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Volumn 10, Issue SUPPL. 1, 2010, Pages

Proteomic approaches to oxidative protein modifications implicated in the mechanism of aging

Author keywords

[No Author keywords available]

Indexed keywords

2,4 DINITROPHENOL; 3 NITROTYROSINE; AMINO ACID; ARGININE; BIOTIN; CREATINE KINASE; CYSTEINE; FLUORESCENT DYE; LYSINE; METHIONINE; METHIONINE SULFOXIDE REDUCTASE; PROLINE; REACTIVE OXYGEN METABOLITE; THREONINE;

EID: 77954667267     PISSN: 14441586     EISSN: 14470594     Source Type: Journal    
DOI: 10.1111/j.1447-0594.2010.00606.x     Document Type: Review
Times cited : (28)

References (64)
  • 1
    • 77049308856 scopus 로고
    • Aging theory based on free radical and radiation chemistry
    • Harman D. Aging theory based on free radical and radiation chemistry. J Gerontol 1956, 2:298-300.
    • (1956) J Gerontol , vol.2 , pp. 298-300
    • Harman, D.1
  • 2
    • 0014558234 scopus 로고
    • Prolongation of life: role of free radical reactions in aging
    • Harman D. Prolongation of life: role of free radical reactions in aging. J Am Geriatr Soc 1969, 17:721-735.
    • (1969) J Am Geriatr Soc , vol.17 , pp. 721-735
    • Harman, D.1
  • 3
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling
    • Finkel T. Oxygen radicals and signaling. Curr Opin Cell Biol 1998, 10:248-253.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 248-253
    • Finkel, T.1
  • 4
    • 0034876025 scopus 로고    scopus 로고
    • V-Ha-Ras overexpression induces superoxide production and alters levels of primary antioxidant enzymes
    • Yang JQ, Li S, Huang Y. V-Ha-Ras overexpression induces superoxide production and alters levels of primary antioxidant enzymes. Antioxid Redox Signal 2001, 3:697-709.
    • (2001) Antioxid Redox Signal , vol.3 , pp. 697-709
    • Yang, J.Q.1    Li, S.2    Huang, Y.3
  • 5
    • 0018049319 scopus 로고
    • Free radicals in cancer
    • Swartz HM. Free radicals in cancer. Ciba Found Symp 1978, 67:107-130.
    • (1978) Ciba Found Symp , vol.67 , pp. 107-130
    • Swartz, H.M.1
  • 6
    • 0020979668 scopus 로고
    • Free oxygen radicals: necessary contributors to tumor promotion and carcinogenesis
    • Troll W, Frenkel K, Teebor G. Free oxygen radicals: necessary contributors to tumor promotion and carcinogenesis. Princess Takamatsu Symp 1983, 14:207-218.
    • (1983) Princess Takamatsu Symp , vol.14 , pp. 207-218
    • Troll, W.1    Frenkel, K.2    Teebor, G.3
  • 7
    • 0025052917 scopus 로고
    • Molecular mechanisms of oxygen radical carcinogenesis and mutagenesis: the role of DNA base damage
    • Breimer LH. Molecular mechanisms of oxygen radical carcinogenesis and mutagenesis: the role of DNA base damage. Mol Carcinog 1990, 3:188-197.
    • (1990) Mol Carcinog , vol.3 , pp. 188-197
    • Breimer, L.H.1
  • 8
    • 0024193695 scopus 로고
    • Measuring oxidative damage in humans: relation to cancer and ageing
    • Ames BN. Measuring oxidative damage in humans: relation to cancer and ageing. IARC Sci Publ 1988, 89:407-416.
    • (1988) IARC Sci Publ , vol.89 , pp. 407-416
    • Ames, B.N.1
  • 9
    • 0023988217 scopus 로고
    • Oxidative damage to DNA: relation to species metabolic rate and life span
    • Adelman R, Saul RL, Ames BN. Oxidative damage to DNA: relation to species metabolic rate and life span. Proc Natl Acad Sci USA 1988, 85:2706-2708.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2706-2708
    • Adelman, R.1    Saul, R.L.2    Ames, B.N.3
  • 10
    • 0029888579 scopus 로고    scopus 로고
    • Non-linear accumulation of 8-hydroxy-2′-deoxyguanosine, a marker of oxidized DNA damage, during aging
    • Kaneko T, Tahara S, Matsuo M. Non-linear accumulation of 8-hydroxy-2′-deoxyguanosine, a marker of oxidized DNA damage, during aging. Mutat Res 1996, 316:277-285.
    • (1996) Mutat Res , vol.316 , pp. 277-285
    • Kaneko, T.1    Tahara, S.2    Matsuo, M.3
  • 11
    • 0344710499 scopus 로고
    • Inactivation of key metabolic enzymes by mixed-function oxidation reactions: possible implication in protein turnover and ageing
    • Fucci L, Oliver CN, Coon MJ, Stadtman ER. Inactivation of key metabolic enzymes by mixed-function oxidation reactions: possible implication in protein turnover and ageing. Proc Natl Acad Sci USA 1983, 80:1521-1525.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 1521-1525
    • Fucci, L.1    Oliver, C.N.2    Coon, M.J.3    Stadtman, E.R.4
  • 13
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman ER. Protein oxidation and aging. Science 1992, 257:1220-1224.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 14
    • 0025790342 scopus 로고
    • Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease
    • Smith CD, Carney JM, Starke-Reed PE. Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease. Proc Natl Acad Sci USA 1991, 88:10540-10543.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10540-10543
    • Smith, C.D.1    Carney, J.M.2    Starke-Reed, P.E.3
  • 15
    • 0008318301 scopus 로고
    • Selective oxidation of cysteine and methionine in normal and senile cataractous lenses
    • Garner MH, Spector A. Selective oxidation of cysteine and methionine in normal and senile cataractous lenses. Proc Natl Acad Sci USA 1980, 77:1274-1277.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1274-1277
    • Garner, M.H.1    Spector, A.2
  • 16
    • 0023600801 scopus 로고
    • Protein oxidation and loss of protease activity may lead to cataract formation in the aged lens
    • Taylor A, Davies KJ. Protein oxidation and loss of protease activity may lead to cataract formation in the aged lens. Free Radic Biol Med 1987, 3:371-377.
    • (1987) Free Radic Biol Med , vol.3 , pp. 371-377
    • Taylor, A.1    Davies, K.J.2
  • 17
    • 0026323623 scopus 로고
    • Macrophages and oxidized low density lipoproteins in the pathogenesis of atherosclerosis
    • Ylä-Herttuala S. Macrophages and oxidized low density lipoproteins in the pathogenesis of atherosclerosis. Ann Med 1991, 23:561-567.
    • (1991) Ann Med , vol.23 , pp. 561-567
    • Ylä-Herttuala, S.1
  • 18
    • 0027537768 scopus 로고
    • Glycation and oxidation: a role in the pathogenesis of atherosclerosis
    • Lyons TJ. Glycation and oxidation: a role in the pathogenesis of atherosclerosis. Am J Cardiol 1993, 71:26B-31.
    • (1993) Am J Cardiol , vol.71
    • Lyons, T.J.1
  • 19
    • 0035793088 scopus 로고    scopus 로고
    • Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins
    • Requena JR, Chao CC, Levine RL, Stadtman ER. Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proc Natl Acad Sci USA 2001, 98:69-74.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 69-74
    • Requena, J.R.1    Chao, C.C.2    Levine, R.L.3    Stadtman, E.R.4
  • 20
    • 0029965252 scopus 로고    scopus 로고
    • Analysis of protein carbonyls with 2,4-dinitrophenyl hydrazine and its antibodies by immunoblot in two-dimensional gel electrophoresis
    • Nakamura A, Goto S. Analysis of protein carbonyls with 2,4-dinitrophenyl hydrazine and its antibodies by immunoblot in two-dimensional gel electrophoresis. J Biochem 1996, 119:768-774.
    • (1996) J Biochem , vol.119 , pp. 768-774
    • Nakamura, A.1    Goto, S.2
  • 21
    • 0032190196 scopus 로고    scopus 로고
    • Identification of oxidized proteins based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunochemical detection, isoelectric focusing, and microsequencing
    • Yan LJ, Orr WC, Sohal RS. Identification of oxidized proteins based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunochemical detection, isoelectric focusing, and microsequencing. Anal Biochem 1998, 263:67-71.
    • (1998) Anal Biochem , vol.263 , pp. 67-71
    • Yan, L.J.1    Orr, W.C.2    Sohal, R.S.3
  • 22
    • 0033558989 scopus 로고    scopus 로고
    • Carbonylated proteins in aging and exercise: immunoblot approaches
    • Goto S, Nakamura A, Radak Z. Carbonylated proteins in aging and exercise: immunoblot approaches. Mech Ageing Dev 1999, 107:245-253.
    • (1999) Mech Ageing Dev , vol.107 , pp. 245-253
    • Goto, S.1    Nakamura, A.2    Radak, Z.3
  • 23
    • 0034578393 scopus 로고    scopus 로고
    • Dietary restriction initiated late in life can reduce mitochondrial protein carbonyls in rat livers: western blot studies
    • Nagai M, Takahashi R, Goto S. Dietary restriction initiated late in life can reduce mitochondrial protein carbonyls in rat livers: western blot studies. Biogerontology 2000, 1:321-328.
    • (2000) Biogerontology , vol.1 , pp. 321-328
    • Nagai, M.1    Takahashi, R.2    Goto, S.3
  • 24
    • 0034024347 scopus 로고    scopus 로고
    • Oxidative modification of creatine kinase BB in Alzheimer's disease brain
    • Aksenov M, Aksenova M, Butterfield DA, Markesbery WR. Oxidative modification of creatine kinase BB in Alzheimer's disease brain. J Neurochem 2000, 74:2520-2527.
    • (2000) J Neurochem , vol.74 , pp. 2520-2527
    • Aksenov, M.1    Aksenova, M.2    Butterfield, D.A.3    Markesbery, W.R.4
  • 27
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71
    • Castegna A, Aksenov M, Thongboonkerd V. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71. J Neurochem 2002, 82:1524-1532.
    • (2002) J Neurochem , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3
  • 28
    • 17644362744 scopus 로고    scopus 로고
    • Affinity chromatographic selection of carbonylated proteins followed by identification of oxidation sites using tandem mass spectrometry
    • Mirzaei H, Regnier F. Affinity chromatographic selection of carbonylated proteins followed by identification of oxidation sites using tandem mass spectrometry. Anal Chem 2005, 77:2386-2392.
    • (2005) Anal Chem , vol.77 , pp. 2386-2392
    • Mirzaei, H.1    Regnier, F.2
  • 30
    • 0035434379 scopus 로고    scopus 로고
    • Reactive carbonyl formation by oxidative and non-oxidative pathways
    • Adams S, Green P, Claxton R. Reactive carbonyl formation by oxidative and non-oxidative pathways. Front Biosci 2001, 6:A17-A24.
    • (2001) Front Biosci , vol.6
    • Adams, S.1    Green, P.2    Claxton, R.3
  • 33
    • 33745611162 scopus 로고    scopus 로고
    • Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease
    • Sacksteder CA, Qian WJ, Knyushko TV. Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease. Biochem 2006, 45:8009-8022.
    • (2006) Biochem , vol.45 , pp. 8009-8022
    • Sacksteder, C.A.1    Qian, W.J.2    Knyushko, T.V.3
  • 34
    • 33847709555 scopus 로고    scopus 로고
    • Proteomic analysis of protein nitration in rat cerebellum: effect of biological aging
    • Gokulrangan G, Zaidi A, Michaelis ML, Schöneich C. Proteomic analysis of protein nitration in rat cerebellum: effect of biological aging. J Neurochem 2007, 100:1494-1504.
    • (2007) J Neurochem , vol.100 , pp. 1494-1504
    • Gokulrangan, G.1    Zaidi, A.2    Michaelis, M.L.3    Schöneich, C.4
  • 35
    • 34548172399 scopus 로고    scopus 로고
    • Proteomic identification of nitrated brain proteins in amnestic mild cognitive impairment: a regional study
    • Sultana R, Reed T, Perluigi M, Coccia R, Pierce WM, Butterfield DA. Proteomic identification of nitrated brain proteins in amnestic mild cognitive impairment: a regional study. J Cell Mol Med 2007, 11:839-851.
    • (2007) J Cell Mol Med , vol.11 , pp. 839-851
    • Sultana, R.1    Reed, T.2    Perluigi, M.3    Coccia, R.4    Pierce, W.M.5    Butterfield, D.A.6
  • 36
    • 34247142905 scopus 로고    scopus 로고
    • Elevated levels of 3-nitrotyrosine in brain from subjects with amnestic mild cognitive impairment: implications for the role of nitration in the progression of Alzheimer's disease
    • Butterfield DA, Reed TT, Perluigi M. Elevated levels of 3-nitrotyrosine in brain from subjects with amnestic mild cognitive impairment: implications for the role of nitration in the progression of Alzheimer's disease. Brain Res 2007, 1148:243-248.
    • (2007) Brain Res , vol.1148 , pp. 243-248
    • Butterfield, D.A.1    Reed, T.T.2    Perluigi, M.3
  • 37
    • 67849126232 scopus 로고    scopus 로고
    • Proteomic identification of nitrated brain proteins in early Alzheimer's disease inferior parietal lobule
    • Reed TT, Pierce WM, Turner DM, Markesbery WR, Butterfield DA. Proteomic identification of nitrated brain proteins in early Alzheimer's disease inferior parietal lobule. J Cell Mol Med 2009, 18:2019-2029.
    • (2009) J Cell Mol Med , vol.18 , pp. 2019-2029
    • Reed, T.T.1    Pierce, W.M.2    Turner, D.M.3    Markesbery, W.R.4    Butterfield, D.A.5
  • 38
    • 24144487120 scopus 로고    scopus 로고
    • Identification of nitrated proteins in the normal rat brain using a proteomics approach
    • Suzuki Y, Tanaka M, Sohmiya M, Ichinose S, Omori A, Okamoto K. Identification of nitrated proteins in the normal rat brain using a proteomics approach. Neurol Res 2005, 27:630-633.
    • (2005) Neurol Res , vol.27 , pp. 630-633
    • Suzuki, Y.1    Tanaka, M.2    Sohmiya, M.3    Ichinose, S.4    Omori, A.5    Okamoto, K.6
  • 39
    • 0021950214 scopus 로고
    • Protein mixed-disulfides in cardiac cells. S-thiolation of soluble proteins in response to diamide
    • Grimm LM, Collison MW, Fisher RA, Thomas JA. Protein mixed-disulfides in cardiac cells. S-thiolation of soluble proteins in response to diamide. Biochim Biophys Acta 1985, 844:50-54.
    • (1985) Biochim Biophys Acta , vol.844 , pp. 50-54
    • Grimm, L.M.1    Collison, M.W.2    Fisher, R.A.3    Thomas, J.A.4
  • 40
    • 2542486403 scopus 로고    scopus 로고
    • Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue
    • Reddy S, Jones AD, Cross CE, Wong PS, Van Der Vliet A. Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue. Biochem J 2000, 347:821-827.
    • (2000) Biochem J , vol.347 , pp. 821-827
    • Reddy, S.1    Jones, A.D.2    Cross, C.E.3    Wong, P.S.4    Van Der Vliet, A.5
  • 41
    • 0034702868 scopus 로고    scopus 로고
    • Oxidant-induced S-glutathiolation inactivates protein kinase C-alpha (PKC-alpha): a potential mechanism of PKC isozyme regulation
    • Ward NE, Stewart JR, Ioannides CG, O'Brian CA. Oxidant-induced S-glutathiolation inactivates protein kinase C-alpha (PKC-alpha): a potential mechanism of PKC isozyme regulation. Biochem 2000, 39:10319-10329.
    • (2000) Biochem , vol.39 , pp. 10319-10329
    • Ward, N.E.1    Stewart, J.R.2    Ioannides, C.G.3    O'Brian, C.A.4
  • 42
    • 33947623122 scopus 로고    scopus 로고
    • Role of reversible, thioredoxin-sensitive oxidative protein modifications in cardiac myocytes
    • Kuster GM, Siwik DA, Pimentel DR, Colucci WS. Role of reversible, thioredoxin-sensitive oxidative protein modifications in cardiac myocytes. Antioxid Redox Signal 2006, 8:2153-2159.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 2153-2159
    • Kuster, G.M.1    Siwik, D.A.2    Pimentel, D.R.3    Colucci, W.S.4
  • 43
    • 0027238801 scopus 로고
    • Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase
    • Gravina SA, Mieyal JJ. Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochem 1993, 32:3368-3376.
    • (1993) Biochem , vol.32 , pp. 3368-3376
    • Gravina, S.A.1    Mieyal, J.J.2
  • 45
    • 0022552759 scopus 로고
    • A thin-gel isoelectric focusing method for quantitation of protein S-thiolation
    • Thomas JA, Beidler D. A thin-gel isoelectric focusing method for quantitation of protein S-thiolation. Anal Biochem 1986, 157:32-38.
    • (1986) Anal Biochem , vol.157 , pp. 32-38
    • Thomas, J.A.1    Beidler, D.2
  • 46
    • 0034702868 scopus 로고    scopus 로고
    • Oxidant-induced S-glutathiolation inactivates protein kinase C-alpha (PKC-alpha): a potential mechanism of PKC isozyme regulation
    • Ward NE, Stewart JR, Ioannides CG, O'Brian CA. Oxidant-induced S-glutathiolation inactivates protein kinase C-alpha (PKC-alpha): a potential mechanism of PKC isozyme regulation. Biochem 2000, 39:10319-10329.
    • (2000) Biochem , vol.39 , pp. 10319-10329
    • Ward, N.E.1    Stewart, J.R.2    Ioannides, C.G.3    O'Brian, C.A.4
  • 47
    • 0037155862 scopus 로고    scopus 로고
    • Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion
    • Eaton P, Byers HL, Leeds N, Ward MA, Shattock MJ. Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion. J Biol Chem 2002, 277:9806-9811.
    • (2002) J Biol Chem , vol.277 , pp. 9806-9811
    • Eaton, P.1    Byers, H.L.2    Leeds, N.3    Ward, M.A.4    Shattock, M.J.5
  • 48
    • 0033524399 scopus 로고    scopus 로고
    • Repair of oxidized calmodulin by methionine sulfoxide reductase restores ability to activate the plasma membrane Ca-ATPase
    • Sun H, Gao J, Ferrington DA, Biesiada H, Williams TD, Squier TC. Repair of oxidized calmodulin by methionine sulfoxide reductase restores ability to activate the plasma membrane Ca-ATPase. Biochem 1999, 38:105-112.
    • (1999) Biochem , vol.38 , pp. 105-112
    • Sun, H.1    Gao, J.2    Ferrington, D.A.3    Biesiada, H.4    Williams, T.D.5    Squier, T.C.6
  • 49
    • 0032815727 scopus 로고    scopus 로고
    • Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase
    • Sharov VS, Ferrington DA, Squier TC, Schöneich C. Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase. FEBS Lett 1999, 455:247-250.
    • (1999) FEBS Lett , vol.455 , pp. 247-250
    • Sharov, V.S.1    Ferrington, D.A.2    Squier, T.C.3    Schöneich, C.4
  • 50
    • 0032564345 scopus 로고    scopus 로고
    • Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress
    • Moskovitz J, Flescher E, Berlett BS, Azare J, Poston JM, Stadtman ER. Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress. Proc Natl Acad Sci USA 1998, 95:14071-14075.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14071-14075
    • Moskovitz, J.1    Flescher, E.2    Berlett, B.S.3    Azare, J.4    Poston, J.M.5    Stadtman, E.R.6
  • 52
    • 0032823578 scopus 로고    scopus 로고
    • Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain
    • Gabbita SP, Aksenov MY, Lovell MA, Markesbery WR. Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain. J Neurochem 1999, 73:1660-1666.
    • (1999) J Neurochem , vol.73 , pp. 1660-1666
    • Gabbita, S.P.1    Aksenov, M.Y.2    Lovell, M.A.3    Markesbery, W.R.4
  • 53
    • 0035339675 scopus 로고    scopus 로고
    • Rat peptide methionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging
    • Pt 3
    • Petropoulos I, Mary J, Perichon M, Friguet B. Rat peptide methionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging. Biochem J 2001, 355:819-825. Pt 3
    • (2001) Biochem J , vol.355 , pp. 819-825
    • Petropoulos, I.1    Mary, J.2    Perichon, M.3    Friguet, B.4
  • 54
    • 15444377616 scopus 로고    scopus 로고
    • Proteomic approach to determination of the significance of protein oxidation in the ageing of mouse hippocampus
    • Toda T, Morimasa T, Kobayashi S, Nomura K, Hatozaki T, Hirota M. Proteomic approach to determination of the significance of protein oxidation in the ageing of mouse hippocampus. Appl Genomics Proteomics 2003, 2:43-50.
    • (2003) Appl Genomics Proteomics , vol.2 , pp. 43-50
    • Toda, T.1    Morimasa, T.2    Kobayashi, S.3    Nomura, K.4    Hatozaki, T.5    Hirota, M.6
  • 55
    • 2542637241 scopus 로고    scopus 로고
    • Altered hippocampal transcript profile accompanies an age-related spatial memory deficit in mice
    • Verbitsky M, Yonan AL, Malleret G, Kandel ER, Gilliam TC, Pavlidis P. Altered hippocampal transcript profile accompanies an age-related spatial memory deficit in mice. Learn Mem 2004, 11:253-260.
    • (2004) Learn Mem , vol.11 , pp. 253-260
    • Verbitsky, M.1    Yonan, A.L.2    Malleret, G.3    Kandel, E.R.4    Gilliam, T.C.5    Pavlidis, P.6
  • 56
    • 0038206578 scopus 로고    scopus 로고
    • Gene microarrays in hippocampal aging: statistical profiling identifies novel processes correlated with cognitive impairment
    • Blalock EM, Chen KC, Sharrow K. Gene microarrays in hippocampal aging: statistical profiling identifies novel processes correlated with cognitive impairment. J Neurosci 2003, 23:3807-3819.
    • (2003) J Neurosci , vol.23 , pp. 3807-3819
    • Blalock, E.M.1    Chen, K.C.2    Sharrow, K.3
  • 57
    • 0031885987 scopus 로고    scopus 로고
    • Loss of conformational stability in calmodulin upon methionine oxidation
    • Gao J, Yin DH, Yao Y. Loss of conformational stability in calmodulin upon methionine oxidation. Biophys J 1998, 74:1115-1134.
    • (1998) Biophys J , vol.74 , pp. 1115-1134
    • Gao, J.1    Yin, D.H.2    Yao, Y.3
  • 58
    • 44949218293 scopus 로고    scopus 로고
    • Limited degradation of oxidized calmodulin by proteasome: formation of peptides
    • Strosova M, Voss P, Engels M, Horakova L, Grune T. Limited degradation of oxidized calmodulin by proteasome: formation of peptides. Arch Biochem Biophys 2008, 475:50-54.
    • (2008) Arch Biochem Biophys , vol.475 , pp. 50-54
    • Strosova, M.1    Voss, P.2    Engels, M.3    Horakova, L.4    Grune, T.5
  • 60
    • 0030567757 scopus 로고    scopus 로고
    • Decreased plasma membrane calcium transport activity in aging brain
    • Michaelis ML, Bigelow DJ, Schöneich C. Decreased plasma membrane calcium transport activity in aging brain. Life Sci 1996, 59:405-412.
    • (1996) Life Sci , vol.59 , pp. 405-412
    • Michaelis, M.L.1    Bigelow, D.J.2    Schöneich, C.3
  • 61
    • 0029969392 scopus 로고    scopus 로고
    • Oxidative modification of a carboxyl-terminal vicinal methionine in calmodulin by hydrogen peroxide inhibits calmodulin-dependent activation of the plasma membrane Ca-ATPase
    • Yao Y, Yin D, Jas GS. Oxidative modification of a carboxyl-terminal vicinal methionine in calmodulin by hydrogen peroxide inhibits calmodulin-dependent activation of the plasma membrane Ca-ATPase. Biochem 1996, 35:2767-2787.
    • (1996) Biochem , vol.35 , pp. 2767-2787
    • Yao, Y.1    Yin, D.2    Jas, G.S.3
  • 62
    • 0032581012 scopus 로고    scopus 로고
    • Progressive decline in the ability of calmodulin isolated from aged brain to activate the plasma membrane Ca-ATPase
    • Gao J, Yin D, Yao Y, Williams TD, Squier TC. Progressive decline in the ability of calmodulin isolated from aged brain to activate the plasma membrane Ca-ATPase. Biochemistry 1998, 37:9536-9548.
    • (1998) Biochemistry , vol.37 , pp. 9536-9548
    • Gao, J.1    Yin, D.2    Yao, Y.3    Williams, T.D.4    Squier, T.C.5
  • 63
  • 64
    • 2542468981 scopus 로고    scopus 로고
    • Dual-polarization interferometry: an analytical technique to measure changes in protein structure in real time, to determine the stoichiometry of binding events, and to differentiate between specific and nonspecific interactions
    • Swann MJ, Peel LL, Carrington S, Freeman NJ. Dual-polarization interferometry: an analytical technique to measure changes in protein structure in real time, to determine the stoichiometry of binding events, and to differentiate between specific and nonspecific interactions. Anal Biochem 2004, 329:190-198.
    • (2004) Anal Biochem , vol.329 , pp. 190-198
    • Swann, M.J.1    Peel, L.L.2    Carrington, S.3    Freeman, N.J.4


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