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Here we reportidentification and characterization of the Drosophila Plenty of SH3s (DPOSH) gene,a candidate that might be associated with theextended longevity phenotype. DPOSHencodes a protein containing a RING fingerdomain and four SH3 domains. We showed thatneural-specific overexpression of DPOSHcould extend the mean longevity of adult fliesby 14% at 25 °C without affectingviability or morphology. In contrast, forcedexpression of DPOSH in developingimaginal discs produced various phenotypesincluding lethality and morphological defectssuch as loss of crossvein, notched wing, anddisordered hair polarity. Puckered, atarget gene of JNK\u002FSAPK pathway, was activatedby overexpression of DPOSH and the forcedexpression phenotypes were suppressed byintroducing a mutation of Drosophila JNK(bsk) or JNKK (hep),suggesting that the JNK\u002FSAPK signaling pathwayis one of the critical elements in thedetermination of longevity.",{"EN":192},"Neural-specific overexpression of Drosophila Plenty of SH3s (DPOSH) extends the longevity of adult flies",{"VOID":194},"[]",{"VOID":196},"Adachi-Yamada T, Fujimura-Kamada K, Nishida Y and Matsumoto K (1999) Distortion of proximodistal information causes JNKdependent apoptosis in Drosophila wing. Nature 400: 166-169\nAdams MD, Celniker SE, Holt RA, Evans CA, Gocayne JD et al. (2000) The genome sequence of Drosophila melanogaster. Science 287: 2185-2195\nBerberich I, Shu G, Siebelt F, Woodgett JR, Kyriakis JM and Clark EA (1996) Cross-linking CD40 on B cells preferentially induces stress-activated protein kinases rather than mitogen-activated protein kinases. 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Blood 94: 853-863\nNishina H, Fischer KD, Radvanyi L, Shahinian A, Hakem R, Rubie EA, Bernstein A, Mak TW, Woodgett JR and Penninger JM (1997) Stress-signalling kinase Sek1 protects thymocytes from apoptosis mediated by CD95 and CD3. Nature 385: 350-353\nOkada S, Kao AW, Ceresa BP, Blaikie P, Margolis B and Pessin JE (1997) The 66-kDa Shc isoform is a negative regulator of the epidermal growth factor-stimulated mitogen-activated protein kinase pathway. J Biol Chem 272: 28042-28049\nParkes TL, Elia AJ, Dickinson D, Hilliker AJ, Phillips JP and Boulianne GL (1998) Extension of Drosophila lifespan by overexpression of human SOD1 in motorneurons. Nat Genet 19: 171-174\nRiesgo-Escovar JR, Jenni M, Fritz A and Hafen E (1996) The Drosophila Jun-N-terminal kinase is required for cell morphogenesis but not for DJun-dependent cell fate specification in the eye. Genes Dev 10: 2759-2768\nRubin GM and Spradling AC (1982) Genetic transformation of Drosophila with transposable element vectors. 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risk increases in elderly, therefore, the understanding of the genetic predisposition of hypercoagulability could make the difference in the prevention of venous and\u002For arterial thrombotic events. Laboratory evaluation of hyperfibrinogenemia, increased Factor VII levels, antiphospholipid antibodies presence and hyperhomocysteinemia are considered to have a consistent high predictivity for arterial thrombophilic diseases. Anyway, a large debate exists on the validity of testing Leiden Factor V (FV) G1691A and\u002For prothrombin (FII) G20210A polymorphisms in patients affected by arterial thrombotic diseases, despite of the several observations described. Here we report data strongly suggesting that at least the FII G20210A polymorphism might be considered an important risk factor for acute myocardial infarction in aged patients (55–80 years old). On the other hand, in spite of a not different genotypic and allelic distribution for the Leiden FV G1691A mutation, the presence of one or both the two polymorphisms is significantly higher among cases than in controls. In conclusion, our data suggest that FII G20210A and\u002For Leiden FV might be involved as risk factor for arterial disorders in about 5% of old subjects, justifying the opportunity of a genetic screening and an eventual preventive treatment, in particular in old subjects in which other and major risk factors, as hypertension and atherosclerosis, are detected.",{"EN":344},"Analysis of polymorphisms Leiden Factor V G1691A and prothrombin G20210A as risk factors for acute myocardial infarction",{"VOID":194},{"VOID":347},"Billeci AM, Agnelli G, Caso V (2009) Stroke pharmacogenomics. Expert Opin Pharmacother 10(18):2947–2957\nDe Stefano V, Leone G (1995) Resistance to activated protein C due to mutated factor V as a novel cause of inherited thrombophilia. Haematologica 80(4):344–356\nDe Stefano V, Finazzi G, Mannucci PM (1996) Inherited thrombophilia: pathogenesis, clinical syndromes, and management. Blood 1 87(9):3531–3544\nForte GI, Scola L, Vaccarino L, Sanacore M, Palmeri M, La Piana S, Pipitone M, Grimaudo S, Caruso C (2009) Analysis of FV-Leiden and Facor II G20210A SNP frequencies in a group of Sicilian nonagenarians. J Nutr Health Aging 13(1):S378\nFranco RF, Trip MD, ten Cate H, van den Ende A, Prins MH, Kastelein JJ, Reitsma PH (1999) The 20210 G → A mutation in the 3′ untranslated region of the prothrombin gene and the risk for arterial thrombotic disease. Br J Haematol 104:50–54\nGemmati D, Serino ML, Moratelli S, Tognazzo S, Ongaro A, Scapoli GL (2001) Coexistence of factor V G1691A and factor II G20210A gene mutations in a thrombotic family is associated with recurrence and early onset of venous thrombosis. Haemostasis 31(2):99–105\nKahn M (2003) Hypercoagulability as a cause of stroke in adults. South Med J 96:350–353\nKim RJ, Becker RC (2003) Association between factor V Leiden, prothrombin G20210A, and methylenetetrahydrofolate reductase C677T mutations and events of the arterial circulatory system: a meta-analysis of published studies. Am Heart J 146(6):948–957\nLane DA, Mannucci PM, Bauer KA, Bertina RM, Bochkov NP, Boulyjenkov V, Chandy M, Dahlbäck B, Ginter EK, Miletich JP, Rosendaal FR, Seligsohn U (1996) Inherited thrombophilia. Thromb Haemost 76(5):651–662\nLio D, Candore G, Crivello A, Scola L, Colonna-Romano G, Cavallone L, Hoffmann E, Caruso M, Licastro F, Caldarera CM, Branzi A, Franceschi C, Caruso C (2004) Opposite effects of interleukin 10 common gene polymorphisms in cardiovascular diseases and in successful ageing: genetic background of male centenarians is protective against coronary heart disease. J Med Genet 41(10):790–794\nListì F, Caruso M, Incalcaterra E, Hoffmann E, Caimi G, Balistreri CR, Vasto S, Scafidi V, Caruso C, Candore G (2008) Pro-inflammatory gene variants in myocardial infarction and longevity: implications for pharmacogenomics. Curr Pharm Des 14(26):2678–2685\nMari D, Coppola R, Provenzano R (2008) Hemostasis factors and aging. Exp Gerontol 43(2):66–73\nMazoyer E, Ripoll L, Gueguen R, Tiret L, Collet JP, dit Sollier CB, Roussi J, Drouet L (2009) Prevalence of factor V Leiden and prothrombin G20210A mutation in a large French population selected for nonthrombotic history: geographical and age distribution. Blood Coagul Fibrinolysis 20(7):503–510\nMiller SA, Dykes DD, Polesky HF (1988) A simple salting out procedure for extracting DNA from human nucleated cells. Nucl Acid Res 16:1215–1220\nMiller GJ, Bauer KA, Barzegar S, Cooper JA, Rosenberg RD (1996) Increased activation of the hemostatic system in men at high risk of fatal coronary heart disease. Thromb Haemost 75:767–771\nOzmen F, Ozmen MM, Ozalp N, Akar N (2009) The prevalence of factor V (G1691A), MTHFR (C677T) and PT (G20210A) gene mutations in arterial thrombosis. Ulus Travma Acil Cerrahi Derg 15(2):113–119\nPeetz D, Schweigert R, Jachmann N, Post F, Schinzel H, Lackner KJ (2006) Method comparison of cardiac marker assays on PATHFAST, StratusCS, AxSYM, Immulite 2000, triage, elecsys and cardiac reader. Clin Lab 52(11–12):605–614\nPoort SR, Rosendaal FR, Reitsma PH, Bertina RM (1996) A common genetic variation in the 3′-untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increase in venous thrombosis. Blood 88:3698–3703\nRidker PM, Hennekens CH, Lindpaintner K, Stampfer MJ, Eisenberg PR, Miletich JP (1995) Mutation in the gene coding for coagulation factor V and the risk of myocardial infarction, stroke, and venous thrombosis in apparently healthy men. N Engl J Med 332(14):912–917\nRidker PM, Hennekens CH, Miletich JP (1999) G20210A mutation in prothrombin gene and risk of myocardial infarction, stroke, and venous thrombosis in a large cohort of US men. Circulation 99(8):999–1004\nRusso C, Girelli D, Olivieri O, Guarini P, Manzato F, Pizzolo F, Zaia B, Mazzucco A, Corrocher R (2001) G20210A prothrombin gene polymorphism and prothrombin activity in subjects with or without angiographically documented coronary artery disease. Circulation 103:2436–2440\nSoare AM, Popa C (2010) Deficiencies of proteins C, S and antithrombin and factor V Leiden and the risk of ischemic strokes. J Med Life 3(3):235–238\nTesta S, Antonucci G, Intra E, Martini G, Pedrini S, Alatri A, Bader R, Manzato F (2004) Gli screening per trombofilia. Riv Med Lab—JLM 5(2):118\nTripodi A, Mannucci PM (2001) Laboratory investigation of thrombophilia. Clin Chem 47(9):1597–1606\nVan Cott E, Laposata M, Prins MH (2002) Laboratory evaluation of hypercoagulability with venous or arterial thrombosis. Arch Pathol Lab Med 126:1281–1295\nSoo L, Davidson P (2007) Laboratory testing for thrombophilia in arterial thrombosis. 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Morbidity associated with age-related delayed wound healing imposes an enormous social and financial burden; unless improved wound care strategies are developed the projected relative and absolute increase in the elderly population will further exacerbate this problem. In recent years insight has been gained into the impact of ageing on cellular and tissue responses, resulting from impaired cytokine signal transduction, unchecked inflammation, an altered balance of protein synthesis and degradation, and subsequent downstream effects on the rate and quality of the wound healing response. Further understanding of the complex interaction between the ageing cell and its microenvironment is essential in order to develop focussed therapeutic strategies to improve healing in the elderly.",{"EN":553},"Ageing and wound healing",{"VOID":555},"[\"8534457541371010736\"]",{"VOID":557},"Aimes RT and Quigley JP (1995) Matrix metalloprotease 2 is an interstitial collagenase. J Biol Chem 270: 5872-5876\nAlbini A, Pontz B, Pulz M, Allavena G, Mensing H and Muller PK (1988) decline of fibroblast chemotaxis with the age of donor and cell passage number. Coll Relat Res 8: 23-37\nArbogast BW, Berry DL and Newell CL (1984) Injury of arterial endothelial cells in diabetic, sucrose-fed and aged rats. Atherosclerosis 51: 31-45\nAshcroft GS, Horan MA and Ferguson MWJ (1997a) The effects of ageing on wound healing: immunolocalisation of growth factors and their receptors in a murine incisional model. J Anat 190: 351-365\nAshcroft GS, Horan MA and Ferguson MWJ (1997b) Ageing is associated with reduced deposition of specific extracellular matrix components, an up-regulation of angiogenesis, and an altered inflammatory response in a murine incisional wound healing model. 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J Invest Derm 91: 440-445\nHerrick S, Ashcroft GS, Ireland G, Horan M, McCollum C and Ferguson M (1996) Up-regulation of elastase in acute wounds of healthy aged humans and chronic venous leg ulcers is associated with matrix degradation. Lab Invest 77: 281-288\nHolm-Pederson P and Zederfeldt B (1971) Strength development of skin incisions in young and old rats. Scand J Plast Rec Surg 5: 7-12\nHolt DR, Kirk SJ, Regan MC, Hurson M, Lindblad WJ and Barbul A (1992) Effect of age on wound healing in healthy human beings. Surgery 112: 293-298\nIiyama M, Shimada Y, Kita T and Ito H (1992) Effect of aging on macrophage adherence to extracellular matrix proteins. Mech Aging Dev 66: 149-158\nKatsuda S, Okada Y, Okada Y, Imai K and Nakanishi I (1994) matrix metalloproteinase-9 can degrade arterial elastin. Am J Pathol 145: 1208-1218\nKhorramizadeh MR, Tredget EE, Telasky C, Shen Q and Ghahary A (1999) Aging differentially modulates the expression of collagen and collagenase in dermal fibroblasts. Mol Cell Biochem 194: 99-108\nKondo H, Nomaguchi TA and Yonezawa Y (1989) Effects of serum from human subjects of different ages on migration in vitro of human fibroblasts. Mech Aging Dev 47: 25-37\nKramer R, Fuh G, Bensch KG and Karasek M (1985) Synthesis of extracellular matrix glycoproteins by cultured microvascular endothelial cells isolated from the dermis of neonatal and adult skin. J Cell Physiol 123: 1-9\nKurban RS and Bhavan J (1990) Histologic changes in skin associated with aging. J Derm Surg Oncol 16: 908-914\nKurkinen M, Vaheri A, Roberts P and Stenman S (1980) Sequential appearance of fibronectin and collagen in experimental granulation tissue. Lab Invest 43: 47-51\nLipschitz DA and Udupa K (1986) Influence of aging and protein deficiency on neutrophil function. 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J Vasc Surg 30: 734-743\nMogford J, Tawil N, Chen A, Gies D, Xia Y and Mustoe TA (2002) Effect of age and hypoxia on TGF beta1 receptor expression and signal transduction in human dermal fibroblasts: impact on cell migration. J Cell Physiol 190: 259-265\nMontagna W and Carlisle K (1990) Structural changes in ageing skin. Br J Derm 122: 61-70\nMuggleton-Harris A, Reisert PS and Burghoff RL (1982) In vitro characterisation of the response to a stimulus (wounding) with regard to ageing in human skin fibroblasts. Mech Aging Dev 19: 37-43\nPeacocke M, Yaar M and Gilchrest BA (1989) Interferon and the epidermis: implications for cellular senescence. Exp Gerontol 24: 415-421\nPienta KJ and Coffey DS (1990) characterisation of the subtypes of cell motility in ageing human skin fibroblasts. Mech Aging Dev 56: 99-105\nPieraggi MJ, Bouissou H, Angelier C, Uhart D, Magnol J and Kokolo J (1985) Le fibroblaste. 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J Cell Physiol 153: 450-459\nVande Berg J, Rudolph R, Hollan C and Haywood-Reid P (1998) Fibroblast senescence in pressure ulcers. Wound Repair Regen 6: 38-49\nVitellaro-Zuccarello L, Cappelletti S, Dal Pozzo Rossi V and Sari-Gorla M (1994) Stereological analysis of collagen and elastic fibers in the normal human dermis: variability with age, sex, and body region. Anat Rec 238: 153-162\nWahl SM, Hunt DA, Wakefield L, McCartney-Francis N, Wahl LM, Roberts AB and Sporn MB (1987) Transforming growth factor type beta induces monocyte chemotaxis and growth factor production. PNAS (USA) 84: 5788-5792\nWerner S, Breeden M, Hubner G, Greenhalgh DG and Longaker M (1994) Induction of keratinocyte growth factor expression is reduced and delayed during wound healing in the genetically diabetic mouse. J Invest Derm 103: 469-473\nWysocki A, Staiano-Coico L and Grinnell F (1993) wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP-9. 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Mech Aging Dev 47: 65-75",{"VOID":559},"10.1023\u002FA:1021399228395","2024-05-16T15:07:23.677+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1023\u002FA:1021399228395",[563,578,593],{"id":564,"sortIndex":22,"researcher":21,"roles":565,"affiliations":566,"properties":575,"displayName":577,"givenName":21,"familyName":21},"09bd546e-6c27-410e-b933-a5cd6f8e0500",[208],[567],{"id":568,"sortIndex":22,"affiliation":569,"properties":21},"e63097f8-9d4f-45b5-89ac-c0e189be41cb",{"id":568,"createTime":21,"updateTime":21,"relativeEntities":570,"slug":21,"properties":571,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":574,"statistic":21},[],{"title":572},{"VI":573},"School of Biological Sciences, 3.239 Stopford Building, University of Manchester, Oxford Road, Manchester, UK",[],{"title":576},{"VI":577},"Gillian S. Ashcroft",{"id":579,"sortIndex":223,"researcher":21,"roles":580,"affiliations":581,"properties":588,"displayName":590,"givenName":21,"familyName":21},"a0efa43a-fa73-4ced-ba28-c811eee4b681",[208],[582],{"id":568,"sortIndex":22,"affiliation":583,"properties":21},{"id":568,"createTime":21,"updateTime":21,"relativeEntities":584,"slug":21,"properties":585,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":587,"statistic":21},[],{"title":586},{"VI":573},[],{"title":589,"gsAuthor":591},{"VI":590},"Stuart J. Mills",{"VOID":592},"[\"wgouwBcAAAAJ\"]",{"id":594,"sortIndex":237,"researcher":21,"roles":595,"affiliations":596,"properties":603,"displayName":605,"givenName":21,"familyName":21},"39f80e64-2fb9-4bb2-9006-21d3c1ced1f1",[208],[597],{"id":568,"sortIndex":22,"affiliation":598,"properties":21},{"id":568,"createTime":21,"updateTime":21,"relativeEntities":599,"slug":21,"properties":600,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":602,"statistic":21},[],{"title":601},{"VI":573},[],{"title":604},{"VI":605},"Jason J. Ashworth",{"url":561,"publisher":607,"properties":657},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":608,"slug":10,"properties":609,"entityType":19,"verifyStatus":20,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":22,"subjectFields":613,"manageAffiliations":626,"indexDatabases":637,"url":21,"thumbnailPath":21,"statistic":652,"gsStatistic":21,"type":177,"analyzePriority":21},[],{"issn":610,"title":611,"eissn":612},{"VOID":15},{"EN":10},{"VOID":13},[614,618,622],{"id":25,"createTime":21,"updateTime":21,"relativeEntities":615,"label":616,"description":617,"parentId":21,"standard":21,"scholarHubFieldId":21},[],{"EN":28},{},{"id":31,"createTime":21,"updateTime":21,"relativeEntities":619,"label":620,"description":621,"parentId":21,"standard":21,"scholarHubFieldId":21},[],{"EN":34},{},{"id":37,"createTime":21,"updateTime":21,"relativeEntities":623,"label":624,"description":625,"parentId":21,"standard":21,"scholarHubFieldId":21},[],{"EN":40},{},[627,632],{"id":44,"createTime":21,"updateTime":21,"relativeEntities":628,"slug":21,"properties":629,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":631,"statistic":21},[],{"title":630},{"EN":48},[50],{"id":52,"createTime":21,"updateTime":21,"relativeEntities":633,"slug":21,"properties":634,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":636,"statistic":21},[],{"title":635},{"EN":56},[],[638,645],{"id":60,"indexDatabase":639,"url":71,"indexYears":72,"academicFieldIds":644,"indexDatabaseRanking":77},{"id":62,"createTime":21,"updateTime":21,"relativeEntities":640,"label":641,"description":642,"key":68,"publicationTags":643,"standard":21},[],{"EN":65,"VI":65},{"EN":65,"VI":67},[70],[74,75,76],{"id":79,"indexDatabase":646,"url":92,"indexYears":21,"academicFieldIds":651,"indexDatabaseRanking":21},{"id":81,"createTime":21,"updateTime":21,"relativeEntities":647,"label":648,"description":649,"key":88,"publicationTags":650,"standard":21},[],{"EN":84,"VI":84},{"EN":86,"VI":87},[90,91],[94],{"impactFactor":22,"impactFactorByYear":653,"i10Index":109,"i10IndexLast5Year":110,"totalPublication":111,"totalPublicationByYear":654,"totalCitation":131,"totalCitationByYear":655,"totalCitationPerPublication":153,"totalCitationPerPublicationByYear":656,"hindexLast5Year":122,"hindex":122},{"2012":97,"2013":98,"2014":99,"2015":100,"2016":101,"2017":102,"2018":103,"2019":104,"2020":105,"2021":106,"2022":107,"2023":108},{"2000":113,"2001":114,"2002":115,"2003":116,"2004":117,"2005":118,"2006":119,"2007":120,"2008":121,"2009":122,"2010":123,"2011":120,"2012":124,"2013":125,"2014":117,"2015":126,"2016":118,"2017":127,"2018":113,"2019":121,"2020":116,"2021":128,"2022":129,"2023":126,"2024":130},{"2003":133,"2004":134,"2005":125,"2006":135,"2007":136,"2008":137,"2009":138,"2010":139,"2011":140,"2012":141,"2013":142,"2014":143,"2015":144,"2016":145,"2017":146,"2018":147,"2019":148,"2020":149,"2021":150,"2022":151,"2023":133,"2024":152},{"2003":155,"2004":156,"2005":157,"2006":158,"2007":159,"2008":160,"2009":161,"2010":162,"2011":163,"2012":164,"2013":165,"2014":166,"2015":167,"2016":168,"2017":169,"2018":170,"2019":171,"2020":172,"2021":173,"2022":174,"2023":175,"2024":176},{"pages":658,"volume":660},{"VOID":659},"337-345",{"VOID":661},"3",{"total":22,"publishYear":663,"statisticByYear":664},2002,{},"2002-11-01","DONE_ANALYZE_CITATION","2026-07-25T13:54:04.391+00:00",[90,77],{"id":670,"createTime":671,"updateTime":672,"relativeEntities":673,"slug":674,"properties":675,"entityType":199,"verifyStatus":200,"verifyTime":685,"verifyNote":202,"languages":21,"translateLanguages":21,"viewCount":22,"primaryUrl":686,"fullTextUrl":21,"authors":687,"publicationType":271,"publisherRelationship":731,"citationCount":21,"citationInfo":21,"publishDate":787,"publishYear":788,"citationAnalyzeStatus":330,"lastCitationAnalyze":789,"indexDatabases":790,"openAccess":21,"references":21,"isForceReanalyzing":333},"9cf09be4-bc8d-4bf9-8134-aee47ec5d54a","2024-01-24T13:15:06.043+00:00","2026-07-10T07:56:43.663+00:00",[],"Mitochondrial-function-and-mitochondrial-DNA-maintenance-with-advancing-age",{"abstract":676,"title":678,"gsPaper":680,"references":681,"doi":683},{"EN":677},"We review the impact of mitochondrial DNA (mtDNA) maintenance and mitochondrial function on the aging process. Mitochondrial function and mtDNA integrity are closely related. In order to create a protective barrier against reactive oxygen and nitrogen species (RONS) attacks and ensure mtDNA integrity, multiple cellular mtDNA copies are packaged together with various proteins in nucleoids. Regulation of antioxidant and RONS balance, DNA base excision repair, and selective degradation of damaged mtDNA copies preserves normal mtDNA quantities. Oxidative damage to mtDNA molecules does not substantially contribute to increased mtDNA mutation frequency; rather, mtDNA replication errors of DNA PolG are the main source of mtDNA mutations. Mitochondrial turnover is the major contributor to maintenance of mtDNA and functionally active mitochondria. Mitochondrial turnover involves mitochondrial biogenesis, mitochondrial dynamics, and selective autophagic removal of dysfunctional mitochondria (i.e., mitophagy). All of these processes exhibit decreased activity during aging and fall under greater nuclear genome control, possibly coincident with the emergence of nuclear genome instability. We suggest that the age-dependent accumulation of mutated mtDNA copies and dysfunctional mitochondria is associated primarily with decreased cellular autophagic and mitophagic activity.",{"EN":679},"Mitochondrial function and mitochondrial DNA maintenance with advancing age",{"VOID":194},{"VOID":682},"Abdullaev SA, Antipova VN, Gaziev AI (2009) Extracellular mutant mitochondrial DNA content is sharply elevated in the blood plasma of irradiated mice. Mol Biol (Mosk) 43:1063–1069\nAkbari M, Keijzers G, Maynard S et al (2014) Overexpression of DNA ligase III in mitochondria protects cells against oxidative stress and improves mitochondrial DNA base excision repair. DNA Repair (Amst) 16:44–53\nAlexeyev MF (2009) Is there more to aging than mitochondrial DNA and reactive oxygen species? 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Nat Med 14:959–965\nZhang Q, Wu Y, Zhang P et al (2012) Exercise induces mitochondrial biogenesis after brain ischemia in rats. Neuroscience 205:10–17\nZhao J, Lendahl U, Nister M (2013) Regulation of mitochondrial dynamics: convergences and divergences between yeast and vertebrates. 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alternative in vitro method exists fordetecting the potential long-term genotoxic effects ofmolecules at subcytotoxic concentrations, in terms ofdays and weeks after exposure(s) to the moleculetested. A theoretical model of cellular senescence ledto the concept that subcytotoxic stresses under anymolecules at subcytotoxic doses, such as moleculesunder development in the pharmaceutical, cosmetics andfood industry, might lead human fibroblasts into a stateclosely related to in vitro senescence. Thisconcept was then experimentally confirmed invitro: many biomarkers of replicative senescence ofhuman fibroblasts were found 72 h after theirexposure to various kinds of stressors used at non-cytotoxic concentrations. This phenomenon has beentermed stress-induced premature senescence (SIPS).Moreover, proteomics studies have revealed that,besides their effects on the appearance of thebiomarkers of senescence, sublethal stresses under avariety of stressors also lead to long-term specificchanges in the expression level of proteins which arestress-specific. These changes have been coined themolecular scars of stress. The proteins correspondingto these molecular scars may be identified using thelatest developments in mass spectrometry. This modelof stress-induced premature senescence may be appliedto the toxicological sciences when testing for thepotential irreversible long-term effects of moleculeson the cell fate.",{"EN":801},"Stress-induced premature senescence as alternativetoxicological method for testing the long-term effectsof molecules under development in the industry",{"VOID":803},"[\"16058153923239987137\"]",{"VOID":805},"Bayreuther K, Rodemann HP, Hommel R, Dittmann K, Albiez M and Francz PI (1988) Human skin fibroblasts in vitro differentiate along a terminal cell lineage. Proc Natl Acad Sci USA 85: 5112–5116\nCampisi J (1996) Replicative senescence: an old lives’ tale? Cell 84: 497–500\nChen QM and Ames BN (1994) Senescence-like growth arrest induced by hydrogen peroxide in human diploid fibroblast F65 cells. Proc Natl Acad Sci USA 91: 4130–4134\nChen QM, Bartholomew JC, Campisi J, Acosta M, Reagan JD and Ames BN (1998) Molecular analysis of H2O2-induced senescent-like growth arrest in normal human fibroblasts: p53 and Rb control G1 arrest but not cell replication. Biochem J 332: 43–50\nDierick J-F, Pascal T, Chainiaux F, Eliaers F, Remacle J, Larsen PM, Roepstorff P and Toussaint O (2000) Transcriptome analysis and proteome analysis in human senescent fibroblasts and fibroblasts undergoing premature senescence induced by repeated sublethal stresses. Ann NY Acad Sci (in press)\nDumont P, Burton M, Chen QM, Gonos ES, Frippiat C, Mazarati J-B, Eliaers F, Remacle J and Toussaint O (2000a) Long term effects of successive sublethal oxidative stresses on the appearance of biomarkers of human fibroblast replicative senescence. Free Radic Med Biol 28: 361–373\nDumont P, Balbeur L, Remacle J and Toussaint O (2000b) Appearance of biomarkers of in vitro ageing after successive stimulations of WI-38 fibroblasts with IL-1α and TNF-α: senescence associated β-galactosidase activity and morphotype transition. J Anat (in press)\nJoint databank of the European Research Group for Alternatives in Toxicity Testing, Fund for the Replacement of Animals in Medical Experiments & European Centre for the Validation of Alternative Methods (http:\u002F\u002Fembryo.ib.amwaw.edu.pl\u002Finvittox\u002F)\naiMartin GM, Austad SN and Johnson TE (1996) Genetic analysis of ageing: role of oxidative damage and environmental stresses. Nature Genet 13: 25–34\nRattan SI (1998) Repeated mild heat shock delays ageing in cultured human skin fibroblasts. Biochem Mol Biol Int 45: 753–759\nRemacle J, Raes M, Toussaint O and Rao G (1995) Low levels of reactive oxygen species as modulators of cell function. Mutation Res 316: 103–122\nSaretzki G, Feng J, von Zglinicki T and Villeponteau B (1998) Similar gene expression pattern in senescent and hyperoxic-treated fibroblasts. J Gerontol Biol Sci 53A:B438–B442\nShelton DN, Chang E, Whitter PS, Choi D and Funk WD (1999) Microarray analysis of replicative senescence. Curr Biol 9: 939–945\nToussaint O and Remacle J (1996) Role of the cellular energetic metabolism in age-related processes. In: Rattan SI and Toussaint O (eds) Molecular Gerontology: Research Status and Strategies. Plenum Press, New York\nToussaint O and Schneider ED (1998) The thermodynamics and evolution of complexity in biological systems. J Comp Physiol Biochem Part A 120A: 3–9\nToussaint O, Raes M and Remacle J (1991) Aging as a multistep process characterized by a lowering of entropy production leading the cell to a sequence of defined stages. Mech Ageing Dev 61: 45–64\nToussaint O, Houbion A and Remacle J (1992) Aging as a multistep process characterized by a lowering of entropy production leading the cell to a sequence of defined stages. II. Experimental results with cultivated cells. Mech Ageing Dev 64: 65–83\nToussaint O, Michiels C, Raes M and Remacle J (1995a) Importance of the energetic factors in cellular ageing. Exp Gerontol 30: 1–22\nToussaint O, Eliaers F, Houbion A, Remacle J and Drieu K (1995b) Protective effect of EGb 761 and bilobalide on mortality and accelerated cellular ageing in stressful conditions. In: Christen Y, Courtois Y and Droy-Lefaix M-T (eds) Advances in Ginkgo biloba Extract Research. Effect of Ginkgo biloba Extracts (EGb 761) on Aging and Age-related Disorders. Vol 4. Elsevier, Paris\nToussaint O, Fuchs SY, Ronai ZA, Isoyama N, Yuko, N, Petronilli V, Bernardi P, Gonos ES, Dumont P and Remacle J (1998) Reciprocal effects between stresses and cellular aging. Molecular & Cellular View. Ann NY Acad Sci 851: 450–465\nToussaint O, Dumont P, Dierick J-F, Pascal T, Frippiat C, Chainiaux F, Magalhaes JP, Eliaers F and Remacle J (2000) Stress-induced premature senescence. Essence of life, evolution, stress & aging. Ann NY Acad Sci (in press)\nVon Zglinicki T, Sarentzki G, Döcke W and Lotze C (1995) Mild hyperoxia shortens telomeres and inhibits proliferation of fibroblasts: a model for senescence? 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is essential for the immune system and elderly people have an increased probability for zinc deficiency, documented by a decline of serum or plasma zinc levels with age. Although most healthy elderly are not classified as clinically zinc deficient, even marginal zinc deprivation can affect immune function. Several striking similarities in the immunological changes during aging and zinc deficiency, including a reduction in the activity of the thymus and thymic hormones, a shift of the T helper cell balance towards TH2, decreased response to vaccination, and impaired functions of innae immune cells indicate that a wide prevalence of marginal zinc deficiency in elderly people may contribute to immunosenescence. Studies with oral zinc supplementation show the potential to improve the immune response of elderly people by restoration of the zinc levels, showing that balancing the zinc status may be a way to healthy aging. This review summarizes the current literature about zinc supplementation in the elderly and thereby defines the rationale for the immunological part of the ZINCAGE project.",{"EN":1007},"Correlation between zinc status and immune function in the elderly",{"VOID":194},{"VOID":1010},"Beck FW, Prasad AS, Kaplan J, Fitzgerald JT, Brewer GJ (1997) Changes in cytokine production and T cell subpopulations in experimentally induced zinc-deficient humans. Am J Physiol 272:E1002–E1007\nBogden JD, Oleske JM, Lavenhar MA, Munves EM, Kemp FW, Bruening KS, Holding KJ, Denny TN, Guarino MA, Holland BK (1990) Effects of one year of supplementation with zinc and other micronutrients on cellular immunity in the elderly. J Am Coll Nutr 9:214–225\nBogden JD, Oleske JM, Munves EM, Lavenhar MA, Bruening KS, Kemp FW, Holding KJ, Denny TN, Louria DB (1987) Zinc and immunocompetence in the elderly: baseline data on zinc nutriture and immunity in unsupplemented subjects. Am J Clin Nutr 46:101–109\nBoukaiba N, Flament C, Acher S, Chappuis P, Piau A, Fusselier M, Dardenne M, Lemonnier D (1993) A physiological amount of zinc supplementation: effects on nutritional, lipid, and thymic status in an elderly population. Am J Clin Nutr 57:566–572\nBriefel RR, Bialostosky K, Kennedy-Stephenson J, McDowell MA, Ervin RB, Wright JD (2000) Zinc intake of the U.S. population: findings from the third National Health and Nutrition Examination Survey, 1988–1994. J Nutr 130:1367S–1373S\nBunker VW, Hinks LJ, Lawson MS, Clayton BE (1984) Assessment of zinc and copper status of healthy elderly people using metabolic balance studies and measurement of leucocyte concentrations. Am J Clin Nutr 40:1096–1102\nBunker VW, Hinks LJ, Stansfield MF, Lawson MS, Clayton BE (1987) Metabolic balance studies for zinc and copper in housebound elderly people and the relationship between zinc balance and leukocyte zinc concentrations. Am J Clin Nutr 46:353–359\nCakman I, Rohwer J, Schutz RM, Kirchner H, Rink L (1996) Dysregulation between TH1 and TH2 T cell subpopulations in the elderly. Mech Ageing Dev 87:197–209\nCossack ZT (1989) T-lymphocyte dysfunction in the elderly associated with zinc deficiency and subnormal nucleoside phosphorylase activity: effect of zinc supplementation. Eur J Cancer Clin Oncol 25:973–976\nDuchateau J, Delepesse G, Vrijens R, Collet H (1981) Beneficial effects of oral zinc supplementation on the immune response of old people. Am J Med 70:1001–1004\nFabris N, Mocchegiani E, Amadio L, Zannotti M, Licastro F, Franceschi C (1984) Thymic hormone deficiency in normal ageing and Down’s syndrome: is there a primary failure of the thymus? Lancet 1:983–986\nFortes C, Forastiere F, Agabiti N, Fano V, Pacifici R, Virgili F, Piras G, Guidi L, Bartoloni C, Tricerri A, Zuccaro P, Ebrahim S, Perucci CA (1998) The effect of zinc and vitamin A supplementation on immune response in an older population. J Am Geriatr Soc 46:19–26\nGirodon F, Blache D, Monget AL, Lombart M, Brunet-Lecompte P, Arnaud J, Richard MJ, Galan P (1997) Effect of a two-year supplementation with low doses of antioxidant vitamins and\u002For minerals in elderly subjects on levels of nutrients and antioxidant defense parameters. J Am Coll Nutr 16:357–365\nGirodon F, Galan P, Monget AL, Boutron-Ruault MC, Brunet-Lecomte P, Preziosi P, Arnaud J, Manuguerra JC, Herchberg S (1999) Impact of trace elements and vitamin supplementation on immunity and infections in institutionalized elderly patients: a randomized controlled trial. MIN. VIT. AOX. geriatric network. Arch Intern Med 159:748–754\nGoode HF, Penn ND, Kelleher J, Walker BE (1991) Evidence of cellular zinc depletion in hospitalized but not in healthy elderly subjects. Age Ageing 20:345–348\nHotz C, Peerson JM, Brown KH (2003) Suggested lower cutoffs of serum zinc concentrations for assessing zinc status: reanalysis of the second National Health and Nutrition Examination Survey data (1976–1980). Am J Clin Nutr 78:756–764\nIbs KH, Gabriel P, Rink L (2003) Zinc and the immune system of elderly. Adv Cell Aging Gerontol 13:243–259\nIbs KH, Rink L (2003) Zinc-altered immune function. J Nutr 133:1452S–1456S\nKaplan J, Hess JW, Prasad AS (1988) Impaired interleukin-2 production in the elderly: association with mild zinc deficiency. J Trace Elem Exp Med 1:3–8\nKreft B, Fischer A, Kruger S, Sack K, Kirchner H, Rink L (2000) The impaired immune response to diphtheria vaccination in elderly chronic hemodialysis patients is related to zinc deficiency. Biogerontology 1:61–66\nLindeman RD, Clark ML, Colmore JP (1971) Influence of age and sex on plasma and red-cell zinc concentrations. J Gerontol 26:358–363\nMaret W, Sandstead HH (2006) Zinc requirements and the risks and benefits of zinc supplementation. J Trace Elem Med Biol 20:3–18\nMocchegiani E, Giacconi R, Muzzioli M, Cipriano C (2000a) Zinc, infections and immunosenescence. Mech Ageing Dev 121:21–35\nMocchegiani E, Muzzioli M, Giacconi R (2000b) Zinc, metallothioneins, immune responses, survival and ageing. Biogerontology 1:133–143\nMocchegiani E, Muzzioli M, Giacconi R, Cipriano C, Gasparini N, Franceschi C, Gaetti R, Cavalieri E, Suzuki H (2003) Metallothioneins\u002FPARP-1\u002FIL-6 interplay on natural killer cell activity in elderly: parallelism with nonagenarians and old infected humans. Effect of zinc supply. Mech Ageing Dev 124:459–468\nPepersack T, Rotsaert P, Benoit F, Willems D, Fuss M, Bourdoux P, Duchateau J (2001) Prevalence of zinc deficiency and its clinical relevance among hospitalised elderly. Arch Gerontol Geriatr 33:243–253\nPrasad AS, Fitzgerald JT, Hess JW, Kaplan J, Pelen F, Dardenne M (1993) Zinc deficiency in elderly patients. Nutrition 9:218–224\nProvinciali M, Montenovo A, Di Stefano G, Colombo M, Daghetta L, Cairati M, Veroni C, Cassino R, Della Torre F, Fabris N (1998) Effect of zinc or zinc plus arginine supplementation on antibody titre and lymphocyte subsets after influenza vaccination in elderly subjects: a randomized controlled trial. Age Ageing 27:715–722\nRavaglia G, Forti P, Maioli F, Bastagli L, Facchini A, Mariani E, Savarino L, Sassi S, Cucinotta D, Lenaz G, (2000a) Effect of micronutrient status on natural killer cell immune function in healthy free-living subjects aged >\u002F = 90 y. Am J Clin Nutr 71:590–598\nRavaglia G, Forti P, Maioli F, Nesi B, Pratelli L, Savarino L, Cucinotta D, Cavalli G, (2000b) Blood micronutrient and thyroid hormone concentrations in the oldest-old. J Clin Endocrinol Metabol 85:2260–2265\nSenapati A, Jenner G, Thompson RP (1989) Zinc in the elderly. Quart J Med 70:81–87\nStafford W, Smith RG, Lewis SJ, Henery E, Stephen PJ, Rafferty J, Simpson GK, Bell PC, O’Rorke K (1988) A study of zinc status of elderly institutionalized patients. Age Ageing 17:42–48\nVallee BL, Falchuk KH (1993) The biochemical basis of zinc physiology. Physiol Rev 73:79–118\nWagner PA, Jernigan JA, Bailey LB, Nickens C, Brazzi GA (1983) Zinc nutriture and cell-mediated immunity in the aged. Int J Vit Nutr Res 53:94–101\nWörwag M, Classen HG, Schumacher E (1999) Prevalence of magnesium and zinc deficiencies in nursing home residents in Germany. 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imposed calorie restriction (CR) is shown to result in the most reproducible endpoint of lifespan extension in all animals models tested. In this presentation, the question of CR’s effect on human longevity is reviewed by discussing data pertinent to the putative efficacy of CR on humans. Arguments are presented in support of this possibility based on CR’s unique abilities to retard biological functional declines and to deter pathological processes, both of which are major targets of deleterious oxidative stress. To delineate the cellular and molecular mechanisms of CR’s efficacy on human longevity, this review elaborates on the modulation of CR on the inflammatory process, a common risk factor for many chronic diseases. Discussions also include evidence from human data on the effect of CR in the loss of body weight, known to suppress inflammatory cytokines, subsequently leading to the reduction of chronic diseases known to compromise the functional longevity of humans.",{"EN":1129},"Why calorie restriction would work for human longevity",{"VOID":1131},"[\"4866733345251872149\"]",{"VOID":1133},"Aruoma OI, Halliwell B (1998) Molecular biology of free radicals in human diseases. OICA International, London, UK\nCaruso C, Candore G, Colonna-Romano G, Lio D, Francceshi C (2004a) Inflammation and life-span. Science 305: 1736–1739\nCaruso C, Lio D, Cavallone L, Franceschi C (2004b) Aging, longevity, inflammation, and cancer. Ann NY Acad Sci 1028:1–13\nChung HY, Kim HJ, Kim WJ, Yu BP (2001) The inflammatory hypothesis of aging: molecular modulation by calorie restriction. Ann NY Acad Sci 928:327–335\nChung HY, Jung KJ, Yu BP (2005) Molecular inflammation as an underlying mechanism of aging: the anti-inflammatory action of calorie restriction. In: Surh YJ, Packer L (eds) Oxidative stress, inflammation, and health. CRC Press, Boca Raton, pp 389–421\nDandona P, Aljada A, Brandyopadhyay A (2004) Inflammation: the link between insulin resistance, obesity and diabetes. Trends Immunol 25:4–7\nDirks AJ, Leeuwenburg C (2006) Calorie restriction in humans: potential pitfalls and health concerns. Mech Ageing Dev 127:1–7\nFerroni P, Basili S, Falco A,and Davi G (2004) Inflammation, insulin, and obesity. Curre Atheroscler Rep 6:424–431\nFontana L, Meyer TE, Klein S, Holloszy JO (2004) Long-term calorie restriction is highly effective in reducing the risk for atherosclerosis in humans. Proc Natl Acad Sci USA 101:6659–6663\nHursting SD, Lavigne JA, Berrigan D, Perkins SN, Barrett JC (2003) Calorie restriction, aging, and cancer prevention: mechanisms of action and applicability to humans. Annu Rev Med 54:131–152\nLicastro F, Candore G, Lio D, Colonna-Romano EP, Franceshi C, Caruso C (2005) Innate immunity and inflammation in ageing: a key for understanding age-related diseases. Immun Ageing 2:8–32\nPhelan JP, Rose MR (2005) Why dietary restriction substantially increases longevity in animal models but won’t in humans. Ageing Res Rev 4:339–350\nRae M (2004) It’s never too late: Calorie restriction is effective in older mammals. Rejuv Res 7:3–8\nSavage DB, Petersen KF, Schulman GI (2005) Mechanisms of insulin resistance in humans and possible links with inflammation. Hypertension 45:828–833\nTracy RP (2003) Emerging relationships of inflammation, cardiovascular disease, and chronic diseases of aging. Int. J Relat Metab Disord 27(Suppl 3):S29–34\nVelthuis-te Wierik EJ, van den Berg H, Schaafsma G, Hendriks HF (1994) Energy restriction, a useful intervention to retard human ageing? Results of a feasibility study. Eur J Clin Nutr 48:138–148\nWalford RL, Mock D, MadCallum T, Laseter JL (1999) Physiologic changes in humans subjects to severe, selective calorie restriction for two years in biospere 2: health, aging, and toxicological perspectives. Toxicol Sci 52: 61–65\nWalford RL, Mock D, Verdery R, MacCallum T (2002) Calorie restriction in biosphere 2: alterations in physiologic, hematologic, hormonal and biochemical parameters in humans restricted for a 2-year period. J Gerontol 57:B211–224\nYu BP, Chung HY (2001) Stress resistance by calorie restriction for longevity. Ann NY Acad Sci 928:39–47\nYu BP (2005a) Calorie restriction as potent anti-aging intervention: modulation of oxidative stress. In: Rattan SIS (ed) Aging interventions and therapies. World Scientific, New Jersey, pp 193–217\nYu BP (2005b) Membrane alteration as a basis of aging and the protective effects of calorie restriction. 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Int J Obes (Lond) 36:805–809",{"doi":1405},{"id":1920,"createTime":1921,"updateTime":1922,"relativeEntities":1923,"slug":1924,"properties":1925,"entityType":199,"verifyStatus":200,"verifyTime":1934,"verifyNote":202,"languages":21,"translateLanguages":21,"viewCount":22,"primaryUrl":1935,"fullTextUrl":21,"authors":1936,"publicationType":271,"publisherRelationship":1980,"citationCount":115,"citationInfo":2036,"publishDate":2038,"publishYear":1116,"citationAnalyzeStatus":20,"lastCitationAnalyze":2039,"indexDatabases":2040,"openAccess":21,"references":2041,"isForceReanalyzing":333},"0f7b8d25-5cbf-401b-802a-59c110fcbbd8","2024-01-16T22:20:33.633+00:00","2026-04-21T13:12:31.289+00:00",[],"Superoxide-dismutase-activities-in-long-lived-Drosophila-melanogaster-females-chico-1-genotypes-and-dietary-dilution",{"abstract":1926,"title":1928,"gsPaper":1930,"doi":1932},{"EN":1927},"Superoxide dismutase (SOD) activities were determined for dietary dilution conditions that extend the life span of Drosophila melanogaster. The hypothesis motivating this research was that elevated SOD activity is associated with increased life span resulting from flies being held on a restricted diet. SOD activities were also measured for chico\n                        1 which is a mutation in the insulin receptor substrate protein gene associated with life span extension. This allowed us to confirm the results of (Clancy et al. 2001) and extend the results by measuring CuZn SOD and Mn SOD activities in addition to the previously determined overall SOD activity. If the same form of SOD activity (CuZn SOD or Mn SOD) was elevated on the dilute diet that extends life span and in the long lived chico\n                        1 homozygotes, then it would suggest that life span extension by dietary restriction and by insulin signaling mutations has a similar underlying mechanism. However, overall SOD activity, and CuZn SOD or Mn SOD activities did not differ among the diets tested. As observed previously (Clancy et al. 2001), overall SOD activity was elevated in chico\n                        1 homozygotes compared to the heterozygote or wild type. Results from the present study indicate that elevated CuZn SOD activity, not Mn SOD, is the basis for the relatively high level of SOD activity in the chico\n                        1 homozygotes.",{"EN":1929},"Superoxide dismutase activities in long-lived Drosophila melanogaster females: chico 1 genotypes and dietary dilution",{"VOID":1931},"[\"10395555872355665316\"]",{"VOID":1933},"10.1007\u002Fs10522-006-9065-3","2024-04-29T19:13:02.628+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10522-006-9065-3",[1937,1952,1967],{"id":1938,"sortIndex":22,"researcher":21,"roles":1939,"affiliations":1940,"properties":1949,"displayName":1951,"givenName":21,"familyName":21},"7b34511f-e842-478c-9355-e37099eb8519",[208],[1941],{"id":1942,"sortIndex":22,"affiliation":1943,"properties":21},"08e9794a-f91f-47f1-8597-bc66551263d6",{"id":1942,"createTime":21,"updateTime":21,"relativeEntities":1944,"slug":21,"properties":1945,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":1948,"statistic":21},[],{"title":1946},{"VI":1947},"School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, USA",[],{"title":1950},{"VI":1951},"Hadise Kabil",{"id":1953,"sortIndex":223,"researcher":21,"roles":1954,"affiliations":1955,"properties":1964,"displayName":1966,"givenName":21,"familyName":21},"bcac61f1-5804-4768-bb4a-652a0fb92bbb",[208],[1956],{"id":1957,"sortIndex":22,"affiliation":1958,"properties":21},"1df7e88a-0b67-41b9-82f3-7672c56ac705",{"id":1957,"createTime":21,"updateTime":21,"relativeEntities":1959,"slug":21,"properties":1960,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":1963,"statistic":21},[],{"title":1961},{"VI":1962},"Department of Biology, University College London, London, UK",[],{"title":1965},{"VI":1966},"Linda Partridge",{"id":1968,"sortIndex":237,"researcher":21,"roles":1969,"affiliations":1970,"properties":1977,"displayName":1979,"givenName":21,"familyName":21},"93622d06-62dd-4878-9946-990cc430b8fa",[208],[1971],{"id":1942,"sortIndex":22,"affiliation":1972,"properties":21},{"id":1942,"createTime":21,"updateTime":21,"relativeEntities":1973,"slug":21,"properties":1974,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":1976,"statistic":21},[],{"title":1975},{"VI":1947},[],{"title":1978},{"VI":1979},"Lawrence G. 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Science 290:147–150",{"doi":1405},{"id":2148,"createTime":2149,"updateTime":2150,"relativeEntities":2151,"slug":2152,"properties":2153,"entityType":199,"verifyStatus":200,"verifyTime":2164,"verifyNote":202,"languages":21,"translateLanguages":21,"viewCount":22,"primaryUrl":2165,"fullTextUrl":21,"authors":2166,"publicationType":271,"publisherRelationship":2212,"citationCount":411,"citationInfo":2268,"publishDate":2271,"publishYear":2269,"citationAnalyzeStatus":20,"lastCitationAnalyze":2150,"indexDatabases":2272,"openAccess":21,"references":21,"isForceReanalyzing":333},"3519c237-8423-4dae-8090-7133729bd590","2023-12-12T02:27:54.030+00:00","2026-04-20T21:17:53.690+00:00",[],"Common-factors-among-three-types-of-cells-aged-in-mice",{"abstract":2154,"title":2156,"gsPaper":2158,"references":2160,"doi":2162},{"EN":2155},"The greatest risk factor for the formation of numerous significant chronic disorders is aging. Understanding the core molecular underpinnings of aging can help to slow down the inevitable process. Systematic study of gene expression or DNA methylation data is possible at the transcriptomics and epigenetics levels. DNA methylation and gene expression are both affected by aging. Gene expression is an important element in the aging of Homo sapiens. In this work, we evaluated the expression of differentially expressed genes (DEGs), proteins, and transcription factors (TFs) in three different types of cells in mice: antibody-secreting cells, cardiac mesenchymal stromal cells, and skeletal muscle cells. The goal of this article is to uncover a common cause during aging among these cells in order to increase understanding about establishing complete techniques for preventing aging and improving people's quality of life. We conducted a comprehensive network-based investigation to establish which genes and proteins are shared by the three different types of aged cells. Our findings clearly indicated that aging induces gene dysregulation in immune, pharmacological, and apoptotic pathways. Furthermore, our research developed a list of hub genes with differential expression in aging responses that should be investigated further to discover viable anti-aging treatments.",{"EN":2157},"Common factors among three types of cells aged in mice",{"VOID":2159},"[\"13568288963588288994\"]",{"VOID":2161},"Agostini S, Costa AS, Mancuso R, Guerini FR, Nemni R, Clerici M (2019) The PILRA G78R variant correlates with higher HSV-1-specific IgG titers in Alzheimer’s disease. Cell Mol Neurobiol 39(8):1217–1221\nBastian M, Heymann S, Jacomy M Gephi (2009) An open source software for exploring and manipulating networks. 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EMBO J 27(13):1852–1862",{"VOID":2163},"10.1007\u002Fs10522-023-10035-0","2024-05-10T05:11:33.661+00:00","https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10522-023-10035-0",[2167,2184,2197],{"id":2168,"sortIndex":22,"researcher":21,"roles":2169,"affiliations":2170,"properties":2179,"displayName":2181,"givenName":21,"familyName":21},"fad04ff2-03d6-4b5a-b15c-36ac87bc1d2b",[208],[2171],{"id":2172,"sortIndex":22,"affiliation":2173,"properties":21},"ad3c4497-1fda-420d-818b-22fcc0b903a4",{"id":2172,"createTime":21,"updateTime":21,"relativeEntities":2174,"slug":21,"properties":2175,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":2178,"statistic":21},[],{"title":2176},{"VI":2177},"Department of Biology, School of Sciences, Razi University, Kermanshah, Islamic Republic of Iran",[],{"title":2180,"gsAuthor":2182},{"VI":2181},"Mehran 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