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Volumn 7, Issue , 2009, Pages

Proteomic study on gender differences in aging kidney of mice

Author keywords

[No Author keywords available]

Indexed keywords

3 HYDROXYISOBUTYRATE DEHYDROGENASE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 9A; ISOCITRATE DEHYDROGENASE 1; OXIDOREDUCTASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; TRANSFERRIN; UNCLASSIFIED DRUG;

EID: 65449154836     PISSN: None     EISSN: 14775956     Source Type: Journal    
DOI: 10.1186/1477-5956-7-16     Document Type: Article
Times cited : (20)

References (54)
  • 1
    • 45049086767 scopus 로고    scopus 로고
    • Comparative proteomic analysis of brains of naturally aging mice
    • 10.1016/j.neuroscience.2008.04.012 18495355
    • Yang S Liu T Li S Zhang X Ding Q Que H Yan X Wei K Liu S Comparative proteomic analysis of brains of naturally aging mice Neuroscience 2008, 154:1107-1120 10.1016/j.neuroscience.2008.04.012 18495355
    • (2008) Neuroscience , vol.154 , pp. 1107-1120
    • Yang, S.1    Liu, T.2    Li, S.3    Zhang, X.4    Ding, Q.5    Que, H.6    Yan, X.7    Wei, K.8    Liu, S.9
  • 2
    • 60549096680 scopus 로고    scopus 로고
    • Proteome profiling of aging in mouse models: Differential expression of proteins involved in metabolism, transport, and stress response in kidney
    • 10.1002/pmic.200700208 19184973
    • Chakravarti B Seshi B Ratanaprayul W Dalal N Lin L Raval A Chakravarti DN Proteome profiling of aging in mouse models: Differential expression of proteins involved in metabolism, transport, and stress response in kidney Proteomics 2009, 9:580-597 10.1002/pmic.200700208 19184973
    • (2009) Proteomics , vol.9 , pp. 580-597
    • Chakravarti, B.1    Seshi, B.2    Ratanaprayul, W.3    Dalal, N.4    Lin, L.5    Raval, A.6    Chakravarti, D.N.7
  • 3
    • 3543138968 scopus 로고    scopus 로고
    • Proteomic analysis of post-mitochondrial fractions of young and old rat kidney
    • 10.1016/j.exger.2004.04.003 15288690
    • Kim CH Park DU Chung AS Zou Y Jung KJ Sung BK Yu BP Chung HY Proteomic analysis of post-mitochondrial fractions of young and old rat kidney Exp Gerontol 2004, 39:1155-1168 10.1016/j.exger.2004.04.003 15288690
    • (2004) Exp Gerontol , vol.39 , pp. 1155-1168
    • Kim, C.H.1    Park, D.U.2    Chung, A.S.3    Zou, Y.4    Jung, K.J.5    Sung, B.K.6    Yu, B.P.7    Chung, H.Y.8
  • 4
    • 0030743137 scopus 로고    scopus 로고
    • Cell aging in vivo and in vitro
    • 10.1016/S0047-6374(97)00067-5 9255755
    • Rubin H Cell aging in vivo and in vitro Mech Ageing Dev 1997, 98:1-35 10.1016/S0047-6374(97)00067-5 9255755
    • (1997) Mech Ageing Dev , vol.98 , pp. 1-35
    • Rubin, H.1
  • 5
    • 0035812845 scopus 로고    scopus 로고
    • The shortest telomere, not average telomere length, is critical for cell viability and chromosome stability
    • 10.1016/S0092-8674(01)00504-9 11595186
    • Hemann MT Strong MA Hao LY Greider CW The shortest telomere, not average telomere length, is critical for cell viability and chromosome stability Cell 2001, 107:67-77 10.1016/S0092-8674(01)00504-9 11595186
    • (2001) Cell , vol.107 , pp. 67-77
    • Hemann, M.T.1    Strong, M.A.2    Hao, L.Y.3    Greider, C.W.4
  • 6
    • 0034745354 scopus 로고    scopus 로고
    • Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth
    • 10.1038/35060068 11231577
    • Song J Takeda M Morimoto RI Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth Nat Cell Biol 2001, 3:276-282 10.1038/35060068 11231577
    • (2001) Nat Cell Biol , vol.3 , pp. 276-282
    • Song, J.1    Takeda, M.2    Morimoto, R.I.3
  • 7
    • 0033912405 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress. Physiologic consequences and potential for a role in aging
    • 10911961
    • Melov S Mitochondrial oxidative stress. Physiologic consequences and potential for a role in aging Ann N Y Acad Sci 2000, 908:219-225 10911961
    • (2000) Ann N Y Acad Sci , vol.908 , pp. 219-225
    • Melov, S.1
  • 8
    • 0038329323 scopus 로고    scopus 로고
    • Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
    • 10.1038/nature01578 12736687
    • Anderson RM Bitterman KJ Wood JG Medvedik O Sinclair DA Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae Nature 2003, 423:181-185 10.1038/nature01578 12736687
    • (2003) Nature , vol.423 , pp. 181-185
    • Anderson, R.M.1    Bitterman, K.J.2    Wood, J.G.3    Medvedik, O.4    Sinclair, D.A.5
  • 9
    • 0142178220 scopus 로고    scopus 로고
    • Healthy animals with extreme longevity
    • 10.1126/science.1089169 14576426
    • Arantes-Oliveira N Berman JR Kenyon C Healthy animals with extreme longevity Science 2003, 302:611 10.1126/science.1089169 14576426
    • (2003) Science , vol.302 , pp. 611
    • Arantes-Oliveira, N.1    Berman, J.R.2    Kenyon, C.3
  • 10
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • 10.1038/35065638 11242085
    • Tissenbaum HA Guarente L Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans Nature 2001, 410:227-230 10.1038/ 35065638 11242085
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 11
    • 33646517324 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of differential protein expression and oxidative modification of specific proteins in the brains of old mice
    • 10.1016/j.neurobiolaging.2005.05.006 15979213
    • Poon HF Vaishnav RA Getchell TV Getchell ML Butterfield DA Quantitative proteomics analysis of differential protein expression and oxidative modification of specific proteins in the brains of old mice Neurobiol Aging 2006, 27:1010-1019 10.1016/j.neurobiolaging.2005.05.006 15979213
    • (2006) Neurobiol Aging , vol.27 , pp. 1010-1019
    • Poon, H.F.1    Vaishnav, R.A.2    Getchell, T.V.3    Getchell, M.L.4    Butterfield, D.A.5
  • 12
    • 0142182397 scopus 로고    scopus 로고
    • Differential expression of the liver proteome in senescence accelerated mice
    • 10.1002/pmic.200300562 14625850
    • Cho YM Bae SH Choi BK Cho SY Song CW Yoo JK Paik YK Differential expression of the liver proteome in senescence accelerated mice Proteomics 2003, 3:1883-1894 10.1002/pmic.200300562 14625850
    • (2003) Proteomics , vol.3 , pp. 1883-1894
    • Cho, Y.M.1    Bae, S.H.2    Choi, B.K.3    Cho, S.Y.4    Song, C.W.5    Yoo, J.K.6    Paik, Y.K.7
  • 13
    • 33847168242 scopus 로고    scopus 로고
    • Differential gene expression profiles in the hippocampus of senescence-accelerated mouse
    • 10.1016/j.neurobiolaging.2006.02.004 16569465
    • Cheng XR Zhou WX Zhang YX Zhou DS Yang RF Chen LF Differential gene expression profiles in the hippocampus of senescence-accelerated mouse Neurobiol Aging 2007, 28:497-506 10.1016/j.neurobiolaging.2006.02.004 16569465
    • (2007) Neurobiol Aging , vol.28 , pp. 497-506
    • Cheng, X.R.1    Zhou, W.X.2    Zhang, Y.X.3    Zhou, D.S.4    Yang, R.F.5    Chen, L.F.6
  • 14
    • 34249829274 scopus 로고    scopus 로고
    • Brain mitochondrial dysfunction in aging: Conditions that improve survival, neurological performance and mitochondrial function
    • 10.2741/2133 17127368
    • Navarro A Boveris A Brain mitochondrial dysfunction in aging: Conditions that improve survival, neurological performance and mitochondrial function Front Biosci 2007, 12:1154-1163 10.2741/2133 17127368
    • (2007) Front Biosci , vol.12 , pp. 1154-1163
    • Navarro, A.1    Boveris, A.2
  • 15
    • 33644554186 scopus 로고    scopus 로고
    • Searching for aging-related proteins in human dermal microvascular endothelial cells treated with anti-aging agents
    • 10.1002/pmic.200500287 16404724
    • Lee JH Chung KY Bang D Lee KH Searching for aging-related proteins in human dermal microvascular endothelial cells treated with anti-aging agents Proteomics 2006, 6:1351-1361 10.1002/pmic.200500287 16404724
    • (2006) Proteomics , vol.6 , pp. 1351-1361
    • Lee, J.H.1    Chung, K.Y.2    Bang, D.3    Lee, K.H.4
  • 16
    • 0242653780 scopus 로고    scopus 로고
    • Proteomic analysis of the genetic premature aging disease Hutchinson Gilford progeria syndrome reveals differential protein expression and glycosylation
    • 10.1021/pr034035k 14582653
    • Robinson LJ Karlsson NG Weiss AS Packer NH Proteomic analysis of the genetic premature aging disease Hutchinson Gilford progeria syndrome reveals differential protein expression and glycosylation J Proteome Res 2003, 2:556-557 10.1021/pr034035k 14582653
    • (2003) J Proteome Res , vol.2 , pp. 556-557
    • Robinson, L.J.1    Karlsson, N.G.2    Weiss, A.S.3    Packer, N.H.4
  • 17
    • 0842305078 scopus 로고    scopus 로고
    • Age-related changes in the glycation of human aortic elastin
    • 10.1016/j.exger.2003.10.003 15036419
    • Konova E Baydanoff S Atanasova M Velkova A Age-related changes in the glycation of human aortic elastin Exp Gerontol 2004, 39:249-254 10.1016/ j.exger.2003.10.003 15036419
    • (2004) Exp Gerontol , vol.39 , pp. 249-254
    • Konova, E.1    Baydanoff, S.2    Atanasova, M.3    Velkova, A.4
  • 18
    • 33645704767 scopus 로고    scopus 로고
    • Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver
    • 16415296
    • Forner F Foster LJ Campanaro S Valle G Mann M Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver Mol Cell Proteomics 2006, 5:608-619 16415296
    • (2006) Mol Cell Proteomics , vol.5 , pp. 608-619
    • Forner, F.1    Foster, L.J.2    Campanaro, S.3    Valle, G.4    Mann, M.5
  • 19
    • 34250336949 scopus 로고    scopus 로고
    • Quantitative proteomic comparison of mouse peroxisomes from liver and kidney
    • 10.1002/pmic.200600638 17474143
    • Mi J Kirchner E Cristobal S Quantitative proteomic comparison of mouse peroxisomes from liver and kidney Proteomics 2007, 7:1916-1928 10.1002/ pmic.200600638 17474143
    • (2007) Proteomics , vol.7 , pp. 1916-1928
    • Mi, J.1    Kirchner, E.2    Cristobal, S.3
  • 20
  • 21
    • 84867548442 scopus 로고    scopus 로고
    • Comparison of Golgi apparatus and endoplasmic reticulum proteins from livers of juvenile and aged rats using a novel technique for separation and enrichment of organelles
    • 2291758 16522856
    • Drahos KL Tran HC Kiri AN Lan W McRorie DK Horn MJ Comparison of Golgi apparatus and endoplasmic reticulum proteins from livers of juvenile and aged rats using a novel technique for separation and enrichment of organelles J Biomol Tech 2005, 16:347-355 2291758 16522856
    • (2005) J Biomol Tech , vol.16 , pp. 347-355
    • Drahos, K.L.1    Tran, H.C.2    Kiri, A.N.3    Lan, W.4    McRorie, D.K.5    Horn, M.J.6
  • 22
    • 0037289173 scopus 로고    scopus 로고
    • Comparative proteomics: Characterization of a two-dimensional gel electrophoresis system to study the effect of aging on mitochondrial proteins
    • 10.1016/S0047-6374(02)00167-7 12618004
    • Chang J Van Remmen H Cornell J Richardson A Ward WF Comparative proteomics: Characterization of a two-dimensional gel electrophoresis system to study the effect of aging on mitochondrial proteins Mech Ageing Dev 2003, 124:33-41 10.1016/S0047-6374(02)00167-7 12618004
    • (2003) Mech Ageing Dev , vol.124 , pp. 33-41
    • Chang, J.1    Van Remmen, H.2    Cornell, J.3    Richardson, A.4    Ward, W.F.5
  • 23
    • 84867523780 scopus 로고    scopus 로고
    • Proteomic changes in bovine heart mitochondria with age: Using a novel technique for organelle separation and enrichment
    • 2291746 16522859
    • Kiri AN Tran HC Drahos KL Lan W McRorie DK Horn MJ Proteomic changes in bovine heart mitochondria with age: Using a novel technique for organelle separation and enrichment J Biomol Tech 2005, 16:371-379 2291746 16522859
    • (2005) J Biomol Tech , vol.16 , pp. 371-379
    • Kiri, A.N.1    Tran, H.C.2    Drahos, K.L.3    Lan, W.4    McRorie, D.K.5    Horn, M.J.6
  • 24
    • 33646708957 scopus 로고    scopus 로고
    • Proteomics analysis provides insight into caloric restriction mediated oxidation and expression of brain proteins associated with age-related impaired cellular processes: Mitochondrial dysfunction, glutamate dysregulation and impaired protein synthesis
    • 10.1016/j.neurobiolaging.2005.05.014 15996793
    • Poon HF Shepherd HM Reed TT Calabrese V Stella AM Pennisi G Cai J Pierce WM Klein JB Butterfield DA Proteomics analysis provides insight into caloric restriction mediated oxidation and expression of brain proteins associated with age-related impaired cellular processes: Mitochondrial dysfunction, glutamate dysregulation and impaired protein synthesis Neurobiol Aging 2006, 27:1020-1034 10.1016/j.neurobiolaging.2005.05.014 15996793
    • (2006) Neurobiol Aging , vol.27 , pp. 1020-1034
    • Poon, H.F.1    Shepherd, H.M.2    Reed, T.T.3    Calabrese, V.4    Stella, A.M.5    Pennisi, G.6    Cai, J.7    Pierce, W.M.8    Klein, J.B.9    Butterfield, D.A.10
  • 25
    • 39049146505 scopus 로고    scopus 로고
    • Age-related subproteomic analysis of mouse liver and kidney peroxisomes
    • 2231346 18042274 10.1186/1477-5956-5-19
    • Mi J Garcia-Arcos I Alvarez R Cristobal S Age-related subproteomic analysis of mouse liver and kidney peroxisomes Proteome Sci 2007, 5:19 2231346 18042274 10.1186/1477-5956-5-19
    • (2007) Proteome Sci , vol.5 , pp. 19
    • Mi, J.1    Garcia-Arcos, I.2    Alvarez, R.3    Cristobal, S.4
  • 26
    • 34250836448 scopus 로고    scopus 로고
    • Proteomics-based method for the assessment of marine pollution using liquid chromatography coupled with two-dimensional electrophoresis
    • 10.1021/pr060689s 17458988
    • Amelina H Apraiz I Sun W Cristobal S Proteomics-based method for the assessment of marine pollution using liquid chromatography coupled with two-dimensional electrophoresis J Proteome Res 2007, 6:2094-2104 10.1021/ pr060689s 17458988
    • (2007) J Proteome Res , vol.6 , pp. 2094-2104
    • Amelina, H.1    Apraiz, I.2    Sun, W.3    Cristobal, S.4
  • 28
    • 0037144512 scopus 로고    scopus 로고
    • Parasites as a viability cost of sexual selection in natural populations of mammals
    • 10.1126/science.1074196 12242433
    • Moore SL Wilson K Parasites as a viability cost of sexual selection in natural populations of mammals Science 2002, 297:2015-2018 10.1126/ science.1074196 12242433
    • (2002) Science , vol.297 , pp. 2015-2018
    • Moore, S.L.1    Wilson, K.2
  • 29
    • 22744459048 scopus 로고    scopus 로고
    • Effects of calorie restriction on reproductive and adrenal systems in Japanese quail: Are responses similar to mammals, particularly primates?
    • 10.1016/j.mad.2005.03.017 15935442
    • Ottinger MA Mobarak M Abdelnabi M Roth G Proudman J Ingram DK Effects of calorie restriction on reproductive and adrenal systems in Japanese quail: Are responses similar to mammals, particularly primates? Mech Ageing Dev 2005, 126:967-975 10.1016/j.mad.2005.03.017 15935442
    • (2005) Mech Ageing Dev , vol.126 , pp. 967-975
    • Ottinger, M.A.1    Mobarak, M.2    Abdelnabi, M.3    Roth, G.4    Proudman, J.5    Ingram, D.K.6
  • 30
    • 0028298529 scopus 로고
    • Age determination and longevity in fishes
    • 10.1159/000213580 7926859
    • Das M Age determination and longevity in fishes Gerontology 1994, 40:70-96 10.1159/000213580 7926859
    • (1994) Gerontology , vol.40 , pp. 70-96
    • Das, M.1
  • 32
    • 0033593550 scopus 로고    scopus 로고
    • Molecular biology of aging
    • 10.1016/S0092-8674(00)80567-X 9988222
    • Johnson FB Sinclair DA Guarente L Molecular biology of aging Cell 1999, 96:291-302 10.1016/S0092-8674(00)80567-X 9988222
    • (1999) Cell , vol.96 , pp. 291-302
    • Johnson, F.B.1    Sinclair, D.A.2    Guarente, L.3
  • 36
    • 0025279652 scopus 로고
    • The biology of transferrin
    • 10.1016/0009-8981(90)90278-Z 2208733
    • de Jong G van Dijk JP van Eijk HG The biology of transferrin Clin Chim Acta 1990, 190:1-46 10.1016/0009-8981(90)90278-Z 2208733
    • (1990) Clin Chim Acta , vol.190 , pp. 1-46
    • de Jong, G.1    van Dijk, J.P.2    van Eijk, H.G.3
  • 37
    • 29844457587 scopus 로고    scopus 로고
    • The evolution of iron chelators for the treatment of iron overload disease and cancer
    • 10.1124/pr.57.4.2 16382108
    • Kalinowski DS Richardson DR The evolution of iron chelators for the treatment of iron overload disease and cancer Pharmacol Rev 2005, 57:547-583 10.1124/pr.57.4.2 16382108
    • (2005) Pharmacol Rev , vol.57 , pp. 547-583
    • Kalinowski, D.S.1    Richardson, D.R.2
  • 38
    • 0035153971 scopus 로고    scopus 로고
    • Iron biology in immune function, muscle metabolism and neuronal functioning
    • discussion 580S. 11160590
    • Beard JL Iron biology in immune function, muscle metabolism and neuronal functioning J Nutr 2001, 131:568S-579S discussion 580S. 11160590
    • (2001) J Nutr , vol.131
    • Beard, J.L.1
  • 39
    • 34548415546 scopus 로고    scopus 로고
    • Age-related change of endocytic receptors megalin and cubilin in the kidney in rats
    • 10.1007/s10522-007-9093-7 17453355
    • Odera K Goto S Takahashi R Age-related change of endocytic receptors megalin and cubilin in the kidney in rats Biogerontology 2007, 8:505-515 10.1007/s10522-007-9093-7 17453355
    • (2007) Biogerontology , vol.8 , pp. 505-515
    • Odera, K.1    Goto, S.2    Takahashi, R.3
  • 40
    • 0026735060 scopus 로고
    • Biochemistry of peroxisomes
    • 10.1146/annurev.bi.61.070192.001105 1353950
    • Bosch van den H Schutgens RB Wanders RJ Tager JM Biochemistry of peroxisomes Annu Rev Biochem 1992, 61:157-197 10.1146/ annurev.bi.61.070192.001105 1353950
    • (1992) Annu Rev Biochem , vol.61 , pp. 157-197
    • Bosch, H.1    Schutgens, R.B.2    Wanders, R.J.3    Tager, J.M.4
  • 41
    • 0037361534 scopus 로고    scopus 로고
    • Cellular defense against singlet oxygen-induced oxidative damage by cytosolic NADP+-dependent isocitrate dehydrogenase
    • 10.1080/1071576021000050429 12688426
    • Kim SY Park JW Cellular defense against singlet oxygen-induced oxidative damage by cytosolic NADP+-dependent isocitrate dehydrogenase Free Radic Res 2003, 37:309-316 10.1080/1071576021000050429 12688426
    • (2003) Free Radic Res , vol.37 , pp. 309-316
    • Kim, S.Y.1    Park, J.W.2
  • 42
    • 0036614971 scopus 로고    scopus 로고
    • Cytosolic NADP(+)-dependent isocitrate dehydrogenase status modulates oxidative damage to cells
    • 10.1016/S0891-5849(02)00815-8 12031902
    • Lee SM Koh HJ Park DC Song BJ Huh TL Park JW Cytosolic NADP(+)-dependent isocitrate dehydrogenase status modulates oxidative damage to cells Free Radic Biol Med 2002, 32:1185-1196 10.1016/S0891-5849(02)00815-8 12031902
    • (2002) Free Radic Biol Med , vol.32 , pp. 1185-1196
    • Lee, S.M.1    Koh, H.J.2    Park, D.C.3    Song, B.J.4    Huh, T.L.5    Park, J.W.6
  • 43
    • 0033997260 scopus 로고    scopus 로고
    • Differences in protein level between neonatal and adult brain
    • 10.1002/(SICI)1522-2683(20000201)21:3<673::AID-ELPS673>3.0.CO;2-Y 10726776
    • Fountoulakis M Hardmaier R Schuller E Lubec G Differences in protein level between neonatal and adult brain Electrophoresis 2000, 21:673-678 10.1002/(SICI)1522-2683(20000201)21:3<673::AID-ELPS673>3.0.CO;2-Y 10726776
    • (2000) Electrophoresis , vol.21 , pp. 673-678
    • Fountoulakis, M.1    Hardmaier, R.2    Schuller, E.3    Lubec, G.4
  • 44
    • 28744432189 scopus 로고    scopus 로고
    • Regulation of replicative senescence by NADP+-dependent isocitrate dehydrogenase
    • 10.1016/j.freeradbiomed.2005.08.021 16337884
    • Kil IS Huh TL Lee YS Lee YM Park JW Regulation of replicative senescence by NADP+-dependent isocitrate dehydrogenase Free Radic Biol Med 2006, 40:110-119 10.1016/j.freeradbiomed.2005.08.021 16337884
    • (2006) Free Radic Biol Med , vol.40 , pp. 110-119
    • Kil, I.S.1    Huh, T.L.2    Lee, Y.S.3    Lee, Y.M.4    Park, J.W.5
  • 45
    • 1942489020 scopus 로고    scopus 로고
    • Protein profile of aging and its retardation by caloric restriction in neural retina
    • 10.1016/j.bbrc.2004.04.022 15110781
    • Li D Sun F Wang K Protein profile of aging and its retardation by caloric restriction in neural retina Biochem Biophys Res Commun 2004, 318:253-258 10.1016/j.bbrc.2004.04.022 15110781
    • (2004) Biochem Biophys Res Commun , vol.318 , pp. 253-258
    • Li, D.1    Sun, F.2    Wang, K.3
  • 46
    • 0033856330 scopus 로고    scopus 로고
    • Proteomic analysis of differential protein expression in primary hepatocytes induced by EGF, tumour necrosis factor alpha or the peroxisome proliferator nafenopin
    • 10.1046/j.1432-1327.2000.01487.x 10903494
    • Chevalier S Macdonald N Tonge R Rayner S Rowlinson R Shaw J Young J Davison M Roberts RA Proteomic analysis of differential protein expression in primary hepatocytes induced by EGF, tumour necrosis factor alpha or the peroxisome proliferator nafenopin Eur J Biochem 2000, 267:4624-4634 10.1046/j.1432-1327.2000.01487.x 10903494
    • (2000) Eur J Biochem , vol.267 , pp. 4624-4634
    • Chevalier, S.1    Macdonald, N.2    Tonge, R.3    Rayner, S.4    Rowlinson, R.5    Shaw, J.6    Young, J.7    Davison, M.8    Roberts, R.A.9
  • 47
    • 0033454076 scopus 로고    scopus 로고
    • Aging, mitochondria, and coenzyme Q(10): The neglected relationship
    • 10.1016/S0300-9084(99)00348-X 10917692
    • Bliznakov EG Aging, mitochondria, and coenzyme Q(10): The neglected relationship Biochimie 1999, 81:1131-1132 10.1016/S0300-9084(99)00348-X 10917692
    • (1999) Biochimie , vol.81 , pp. 1131-1132
    • Bliznakov, E.G.1
  • 48
    • 33748423353 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: An approach to understand pathological and biochemical alterations in AD
    • 10.1016/j.neurobiolaging.2005.09.021 16271804
    • Sultana R Boyd-Kimball D Poon HF Cai J Pierce WM Klein JB Merchant M Markesbery WR Butterfield DA Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: An approach to understand pathological and biochemical alterations in AD Neurobiol Aging 2006, 27:1564-1576 10.1016/j.neurobiolaging.2005.09.021 16271804
    • (2006) Neurobiol Aging , vol.27 , pp. 1564-1576
    • Sultana, R.1    Boyd-Kimball, D.2    Poon, H.F.3    Cai, J.4    Pierce, W.M.5    Klein, J.B.6    Merchant, M.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 51
    • 0037653659 scopus 로고    scopus 로고
    • Gender difference in glutathione metabolism during aging in mice
    • 10.1016/S0531-5565(03)00036-6 12742528
    • Wang H Liu H Liu RM Gender difference in glutathione metabolism during aging in mice Exp Gerontol 2003, 38:507-517 10.1016/ S0531-5565(03)00036-6 12742528
    • (2003) Exp Gerontol , vol.38 , pp. 507-517
    • Wang, H.1    Liu, H.2    Liu, R.M.3
  • 52
    • 58149498813 scopus 로고    scopus 로고
    • Glomerular function, structure, and number in renal allografts from older deceased donors
    • 10.1681/ASN.2008030306 18815243
    • Tan JC Workeneh B Busque S Blouch K Derby G Myers BD Glomerular function, structure, and number in renal allografts from older deceased donors J Am Soc Nephrol 2009, 20:181-188 10.1681/ASN.2008030306 18815243
    • (2009) J Am Soc Nephrol , vol.20 , pp. 181-188
    • Tan, J.C.1    Workeneh, B.2    Busque, S.3    Blouch, K.4    Derby, G.5    Myers, B.D.6
  • 53
    • 0031807109 scopus 로고    scopus 로고
    • Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis
    • 10.1002/elps.1150190526 9629911
    • Rabilloud T Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis Electrophoresis 1998, 19:758-760 10.1002/elps.1150190526 9629911
    • (1998) Electrophoresis , vol.19 , pp. 758-760
    • Rabilloud, T.1
  • 54
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3 942051
    • Bradford MM A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 1976, 72:248-254 10.1016/0003-2697(76)90527-3 942051
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1


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