of anthracene derivatives towards singlet molecular oxygen",{"VOID":551},"10.1016\u002F1011-1344(89)80025-9","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002F1011134489800259",[554,569,581],{"id":555,"sortIndex":19,"researcher":18,"roles":556,"affiliations":557,"properties":566},"720a7b34-6c2e-4449-8ffa-4ad4e6ed90ab",[145],[558],{"id":18,"sortIndex":19,"affiliation":559,"properties":18},{"id":560,"createTime":561,"updateTime":561,"relativeEntities":562,"slug":18,"properties":563,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"a8cebf5b-45bc-4957-b462-40b82f60042f","2024-01-17T00:23:32.846+00:00",[],{"title":564},{"VI":565},"Departamento de Química, Facultad de Ciencias, Universidad de Santiago de Chile, Casilla 5659, Correo 2, Santiago, Chile",{"title":567},{"VI":568},"M.V. Encinas",{"id":570,"sortIndex":143,"researcher":18,"roles":571,"affiliations":572,"properties":578},"360bdb63-fe56-4a2f-b7d9-a95b1b089232",[145],[573],{"id":18,"sortIndex":19,"affiliation":574,"properties":18},{"id":560,"createTime":561,"updateTime":561,"relativeEntities":575,"slug":18,"properties":576,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":577},{"VI":565},{"title":579},{"VI":580},"E.A. Lissi",{"id":582,"sortIndex":159,"researcher":18,"roles":583,"affiliations":584,"properties":590},"acfe71c8-ca86-45f5-89e4-f842325efa56",[145],[585],{"id":18,"sortIndex":19,"affiliation":586,"properties":18},{"id":560,"createTime":561,"updateTime":561,"relativeEntities":587,"slug":18,"properties":588,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":589},{"VI":565},{"title":591},{"VI":592},"E. Lemp",{"url":552,"publisher":594,"properties":616},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":595,"slug":10,"properties":596,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":599,"manageAffiliations":600,"indexDatabases":601,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":597,"title":598},{"VOID":13},{"EN":15},[],[],[602,609],{"id":78,"indexDatabase":603,"url":91,"indexYears":92,"academicFieldIds":608,"indexDatabaseRanking":98},{"id":80,"createTime":81,"updateTime":82,"relativeEntities":604,"label":605,"description":606,"key":88,"publicationTags":607,"standard":18},[],{"EN":85,"VI":85},{"EN":85,"VI":87},[90],[94,95,96,97],{"id":100,"indexDatabase":610,"url":115,"indexYears":18,"academicFieldIds":615,"indexDatabaseRanking":18},{"id":102,"createTime":103,"updateTime":104,"relativeEntities":611,"label":612,"description":613,"key":111,"publicationTags":614,"standard":18},[],{"EN":107,"VI":107},{"VI":109,"EN":110},[113,114],[117,118],{"volume":617,"pages":619},{"VOID":618},"3",{"VOID":620},"113-122","1989-02-01",1989,{"id":624,"createTime":625,"updateTime":626,"relativeEntities":627,"slug":628,"properties":629,"entityType":136,"verifyStatus":137,"verifyTime":626,"verifyNote":138,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":636,"fullTextUrl":18,"authors":637,"publicationType":238,"publisherRelationship":804,"citationCount":18,"citationInfo":18,"publishDate":267,"publishYear":268,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":269},"3342f19f-afa6-428a-9597-7653a060cf29","2023-12-07T07:20:13.617+00:00","2025-01-04T23:54:59.873+00:00",[],"Inhibition-of-SIRT1-promotes-ultraviolet-B-induced-cataract-via-downregulation-of-the-KEAP1-NFE2L2-signaling-pathway",{"references":630,"title":632,"doi":634},{"VOID":631},"Tenkate, 2019, WHO\u002FILO work-related burden of disease and injury: Protocol for systematic reviews of occupational exposure to solar ultraviolet radiation and of the effect of occupational exposure to solar ultraviolet radiation on cataract, Environ. Int., 125, 542, 10.1016\u002Fj.envint.2018.10.001\nAng, 2021, Cataract and systemic disease: a review, Clin. Exp. Ophthalmol., 49, 118, 10.1111\u002Fceo.13892\nTanito, 2021, Reported evidence of vitamin E protection against cataract and glaucoma, Free Radic. Biol. Med., 177, 100, 10.1016\u002Fj.freeradbiomed.2021.10.027\nSlominski, 2018, How UV light touches the brain and endocrine system through skin, and why, Endocrinology, 159, 1992, 10.1210\u002Fen.2017-03230\nGuo, 2022, The protective mechanism of Grx2 in ultraviolet-B (UVB)-induced cataract formation, Biochem. Biophys. Res. Commun., 613, 107, 10.1016\u002Fj.bbrc.2022.04.056\nHaag, 2021, Cataract development by exposure to ultraviolet and blue visible light in porcine lenses, Medicina (Kaunas, Lithuania), 57\nSi, 2019, A novel MAF missense mutation leads to congenital nuclear cataract by impacting the transactivation of crystallin and noncrystallin genes, Gene, 692, 113, 10.1016\u002Fj.gene.2019.01.011\nKamari, 2019, Phototoxicity of environmental radiations in human lens: revisiting the pathogenesis of UV-induced cataract, Graefe's archive for clinical and experimental ophthalmology =, Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie, 257, 2065, 10.1007\u002Fs00417-019-04390-3\nSchuch, 2017, Sunlight damage to cellular DNA: Focus on oxidatively generated lesions, Free Radic. Biol. Med., 107, 110, 10.1016\u002Fj.freeradbiomed.2017.01.029\nHua, 2019, Protective effects of lanosterol synthase up-regulation in UV-B-induced oxidative stress, Front. Pharmacol., 10, 947, 10.3389\u002Ffphar.2019.00947\nWishart, 2021, Hallmarks of lens aging and cataractogenesis, Exp. Eye Res., 210, 10.1016\u002Fj.exer.2021.108709\nHong, 2020, Exosomes from adipose-derived stem cells attenuate UVB-induced apoptosis, ROS, and the Ca(2+) level in HLEC cells, Exp. Cell Res., 396, 10.1016\u002Fj.yexcr.2020.112321\nLee, 2016, Alpha B-crystallin protects rat articular chondrocytes against casein kinase II inhibition-induced apoptosis, PLoS One, 11, 10.1371\u002Fjournal.pone.0166450\nPaudel, 2020, Rutin loaded liquid crystalline nanoparticles inhibit lipopolysaccharide induced oxidative stress and apoptosis in bronchial epithelial cells in vitro, Toxicol. In Vitro, 68, 10.1016\u002Fj.tiv.2020.104961\nTsai, 2019, Protective effects of rosmarinic acid against selenite-induced cataract and oxidative damage in rats, Int. J. Med. Sci., 16, 729, 10.7150\u002Fijms.32222\nSajadimajd, 2018, Oxidative stress and cancer: the role of Nrf2, Curr. Cancer Drug Targets, 18, 538, 10.2174\u002F1568009617666171002144228\nUlasov, 2022, Nrf2\u002FKeap1\u002FARE signaling: towards specific regulation, Life Sci., 291, 10.1016\u002Fj.lfs.2021.120111\nOoi, 2017, oxidative stress in cardiovascular diseases: involvement of Nrf2 antioxidant redox signaling in macrophage foam cells formation, Int. J. Mol. Sci., 18, 10.3390\u002Fijms18112336\nYe, 2020, LncRNA MALAT1 regulates miR-144-3p to facilitate epithelial-mesenchymal transition of lens epithelial cells via the ROS\u002FNRF2\u002FNotch1\u002Fsnail pathway, Oxidative Med. Cell. Longev., 2020, 8184314, 10.1155\u002F2020\u002F8184314\nYang, 2022, Acetyl-11-keto-beta boswellic acid (AKBA) protects lens epithelial cells against H(2)O(2)-induced oxidative injury and attenuates cataract progression by activating Keap1\u002FNrf2\u002FHO-1 signaling, Front. Pharmacol., 13\nWątroba, 2017, Sirtuins, epigenetics and longevity, Ageing Res. Rev., 40, 11, 10.1016\u002Fj.arr.2017.08.001\nYao, 2019, The protective effect of lithocholic acid on the intestinal epithelial barrier is mediated by the vitamin D receptor via a SIRT1\u002FNrf2 and NF-κB dependent mechanism in Caco-2 cells, Toxicol. Lett., 316, 109, 10.1016\u002Fj.toxlet.2019.08.024\nQiongyue, 2022, Post-treatment with irisin attenuates acute kidney injury in sepsis mice through anti-ferroptosis via the SIRT1\u002FNrf2 Pathway, Front. Pharmacol., 13, 10.3389\u002Ffphar.2022.857067\nArioz, 2019, Melatonin attenuates LPS-induced acute depressive-like behaviors and microglial NLRP3 inflammasome activation through the SIRT1\u002FNrf2 pathway, Front. Immunol., 10, 1511, 10.3389\u002Ffimmu.2019.01511\nXia, 2017, NFAT5 protects astrocytes against oxygen-glucose-serum deprivation\u002Frestoration damage via the SIRT1\u002FNrf2 pathway, J. Mol. Neurosci., 61, 96, 10.1007\u002Fs12031-016-0849-x\nZhang, 2016, Resveratrol ameliorated vascular calcification by regulating Sirt-1 and Nrf2, Transplant. Proc., 48, 3378, 10.1016\u002Fj.transproceed.2016.10.023\nDeng, 2019, The role of sirtuin 1 and its activator, resveratrol in osteoarthritis, Biosci. Rep., 39, 10.1042\u002FBSR20190189\nFu, 2019, Activation of SIRT1 ameliorates LPS-induced lung injury in mice via decreasing endothelial tight junction permeability, Acta Pharmacol. Sin., 40, 630, 10.1038\u002Fs41401-018-0045-3\nSingh, 2020, Resveratrol delay the cataract formation against naphthalene-induced experimental cataract in the albino rats, J. Biochem. Mol. Toxicol., 34, 10.1002\u002Fjbt.22420\nLi, 2021, Resveratrol attenuates rotenone-induced inflammation and oxidative stress via STAT1 and Nrf2\u002FKeap1\u002FSLC7A11 pathway in a microglia cell line, Pathol. Res. Pract., 225\nLiu, 2017, Nrf2 as a target for prevention of age-related and diabetic cataracts by against oxidative stress, Aging Cell, 16, 934, 10.1111\u002Facel.12645\nKang, 2020, Resveratrol prevents benzo(a)pyrene-induced disruption of mitochondrial homeostasis via the AMPK signaling pathway in primary cultured neurons, Environ. Pollut., 261, 10.1016\u002Fj.envpol.2020.114207\nMa, 2020, Manganese induces autophagy dysregulation: The role of S-nitrosylation in regulating autophagy related proteins in vivo and in vitro, Sci. Total Environ., 698, 10.1016\u002Fj.scitotenv.2019.134294\nZhang, 2021, Astaxanthin ameliorates oxidative stress and neuronal apoptosis via SIRT1\u002FNRF2\u002FPrx2\u002FASK1\u002Fp38 after traumatic brain injury in mice, Br. J. Pharmacol., 178, 1114, 10.1111\u002Fbph.15346\nKauh, 2016, Geographic variation in the rate and timing of cataract surgery among US communities, JAMA Ophthalmol., 134, 267, 10.1001\u002Fjamaophthalmol.2015.5322\nIvanov, 2018, Ultraviolet radiation oxidative stress affects eye health, J. Biophotonics, 11\nZhao, 2020, NAD(+) precursors protect corneal endothelial cells from UVB-induced apoptosis, Am. J. Physiol. Cell Physiol., 318, C796, 10.1152\u002Fajpcell.00445.2019\nJia, 2018, UVB induces apoptosis via downregulation of CALML3-dependent JNK1\u002F2 and ERK1\u002F2 pathways in cataract, Int. J. Mol. Med., 41, 3041\nWang, 2021, Orai3 exacerbates apoptosis of lens epithelial cells by disrupting Ca(2+) homeostasis in diabetic cataract, Clin. Transl. Med., 11\nKim, 2020, Alpha B-crystallin overexpression protects oligodendrocyte precursor cells against oxidative stress-induced apoptosis through the akt pathway, J. Mol. Neurosci., 70, 751, 10.1007\u002Fs12031-020-01485-z\nYing, 2014, Endogenous α-crystallin inhibits expression of caspase-3 induced by hypoxia in retinal neurons, Life Sci., 111, 42, 10.1016\u002Fj.lfs.2014.07.008\nFrankfater, 2020, Alpha-crystallin mutations alter lens metabolites in mouse models of human cataracts, PLoS One, 15, 10.1371\u002Fjournal.pone.0238081\nWang, 2022, Oxysterol compounds in mouse mutant αA- and αB-crystallin lenses can improve the optical properties of the lens, Invest. Ophthalmol. Vis. Sci., 63, 15, 10.1167\u002Fiovs.63.5.15\nYoshitomi, 2019, Ultraviolet B-induced Otx2 expression in lens epithelial cells promotes epithelial-mesenchymal transition, Biol. Open, 8\nSin, 2015, Effects of long-term resveratrol-induced SIRT1 activation on insulin and apoptotic signalling in aged skeletal muscle, Acta Diabetol., 52, 1063, 10.1007\u002Fs00592-015-0767-3\nPeriyasamy, 2017, Age-related cataracts: Role of unfolded protein response, Ca(2+) mobilization, epigenetic DNA modifications, and loss of Nrf2\u002FKeap1 dependent cytoprotection, Prog. Retin. Eye Res., 60, 1, 10.1016\u002Fj.preteyeres.2017.08.003\nPark, 2021, Malonic acid isolated from Pinus densiflora inhibits UVB-induced oxidative stress and inflammation in HaCaT keratinocytes, Polymers, 13\nCosín-Tomàs, 2019, Role of resveratrol and selenium on oxidative stress and expression of antioxidant and anti-aging genes in immortalized lymphocytes from Alzheimer's disease patients, Nutrients, 11, 10.3390\u002Fnu11081764\nMeng, 2018, Dietary resveratrol improves antioxidant status of sows and piglets and regulates antioxidant gene expression in placenta by Keap1-Nrf2 pathway and Sirt1, J. Anim. Sci. Biotechnol., 9, 34, 10.1186\u002Fs40104-018-0248-y\nXu, 2019, Resveratrol increase myocardial Nrf2 expression in type 2 diabetic rats and alleviate myocardial ischemia\u002Freperfusion injury (MIRI), Ann. Palliative Med., 8, 565, 10.21037\u002Fapm.2019.11.25\nKo, 2021, Ergothioneine alleviates senescence of fibroblasts induced by UVB damage of keratinocytes via activation of the Nrf2\u002FHO-1 pathway and HSP70 in keratinocytes, Exp. Cell Res., 400, 10.1016\u002Fj.yexcr.2021.112516\nWang, 2019, Red raspberry extract protects the skin against UVB-induced damage with antioxidative and anti-inflammatory properties, Oxidative Med. Cell. Longev., 2019, 9529676\nWang, 2020, Resveratrol ameliorates rheumatoid arthritis via activation of SIRT1-Nrf2 signaling pathway, BioFactors, 46, 441, 10.1002\u002Fbiof.1599\nZhuang, 2019, Resveratrol attenuates oxidative stress-induced intestinal barrier injury through PI3K\u002FAkt-Mediated Nrf2 signaling pathway, Oxidative Med. Cell. Longev., 2019, 7591840, 10.1155\u002F2019\u002F7591840\nKim, 2018, Resveratrol, an Nrf2 activator, ameliorates aging-related progressive renal injury, Aging, 10, 83, 10.18632\u002Faging.101361\nXu, 2021, Protection of the enhanced Nrf2 deacetylation and its downstream transcriptional activity by SIRT1 in myocardial ischemia\u002Freperfusion injury, Int. J. Cardiol., 342, 82, 10.1016\u002Fj.ijcard.2021.08.007\nDang, 2022, Edaravone ameliorates depressive and anxiety-like behaviors via Sirt1\u002FNrf2\u002FHO-1\u002FGpx4 pathway, J. Neuroinflammation, 19, 41, 10.1186\u002Fs12974-022-02400-6\nHuang, 2017, The crosstalk between Sirt1 and Keap1\u002FNrf2\u002FARE anti-oxidative pathway forms a positive feedback loop to inhibit FN and TGF-β1 expressions in rat glomerular mesangial cells, Exp. Cell Res., 361, 63, 10.1016\u002Fj.yexcr.2017.09.042\nWang, 2020, Total glycosides of Cistanche deserticola promote neurological function recovery by inducing neurovascular regeneration via Nrf-2\u002FKeap-1 pathway in MCAO\u002FR rats, Front. Pharmacol., 11, 236, 10.3389\u002Ffphar.2020.00236\nSkobowiat, 2018, Melatonin and its derivatives counteract the ultraviolet B radiation-induced damage in human and porcine skin ex vivo, J. Pineal Res., 65, 10.1111\u002Fjpi.12501",{"EN":633},"Inhibition of SIRT1 promotes ultraviolet B induced cataract via downregulation of the KEAP1\u002FNFE2L2 signaling pathway",{"VOID":635},"10.1016\u002Fj.jphotobiol.2023.112753","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1011134423001070",[638,663,682,701,728,747,766,785],{"id":639,"sortIndex":285,"researcher":18,"roles":640,"affiliations":641,"properties":660},"4cbde8a6-17bf-415e-a73d-0045a285854d",[145],[642,650],{"id":18,"sortIndex":19,"affiliation":643,"properties":18},{"id":644,"createTime":645,"updateTime":645,"relativeEntities":646,"slug":18,"properties":647,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"684e2221-9cf0-402a-8a0a-23d50d06b5cb","2023-12-07T07:20:13.635+00:00",[],{"title":648},{"VI":649},"Key Laboratory of Environmental Stress and Chronic Disease Control & Prevention (China Medical University), Ministry of Education, Shenyang, Liaoning 110122, China",{"id":651,"sortIndex":159,"affiliation":652,"properties":659},"09e35807-521c-44a2-ad44-51332ada6497",{"id":653,"createTime":654,"updateTime":654,"relativeEntities":655,"slug":18,"properties":656,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"56bc344c-6317-4664-bd2a-65186153c176","2023-12-07T07:20:13.639+00:00",[],{"title":657},{"VI":658},"Department of Environmental Health, School of Public Health, China Medical University, Shenyang, Liaoning 110122, China",{},{"title":661},{"VI":662},"Wei Liu",{"id":664,"sortIndex":195,"researcher":18,"roles":665,"affiliations":666,"properties":679},"18a21c2b-97c7-4286-943a-f6abf54a5798",[145],[667,672],{"id":18,"sortIndex":19,"affiliation":668,"properties":18},{"id":644,"createTime":645,"updateTime":645,"relativeEntities":669,"slug":18,"properties":670,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":671},{"VI":649},{"id":673,"sortIndex":159,"affiliation":674,"properties":678},"08e37bcd-0632-4a1d-ac21-6837368884ea",{"id":653,"createTime":654,"updateTime":654,"relativeEntities":675,"slug":18,"properties":676,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":677},{"VI":658},{},{"title":680},{"VI":681},"Huiying Du",{"id":683,"sortIndex":19,"researcher":18,"roles":684,"affiliations":685,"properties":698},"defa48d6-3819-473c-91c3-09d390f068e4",[145],[686,691],{"id":18,"sortIndex":19,"affiliation":687,"properties":18},{"id":644,"createTime":645,"updateTime":645,"relativeEntities":688,"slug":18,"properties":689,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":690},{"VI":649},{"id":692,"sortIndex":159,"affiliation":693,"properties":697},"3111d1c5-792d-41b8-8b58-611c6def42b1",{"id":653,"createTime":654,"updateTime":654,"relativeEntities":694,"slug":18,"properties":695,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":696},{"VI":658},{},{"title":699},{"VI":700},"Feiying Wu",{"id":702,"sortIndex":367,"researcher":18,"roles":703,"affiliations":704,"properties":725},"2b0c4915-1d4a-4c8a-a5e5-2dd62c184878",[145],[705,715],{"id":18,"sortIndex":19,"affiliation":706,"properties":18},{"id":707,"createTime":708,"updateTime":709,"relativeEntities":710,"slug":711,"properties":712,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"23795694-60f5-46b5-918c-96d417c2a266","2024-01-04T20:59:06.160+00:00","2024-09-29T03:44:03.551+00:00",[],"The-International-Peace-Maternity-Child-Health-Hospital-Shanghai-Jiao-Tong-University-School-of-Medicine-Shanghai-200030-China",{"title":713},{"VI":714},"The International Peace Maternity & Child Health Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200030, China",{"id":716,"sortIndex":159,"affiliation":717,"properties":724},"b2f9f12c-247d-49c0-9921-8f8a2b21daa3",{"id":718,"createTime":719,"updateTime":719,"relativeEntities":720,"slug":18,"properties":721,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"342cc43b-6ac3-4cd0-9183-bc4708f4a7aa","2023-12-07T07:20:13.795+00:00",[],{"title":722},{"VI":723},"Shanghai Key Laboratory of Embryo Original Disease, Shanghai 200030, China",{},{"title":726},{"VI":727},"Hui Hua",{"id":729,"sortIndex":64,"researcher":18,"roles":730,"affiliations":731,"properties":744},"f4acf4b0-3bad-4fba-823c-1e24b1332f4f",[145],[732,737],{"id":18,"sortIndex":19,"affiliation":733,"properties":18},{"id":644,"createTime":645,"updateTime":645,"relativeEntities":734,"slug":18,"properties":735,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":736},{"VI":649},{"id":738,"sortIndex":159,"affiliation":739,"properties":743},"8bb150a8-a560-45ee-b927-d6f06b2365c8",{"id":653,"createTime":654,"updateTime":654,"relativeEntities":740,"slug":18,"properties":741,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":742},{"VI":658},{},{"title":745},{"VI":746},"Bin Xu",{"id":748,"sortIndex":143,"researcher":18,"roles":749,"affiliations":750,"properties":763},"ccc94bd5-ea23-4681-9364-8a48779b8271",[145],[751,756],{"id":18,"sortIndex":19,"affiliation":752,"properties":18},{"id":644,"createTime":645,"updateTime":645,"relativeEntities":753,"slug":18,"properties":754,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":755},{"VI":649},{"id":757,"sortIndex":159,"affiliation":758,"properties":762},"9bbead49-36b3-4acb-a6a0-0ef5d2c8b33b",{"id":653,"createTime":654,"updateTime":654,"relativeEntities":759,"slug":18,"properties":760,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":761},{"VI":658},{},{"title":764},{"VI":765},"Ting Lei",{"id":767,"sortIndex":380,"researcher":18,"roles":768,"affiliations":769,"properties":782},"24815b84-6414-432d-be49-b43eaad1eac2",[145],[770,775],{"id":18,"sortIndex":19,"affiliation":771,"properties":18},{"id":644,"createTime":645,"updateTime":645,"relativeEntities":772,"slug":18,"properties":773,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":774},{"VI":649},{"id":776,"sortIndex":159,"affiliation":777,"properties":781},"763348ca-3fa8-4453-a9c4-3e01f91700a8",{"id":653,"createTime":654,"updateTime":654,"relativeEntities":778,"slug":18,"properties":779,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":780},{"VI":658},{},{"title":783},{"VI":784},"Tianyao Yang",{"id":786,"sortIndex":159,"researcher":18,"roles":787,"affiliations":788,"properties":801},"affbb77d-6be2-465e-9f64-63eb29e943fe",[145],[789,794],{"id":18,"sortIndex":19,"affiliation":790,"properties":18},{"id":644,"createTime":645,"updateTime":645,"relativeEntities":791,"slug":18,"properties":792,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":793},{"VI":649},{"id":795,"sortIndex":159,"affiliation":796,"properties":800},"f68eed94-c551-4fe9-a9cb-2024f31dda48",{"id":653,"createTime":654,"updateTime":654,"relativeEntities":797,"slug":18,"properties":798,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":799},{"VI":658},{},{"title":802},{"VI":803},"Xinyu Xia",{"url":636,"publisher":805,"properties":827},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":806,"slug":10,"properties":807,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":810,"manageAffiliations":811,"indexDatabases":812,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":808,"title":809},{"VOID":13},{"EN":15},[],[],[813,820],{"id":78,"indexDatabase":814,"url":91,"indexYears":92,"academicFieldIds":819,"indexDatabaseRanking":98},{"id":80,"createTime":81,"updateTime":82,"relativeEntities":815,"label":816,"description":817,"key":88,"publicationTags":818,"standard":18},[],{"EN":85,"VI":85},{"EN":85,"VI":87},[90],[94,95,96,97],{"id":100,"indexDatabase":821,"url":115,"indexYears":18,"academicFieldIds":826,"indexDatabaseRanking":18},{"id":102,"createTime":103,"updateTime":104,"relativeEntities":822,"label":823,"description":824,"key":111,"publicationTags":825,"standard":18},[],{"EN":107,"VI":107},{"VI":109,"EN":110},[113,114],[117,118],{"volume":828,"pages":829},{"VOID":264},{"VOID":830},"112753",{"id":832,"createTime":833,"updateTime":834,"relativeEntities":835,"slug":836,"properties":837,"entityType":136,"verifyStatus":137,"verifyTime":834,"verifyNote":138,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":844,"fullTextUrl":18,"authors":845,"publicationType":238,"publisherRelationship":994,"citationCount":18,"citationInfo":18,"publishDate":1022,"publishYear":1023,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":269},"39d1cbd2-2734-4389-b2dc-6948c03c0229","2023-12-18T01:30:57.070+00:00","2025-02-22T23:54:50.665+00:00",[],"Metformin-associated-with-photodynamic-therapy-A-novel-oncological-direction",{"references":838,"title":840,"doi":842},{"VOID":839},"Hursting, 2010, Energy balance, host-related factors, and cancer progression, J. Clin. Oncol., 28, 4058, 10.1200\u002FJCO.2010.27.9935\nWitters, 2001, The blooming of the French lilac, J. Clin. Invest., 108, 1105, 10.1172\u002FJCI14178\nBailey, 1996, Metformin, N. Engl. J. Med., 334, 574, 10.1056\u002FNEJM199602293340906\nZakikhani, 2006, Metformin is an AMP kinase-dependent growth inhibitor for breast cancer cells, Cancer Res., 66, 10269, 10.1158\u002F0008-5472.CAN-06-1500\nChen, 2012, Metformin inhibits growth of thyroid carcinoma cells, suppresses self-renewal of derived cancer stem cells, and potentiates the effect of chemotherapeutic agents, J. Clin. Endocrinol. Metab., 97, 10.1210\u002Fjc.2011-1754\nHirsch, 2009, Metformin selectively targets cancer stem cells, and acts together with chemotherapy to block tumour growth and prolong remission, Cancer Res., 69, 7507, 10.1158\u002F0008-5472.CAN-09-2994\nAgostinis, 2011, Photodynamic therapy of cancer: an update, CA Cancer J. Clin., 61, 250, 10.3322\u002Fcaac.20114\nPascu, 2003, Spectroscopic characteristics of metalloporphyrins used in photodynamic therapy, Oftalmologia, 57, 73\nIon, 1996, Spectral studies of TSPP and TSNP used in PDT. Monomer-dimer equilibrium, Rom. J. Biophys., 6, 213\nFilip, 2011, The effects of grape seeds polyphenols on SKH-1 mice skin irradiated with multiple doses of UV-B, J. Photochem. Photobiol., B, 105, 133, 10.1016\u002Fj.jphotobiol.2011.08.002\nNoble, 2000, Quantitation of protein, Methods Enzymol., 463, 73, 10.1016\u002FS0076-6879(09)63008-1\nConti, 1991, Improved fluorimetric determination of malondialdehyde, Clin. Chem., 37, 1273, 10.1093\u002Fclinchem\u002F37.7.1273\nReznick, 1994, Oxidative damage to proteins: spectrophotometric method for carbonyl assay, Methods Enzymol., 233, 357, 10.1016\u002FS0076-6879(94)33041-7\nHu, 1994, Measurement of protein thiol groups and glutathione in plasma, Methods Enzymol., 233, 380, 10.1016\u002FS0076-6879(94)33044-1\nTitheradge, 1998, The enzymatic measurement of nitrate and nitrite, Methods Mol. Biol., 100, 83\nFilip, 2012, Calluna Vulgaris extract modulates NF-kB\u002FERK 1\u002F2 signaling pathway and MMP expression in SKH-1 hairless mice skin exposed to UVB, J. Physiol. Pharmacol., 63, 423\nAaltomaa, 2000, The prognostic value of inducible nitric oxide synthase in local prostate cancer, BJU Int., 86, 234, 10.1046\u002Fj.1464-410x.2000.00787.x\nBolfa, 2013, Photoprotective effects of Romanian propolis on skin of mice exposed to UVB irradiation, Food Chem. Toxicol., 62, 329, 10.1016\u002Fj.fct.2013.08.078\nDowling, 2011, Understanding the benefit of metformin use in cancer treatment, BMC Med., 9, 33, 10.1186\u002F1741-7015-9-33\nEvans, 2005, Metformin and reduced risk of cancer in diabetic patients, BMJ, 330, 1304, 10.1136\u002Fbmj.38415.708634.F7\nVazquez-Martin, 2010, Metformin regulates breast cancer stem cell ontogeny by transcriptional regulation of the epithelial–mesenchymal transition (EMT) status, Cell Cycle, 9, 3807, 10.4161\u002Fcc.9.18.13131\nAnisimov, 2005, Effect of metformin on life span and on the development of spontaneous mammary tumours in HER-2\u002Fneu transgenic mice, Exp. Gerontol., 40, 685, 10.1016\u002Fj.exger.2005.07.007\nFonseca, 2011, Metformin reduces the stimulatory effect of obesity on in vivo Walker-256 tumour development and increases the area of tumour necrosis, Life Sci., 88, 846, 10.1016\u002Fj.lfs.2011.03.005\nHadad, 2011, Evidence for biological effects of metformin in operable breast cancer: a pre-operative, window-of-opportunity, randomized trial, Breast Cancer Res. Treat., 128, 783, 10.1007\u002Fs10549-011-1612-1\nHosono, 2010, Metformin suppresses colorectal aberrant crypt foci in a short-term clinical trial, Cancer Prev. Res. (Phila.), 3, 1077, 10.1158\u002F1940-6207.CAPR-10-0186\nPatel, 2010, Clinical outcomes after radical prostatectomy in diabetic patients treated with metformin, Urology, 76, 1240, 10.1016\u002Fj.urology.2010.03.059\nZepp, 1986, Degradation of insulin and glucagon by a factor associated with Walker 256 carcinosarcoma cells, Cancer Lett., 31, 77, 10.1016\u002F0304-3835(86)90169-2\nBuytaert, 2007, Molecular effectors of multiple cell death pathways initiated by photodynamic therapy, Biochim. Biophys. Acta, 1776, 86\nConstantin, 2004, The effect of laser activation of 5, 10, 15, 20-tetra-sulphophenyl-porphyrin loaded in K562 cells and human normal mononuclear cells, Roum. Arch. Microbiol. Immunol., 63, 159\nClichici, 2010, The dynamics of reactive oxygen species in photodynamic therapy with tetra sulfophenyl-porphyrin, Acta Physiol. Hung., 97, 41, 10.1556\u002FAPhysiol.97.2010.1.5\nAlgire, 2012, Metformin reduces endogenous reactive oxygen species and associated DNA damage, Cancer Prev. Res. (Phila.), 5, 536, 10.1158\u002F1940-6207.CAPR-11-0536\nMehta, 2009, Cytoprotective mechanisms of carbonyl scavenging drugs in isolated rat hepatocytes, Chem. Biol. Interact., 178, 317, 10.1016\u002Fj.cbi.2008.10.026\nBelgorosky, 2013, Inhibition of nitric oxide is a good therapeutic target for bladder tumours that express iNOS, Nitric Oxide C, 36, 11, 10.1016\u002Fj.niox.2013.10.010\nGately, 2000, The contributions of cyclooxygenase-2 to tumour angiogenesis, Cancer Metastasis Rev., 19, 19, 10.1023\u002FA:1026575610124\nCerezo, 2013, Metformin blocks melanoma invasion and metastasis development in AMPK\u002Fp53-dependent manner, Mol. Cancer Ther., 12, 1605, 10.1158\u002F1535-7163.MCT-12-1226-T\nHirsch, 2013, Metformin inhibits the inflammatory response associated with cellular transformation and cancer stem cell growth, Proc. Natl. Acad. Sci. U. S. A., 110, 972, 10.1073\u002Fpnas.1221055110\nWang, 2008, Metformin induces apoptosis of pancreatic cancer cells, World J. Gastroenterol., 14, 7192, 10.3748\u002Fwjg.14.7192\nZheng, 2013, Prognostic significance of AMPK activation and therapeutic effects of metformin in hepatocellular carcinoma, Clin. Cancer Res., 19, 5372, 10.1158\u002F1078-0432.CCR-13-0203\nAlimova, 2009, Metformin inhibits breast cancer cell growth, colony formation and induces cell cycle arrest in vitro, Cell Cycle, 8, 909, 10.4161\u002Fcc.8.6.7933\nBarathan, 2013, Hypericin–photodynamic therapy leads to interleukin-6 secretion by HepG2 cells and their apoptosis via recruitment of BH3 interacting-domain death agonist and caspases, Cell Death Dis., 4, e697, 10.1038\u002Fcddis.2013.219\nYasmeen, 2011, Induction of apoptosis by metformin in epithelial ovarian cancer: involvement of the Bcl-2 family proteins, Gynecol. Oncol., 121, 492, 10.1016\u002Fj.ygyno.2011.02.021\nZou, 2004, Activation of the AMP-activated protein kinase by the anti-diabetic drug metformin in vivo. Role of mitochondrial reactive nitrogen species, J. Biol. Chem., 279, 43940, 10.1074\u002Fjbc.M404421200\nZhou, 2001, Role of AMP-activated protein kinase in mechanism of metformin action, J. Clin. Invest., 108, 1167, 10.1172\u002FJCI13505\nTowler, 2007, AMP-activated protein kinase in metabolic control and insulin signaling, Circ. Res., 100, 328, 10.1161\u002F01.RES.0000256090.42690.05",{"EN":841},"Metformin associated with photodynamic therapy – A novel oncological direction",{"VOID":843},"10.1016\u002Fj.jphotobiol.2014.04.027","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1011134414001353",[846,863,878,890,902,915,927,939,964,981],{"id":847,"sortIndex":367,"researcher":18,"roles":848,"affiliations":849,"properties":860},"4e2ec9e3-cfa1-4634-b862-042b4e78c58d",[145],[850],{"id":18,"sortIndex":19,"affiliation":851,"properties":18},{"id":852,"createTime":853,"updateTime":854,"relativeEntities":855,"slug":856,"properties":857,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"e7401f1b-52f5-47b6-9322-c67cbec03809","2024-01-11T03:57:22.155+00:00","2024-09-30T22:11:33.657+00:00",[],"Department-of-Physiology-Iuliu-Hatieganu-University-of-Medicine-and-Pharmacy-1-Clinicilor-Street-400006-Cluj-Napoca-Romania",{"title":858},{"VI":859},"Department of Physiology,“Iuliu Hatieganu” University of Medicine and Pharmacy, 1 Clinicilor Street, 400006 Cluj-Napoca, Romania",{"title":861},{"VI":862},"Diana Olteanu",{"id":864,"sortIndex":285,"researcher":18,"roles":865,"affiliations":866,"properties":875},"3acbd8d1-0e7f-40ad-b8f5-e0a52bafb7ff",[145],[867],{"id":18,"sortIndex":19,"affiliation":868,"properties":18},{"id":869,"createTime":870,"updateTime":870,"relativeEntities":871,"slug":18,"properties":872,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"c7eb4f85-0a66-41b5-bebd-92ef0cd03527","2023-12-18T01:30:57.141+00:00",[],{"title":873},{"VI":874},"Departments of Radiobiology and Tumor Biology, Oncology Institute “Prof. I. Chiricuta”, 34-36 Republicii Street, 400015 Cluj-Napoca, Romania",{"title":876},{"VI":877},"Corina Tatomir",{"id":879,"sortIndex":159,"researcher":18,"roles":880,"affiliations":881,"properties":887},"766cc37a-3866-4ddf-9e3a-a244f5544b07",[145],[882],{"id":18,"sortIndex":19,"affiliation":883,"properties":18},{"id":852,"createTime":853,"updateTime":854,"relativeEntities":884,"slug":856,"properties":885,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":886},{"VI":859},{"title":888},{"VI":889},"Tiberiu Popescu",{"id":891,"sortIndex":143,"researcher":18,"roles":892,"affiliations":893,"properties":899},"47a41d74-7c9b-4aa0-b7f4-6b91ac229026",[145],[894],{"id":18,"sortIndex":19,"affiliation":895,"properties":18},{"id":852,"createTime":853,"updateTime":854,"relativeEntities":896,"slug":856,"properties":897,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":898},{"VI":859},{"title":900},{"VI":901},"Mihaela D. Aldea",{"id":903,"sortIndex":904,"researcher":18,"roles":905,"affiliations":906,"properties":912},"dab68c00-6caf-484f-ae2b-065827fa0b54",9,[145],[907],{"id":18,"sortIndex":19,"affiliation":908,"properties":18},{"id":852,"createTime":853,"updateTime":854,"relativeEntities":909,"slug":856,"properties":910,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":911},{"VI":859},{"title":913},{"VI":914},"Adriana G. Filip",{"id":916,"sortIndex":19,"researcher":18,"roles":917,"affiliations":918,"properties":924},"e01bbeb2-0ad6-47c5-b82e-054d1969ec19",[145],[919],{"id":18,"sortIndex":19,"affiliation":920,"properties":18},{"id":852,"createTime":853,"updateTime":854,"relativeEntities":921,"slug":856,"properties":922,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":923},{"VI":859},{"title":925},{"VI":926},"Iuliana Nenu",{"id":928,"sortIndex":195,"researcher":18,"roles":929,"affiliations":930,"properties":936},"91955ff2-b2ed-4227-84a1-762996570b5e",[145],[931],{"id":18,"sortIndex":19,"affiliation":932,"properties":18},{"id":852,"createTime":853,"updateTime":854,"relativeEntities":933,"slug":856,"properties":934,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":935},{"VI":859},{"title":937},{"VI":938},"Lucian Craciun",{"id":940,"sortIndex":64,"researcher":18,"roles":941,"affiliations":942,"properties":961},"33fb923b-3b09-415e-b34b-1d3e1eecf945",[145],[943,953],{"id":944,"sortIndex":159,"affiliation":945,"properties":952},"10240812-fddb-4c2b-86b3-938a35d56fe0",{"id":946,"createTime":947,"updateTime":947,"relativeEntities":948,"slug":18,"properties":949,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"71434361-08a7-4e90-8849-67decbafd48f","2023-12-18T01:30:57.159+00:00",[],{"title":950},{"VI":951},"Department of Biomedical Sciences, Ross University School of Veterinary Medicine Basseterre, PO Box 334, Saint Kitts and Nevis",{},{"id":18,"sortIndex":19,"affiliation":954,"properties":18},{"id":955,"createTime":956,"updateTime":956,"relativeEntities":957,"slug":18,"properties":958,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"5e929188-471e-497a-8f92-1254e0f2659b","2023-12-18T01:30:57.154+00:00",[],{"title":959},{"VI":960},"Department of Pathology, Cluj-Napoca, University of Agricultural Sciences and Veterinary Medicine, 3-5 Calea Manastur, 400372 Cluj-Napoca, Romania",{"title":962},{"VI":963},"Pompei Bolfa",{"id":965,"sortIndex":380,"researcher":18,"roles":966,"affiliations":967,"properties":978},"61ec8a7e-bb41-4d3f-8db0-75d8deef3480",[145],[968],{"id":18,"sortIndex":19,"affiliation":969,"properties":18},{"id":970,"createTime":971,"updateTime":972,"relativeEntities":973,"slug":974,"properties":975,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"8ca9f4b8-b379-45a4-be43-0c5fa06fdb4e","2023-12-18T01:30:39.543+00:00","2024-09-30T22:17:48.699+00:00",[],"National-Research-Development-Institute-for-Chemistry-and-Petrochemistry-ICECHIM-202-Splaiul-Independentei-060021-Bucharest-Romania",{"title":976},{"VI":977},"National Research & Development Institute for Chemistry and Petrochemistry ICECHIM 202 Splaiul Independentei, 060021 Bucharest, Romania",{"title":979},{"VI":980},"Rodica M. Ion",{"id":982,"sortIndex":983,"researcher":18,"roles":984,"affiliations":985,"properties":991},"9abdca19-8b29-4b96-b6fe-f8efe0a9ff61",8,[145],[986],{"id":18,"sortIndex":19,"affiliation":987,"properties":18},{"id":852,"createTime":853,"updateTime":854,"relativeEntities":988,"slug":856,"properties":989,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":990},{"VI":859},{"title":992},{"VI":993},"Adriana Muresan",{"url":844,"publisher":995,"properties":1017},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":996,"slug":10,"properties":997,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":1000,"manageAffiliations":1001,"indexDatabases":1002,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":998,"title":999},{"VOID":13},{"EN":15},[],[],[1003,1010],{"id":78,"indexDatabase":1004,"url":91,"indexYears":92,"academicFieldIds":1009,"indexDatabaseRanking":98},{"id":80,"createTime":81,"updateTime":82,"relativeEntities":1005,"label":1006,"description":1007,"key":88,"publicationTags":1008,"standard":18},[],{"EN":85,"VI":85},{"EN":85,"VI":87},[90],[94,95,96,97],{"id":100,"indexDatabase":1011,"url":115,"indexYears":18,"academicFieldIds":1016,"indexDatabaseRanking":18},{"id":102,"createTime":103,"updateTime":104,"relativeEntities":1012,"label":1013,"description":1014,"key":111,"publicationTags":1015,"standard":18},[],{"EN":107,"VI":107},{"VI":109,"EN":110},[113,114],[117,118],{"volume":1018,"pages":1020},{"VOID":1019},"138",{"VOID":1021},"80-91","2014-09-01",2014,{"id":1025,"createTime":1026,"updateTime":1027,"relativeEntities":1028,"slug":1029,"properties":1030,"entityType":136,"verifyStatus":137,"verifyTime":1027,"verifyNote":138,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":1037,"fullTextUrl":18,"authors":1038,"publicationType":238,"publisherRelationship":1134,"citationCount":18,"citationInfo":18,"publishDate":1162,"publishYear":1163,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":269},"9ece3da8-fe65-40c9-8207-6d4f294855d0","2024-02-09T18:35:49.289+00:00","2024-09-27T23:54:16.089+00:00",[],"Photodynamic-effects-induced-by-meso-tetrakis-4-carboxymethyleneoxy-phenyl-porphyrin-on-isolated-Sarcoma-180-ascites-mitochondria",{"references":1031,"title":1033,"doi":1035},{"VOID":1032},"Schuitmaker, 1996, New trend in photobiology [invited review]: photodynamic therapy: a promising new modality for the treatment of cancer, J. Photochem. Photobiol. B: Biol., 34, 3, 10.1016\u002F1011-1344(96)07342-3\nJori, 1995, Tumour photosensitizers: approaches to enhance the selectivity and efficiency of photodynamic therapy, J. Photochem. Photobiol. B: Biol., 36, 87, 10.1016\u002FS1011-1344(96)07352-6\nOrtel, 1996, Perspectives in cutaneous photodynamic sensitization, J. Photochem. Photobiol. B: Biol., 36, 209, 10.1016\u002FS1011-1344(96)07374-5\nPenning, 1994, Fundamentals of photodynamic therapy: cellular and biochemical aspects, Anti-cancer Drugs, 5, 139, 10.1097\u002F00001813-199404000-00003\nBonnett, 1995, Photosensitizers of the porphyrin and phthalocyanine series for photodynamic therapy, Chem. Soc. Rev., 24, 19, 10.1039\u002Fcs9952400019\nHenderson, 1992, How does photodynamic therapy work?, Photochem. Photobiol., 55, 145, 10.1111\u002Fj.1751-1097.1992.tb04222.x\nHamblin, 1994, On the mechanism of tumour localising effect in photodynamic therapy, J. Photochem. Photobiol. B: Biol., 23, 3, 10.1016\u002FS1011-1344(94)80018-9\nSalet, 1990, New trends in photobiology, J. Photochem. Photobiol. B: Biol., 5, 133, 10.1016\u002F1011-1344(90)80002-F\nHilf, 1992, Cellular targets of photodynamic therapy as a guide to mechanisms, 47\nZaidi, 1992, Apoptosis during photodynamic therapy-induced ablation of RIF-1 tumors in C3H mice: electron microscopic, histopathologic and biochemical evidence, Photochem. Photobiol., 58, 771, 10.1111\u002Fj.1751-1097.1993.tb04969.x\nKessel, 1997, Subcellular localization of photosensitizing agents, Photochem. Photobiol., 65, 387, 10.1111\u002Fj.1751-1097.1997.tb08575.x\nKessel, 1997, The role of subcellular localization in initiation of apoptosis by photodynamic therapy, Photochem. Photobiol., 65, 422, 10.1111\u002Fj.1751-1097.1997.tb08581.x\nChatterjee, 1997, Photodynamic effects induced by meso-tetrakis[4-(carboxymethyleneoxy)phenyl]porphyrin using rat hepatic microsomes as model membranes, Arch. Biochem. Biophys., 339, 242, 10.1006\u002Fabbi.1996.9846\nKeinan, 1992, Catalytic antibodies, Inorg. Chem., 31, 5433, 10.1021\u002Fic00052a019\nLowry, 1951, Protein measurement with folin phenol reagent, J. Biol. Chem., 193, 265, 10.1016\u002FS0021-9258(19)52451-6\nHunter, 1963, Swelling and lysis of rat liver mitochondria induced by ferrous ions, J. Biol. Chem., 238, 828, 10.1016\u002FS0021-9258(18)81341-2\nHicks, 1979, A specific method for determination of lipid hydroperoxides, Anal. Biochem., 99, 249, 10.1016\u002FS0003-2697(79)80003-2\nKraljic, 1978, A new method for detection of singlet oxygen in aqueous solutions, Photochem. Photobiol., 28, 577, 10.1111\u002Fj.1751-1097.1978.tb06972.x\nBlazek, 1989, Singlet oxygen induces frank strand breaks as well as alkali- and piperidine-labile sites in supercoiled plasmid DNA, Photochem. Photobiol., 49, 607, 10.1111\u002Fj.1751-1097.1989.tb08431.x\nCaplan, 1968, The effect of osmotic lysis on the oxidative phosphorylation and compartmentation, J. Cell Biol., 36, 15, 10.1083\u002Fjcb.36.1.15\nParker, 1956, A new sensitive method of chemical actionmetry, 235, 518\nPeriasamy, 1984, Singlet molecular oxygen quantum yield measurements of some porphyrins and metalloporphyrins, 93, 1361\nRodgers, 1982, Lifetime of O2 (1Δg) in liquid water as determined by time-resolved infrared luminescence measurements, J. Am. Chem. Soc., 104, 5541, 10.1021\u002Fja00384a070\nBonnett, 1988, Photophysical properties of meso-tetra(hydroxyphenyl)porphyrins, Photochem. Photobiol., 48, 271, 10.1111\u002Fj.1751-1097.1988.tb02820.x\nKelley, 1997, Production of lipid-derived free radicals in L1210 murine leukemia cells is an early oxidative event in the photodynamic action of photofrin, Photochem. Photobiol., 65, 576, 10.1111\u002Fj.1751-1097.1997.tb08608.x\nValenzeno, 1991, Membrane photomodification and its use to study reactive oxygen effects, vol. III, 137\nKessel, 1986, Sites of photosensitization by derivatives of haematoporphyrin, Photochem. Photobiol., 44, 489, 10.1111\u002Fj.1751-1097.1986.tb04697.x\nLevy, 1994, Photosensitizers in photodynamic therapy, Semin. Oncol., 21, 4\nKessel, 1989, In vitro photosensitization with a benzoporphyrin derivative, Photochem. Photobiol., 49, 579, 10.1111\u002Fj.1751-1097.1989.tb08426.x\nBachowski, 1988, Porphyrin sensitized photoreactions in the presence of ascorbate: oxidation of cell membrane lipids and hydroxyl radical traps, Photochem. Photobiol., 47, 635, 10.1111\u002Fj.1751-1097.1988.tb02759.x\nBertoloni, 1984, Hematoporphyrin-sensitized photoinactivation of Streptococcus faecalis, Photochem. Photobiol., 39, 811, 10.1111\u002Fj.1751-1097.1984.tb08864.x\nFirey, 1988, Photochemical properties of erythrocyte ghosts containing porphyrin, Photochem. Photobiol., 47, 615, 10.1111\u002Fj.1751-1097.1988.tb02756.x\nMoan, 1988, Photoinduced degradation and modification of Photofrin II in cells in vitro, Photochem. Photobiol., 47, 363, 10.1111\u002Fj.1751-1097.1988.tb02738.x\nHilf, 1986, Relationship of mitochondrial function with cellular adenosine triphosphatase levels to hematoporphyrin derivative-induced photosensitization in R3230 AC mammary tumours, Cancer Res., 46, 211\nPaillous, 1994, Interest of photochemical methods for induction of lipid peroxidation, Biochimie, 76, 355, 10.1016\u002F0300-9084(94)90109-0\nFoote, 1991, Definition of Type I and Type II photosensitized oxidation, Photochem. Photobiol., 54, 659, 10.1111\u002Fj.1751-1097.1991.tb02071.x\nBrown, 1993, New light on cancer therapy, Chem. Br., 29, 955\nGirotti, 1990, Photodynamic lipid peroxidation in biological systems, Photochem. Photobiol., 51, 497, 10.1111\u002Fj.1751-1097.1990.tb01744.x\nBensasson, 1993, Excited States and Free Radicals in Biology and Medicine, 320\nHalliwell, 1990, Role of free radicals and catalytic metal ions in human disease: an overview, Methods Enzymol., 186, 1, 10.1016\u002F0076-6879(90)86093-B",{"EN":1034},"Photodynamic effects induced by meso-tetrakis[4-(carboxymethyleneoxy)phenyl] porphyrin on isolated Sarcoma 180 ascites mitochondria",{"VOID":1036},"10.1016\u002Fs1011-1344(99)00073-1","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1011134499000731",[1039,1054,1069,1098,1110,1122],{"id":1040,"sortIndex":195,"researcher":18,"roles":1041,"affiliations":1042,"properties":1051},"a0192220-6703-4c28-a3c8-368fd99bd79d",[145],[1043],{"id":18,"sortIndex":19,"affiliation":1044,"properties":18},{"id":1045,"createTime":1046,"updateTime":1046,"relativeEntities":1047,"slug":18,"properties":1048,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"1dc33c0a-b643-44ea-aa8c-cfa2fe895c23","2024-02-02T07:55:17.459+00:00",[],{"title":1049},{"VI":1050},"Cell Biology Division, Bhabha Atomic Research Centre, Mumbai 400 085, India",{"title":1052},{"VI":1053},"J.P. Kamat",{"id":1055,"sortIndex":159,"researcher":18,"roles":1056,"affiliations":1057,"properties":1066},"91495762-f74b-43df-bf60-a0933e272742",[145],[1058],{"id":18,"sortIndex":19,"affiliation":1059,"properties":18},{"id":1060,"createTime":1061,"updateTime":1061,"relativeEntities":1062,"slug":18,"properties":1063,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"165fe05f-76b9-439e-badc-bdf9d77deb0e","2024-02-09T18:35:49.326+00:00",[],{"title":1064},{"VI":1065},"Institute for Medical Neurobiology, Otto-von-Guericke Universität, D-39120 Magdeburg, Germany",{"title":1067},{"VI":1068},"Heiko Possel",{"id":1070,"sortIndex":19,"researcher":18,"roles":1071,"affiliations":1072,"properties":1095},"b681e0f5-f476-41e4-8a01-f60f50bfda31",[145],[1073,1080,1088],{"id":1074,"sortIndex":143,"affiliation":1075,"properties":1079},"0bd51ab3-5f39-44c7-b4c8-458a497d05c8",{"id":1060,"createTime":1061,"updateTime":1061,"relativeEntities":1076,"slug":18,"properties":1077,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1078},{"VI":1065},{},{"id":18,"sortIndex":19,"affiliation":1081,"properties":18},{"id":1082,"createTime":1083,"updateTime":1083,"relativeEntities":1084,"slug":18,"properties":1085,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"e4beac47-17a1-41d0-952f-d6e7ee2ce89b","2024-01-18T18:32:51.244+00:00",[],{"title":1086},{"VI":1087},"Department of Chemistry, Indian Institute of Technology, Powai, Mumbai-400 076, India",{"id":1089,"sortIndex":159,"affiliation":1090,"properties":1094},"b7c037d7-555a-4215-b4ac-dadcfc980d26",{"id":1045,"createTime":1046,"updateTime":1046,"relativeEntities":1091,"slug":18,"properties":1092,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1093},{"VI":1050},{},{"title":1096},{"VI":1097},"Shampa R. Chatterjee",{"id":1099,"sortIndex":143,"researcher":18,"roles":1100,"affiliations":1101,"properties":1107},"22f2578f-f9e3-4353-abc5-531263a5b2f7",[145],[1102],{"id":18,"sortIndex":19,"affiliation":1103,"properties":18},{"id":1082,"createTime":1083,"updateTime":1083,"relativeEntities":1104,"slug":18,"properties":1105,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1106},{"VI":1087},{"title":1108},{"VI":1109},"T.S. Srivastava",{"id":1111,"sortIndex":367,"researcher":18,"roles":1112,"affiliations":1113,"properties":1119},"53cf3995-d6fe-415a-9967-303b0989e173",[145],[1114],{"id":18,"sortIndex":19,"affiliation":1115,"properties":18},{"id":1060,"createTime":1061,"updateTime":1061,"relativeEntities":1116,"slug":18,"properties":1117,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1118},{"VI":1065},{"title":1120},{"VI":1121},"Gerald Wolf",{"id":1123,"sortIndex":285,"researcher":18,"roles":1124,"affiliations":1125,"properties":1131},"da26389b-60d1-4517-baff-436f6661e013",[145],[1126],{"id":18,"sortIndex":19,"affiliation":1127,"properties":18},{"id":1045,"createTime":1046,"updateTime":1046,"relativeEntities":1128,"slug":18,"properties":1129,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1130},{"VI":1050},{"title":1132},{"VI":1133},"T.P.A. Devasagayam",{"url":1037,"publisher":1135,"properties":1157},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1136,"slug":10,"properties":1137,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":1140,"manageAffiliations":1141,"indexDatabases":1142,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":1138,"title":1139},{"VOID":13},{"EN":15},[],[],[1143,1150],{"id":78,"indexDatabase":1144,"url":91,"indexYears":92,"academicFieldIds":1149,"indexDatabaseRanking":98},{"id":80,"createTime":81,"updateTime":82,"relativeEntities":1145,"label":1146,"description":1147,"key":88,"publicationTags":1148,"standard":18},[],{"EN":85,"VI":85},{"EN":85,"VI":87},[90],[94,95,96,97],{"id":100,"indexDatabase":1151,"url":115,"indexYears":18,"academicFieldIds":1156,"indexDatabaseRanking":18},{"id":102,"createTime":103,"updateTime":104,"relativeEntities":1152,"label":1153,"description":1154,"key":111,"publicationTags":1155,"standard":18},[],{"EN":107,"VI":107},{"VI":109,"EN":110},[113,114],[117,118],{"volume":1158,"pages":1160},{"VOID":1159},"50",{"VOID":1161},"79-87","1999-01-01",1999,{"id":1165,"createTime":1166,"updateTime":1166,"relativeEntities":1167,"slug":18,"properties":1168,"entityType":136,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":1175,"fullTextUrl":18,"authors":1176,"publicationType":238,"publisherRelationship":1228,"citationCount":18,"citationInfo":18,"publishDate":1256,"publishYear":1257,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":269},"14762133-07ba-4279-bb44-0f13614ef9d5","2023-12-06T23:54:15.167+00:00",[],{"references":1169,"title":1171,"doi":1173},{"VOID":1170},"Henry, 1980, Comparative pharmacology of calcium antagonists: nifedipine, verapamil and diltiazem, Am. J. Cardiol., 46, 1047, 10.1016\u002F0002-9149(80)90366-5\nGrunwald, 1982, Painful edema, erythematous rash, and burning sensation due to nifedipine, Drug Intell. Clin. Pharm., 16, 492\nFisher, 1983, Nifedipine and erythromelalgia, Ann. Intern. Med., 98, 671, 10.7326\u002F0003-4819-98-5-671_2\nAlcalay, 1987, Cutaneous reactions to nifedipine, Dermatologica, 175, 191, 10.1159\u002F000248824\nThomas, 1986, Photosensitivity reactions associated with nifedipine, Br. Med. J., 292, 992\nGuarrera, 1990, Is nifedipine phototoxic?, Photodermatol. Photoimmunol. Photomed., 7, 25\nZenarola, 1991, Photodermatitis due to nifedipine: report of 2 cases, Dermatologica, 182, 196, 10.1159\u002F000247783\nMajeed, 1987, Spectrophotometric study of the photodecomposition kinetics of nifedipine, J. Pharm. Pharmacol., 39, 1044, 10.1111\u002Fj.2042-7158.1987.tb03160.x\nvan Henegouwen, 1991, (Systemic) phototoxicity of drugs and other xenobiotics, J. Photochem. Photobiol. B: Biol., 10, 183, 10.1016\u002F1011-1344(91)85002-X\nPietta, 1981, High-performance liquid chromatography of nifedipine, its metabolites and photodegradation products, J. Chromatogr., 210, 516, 10.1016\u002FS0021-9673(00)80344-1\nJakobsen, 1979, Gas chromatographic determination of nifedipine and one of its metabolites using electron capture detection, J. Chromatogr., 162, 81, 10.1016\u002FS0378-4347(00)82066-6\nSquella, 1990, Polarography as a technique for determining photodegradation in calcium antagonists, Bioelectrochem Bionerg., 23, 161, 10.1016\u002F0302-4598(90)85005-3\nEbel, 1978, Untersuchungen zur Analytik von Nifedipin unter besonderer Berucksichtigung der bei Lichtexposition entstehenden Umwandlungsprodukte, Arzneimforsch., Drug Res., 28, 2188\nTesta, 1979, GLC determination of nifedipine, a light sensitive drug, in plasma, Farmaco, Ed. Prat., 34, 463\nThoma, 1985, Untersuchungen zur Photoinstabilitat van Nifedipin; Zerset-zungskinetik and Reaktionmechanismus, Pharm. Ind., 47, 207\nThoma, 1985, Untersuchungen zur Photoinstabilitat van Nifedipin; Einfluss van Milieubedingungen, Pharm. Ind., 47, 319\nMorad, 1983, Rapid photochemical inactivation of Ca2+-antagonists shows that Ca2+ entry directly activates contraction in frog heart, Nature, 304, 635, 10.1038\u002F304635a0\nTeraoka, 1988, Quantitative design for photostabilization of nifedipine by using titanium dioxide and\u002For tartrazine as colourants in model film coating systems, J. Pharm. Pharmacol., 41, 293, 10.1111\u002Fj.2042-7158.1989.tb06459.x\nDaniels, 1965, A simple microbiological method for demonstrating phototoxic compounds, J. Invest. Dermatol., 44, 259, 10.1038\u002Fjid.1965.47\nHetherington, 1984, Photohaemolysis, Photodermatology, 1, 255\nMossman, 1983, Rapid calorimetric assay for cellular growth and survival: application to proliferation and cytotoxic assays, J. Immunol. Methods, 65, 55, 10.1016\u002F0022-1759(83)90303-4\nDuffy, 1987, Prediction of phototoxic potential using human A431 cells and mouse 3T3 cells, Mol. Toxicol, 1, 579\nNilsson, 1975, Primary mechanisms of erythrocyte photolysis induced by biological sensitizers and phototoxic drugs, Photochem. Photobiol., 22, 183, 10.1111\u002Fj.1751-1097.1975.tb06734.x\nSlater, 1963, Studies on succinate-tetrazolium reductase systems III. Points of coupling of four different tetrazolium salts, Biochim. Biophys. Acta, 77, 383, 10.1016\u002F0006-3002(63)90513-4\nOdar-Cederlof, 1990, Nifedipine as an antihypertensive drug in patients with renal failure—pharmacokinetics and effects, J. Intern. Med., 227, 329, 10.1111\u002Fj.1365-2796.1990.tb00168.x\nTucker, 1985, Study of nifedipine photodecomposition in plasma and whole blood using capillary gas—liquid chromatography, J. Chromatogr., 342, 193, 10.1016\u002FS0378-4347(00)84503-X",{"EN":1172},"In vitro phototoxicity of nifedipine: Sequential induction of toxic and non-toxic photoproducts with UVA radiation",{"VOID":1174},"10.1016\u002F1011-1344(92)85067-5","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002F1011134492850675",[1177,1192,1204,1216],{"id":1178,"sortIndex":195,"researcher":18,"roles":1179,"affiliations":1180,"properties":1189},"a033ec83-78ec-4b3f-a561-cf4d4b704c10",[145],[1181],{"id":18,"sortIndex":19,"affiliation":1182,"properties":18},{"id":1183,"createTime":1184,"updateTime":1184,"relativeEntities":1185,"slug":18,"properties":1186,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"6d9973ae-9445-4aff-af57-9063a0633ede","2023-12-31T07:26:47.358+00:00",[],{"title":1187},{"VI":1188},"Photobiology Unit, Ninewells Hospital and Medical School, Dundee DD1 9SY, UK",{"title":1190},{"VI":1191},"James Ferguson",{"id":1193,"sortIndex":19,"researcher":18,"roles":1194,"affiliations":1195,"properties":1201},"8444b19e-2ab9-49a1-9dbf-ea9a3e29744d",[145],[1196],{"id":18,"sortIndex":19,"affiliation":1197,"properties":18},{"id":1183,"createTime":1184,"updateTime":1184,"relativeEntities":1198,"slug":18,"properties":1199,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1200},{"VI":1188},{"title":1202},{"VI":1203},"Neil K. Gibbs",{"id":1205,"sortIndex":159,"researcher":18,"roles":1206,"affiliations":1207,"properties":1213},"bbfdbaab-21cb-4bb0-bd82-6485b2261082",[145],[1208],{"id":18,"sortIndex":19,"affiliation":1209,"properties":18},{"id":1183,"createTime":1184,"updateTime":1184,"relativeEntities":1210,"slug":18,"properties":1211,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1212},{"VI":1188},{"title":1214},{"VI":1215},"Nicola J. Traynor",{"id":1217,"sortIndex":143,"researcher":18,"roles":1218,"affiliations":1219,"properties":1225},"d5c1cb86-a26b-477d-b36a-d10565a3fdac",[145],[1220],{"id":18,"sortIndex":19,"affiliation":1221,"properties":18},{"id":1183,"createTime":1184,"updateTime":1184,"relativeEntities":1222,"slug":18,"properties":1223,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1224},{"VI":1188},{"title":1226},{"VI":1227},"Brian E. Johnson",{"url":1175,"publisher":1229,"properties":1251},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1230,"slug":10,"properties":1231,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":1234,"manageAffiliations":1235,"indexDatabases":1236,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":1232,"title":1233},{"VOID":13},{"EN":15},[],[],[1237,1244],{"id":78,"indexDatabase":1238,"url":91,"indexYears":92,"academicFieldIds":1243,"indexDatabaseRanking":98},{"id":80,"createTime":81,"updateTime":82,"relativeEntities":1239,"label":1240,"description":1241,"key":88,"publicationTags":1242,"standard":18},[],{"EN":85,"VI":85},{"EN":85,"VI":87},[90],[94,95,96,97],{"id":100,"indexDatabase":1245,"url":115,"indexYears":18,"academicFieldIds":1250,"indexDatabaseRanking":18},{"id":102,"createTime":103,"updateTime":104,"relativeEntities":1246,"label":1247,"description":1248,"key":111,"publicationTags":1249,"standard":18},[],{"EN":107,"VI":107},{"VI":109,"EN":110},[113,114],[117,118],{"volume":1252,"pages":1254},{"VOID":1253},"13",{"VOID":1255},"275-288","1992-05-01",1992,{"id":1259,"createTime":1260,"updateTime":1260,"relativeEntities":1261,"slug":18,"properties":1262,"entityType":136,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":1269,"fullTextUrl":18,"authors":1270,"publicationType":238,"publisherRelationship":1346,"citationCount":18,"citationInfo":18,"publishDate":1374,"publishYear":1375,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":269},"9a70c059-375c-4936-ba70-abb365b1f9b6","2024-01-05T23:53:31.307+00:00",[],{"references":1263,"title":1265,"doi":1267},{"VOID":1264},"Larsen, 1986, Bis-benzimidazole-appended binucleating porphyrin ligands: synthesis, characterization, and X-ray structure, J. Am. Chem. Soc., 108, 6950, 10.1021\u002Fja00282a020\nMichael, 1997, Effect of a chemical modification on the hydrated adenosine intermediate produced by adenosine deaminase and a model reaction for a potential mechanism of action of 5-aminoimidazole ribonucleotide carboxylase, J. Med. Chem., 40, 3336, 10.1021\u002Fjm970301s\nSzyszka, 1995, Halogenated benzimidazoles and benzotriazoles as selective inhibitors of protein kinases CK-I and CK-II from Saccharomyces cerevisiae and other sources, Biochem. Biophys. Res. Commun., 208, 418, 10.1006\u002Fbbrc.1995.1354\nPilch, 1996, Characterizing the DNA binding modes of a topoisomerase I-poisoning terbenzimidazole: evidence for both intercalative and minor groove binding properties, Drug Des. Discov., 13, 115\nWillis, 2010, Triple recognition of B-DNA by a neomycin–hoechst 33258–pyrene conjugate, Biochemistry, 49, 452, 10.1021\u002Fbi9016796\nClarke, 2003, Ruthenium metallopharmaceuticals, Coord. Chem. Rev., 236, 209, 10.1016\u002FS0010-8545(02)00312-0\nHartinger, 2006, From bench to bedside – preclinical and early clinical development of the anticancer agent imidazolium trans-[tetrachlorobis(1H-indazole)ruthenate(III)] (KP1019 or FFC14A), J. Inorg. Biochem., 100, 891, 10.1016\u002Fj.jinorgbio.2006.02.013\nSathyaraj, 2010, Synthesis, characterization and DNA binding studies of new ruthenium(II)bisterpyridine complexes, Eur. J. Med. Chem., 45, 284, 10.1016\u002Fj.ejmech.2009.10.008\nErkkila, 1999, Recognition and reaction of metallointercalators with DNA, Chem. Rev., 99, 2777, 10.1021\u002Fcr9804341\nMetcalfe, 2003, Kinetically inert transition metal complexes that reversibly bind to DNA, Chem. Soc. Rev., 32, 215, 10.1039\u002Fb201945k\nXiong, 1999, Synthesis, DNA-binding and DNA-mediated luminescence quenching of Ru(II) polypyridine complexes, Coord. Chem. Rev., 185, 711, 10.1016\u002FS0010-8545(99)00019-3\nBlasius, 2004, photoadducts of metallic compounds with nucleic acids – role played by the photoelectron transfer process and by the TAP and HAT ligands in the RuII complexes, Eur. J. Inorg. Chem., 2004, 3971, 10.1002\u002Fejic.200400489\nUma, 2005, Oxidative DNA cleavage mediated by a new copper (II) terpyridine complex: crystal structure and DNA binding studies, J. Inorg. Biochem., 99, 2299, 10.1016\u002Fj.jinorgbio.2005.08.011\nZhou, 2006, Crystal structure and DNA-binding studies of a new Cu(II) complex involving benzimidazole, Inorg. Chim. Acta, 359, 1200, 10.1016\u002Fj.ica.2005.11.003\nLi, 2007, DNA-binding and cleavage studies of novel binuclear copper(II) complex with 1,1′-dimethyl-2,2′-biimidazole ligand, J. Inorg. Biochem., 101, 283, 10.1016\u002Fj.jinorgbio.2006.10.004\nDong, 2011, Synthesis, crystal structure and DNA-binding properties of a new copper(II) complex with l-valine Schiff base and 1,10-phenanthroline, J. Mol. Struct., 986, 57, 10.1016\u002Fj.molstruc.2010.11.036\nAmes, 1993, Oxidants, antioxidants, and the degenerative diseases of aging, Proc. Natl. Acad. Sci. USA, 90, 7915, 10.1073\u002Fpnas.90.17.7915\nHorton, 1987, Lipid peroxidation and mechanisms of toxicity, Crit. Rev. Toxicol., 18, 27, 10.3109\u002F10408448709089856\nWang, 2006, Synthesis, characterization and the antioxidative activity of copper(II), zinc(II) and nickel(II) complexes with naringenin, Transit. Met. Chem., 31, 470, 10.1007\u002Fs11243-006-0015-3\nWu, 2009, Synthesis, crystal structure and electrochemical properties of the copper(II) complex with 1,3-bis(benzimidazol-2-yl)-2-oxopropane, Synth. React. Inorg. Met. Org. Nano. Met. Chem., 39, 406, 10.1080\u002F15533170903129802\nWu, 2010, Copper(II) supramolecular complex: synthesis, crystal structure, and electrochemical property, Z. Anorg. Allg. Chem., 636, 1397, 10.1002\u002Fzaac.200900454\nChen, 2011, 1,3-Bis(1H-benzimidazol-2-yl)-2-oxapropane, Acta Cryst., E65, o948\nWu, 2011, 1,3-Bis(1-benzyl-1H-benzimidazol-2-yl)-2-oxapropane, Acta Cryst., E65, o1014\nSatyanarayana, 1993, Tris(phenanthroline)ruthenium(II) enantiomer interactions with DNA: mode and specificity of binding, Biochemistry, 32, 2573, 10.1021\u002Fbi00061a015\nReichmann, 1954, A further examination of the molecular weight and size of desoxypentose nucleic acid, J. Am. Chem. Soc., 76, 3047, 10.1021\u002Fja01640a067\nKou, 2011, 1,3-Bis(1-methyl-1H-benzimidazol-2-yl)-2-oxapropane, Acta Cryst., E67, o1439\nBruker, APEX2 and SAINT, Bruker Axs, Inc., Madison, WI, USA, 2007.\nG.M. Sheldrick, SHELXTL, Siemens Analytical X-ray Instruments, Inc., Madison, WI, USA, 1996.\nPyle, 1989, Mixed-ligand complexes of ruthenium(II): factors governing binding to DNA, J. Am. Chem. Soc., 111, 3051, 10.1021\u002Fja00190a046\nWolf, 1987, Biochemistry, 26, 6392, 10.1021\u002Fbi00394a013\nBaguley, 1984, Polycyclic aromatic hydrocarbons physically intercalate into duplex regions of denatured DNA, Biochemistry, 23, 937, 10.1021\u002Fbi00300a022\nLakowicz, 1973, Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules, Biochemistry, 12, 4161, 10.1021\u002Fbi00745a020\nTan, 2008, Synthesis, structural characteristics, DNA binding properties and cytotoxicity studies of a series of Ru(III) complexes, J. Inorg. Biochem., 102, 1644, 10.1016\u002Fj.jinorgbio.2008.03.005\nWinterbourn, 1981, Hydroxyl radical production in body fluids. Roles of metal ions, ascorbate and superoxide, Biochem. J., 198, 125, 10.1042\u002Fbj1980125\nWinterbourn, 1979, Comparison of superoxide with other reducing agents in the biological production of hydroxyl radicals, Biochem. J., 182, 625, 10.1042\u002Fbj1820625\nGuo, 2005, The synthesis and antioxidant activity of the Schiff bases of chitosan and carboxymethyl chitosan, Bioorg. Med. Chem. Lett., 15, 4600, 10.1016\u002Fj.bmcl.2005.06.095\nBeauchamp, 1971, Superoxide dismutase: improved assays and an assay applicable to acrylamide gels, Anal. Biochem., 44, 276, 10.1016\u002F0003-2697(71)90370-8\nLuo, 1993, A study on the structure and properties of a new model compound of Cu(II)–Zn(II)–superoxide dismutase, J. Inorg. Biochem., 51, 655, 10.1016\u002F0162-0134(93)85037-9\nGeary, 1971, The use of conductivity measurements in organic solvents for the characterisation of coordination compounds, Coord. Chem. Rev., 7, 81, 10.1016\u002FS0010-8545(00)80009-0\nMcKee, 1985, Further insight into magnetostructural correlations in binuclear copper(II) species related to methemocyanin: X-ray crystal structure of 1,2-mu-nitrito complex, Inorg. Chem., 24, 2914, 10.1021\u002Fic00213a009\nThompson, 1977, Cobalt(II) and zinc(II) complexes of the ‘tripod’ ligand tris(2-benzimidazylmethyl)amine. Some five-coordinate derivatives and some with mixed stereochemistries, Can. J. Chem., 55, 878, 10.1139\u002Fv77-122\nAddison, 1981, Copper complexes of the “tripod” ligand tris(2-benzimidazolylmethyl)amine: five- and six-coordinate copper(II) derivatives and some copper(I) derivatives, Inorg. Chem., 20, 103, 10.1021\u002Fic50215a024\nKoppenol, 1986, Catalysis of superoxide dismutation by manganese aminopolycarboxylate complexes, Arch. Biochem. Biophys., 251, 594, 10.1016\u002F0003-9861(86)90368-1\nWu, 2010, A V-shaped ligand 2,6-bis(2-benzimidazolyl)pyridine and its picrate Mn(II) complex: synthesis, crystal structure and DNA-binding properties, Eur. J. Med. Chem., 45, 5324, 10.1016\u002Fj.ejmech.2010.08.055\nZhang, 2004, DNA-binding and photoactivated enantiospecific cleavage of chiral polypyridyl ruthenium(II) complexes, J. Inorg. Biochem., 98, 1405, 10.1016\u002Fj.jinorgbio.2004.05.007\nIndumathy, 2010, Biimidazole containing cobalt(III) mixed ligand complexes: crystal structure and photonuclease activity, Dalton Trans., 39, 2087, 10.1039\u002Fb913464f\nLepecq, 1967, A fluorescent complex between ethidium bromide and nucleic acids: physical–chemical characterization, J. Mol. Biol., 27, 87, 10.1016\u002F0022-2836(67)90353-1\nZhou, 2006, Synthesis, crystal structure and DNA binding studies of Zn(II) complex with 1,3-bis(benzimidazol-2-yl)-2-oxapropane, Acta Chim. Sin., 64, 793\nSatyanarayana, 1992, Neither DELTA-nor LAMBDA-tris(phenanthroline)ruthenium(II) binds to DNA by classical intercalation, Biochemistry, 31, 9319, 10.1021\u002Fbi00154a001\nSatyanarayana, 1993, Tris(phenanthroline)ruthenium(II) enantiomer interactions with DNA: mode and specificity of binding, Biochemistry, 32, 2573, 10.1021\u002Fbi00061a015\nLi, 2008, Synthesis, characterization, antioxidant activity and DNA-binding studies of two rare earth(III) complexes with naringenin-2-hydroxy benzoyl hydrazone ligand, Eur. J. Med. Chem., 43, 1688, 10.1016\u002Fj.ejmech.2007.10.006\nSchepetkin, 2006, Decomposition of reactive oxygen species by copper(II) bis(1-pyrazolyl)methane complexes, J. Biol. Inorg. Chem., 11, 499, 10.1007\u002Fs00775-006-0101-1\nPatel, 2010, SOD mimic activity, DNA binding and in-vitro antibacterial studies of drug based copper(II) complexes, Inorg. Chem. Commun., 13, 618, 10.1016\u002Fj.inoche.2010.03.001\nWeder, 2002, Copper complexes of non-steroidal anti-inflammatory drugs: an opportunity yet to be realized, Coord. Chem. Rev., 232, 95, 10.1016\u002FS0010-8545(02)00086-3\nSuksrichavalit, 2008, Copper complexes of nicotinic–aromatic carboxylic acids as superoxide dismutase mimetics, Molecules, 13, 3040, 10.3390\u002Fmolecules13123040\nBelichi-Ferrari, 1999, Synthesis, structural characterization and biological activity of helicin thiosemicarbazone monohydrate and a copper(II) complex of salicylaldehyde thiosemicarbazone, Inorg. Chim. Acta, 286, 134, 10.1016\u002FS0020-1693(98)00383-1\nDevereux, 2007, J. Inorg. Biohem., 101, 881, 10.1016\u002Fj.jinorgbio.2007.02.002",{"EN":1266},"A V-shaped ligand 1,3-bis(1-methylbenzimidazol-2-yl)-2-oxapropane and its Cu(II) complex: Synthesis, crystal structure, antioxidation and DNA-binding properties",{"VOID":1268},"10.1016\u002Fj.jphotobiol.2011.09.001","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1011134411001990",[1271,1286,1298,1310,1322,1334],{"id":1272,"sortIndex":19,"researcher":18,"roles":1273,"affiliations":1274,"properties":1283},"a47e2e46-5918-4691-a72a-ea932c9762b3",[145],[1275],{"id":18,"sortIndex":19,"affiliation":1276,"properties":18},{"id":1277,"createTime":1278,"updateTime":1278,"relativeEntities":1279,"slug":18,"properties":1280,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"163e55f2-7ff9-472f-98fb-91a5f3a1be50","2024-01-15T06:20:19.488+00:00",[],{"title":1281},{"VI":1282},"School of Chemical and Biological Engineering, Lanzhou Jiaotong University, Lanzhou 730070, PR China",{"title":1284},{"VI":1285},"Huilu Wu",{"id":1287,"sortIndex":367,"researcher":18,"roles":1288,"affiliations":1289,"properties":1295},"2050a88c-140a-4011-bf5f-3ebe1b2b5899",[145],[1290],{"id":18,"sortIndex":19,"affiliation":1291,"properties":18},{"id":1277,"createTime":1278,"updateTime":1278,"relativeEntities":1292,"slug":18,"properties":1293,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1294},{"VI":1282},{"title":1296},{"VI":1297},"Jingkun Yuan",{"id":1299,"sortIndex":195,"researcher":18,"roles":1300,"affiliations":1301,"properties":1307},"d2af699d-9657-4991-a0e2-4e37d3bf2680",[145],[1302],{"id":18,"sortIndex":19,"affiliation":1303,"properties":18},{"id":1277,"createTime":1278,"updateTime":1278,"relativeEntities":1304,"slug":18,"properties":1305,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1306},{"VI":1282},{"title":1308},{"VI":1309},"Bin Liu",{"id":1311,"sortIndex":159,"researcher":18,"roles":1312,"affiliations":1313,"properties":1319},"4b63f8d1-1cae-4b92-a6c6-21eb1b7b4960",[145],[1314],{"id":18,"sortIndex":19,"affiliation":1315,"properties":18},{"id":1277,"createTime":1278,"updateTime":1278,"relativeEntities":1316,"slug":18,"properties":1317,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1318},{"VI":1282},{"title":1320},{"VI":1321},"Fan Kou",{"id":1323,"sortIndex":143,"researcher":18,"roles":1324,"affiliations":1325,"properties":1331},"e0853cfd-bfe0-4b38-a94c-3ae096ff8776",[145],[1326],{"id":18,"sortIndex":19,"affiliation":1327,"properties":18},{"id":1277,"createTime":1278,"updateTime":1278,"relativeEntities":1328,"slug":18,"properties":1329,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1330},{"VI":1282},{"title":1332},{"VI":1333},"Fei Jia",{"id":1335,"sortIndex":285,"researcher":18,"roles":1336,"affiliations":1337,"properties":1343},"58e4f72e-da89-4ec9-90f5-28dca37151f8",[145],[1338],{"id":18,"sortIndex":19,"affiliation":1339,"properties":18},{"id":1277,"createTime":1278,"updateTime":1278,"relativeEntities":1340,"slug":18,"properties":1341,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1342},{"VI":1282},{"title":1344},{"VI":1345},"Ying Bai",{"url":1269,"publisher":1347,"properties":1369},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1348,"slug":10,"properties":1349,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":1352,"manageAffiliations":1353,"indexDatabases":1354,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":1350,"title":1351},{"VOID":13},{"EN":15},[],[],[1355,1362],{"id":78,"indexDatabase":1356,"url":91,"indexYears":92,"academicFieldIds":1361,"indexDatabaseRanking":98},{"id":80,"createTime":81,"updateTime":82,"relativeEntities":1357,"label":1358,"description":1359,"key":88,"publicationTags":1360,"standard":18},[],{"EN":85,"VI":85},{"EN":85,"VI":87},[90],[94,95,96,97],{"id":100,"indexDatabase":1363,"url":115,"indexYears":18,"academicFieldIds":1368,"indexDatabaseRanking":18},{"id":102,"createTime":103,"updateTime":104,"relativeEntities":1364,"label":1365,"description":1366,"key":111,"publicationTags":1367,"standard":18},[],{"EN":107,"VI":107},{"VI":109,"EN":110},[113,114],[117,118],{"volume":1370,"pages":1372},{"VOID":1371},"105",{"VOID":1373},"190-197","2011-12-01",2011,{"id":1377,"createTime":1378,"updateTime":1379,"relativeEntities":1380,"slug":1381,"properties":1382,"entityType":136,"verifyStatus":137,"verifyTime":1379,"verifyNote":138,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":1389,"fullTextUrl":18,"authors":1390,"publicationType":238,"publisherRelationship":1406,"citationCount":18,"citationInfo":18,"publishDate":1434,"publishYear":1375,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":269},"6f19e165-e2fe-4200-aea3-c9f982c89a0d","2023-12-20T14:19:41.424+00:00","2025-02-15T23:53:26.865+00:00",[],"Recent-theoretical-studies-of-water-oxidation-in-photosystem-II",{"references":1383,"title":1385,"doi":1387},{"VOID":1384},"Ferreira, 2004, Science, 303, 1831, 10.1126\u002Fscience.1093087\nLoll, 2005, Nature, 438, 1040, 10.1038\u002Fnature04224\nGuskov, 2009, J. Nat. Struct. Biol., 16, 334, 10.1038\u002Fnsmb.1559\nYano, 2006, Science, 314, 821, 10.1126\u002Fscience.1128186\nHaumann, 2005, Biochemistry, 44, 1894, 10.1021\u002Fbi048697e\nYano, 2005, Proc. Natl. Acad. Sci. USA, 102, 12047, 10.1073\u002Fpnas.0505207102\nSiegbahn, 2008, Chem. Eur. J., 27, 8290, 10.1002\u002Fchem.200800445\nSproviero, 2008, Am. Chem. Soc., 130, 3428, 10.1021\u002Fja076130q\nSiegbahn, 2009, Acc. Chem. Res., 42, 1871, 10.1021\u002Far900117k\nP.E.M. Siegbahn, in: T.J. Wydrzynski, W. Hillier (Eds.), Molecular Solar Fuels, RSC Publishing, Cambridge, England, in press.\nSiegbahn, 2009, Dalton Trans., 10063, 10.1039\u002Fb909470a\nBabcock, 1995, vol. 2, 209\nHaumann, 1999, Biochemistry, 38, 1258, 10.1021\u002Fbi981557i\nSiegbahn, 2010, Chem. Rev., 110, 7040, 10.1021\u002Fcr100070p\nGrimme, 2006, Chem. Phys., 124, 034108\nSchwabe, 2007, Phys. Chem. Chem. Phys., 9, 3397, 10.1039\u002Fb704725h\nSiegbahn, 2010, Chem. Theory Comput., 6, 2040, 10.1021\u002Fct100213e\nBecke, 1993, Chem. Phys., 98, 5648\nReiher, 2001, Theor. Chem. Acc., 107, 48, 10.1007\u002Fs00214-001-0300-3\nSiegbahn, 2006, J. Biol. Inorg. Chem., 11, 695, 10.1007\u002Fs00775-006-0137-2\nJaguar 5.5, L.L.C. Schrödinger, Portland, OR, 1991–2003.\nM.J. Frisch, et al., Gaussian 03, Revision B.03. Gaussian Inc., Pittsburg, PA, 2003.\nSiegbahn, 2008, 57\nSiegbahn, 1999, J. Am. Chem. Soc., 121, 117, 10.1021\u002Fja982290d\nSiegbahn, 2000, Inorg. Chem., 39, 2923, 10.1021\u002Fic9911872\nSiegbahn, 2005, Photochem. Photobiol. Sci., 4, 1035, 10.1039\u002Fb506746b\nDau, 2007, Biochim. Biophys. Acta, 1767, 472, 10.1016\u002Fj.bbabio.2007.02.022\nSiegbahn, 2006, Chem. Eur. J., 12, 9217, 10.1002\u002Fchem.200600774\nLundberg, 2005, Chem. Phys. Lett., 44, 3311\nLundberg, 2005, J. Phys. Chem. B, 109, 10513, 10.1021\u002Fjp051116q\nKulik, 2007, J. Am. Chem. Soc., 129, 13421, 10.1021\u002Fja071487f\nMessinger, 2008, vol. 9, 291\nSiegbahn, 2009, J. Am. Chem. Soc., 131, 18238, 10.1021\u002Fja908712a\nDau, 2008, Philos. Trans. Roy. Soc. B, 363, 1237, 10.1098\u002Frstb.2007.2220\nDiner, 2001, Biochim. Biophys. Acta, 1503, 147, 10.1016\u002FS0005-2728(00)00220-6\nRappaport, 2001, Biochim. Biophys. Acta, 1503, 246, 10.1016\u002FS0005-2728(00)00228-0\nHaumann, 2005, Science, 310, 1019, 10.1126\u002Fscience.1117551\nHillier, 2004, Phys. Chem. Chem. Phys., 6, 4882, 10.1039\u002Fb407269c\nSuzuki, 2008, Biochemistry, 47, 11024, 10.1021\u002Fbi801580e\nRenger, 1997, Physiol. Plantarum, 100, 828, 10.1111\u002Fj.1399-3054.1997.tb00009.x\nFörster, 1985, Photochem. Photobiol., 41, 183, 10.1111\u002Fj.1751-1097.1985.tb03469.x\nX. Li, E.M. Sproviero, U. Ryde, P.E.M. Siegbahn, V.S. Batista, G. Chen, submitted for publication.\nSchinzel, 2010, Chem. Eur. J., 16, 10424, 10.1002\u002Fchem.201000584\nSiegbahn, 2008, Proc. Roy. Soc., 363, 1221",{"EN":1386},"Recent theoretical studies of water oxidation in photosystem II",{"VOID":1388},"10.1016\u002Fj.jphotobiol.2011.01.014","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1011134411000182",[1391],{"id":1392,"sortIndex":19,"researcher":18,"roles":1393,"affiliations":1394,"properties":1403},"8ae5209d-7eca-4429-b507-cfd7eab6d06f",[145],[1395],{"id":18,"sortIndex":19,"affiliation":1396,"properties":18},{"id":1397,"createTime":1398,"updateTime":1398,"relativeEntities":1399,"slug":18,"properties":1400,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"b0e2baf9-e70b-4159-974e-38a3abe5568f","2023-12-20T14:19:41.438+00:00",[],{"title":1401},{"VI":1402},"Department of Physics, ALBA NOVA and Department of Biochemistry and Biophysics, Arrhenius Laboratory, Stockholm University, SE-106 91 Stockholm, Sweden",{"title":1404},{"VI":1405},"Per E.M. Siegbahn",{"url":1389,"publisher":1407,"properties":1429},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1408,"slug":10,"properties":1409,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":1412,"manageAffiliations":1413,"indexDatabases":1414,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":1410,"title":1411},{"VOID":13},{"EN":15},[],[],[1415,1422],{"id":78,"indexDatabase":1416,"url":91,"indexYears":92,"academicFieldIds":1421,"indexDatabaseRanking":98},{"id":80,"createTime":81,"updateTime":82,"relativeEntities":1417,"label":1418,"description":1419,"key":88,"publicationTags":1420,"standard":18},[],{"EN":85,"VI":85},{"EN":85,"VI":87},[90],[94,95,96,97],{"id":100,"indexDatabase":1423,"url":115,"indexYears":18,"academicFieldIds":1428,"indexDatabaseRanking":18},{"id":102,"createTime":103,"updateTime":104,"relativeEntities":1424,"label":1425,"description":1426,"key":111,"publicationTags":1427,"standard":18},[],{"EN":107,"VI":107},{"VI":109,"EN":110},[113,114],[117,118],{"volume":1430,"pages":1432},{"VOID":1431},"104",{"VOID":1433},"94-99","2011-07-01"]