메뉴 건너뛰기




Volumn 694, Issue , 2010, Pages 1-13

Synthesis, modification and turnover of proteins during aging

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; MESSENGER RNA; PROTEASOME; RIBOSOME RNA; PROTEIN;

EID: 78049387574     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-7002-2_1     Document Type: Article
Times cited : (37)

References (118)
  • 1
    • 0029983808 scopus 로고    scopus 로고
    • Synthesis, modifications, and turnover of proteins during aging
    • DOI 10.1016/0531-5565(95)02022-5
    • Rattan SIS. Synthesis, modifications and turnover of proteins during aging. Exp Gerontol 1996; 31:33-47. (Pubitemid 26079660)
    • (1996) Experimental Gerontology , vol.31 , Issue.1-2 , pp. 33-47
    • Rattan, S.I.S.1
  • 3
    • 0347318051 scopus 로고    scopus 로고
    • Translational factors: In sickness and in health
    • Abbott CM, Proud CG. Translational factors: in sickness and in health. Trends Biochem Sci 2004; 29:25-31.
    • (2004) Trends Biochem Sci , vol.29 , pp. 25-31
    • Abbott, C.M.1    Proud, C.G.2
  • 4
    • 0030018016 scopus 로고    scopus 로고
    • The current status of the protein error theory of aging
    • DOI 10.1016/0531-5565(96)00008-3
    • Holliday R. The current status of the protein error theory of aging. Exp Gerontol 1996; 31:449-52. (Pubitemid 26234901)
    • (1996) Experimental Gerontology , vol.31 , Issue.4 , pp. 449-452
    • Holliday, R.1
  • 5
    • 33646793360 scopus 로고    scopus 로고
    • Accumulation of altered proteins and ageing: Causes and effects
    • DOI 10.1016/j.exger.2006.03.004, PII S0531556506000702
    • Hipkiss A. Accumulation of altered proteins and ageing: causes and effects. Exp Gerontol 2006; 41:464-73. (Pubitemid 43765899)
    • (2006) Experimental Gerontology , vol.41 , Issue.5 , pp. 464-473
    • Hipkiss, A.R.1
  • 7
    • 0023634740 scopus 로고
    • Altered sensitivity of protein synthesis to paromomycin in extracts from aging human diploid fibroblasts
    • DOI 10.1016/0531-5565(87)90037-4
    • Luce MC, Bunn CL. Altered sensitivity of protein synthesis to paromomycin in extracts from aging human diploid fibroblasts. Exp Gerontol 1987; 22:165-77. (Pubitemid 17152560)
    • (1987) Experimental Gerontology , vol.22 , Issue.3 , pp. 165-177
    • Luce, M.C.1    Bunn, C.L.2
  • 8
    • 0024580503 scopus 로고
    • Decreased accuracy of protein synthesis in extracts from aging human diploid fibroblasts
    • DOI 10.1016/0531-5565(89)90022-3
    • Luce MC, Bunn CL. Decreased accuracy of protein synthesis in extracts from aging human diploid fibroblasts. Exp Gerontol 1989; 24:113-25. (Pubitemid 19078524)
    • (1989) Experimental Gerontology , vol.24 , Issue.2 , pp. 113-125
    • Luce, M.C.1    Bunn, C.L.2
  • 9
    • 0021305472 scopus 로고
    • Evidence that paromomycin induces premature ageing in human fibroblasts
    • Holliday R, Rattan SIS. Evidence that paromomycin induces premature ageing in human fibroblasts. Monogr Devl Biol 1984; 17:221-33.
    • (1984) Monogr Devl Biol , vol.17 , pp. 221-233
    • Holliday, R.1    Rattan, S.I.S.2
  • 10
    • 0023131097 scopus 로고
    • Aminoglycoside antibiotic treatment of human fibroblasts: Intracellular accumulation, molecular changes and the loss of ribosomal accuracy
    • Buchanan JH, Stevens A, Sidhu J. Aminoglycoside antibiotic treatment of human fibroblasts: intracellular accumulation, molecular changes and the loss of ribosomal accuracy. Eur J Cell Biol 1987; 43:141-7. (Pubitemid 17025030)
    • (1987) European Journal of Cell Biology , vol.43 , Issue.1 , pp. 141-147
    • Buchanan, J.H.1    Stevens, A.2    Sidhu, J.3
  • 11
    • 0036725380 scopus 로고    scopus 로고
    • Translational fidelity, protein oxidation, and senescence: Lessons from bacteria
    • DOI 10.1016/S1568-1637(02)00028-4, PII S1568163702000284
    • Nyström T. Translational fidelity, protein oxidation and senescence: lessons from bacteria. Ageing Res Rev 2002; 1:693-703. (Pubitemid 38340325)
    • (2002) Ageing Research Reviews , vol.1 , Issue.4 , pp. 693-703
    • Nystrom, T.1
  • 12
    • 0036898921 scopus 로고    scopus 로고
    • Aging in bacteria
    • DOI 10.1016/S1369-5274(02)00367-3
    • Nyström T. Aging in bacteria. Curr Opin Microbiol 2002; 5:596-601. (Pubitemid 35434550)
    • (2002) Current Opinion in Microbiology , vol.5 , Issue.6 , pp. 596-601
    • Nystrom, T.1
  • 13
    • 0034575086 scopus 로고    scopus 로고
    • Deletion and dosage modulation of the eEF1A gene in Podospora anserina: Effect on the life cycle
    • Silar P, Rossignol M, Haedens V et al. Deletion and dosage modulation of the eEF1A gene in Podospora anserina: effect on the life cycle. Biogerontology 2000; 1:47-54.
    • (2000) Biogerontology , vol.1 , pp. 47-54
    • Silar, P.1    Rossignol, M.2    Haedens, V.3
  • 15
    • 0033213918 scopus 로고    scopus 로고
    • Translation initiation: Adept at adapting
    • DOI 10.1016/S0968-0004(99)01457-7, PII S0968000499014577
    • Dever TE. Translation initiation: adept at adapting. TIBS 1999; 24:398-403. (Pubitemid 29450448)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.10 , pp. 398-403
    • Dever, T.E.1
  • 16
    • 0000091608 scopus 로고    scopus 로고
    • Sonenberg N, Hershey JWB, Mathews MB, eds. Translational Control of Gene Expression. New York: Cold Spring Harbor Laboratory Press
    • Hershey JWB, Merrick WC. The pathway and mechanism of inititation of protein synthesis. In: Sonenberg N, Hershey JWB, Mathews MB, eds. Translational Control of Gene Expression. New York: Cold Spring Harbor Laboratory Press, 2000:33-88.
    • (2000) The Pathway and Mechanism of Inititation of Protein Synthesis , pp. 33-88
    • Jwb, H.1    Merrick, W.C.2
  • 17
    • 0030890292 scopus 로고    scopus 로고
    • Dramatic attenuation of hypusine formation on eukaryotic initiation factor 5A during senescence of IMR-90 human diploid fibroblasts
    • DOI 10.1002/(SICI)1097-4652(19970 3)170:3<248::AID-JCP5>3.0.CO;2-O
    • Chen ZP, Chen KY. Dramatic attenuation of hypusine formation on eukaryotic initiation factor 5A during senescence of IMR-90 human diploid fibroblasts. J Cell Physiol 1997; 170:248-54. (Pubitemid 27117908)
    • (1997) Journal of Cellular Physiology , vol.170 , Issue.3 , pp. 248-254
    • Chen, Z.P.1    Chen, K.Y.2
  • 18
    • 65549167195 scopus 로고    scopus 로고
    • Hypusine-containing protein eIF5A promotes translation elongation
    • Saini P, Eyler DE, Green R et al. Hypusine-containing protein eIF5A promotes translation elongation. Nature 2009; 459:118-21.
    • (2009) Nature , vol.459 , pp. 118-121
    • Saini, P.1    Eyler, D.E.2    Green, R.3
  • 19
    • 0025749689 scopus 로고
    • Effect of age on liver protein synthesis and degradation
    • Ward W, Richardson A. Effect of age on liver protein synthesis and degradation. Hepatol 1991; 14:935-48.
    • (1991) Hepatol , vol.14 , pp. 935-948
    • Ward, W.1    Richardson, A.2
  • 21
    • 0025027287 scopus 로고
    • Eukaryotic protein elongation factors
    • Riis B, Rattan SIS, Clark BFC et al. Eukaryotic protein elongation factors. TIBS 1990; 15:420-4.
    • (1990) TIBS , vol.15 , pp. 420-424
    • Riis, B.1    Sis, R.2    Bfc, C.3
  • 22
    • 0043159108 scopus 로고    scopus 로고
    • Elongation factors in protein biosynthesis
    • DOI 10.1016/S0968-0004(03)00162-2
    • Andersen GR, Nissen P, Nyborg J. Elongation factors in protein biosynthesis. Trends Biochem Sci 2003; 28:434-41. (Pubitemid 36976746)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.8 , pp. 434-441
    • Andersen, G.R.1    Nissen, P.2    Nyborg, J.3
  • 23
    • 0026718508 scopus 로고
    • Mechanism and regulation of eukaryotic protein synthesis
    • Merrick WC. Mechanism and regulation of eukaryotic protein synthesis. Microbiol Rev 1992; 56:291-315.
    • (1992) Microbiol Rev , vol.56 , pp. 291-315
    • Merrick, W.C.1
  • 24
    • 0000825748 scopus 로고
    • Effect of aging on translation and transcription
    • Richardson A, Semsei I. Effect of aging on translation and transcription. Rev Biol Res Aging 1987; 3:467-83.
    • (1987) Rev Biol Res Aging , vol.3 , pp. 467-483
    • Richardson, A.1    Semsei, I.2
  • 25
    • 0025735660 scopus 로고
    • Effect of age and restricted feeding on polypeptide chain assembly kinetics in liver protein synthesis in vivo
    • Merry BJ, Holehan AM. Effect of age and restricted feeding on polypeptide chain assembly kinetics in liver protein synthesis in vivo. Mech Ageing Develop 1991; 58:139-50.
    • (1991) Mech Ageing Develop , vol.58 , pp. 139-150
    • Merry, B.J.1    Holehan, A.M.2
  • 26
    • 0005144210 scopus 로고
    • Regulation of protein synthesis during ageing
    • Rattan SIS. Regulation of protein synthesis during ageing. Eur J Gerontol 1992; 1:128-36.
    • (1992) Eur J Gerontol , vol.1 , pp. 128-136
    • Rattan, S.I.S.1
  • 27
    • 0001095194 scopus 로고
    • Sohal RS, Birnbaum LS, Cutler RG, editors. Molecular Biology of Aging: Gene Stability and Gene Expression. New York: Raven Press
    • Webster GC. Protein synthesis in aging organisms. In: Sohal RS, Birnbaum LS, Cutler RG, editors. Molecular Biology of Aging: Gene Stability and Gene Expression. New York: Raven Press; 1985:263-89.
    • (1985) Protein Synthesis in Aging Organisms , pp. 263-289
    • Webster, G.C.1
  • 29
    • 0022312147 scopus 로고
    • Accumulation of heat-labile elongation factor 2 in the liver of mice and rats
    • DOI 10.1016/0531-5565(85)90012-9
    • Takahashi R, Mori N, Goto S. Accumulation of heat-labile elongation factor 2 in the liver of mice and rats. Exp Gerontol 1985; 20:325-31. (Pubitemid 16152738)
    • (1985) Experimental Gerontology , vol.20 , Issue.6 , pp. 325-331
    • Takahashi, R.1    Mori, N.2    Goto, S.3
  • 30
    • 0025297174 scopus 로고
    • Reduced levels of ADP-ribosylatable elongation factor-2 in aged and SV40-transformed human cell cultures
    • DOI 10.1016/0014-5793(90)81502-F
    • Riis B, Rattan SIS, Derventzi A et al. Reduced levels of ADP-ribosylatable elongation factor-2 in aged and SV40-transformed human cells. FEBS Lett 1990; 266:45-7. (Pubitemid 20194169)
    • (1990) FEBS Letters , vol.266 , Issue.1-2 , pp. 45-47
    • Riis, B.1    Rattan, S.I.S.2    Derventzi, A.3    Clark, B.F.C.4
  • 31
    • 0026070525 scopus 로고
    • Dietary calorie restriction does not affect the levels of protein elongation factors in rat livers during ageing
    • Rattan SIS, Ward WF, Glenting M et al. Dietary calorie restriction does not affect the levels of protein elongation factors in rat livers during ageing. Mech Ageing Develop 1991; 58:85-91.
    • (1991) Mech Ageing Develop , vol.58 , pp. 85-91
    • Sis, R.1    Ward, W.F.2    Glenting, M.3
  • 32
    • 0032901078 scopus 로고    scopus 로고
    • Effects of aging on the various steps of protein synthesis: Fragmentation of elongation factor 2
    • DOI 10.1016/S0891-5849(98)00202-0, PII S0891584998002020
    • Parrado J, Bougria M, Ayala A et al. Effects of aging on the various steps of protein synthesis: fragmentation of elongation factor 2. Free Rad Biol Med 1999; 26:362-70. (Pubitemid 29013468)
    • (1999) Free Radical Biology and Medicine , vol.26 , Issue.3-4 , pp. 362-370
    • Parrado, J.1    Bougria, M.2    Ayala, A.3    Castano, A.4    Machado, A.5
  • 34
    • 40649129442 scopus 로고    scopus 로고
    • Nonenzymatic post-translational protein modifications in ageing
    • Soskic V, Groebe K, Schrattenholz A. Nonenzymatic post-translational protein modifications in ageing. Exp Gerontol 2008; 43:247-57.
    • (2008) Exp Gerontol , vol.43 , pp. 247-257
    • Soskic, V.1    Groebe, K.2    Schrattenholz, A.3
  • 35
    • 79959714765 scopus 로고    scopus 로고
    • Protein folding and misfolding, relevance to disease and biological function
    • Smith HJ, Simons C, Seewell RDE, Eds. Boca Raton: CRC Press
    • Stefani M. Protein folding and misfolding, relevance to disease and biological function. In: Smith HJ, Simons C, Seewell RDE, eds. Protein Misfolding in Neurodegenerative Diseases: Mechanisms and Therapeutic Strategies. Boca Raton: CRC Press, 2008:2-66.
    • (2008) Protein Misfolding in Neurodegenerative Diseases: Mechanisms and Therapeutic Strategies , pp. 2-66
    • Stefani, M.1
  • 36
    • 49449085504 scopus 로고    scopus 로고
    • A quantitative atlas of mitotic phosphorylation
    • Dephoure N, Zhou C, Villén J et al. A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci USA 2008; 105:10762-7.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10762-10767
    • Dephoure, N.1    Zhou, C.2    Villén, J.3
  • 37
    • 84881556500 scopus 로고    scopus 로고
    • Cellular senescence in vitro
    • doi:10.1002/9780470015902. pub2
    • Rattan SIS. Cellular senescence in vitro. Encyclopedia of Life Sciences 2008; doi:10.1002/9780470015902. a0002567.pub2.
    • (2008) Encyclopedia of Life Sciences
    • Rattan, S.I.S.1
  • 38
    • 0029317383 scopus 로고
    • Origins of G1 arrest in senescent human fibroblasts
    • Stein GH, Dulic V. Origins of G1 arrest in senescent human fibroblasts. BioEssays 1995; 17:537-43.
    • (1995) BioEssays , vol.17 , pp. 537-543
    • Stein, G.H.1    Dulic, V.2
  • 39
    • 33947513279 scopus 로고    scopus 로고
    • Modulation of replicative senescence of diploid human cells by nuclear ERK signaling
    • DOI 10.1074/jbc.M604955200
    • Tresini M, Lorenzini A, Torres C et al. Modulation of replicative senescence of diploid human cells by nuclear ERK signaling. J Biol Chem 2007; 282:4136-51. (Pubitemid 47084490)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.6 , pp. 4136-4151
    • Tresini, M.1    Lorenzini, A.2    Torres, C.3    Cristofalo, V.J.4
  • 40
    • 40149101710 scopus 로고    scopus 로고
    • FoxO transcription factors in oxidative stress response and ageing - A new fork on the way to longevity?
    • DOI 10.1515/BC.2008.033
    • Sedding DG. FoxO transcription factors in oxidative stress response and ageing-a new fork on the way to longevity? Biol Chem 2008; 389:279-83. (Pubitemid 351329031)
    • (2008) Biological Chemistry , vol.389 , Issue.3 , pp. 279-283
    • Sedding, D.G.1
  • 41
  • 44
    • 79959718980 scopus 로고
    • Failure in S6 protein phosphorylation by serum stimulation of senescent human diploid fibroblasts
    • Kihara F, Ninomyia-Tsuji J, Ishibashi S et al. Failure in S6 protein phosphorylation by serum stimulation of senescent human diploid fibroblasts, TIG-1. Mech Ageing Dev 1986; 20:305-13.
    • (1986) TIG-1. Mech Ageing Dev , vol.20 , pp. 305-313
    • Kihara, F.1    Ninomyia-Tsuji, J.2    Ishibashi, S.3
  • 45
    • 0027431143 scopus 로고
    • Serine/threonine protein kinases and calcium-dependent protease in senescent IMR-90 fibroblasts
    • Blumenthal EJ, Miller ACK, Stein GH et al. Serine/threonine protein kinases and calcium-dependent protease in senescent IMR-90 fibroblasts. Mech Ageing Dev 1993; 72:13-24.
    • (1993) Mech Ageing Dev , vol.72 , pp. 13-24
    • Blumenthal, E.J.1    Ack, M.2    Stein, G.H.3
  • 46
    • 0027208232 scopus 로고
    • Effect of the tumor promoter phorbol 12-myristate 13-acetate (PMA) on proliferation of young and senescent WI-38 human diploid fibroblasts
    • DOI 10.1006/excr.1993.1085
    • De Tata V, Ptasznik A, Cristofalo VJ. Effect of tumor promoter phorbol 12-myristate 13-acetate (PMA) on proliferation of young and senescent WI-38 human diploid fibroblasts. Exp Cell Res 1993; 205:261-9. (Pubitemid 23192130)
    • (1993) Experimental Cell Research , vol.205 , Issue.2 , pp. 261-269
    • De Tata, V.1    Ptasznik, A.2    Cristofalo, V.J.3
  • 48
    • 0027257988 scopus 로고
    • Phorbol ester PMA stimulates protein synthesis and increases the levels of active elongation factors EF-1a and EF-2 in ageing human fibroblasts
    • Derventzi A, Rattan SIS, Clark BFC. Phorbol ester PMA stimulates protein synthesis and increases the levels of active elongation factors EF-1a and EF-2 in ageing human fibroblasts. Mech Ageing Dev 1993; 69:193-205.
    • (1993) Mech Ageing Dev , vol.69 , pp. 193-205
    • Derventzi, A.1    Sis, R.2    Clark, B.F.C.3
  • 49
    • 0028268894 scopus 로고
    • Aging and immune function: Cellular and biochemical analyses
    • DOI 10.1016/0531-5565(94)90060-4
    • Miller RA. Aging and immune function: cellular and biochemical analyses. Exp Gerontol 1994; 29:21-35. (Pubitemid 24072658)
    • (1994) Experimental Gerontology , vol.29 , Issue.1 , pp. 21-35
    • Miller, R.A.1
  • 50
    • 33846050032 scopus 로고    scopus 로고
    • 3-dependent activation of p38 MAPK in rat intestinal cells
    • DOI 10.1007/s10522-006-9031-0
    • Pardo VG, Facchinetti MM, Curino A et al. Age-related alteration of 1alpha,25(OH)(2)-vitamin D (3)-dependent activation of p38 MAPK in rat intestinal cells. Biogerontology 2007; 8:13-24. (Pubitemid 46062617)
    • (2007) Biogerontology , vol.8 , Issue.1 , pp. 13-24
    • Pardo, V.G.1    Facchinetti, M.M.2    Curino, A.3    Boland, R.4    Boland, A.R.5
  • 52
    • 0036569401 scopus 로고    scopus 로고
    • Carbonyl modified proteins in cellular regulation, aging, and disease
    • DOI 10.1016/S0891-5849(02)00765-7, PII S0891584902007657
    • Levine RL. Carbonyl modified proteins in cellular regulation, aging and disease. Free Rad Biol Med 2002; 32:790-6. (Pubitemid 34439249)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.9 , pp. 790-796
    • Levine, R.L.1
  • 54
    • 0034571026 scopus 로고    scopus 로고
    • Oxidative stress, aging and the proteasomal system
    • Grune T. Oxidative stress, aging and the proteasomal system. Biogerontology 2000; 1:31-40.
    • (2000) Biogerontology , vol.1 , pp. 31-40
    • Grune, T.1
  • 55
    • 3442898781 scopus 로고    scopus 로고
    • Post-translational modifications of proteins: Implications for aging, antigen recognition, and autoimmunity
    • DOI 10.1023/B:BGEN.0000031152.31352.8b
    • Cloos PA, Christgau S. Post-translational modifications of proteins: implications for aging, antigen recognition and autoimmunity. Biogerontology 2004; 5:139-58. (Pubitemid 39004541)
    • (2004) Biogerontology , vol.5 , Issue.3 , pp. 139-158
    • Cloos, P.A.C.1    Christgau, S.2
  • 56
    • 62549088648 scopus 로고    scopus 로고
    • Protein stability and resistance to oxidative stress are determinants of longevity in the longest-living rodent, the naked mole-rat
    • Perez VI, Buffenstein R, Masamsetti V et al. Protein stability and resistance to oxidative stress are determinants of longevity in the longest-living rodent, the naked mole-rat. Proc Natl Acad Sci USA 2009.
    • (2009) Proc Natl Acad Sci USA
    • Perez, V.I.1    Buffenstein, R.2    Masamsetti, V.3
  • 57
    • 0035894209 scopus 로고    scopus 로고
    • Reduced levels of oxidized and glycoxidized proteins in human fibroblasts exposed to repeated mild heat shock during serial passaging in vitro
    • DOI 10.1016/S0891-5849(01)00752-3, PII S0891584901007523
    • Verbeke P, Clark BFC, Rattan SIS. Reduced levels of oxidized and glycoxidized proteins in human fibroblasts exposed to repeated mild heat shock during serial passaging in vitro. Free Rad Biol Med 2001; 31:1593-602. (Pubitemid 34024981)
    • (2001) Free Radical Biology and Medicine , vol.31 , Issue.12 , pp. 1593-1602
    • Verbeke, P.1    Clark, B.F.C.2    Rattan, S.I.S.3
  • 61
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • DOI 10.1016/S0891-5849(02)00780-3, PII S0891584902007803
    • Beal MF. Oxidatively modified proteins in aging and disease. Free Rad Biol Med 2002; 32:797-803. (Pubitemid 34439250)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.9 , pp. 797-803
    • Beal M.Flint1
  • 64
    • 0024350029 scopus 로고
    • Implication of lysine residues in the loss of enzymatic activity in rat liver 6-phosphogluconate dehydrogenase found in aging
    • Gordillo E, Ayala A, Bautista J et al. Implication of lysine residues in the loss of enzymatic activity in rat liver 6-phosphogluconate dehydrogenase found in aging. J Biol Chem 1989; 264:17024-8. (Pubitemid 19255530)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.29 , pp. 17024-17028
    • Gordillo, E.1    Ayala, A.2    Bautista, J.3    Machado, A.4
  • 65
    • 0001582194 scopus 로고
    • Age-related effects in enzyme metabolism and catalysis
    • Gafni A. Age-related effects in enzyme metabolism and catalysis. Rev Biol Res Aging 1990; 4:315-36.
    • (1990) Rev Biol Res Aging , vol.4 , pp. 315-336
    • Gafni, A.1
  • 66
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman ER. Protein oxidation and aging. Science 1992; 257:1220-4.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 67
  • 69
    • 0034122917 scopus 로고    scopus 로고
    • Increase of oxidatively modified protein is associated with a decrease of proteasome activity and content in aging epidermal cells
    • Petropoulos I, Conconi M, Wang X et al. Increase of oxidatively modified protein is associated with a decrease of proteasome activity and content in aging epidermal cells. J Gerontol Biol Sci 2000; 55A:B220-B7.
    • (2000) J Gerontol Biol Sci , vol.55 A
    • Petropoulos, I.1    Conconi, M.2    Wang, X.3
  • 70
    • 68549135300 scopus 로고    scopus 로고
    • 2-mediated oxidative stress affects human hair color by blunting methionine sulfoxide repair
    • 2-mediated oxidative stress affects human hair color by blunting methionine sulfoxide repair. FASEB J 2009.
    • (2009) FASEB J
    • Wood, J.M.1    Decker, H.2    Hartmann, H.3
  • 73
    • 31044442243 scopus 로고    scopus 로고
    • Methylglyoxal comes of AGE
    • DOI 10.1016/j.cell.2006.01.002, PII S009286740600050X
    • Ramasamy R, Yan SF, Schmidt AM. Methylglyoxal comes of AGE. Cell 2006; 124:258-60. (Pubitemid 43121973)
    • (2006) Cell , vol.124 , Issue.2 , pp. 258-260
    • Ramasamy, R.1    Yan, S.F.2    Schmidt, A.M.3
  • 75
    • 0023805011 scopus 로고
    • A study of the age-related acceleration of glycation of tissue proteins in rats
    • Oimomi M, Maeda Y, Hata F et al. A study of the age-related acceleration of glycation of tissue proteins in rats. J Gerontol 1988; 43:B98-101.
    • (1988) J Gerontol , vol.43
    • Oimomi, M.1    Maeda, Y.2    Hata, F.3
  • 76
    • 0025883029 scopus 로고
    • Changes in the amount of e-hexosyllysine, UV absorbance and fluorescence of collagen with age in different animal species
    • Miksík I, Deyl Z. Changes in the amount of e-hexosyllysine, UV absorbance and fluorescence of collagen with age in different animal species. J Gerontol 1991; 46:B111-6.
    • (1991) J Gerontol , vol.46
    • Miksík, I.1    Deyl, Z.2
  • 78
    • 0026452158 scopus 로고
    • Hemoglobin-AGE: A circulating marker of advanced glycosylation
    • Makita Z, Vlassara H, Rayfield E et al. Hemoglobin-AGE: a circulating marker of advanced glycosylation. Science 1992; 258:651-3.
    • (1992) Science , vol.258 , pp. 651-653
    • Makita, Z.1    Vlassara, H.2    Rayfield, E.3
  • 80
    • 0022538894 scopus 로고
    • Molecular basis of the isozymes of bovine glucose-6-phosphate isomerase
    • Cini JK, Gracy RW. Molecular basis of the isozyme of bovine glucose-6-phosphate isomerase. Arch Biochem Biophys 1986; 249:500-5. (Pubitemid 16023765)
    • (1986) Archives of Biochemistry and Biophysics , vol.249 , Issue.2 , pp. 500-505
    • Cini, J.K.1    Gracy, R.W.2
  • 81
    • 0023031858 scopus 로고
    • Age-dependent accumulation of protein residues which can be hydrolyzed to D-aspartic acid in human erythrocytes
    • Brunauer LS, Clarke S. Age-dependent accumulation of protein residues which can be hydrolyzed to d-aspartic acid in human erythrocytes. J Biol Chem 1986; 261:12538-43. (Pubitemid 17204202)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.27 , pp. 12538-12543
    • Brunauer, L.S.1    Clarke, S.2
  • 83
    • 0033740223 scopus 로고    scopus 로고
    • Comparative characterization of poly(ADP-ribose) polymerase-1 from two mammalian species with different life span
    • Beneke S, Alvarez-Gonzalez R, Bürkle A. Comparative characterization of poly(ADP-ribose) polymerase-1 from two mammalian species with different life span. Exp Gerontol 2000; 35:989-1002.
    • (2000) Exp Gerontol , vol.35 , pp. 989-1002
    • Beneke, S.1    Alvarez-Gonzalez, R.2    Bürkle, A.3
  • 84
    • 0034814670 scopus 로고    scopus 로고
    • Physiology and pathophysiology of poly(ADP-ribosyl)ation
    • DOI 10.1002/bies.1115
    • Bürkle A. Physiology and pathophysiology of poly(ADP-ribosyl)ation. BioEssays 2001; 23:795-806. (Pubitemid 32901331)
    • (2001) BioEssays , vol.23 , Issue.9 , pp. 795-806
    • Burkle, A.1
  • 85
    • 0025981326 scopus 로고
    • Decline of Poly(ADP-ribosyl)ation during in vitro senescence in human diploid fibroblasts
    • Dell'Orco RT, Anderson LE. Decline of poly(ADP-ribosyl)ation during in vitro senescence in human diploid fibroblasts. J Cell Physiol 1991; 146:216-21. (Pubitemid 21910043)
    • (1991) Journal of Cellular Physiology , vol.146 , Issue.2 , pp. 216-221
    • Dell'Orco, R.T.1    Anderson, L.E.2
  • 86
    • 0027081044 scopus 로고
    • Poly(ADP-ribose) polymerase activity in mononuclear leukocytes of 13 mammalian species correlates with species-specific life span
    • DOI 10.1073/pnas.89.24.11759
    • Grube K, Bürkle A. Poly(ADP-ribose) polymerase activity in mononuclear leukocytes of 13 mammalian species correlates with species-specific life span. Proc Natl Acad Sci USA 1992; 89:11759-63. (Pubitemid 23004723)
    • (1992) Proceedings of the National Academy of Sciences of the United States of America , vol.89 , Issue.24 , pp. 11759-11763
    • Grube, K.1    Burkle, A.2
  • 87
    • 0035854372 scopus 로고    scopus 로고
    • State of the Arg: Protein methylation at arginine comes of age
    • DOI 10.1016/S0092-8674(01)00423-8
    • McBride AE, Silver PA. State of the Arg: protein methylation at arginine comes of age. Cell 2001; 106:5-8. (Pubitemid 32709951)
    • (2001) Cell , vol.106 , Issue.1 , pp. 5-8
    • McBride, A.E.1    Silver, P.A.2
  • 88
    • 0027096061 scopus 로고
    • Protein syn thesis, post-translational modifications and aging
    • Rattan SIS, Derventzi A, Clark BFC. Protein synthesis, post-translational modifications and aging. Ann NY Acad Sci 1992; 663:48-62.
    • (1992) Ann NY Acad Sci , vol.663 , pp. 48-62
    • Sis, R.1    Derventzi, A.2    Clark, B.F.C.3
  • 89
    • 0342362985 scopus 로고
    • Macromolecular methylation during aging
    • Mays-Hoopes LL. Macromolecular methylation during aging. Rev Biol Res Aging 1985; 2:361-93.
    • (1985) Rev Biol Res Aging , vol.2 , pp. 361-393
    • Mays-Hoopes, L.L.1
  • 90
    • 0022457847 scopus 로고
    • Protein carboxyl methyltransferase and methyl acceptor proteins in aging and cataractous tissue of the human eye lens
    • DOI 10.1016/0047-6374(86)90107-7
    • McFadden PN, Clarke S. Protein carboxyl methyltransferase and methyl acceptor proteins in aging and cataractus tissue of the human eye lens. Mech Ageing Develop 1986; 34:91-105. (Pubitemid 16082842)
    • (1986) Mechanisms of Ageing and Development , vol.34 , Issue.1 , pp. 91-105
    • McFadden, P.N.1    Clarke, S.2
  • 91
    • 0023933032 scopus 로고
    • The carboxylmethylation of cerebral membrane-bound proteins increases with age
    • Sellinger OZ, Kramer CM, Conger A et al. The carboxylmethylation of cerebral membrane-bound proteins increases with age. Mech Ageing Develop 1988; 43:161-73.
    • (1988) Mech Ageing Develop , vol.43 , pp. 161-173
    • Sellinger, O.Z.1    Kramer, C.M.2    Conger, A.3
  • 93
    • 0026588862 scopus 로고
    • Common senescent cell-specific antibody epitopes on fibronectin in species and cells of varied origin
    • Porter MB, Pereira-Smith OM, Smith JR. Common senescent cell-specific antibody epitopes on fibronectin in species and cells of varied origin. J Cell Physiol 1992; 150:545-51.
    • (1992) J Cell Physiol , vol.150 , pp. 545-551
    • Porter, M.B.1    Pereira-Smith, O.M.2    Smith, J.R.3
  • 94
    • 0028278299 scopus 로고
    • Commitment to cell death is signaled by the appearance of a terminin protein of 30 kDa
    • DOI 10.1006/excr.1994.1002
    • Hébert L, Pandey S, Wang E. Commitment to cell death is signaled by the appearance of a terminin protein of 30 kDa. Exp Cell Res 1994; 210:10-8. (Pubitemid 24168488)
    • (1994) Experimental Cell Research , vol.210 , Issue.1 , pp. 10-18
    • Hebert, L.1    Pandey, S.2    Wang, E.3
  • 95
    • 0026970395 scopus 로고
    • Aging brain, aging mind
    • Selkoe DJ. Aging brain, aging mind. Sci Amer 1992; 267:135-42.
    • (1992) Sci Amer , vol.267 , pp. 135-142
    • Selkoe, D.J.1
  • 96
    • 0035943345 scopus 로고    scopus 로고
    • A portrait of Alzheimer secretases - New features and familiar faces
    • DOI 10.1126/science.1064638
    • Esler WP, Wolfe MS. A portrait of Alzheimer secretases-new features and familiar faces. Science 2001; 293:1449-54. (Pubitemid 32801541)
    • (2001) Science , vol.293 , Issue.5534 , pp. 1449-1454
    • Esler, W.P.1    Wolfe, M.S.2
  • 97
    • 0026800776 scopus 로고
    • Overexpression of the two-chain form of cathepsin B in senescent WI-38 cells
    • DiPaolo BR, Pignolo RJ, Cristofalo VJ. Overexpression of the two-chain form of cathepsin B in senescent WI-38 cells. Exp Cell Res 1992; 201:500-5.
    • (1992) Exp Cell Res , vol.201 , pp. 500-505
    • Dipaolo, B.R.1    Pignolo, R.J.2    Cristofalo, V.J.3
  • 98
    • 0024541932 scopus 로고
    • Regulation of collagenase and collagenase mRNA production in early- and late-passage human diploid fibroblasts
    • DOI 10.1002/jcp.1041380209
    • Sottile J, Mann DM, Diemer V et al. Regulation of collagenase and collagenase mRNA production in early- and late-passage human diploid fibroblasts. J Cell Physiol 1989; 138:281-90. (Pubitemid 19061208)
    • (1989) Journal of Cellular Physiology , vol.138 , Issue.2 , pp. 281-290
    • Sottile, J.1    Mann, D.M.2    Diemer, V.3    Millis, A.J.T.4
  • 99
    • 0024414072 scopus 로고
    • Murine elongation factor 1a (EF-1a) is post-translationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties
    • Whiteheart SW, Shenbagamurthi P, Chen L et al. Murine elongation factor 1a (EF-1a) is post-translationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. J Biol Chem 1989; 264:14334-41.
    • (1989) J Biol Chem , vol.264 , pp. 14334-14341
    • Whiteheart, S.W.1    Shenbagamurthi, P.2    Chen, L.3
  • 100
    • 0027370986 scopus 로고
    • Is hypusine essential for eukaryotic cell proliferation?
    • DOI 10.1016/0968-0004(93)90010-K
    • Park MH, Wolff EC, Folk JE. Is hypusine essential for eukaryotic cell proliferation? TIBS 1993; 18:475-9. (Pubitemid 23362305)
    • (1993) Trends in Biochemical Sciences , vol.18 , Issue.12 , pp. 475-479
    • Park, M.H.1    Wolff, E.C.2    Folk, J.E.3
  • 102
    • 0001214436 scopus 로고    scopus 로고
    • Distinction between differentiation and senescence and the absence of increased apoptosis in human keratinocytes undergoing cellular aging in vitro
    • DOI 10.1016/0531-5565(96)00011-3
    • Norsgaard H, Clark BFC, Rattan SIS. Distinction between differentiation and senescence and the absence of increased apoptosis in human keratinocytes undergoing cellular aging in vitro. Exp Gerontol 1996; 31:563-70. (Pubitemid 26314999)
    • (1996) Experimental Gerontology , vol.31 , Issue.5 , pp. 563-570
    • Norsgaard, H.1    Clark, B.F.C.2    Rattan, S.I.S.3
  • 103
    • 0001281761 scopus 로고
    • Protein tyrosine sulfation
    • Huttner WB. Protein tyrosine sulfation. TIBS 1987; 12:361-3.
    • (1987) TIBS , vol.12 , pp. 361-363
    • Huttner, W.B.1
  • 104
    • 0027284950 scopus 로고
    • Protein prenylation: A mediator of protein-protein interactions
    • Marshall CJ. Protein prenylation: a mediator of protein-protein interactions. Science 1993; 259:1865-6. (Pubitemid 23124458)
    • (1993) Science , vol.259 , Issue.5103 , pp. 1865-1866
    • Marshall, C.J.1
  • 106
    • 0033788162 scopus 로고    scopus 로고
    • Proteolysis of oxidised proteins and cellular senescence
    • Merker K, Grune T. Proteolysis of oxidised proteins and cellular senescence. Exp Gerontol 2000; 35:779-86.
    • (2000) Exp Gerontol , vol.35 , pp. 779-786
    • Merker, K.1    Grune, T.2
  • 107
    • 0035050618 scopus 로고    scopus 로고
    • Caretaker or undertaker? The role of the proteasome in aging
    • DOI 10.1016/S0047-6374(00)00246-3, PII S0047637400002463
    • Gaczynska M, Osmulski PA, Ward WF. Caretaker or undertaker? The role of the proteasome in aging. Mech Ageing Dev 2001; 122:235-54. (Pubitemid 32322442)
    • (2001) Mechanisms of Ageing and Development , vol.122 , Issue.3 , pp. 235-254
    • Gaczynska, M.1    Osmulskil, P.A.2    Ward, W.F.3
  • 108
    • 0036591853 scopus 로고    scopus 로고
    • Protein turnover by the proteasome in aging and disease
    • DOI 10.1016/S0891-5849(02)00824-9, PII S0891584902008249
    • Shringaarpure R, Davies KJA. Protein turnover by the proteasome in aging and disease. Free Rad Biol Med 2002; 32:1084-9. (Pubitemid 34603346)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.11 , pp. 1084-1089
    • Shringarpure, R.1    Davies, K.J.A.2
  • 109
    • 0027386791 scopus 로고
    • Ubiquitin pools, ubiquitin mRNA levels, and ubiquitin-mediated proteolysis in aging human fibroblasts
    • DOI 10.1016/0531-5565(93)90018-9
    • Pan J-X, Short SR, Goff SA et al. Ubiquitin pools, ubiquitin mRNA levels and ubiquitin-mediated proteolysis in aging human fibroblasts. Exp Gerontol 1993; 28:39-49. (Pubitemid 23035028)
    • (1993) Experimental Gerontology , vol.28 , Issue.1 , pp. 39-49
    • Pan, J.-X.1    Short, S.R.2    Goff, S.A.3    Dice, J.F.4
  • 110
    • 0033785045 scopus 로고    scopus 로고
    • Age-related alterations of proteasome structure and function in aging epidermis
    • Bulteau AL, Petropoulos I, Friguet B. Age-related alterations of proteasome structure and function in aging epidermis. Exp Gerontol 2000; 35:767-77.
    • (2000) Exp Gerontol , vol.35 , pp. 767-777
    • Bulteau, A.L.1    Petropoulos, I.2    Friguet, B.3
  • 111
    • 31344434396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system at the crossroads of stress-response and ageing pathways: A handle for skin care?
    • DOI 10.1016/j.arr.2005.09.002, PII S1568163705000486
    • Brégégére F, Milner Y, Friguet B. The ubiquitin-proteasome system at the crossroads of stress-response and ageing pathways: a handle for skin care? Aging Res Rev 2006; 5:60-90. (Pubitemid 43139668)
    • (2006) Ageing Research Reviews , vol.5 , Issue.1 , pp. 60-90
    • Bregegere, F.1    Milner, Y.2    Friguet, B.3
  • 113
    • 33749146320 scopus 로고    scopus 로고
    • Lysosomal labilization
    • DOI 10.1080/15216540600904885, PII J375811642077257
    • Terman A, Kurz T, Gustafsson B et al. Lysosomal labilization. IUBMB LIfe 2006; 58:531-9. (Pubitemid 44470239)
    • (2006) IUBMB Life , vol.58 , Issue.9 , pp. 531-539
    • Terman, A.1    Kurz, T.2    Gustafsson, B.3    Brunk, U.T.4
  • 114
    • 33846702991 scopus 로고    scopus 로고
    • Autophagy, organelles and ageing
    • DOI 10.1002/path.2094
    • Terman A, Gustafsson B, Brunk UT. Autophagy, organelles and ageing. J Pathol 2007; 211:134-43. (Pubitemid 46195512)
    • (2007) Journal of Pathology , vol.211 , Issue.2 , pp. 134-143
    • Terman, A.1    Gustafsson, B.2    Brunk, U.T.3
  • 115
    • 0028304454 scopus 로고
    • 1 progression, mitogenic stimulation, differentiation, and senescence
    • Wick M, Bürger C, Brüsselbach S et al. A novel member of human tissue inhibitor of metalloproteinases (TIMP) gene family is regulated during G1 progression, mitogenic stimulation, differentiation and senescence. J Biol Chem 1994; 269:18953-60. (Pubitemid 24226211)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.29 , pp. 18953-18960
    • Wick, M.1    Burger, C.2    Brusselbach, S.3    Lucibello, F.C.4    Muller, R.5
  • 117
    • 33750729203 scopus 로고    scopus 로고
    • Theories of biological aging: Genes, proteins, and free radicals
    • DOI 10.1080/10715760600911303, PII U612176808538538, Free Radicals in the Aging Process - The 'Free Radical Theory of Aging' 50 years after -
    • Rattan SIS. Theories of biological aging : genes, proteins and free radicals. Free Rad Res 2006; 40:1230-8. (Pubitemid 44698271)
    • (2006) Free Radical Research , vol.40 , Issue.12 , pp. 1230-1238
    • Rattan, S.I.S.1
  • 118
    • 40149089557 scopus 로고    scopus 로고
    • Increased molecular damage and heterogeneity as the basis of aging
    • DOI 10.1515/BC.2008.030
    • Rattan SIS. Increased molecular damage and heterogeneity as the basis of aging. Biol Chem 2008; 389:267-72. (Pubitemid 351329028)
    • (2008) Biological Chemistry , vol.389 , Issue.3 , pp. 267-272
    • Rattan, S.I.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.