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Volumn 20, Issue 18, 2014, Pages 3040-3051

Protein oxidation and proteolytic signalling in aging

Author keywords

Aging; Autophagy; Immunoproteasome; Nrf2; Oxidative stress; p62; Proteasome; Protein oxidation; Proteolysis

Indexed keywords

PROTEASOME; UBIQUITIN; ANTIOXIDANT; FREE RADICAL; PROTEIN; REACTIVE OXYGEN METABOLITE;

EID: 84903705338     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/13816128113196660709     Document Type: Article
Times cited : (17)

References (189)
  • 1
    • 0017177978 scopus 로고
    • Free radical theory of aging: Inhibition of amyloidosis in mice by antioxidants;possible mechanism
    • Harman D, Eddy DE, Noffsinger J. Free radical theory of aging: inhibition of amyloidosis in mice by antioxidants;possible mechanism. J Am Geriatr Soc 1976; 24: 203-10.
    • (1976) J Am Geriatr Soc , vol.24 , pp. 203-210
    • Harman, D.1    Eddy, D.E.2    Noffsinger, J.3
  • 2
    • 0030038103 scopus 로고    scopus 로고
    • Oxidative stress, caloric restriction, and aging
    • Sohal RS, Weindruch R. Oxidative stress, caloric restriction, and aging. Science 1996; 273: 59-63.
    • (1996) Science , vol.273 , pp. 59-63
    • Sohal, R.S.1    Weindruch, R.2
  • 3
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman ER, Berlett BS. Reactive oxygen-mediated protein oxidation in aging and disease. Chem Res Toxicol 1997;10: 485-94.
    • (1997) Chem Res Toxicol , vol.10 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 4
    • 56449094841 scopus 로고    scopus 로고
    • Autophagy and the ubiquitinproteasome system: Collaborators in neuroprotection
    • Nedelsky NB, Todd PK, Taylor JP. Autophagy and the ubiquitinproteasome system: collaborators in neuroprotection. Biochim Biophys Acta 2008; 1782: 691-9.
    • (2008) Biochim Biophys Acta , vol.1782 , pp. 691-699
    • Nedelsky, N.B.1    Todd, P.K.2    Taylor, J.P.3
  • 5
    • 59849107267 scopus 로고    scopus 로고
    • Age-related differences in oxidative protein-damage in young and senescent fibroblasts
    • Jung T, Hohn A, Catalgol B, Grune T. Age-related differences in oxidative protein-damage in young and senescent fibroblasts. Arch Biochem Biophys 2009; 483: 127-35.
    • (2009) Arch Biochem Biophys , vol.483 , pp. 127-135
    • Jung, T.1    Hohn, A.2    Catalgol, B.3    Grune, T.4
  • 6
    • 0022428152 scopus 로고
    • Oxidative stress: Damage to intact cells and organs
    • Sies H, Cadenas E. Oxidative stress: damage to intact cells and organs. Philos Trans R Soc Lond B Biol Sci 1985; 311: 617-31.
    • (1985) Philos Trans R Soc Lond B Biol Sci , vol.311 , pp. 617-631
    • Sies, H.1    Cadenas, E.2
  • 7
    • 79959534486 scopus 로고    scopus 로고
    • Oxidative protein damage and the proteasome
    • Grimm S, Hohn A, Grune T. Oxidative protein damage and the proteasome. Amino Acids 2012; 42: 23-38.
    • (2012) Amino Acids , vol.42 , pp. 23-38
    • Grimm, S.1    Hohn, A.2    Grune, T.3
  • 8
    • 0034566190 scopus 로고    scopus 로고
    • Oxidative modifications of protein structures
    • Naskalski JW, Bartosz G. Oxidative modifications of protein structures. Adv Clin Chem 2000; 35: 161-253.
    • (2000) Adv Clin Chem , vol.35 , pp. 161-253
    • Naskalski, J.W.1    Bartosz, G.2
  • 12
    • 34249827861 scopus 로고    scopus 로고
    • Oxidized proteins: Intracellular distribution and recognition by the proteasome
    • Jung T, Bader N, Grune T. Oxidized proteins: intracellular distribution and recognition by the proteasome. Arch Biochem Biophys 2007; 462: 231-7.
    • (2007) Arch Biochem Biophys , vol.462 , pp. 231-237
    • Jung, T.1    Bader, N.2    Grune, T.3
  • 13
    • 57449113835 scopus 로고    scopus 로고
    • Turnover of oxidatively modified proteins: The usage of in vitro and metabolic labeling
    • Catalgol B, Grune T. Turnover of oxidatively modified proteins: the usage of in vitro and metabolic labeling. Free Radic Biol Med 2009; 46: 8-13.
    • (2009) Free Radic Biol Med , vol.46 , pp. 8-13
    • Catalgol, B.1    Grune, T.2
  • 14
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett BS, Stadtman ER. Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 1997; 272: 20313-6.
    • (1997) J Biol Chem , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 15
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals. I. general aspects
    • Davies KJ. Protein damage and degradation by oxygen radicals. I. general aspects. J Biol Chem 1987; 262: 9895-901.
    • (1987) J Biol Chem , vol.262 , pp. 9895-9901
    • Davies, K.J.1
  • 17
    • 0031051893 scopus 로고    scopus 로고
    • Quantification of malondialdehyde and 4-hydroxynonenal adducts to lysine residues in native and oxidized human low-density lipoprotein
    • Requena JR, Fu MX, Ahmed MU, et al. Quantification of malondialdehyde and 4-hydroxynonenal adducts to lysine residues in native and oxidized human low-density lipoprotein. Biochem J 1997; 322: 317-25.
    • (1997) Biochem J , vol.322 , pp. 317-325
    • Requena, J.R.1    Fu, M.X.2    Ahmed, M.U.3
  • 19
    • 84856293321 scopus 로고    scopus 로고
    • The redox stress hypothesis of aging
    • Sohal RS, Orr WC. The redox stress hypothesis of aging. Free Radic Biol Med 2012; 52: 539-55.
    • (2012) Free Radic Biol Med , vol.52 , pp. 539-555
    • Sohal, R.S.1    Orr, W.C.2
  • 21
    • 33646058316 scopus 로고    scopus 로고
    • Intracellular distribution of oxidized proteins and proteasome in HT22 cells during oxidative stress
    • Jung T, Engels M, Kaiser B, Poppek D, Grune T. Intracellular distribution of oxidized proteins and proteasome in HT22 cells during oxidative stress. Free Radic Biol Med 2006; 40: 1303-12.
    • (2006) Free Radic Biol Med , vol.40 , pp. 1303-1312
    • Jung, T.1    Engels, M.2    Kaiser, B.3    Poppek, D.4    Grune, T.5
  • 22
    • 0036628724 scopus 로고    scopus 로고
    • Role of oxidative stress and protein oxidation in the aging process
    • Sohal RS. Role of oxidative stress and protein oxidation in the aging process. Free Radic Biol Med 2002; 33: 37-44.
    • (2002) Free Radic Biol Med , vol.33 , pp. 37-44
    • Sohal, R.S.1
  • 23
    • 79956189909 scopus 로고    scopus 로고
    • Mitochondrial changes in ageing Caenorhabditis elegans--what do we learn from superoxide dismutase knockouts?
    • doi: 10.1371/journal.pone. 0019444
    • Gruber J, Ng LF, Fong S, et al. Mitochondrial changes in ageing Caenorhabditis elegans--what do we learn from superoxide dismutase knockouts? PLoS One 2011; 6: e19444. doi: 10.1371/journal.pone. 0019444.
    • (2011) PLoS One , vol.6
    • Gruber, J.1    Ng, L.F.2    Fong, S.3
  • 24
    • 79957933700 scopus 로고    scopus 로고
    • Ubiquitin-proteasome pathway and cellular responses to oxidative stress
    • Shang F, Taylor A. Ubiquitin-proteasome pathway and cellular responses to oxidative stress. Free Radic Biol Med 2011; 51: 5-16.
    • (2011) Free Radic Biol Med , vol.51 , pp. 5-16
    • Shang, F.1    Taylor, A.2
  • 25
    • 84857333927 scopus 로고    scopus 로고
    • Rapid and sensitive determination of protein-nitrotyrosine by ELISA: Application to human plasma
    • Weber D, Kneschke N, Grimm S, Bergheim I, Breusing N, Grune T. Rapid and sensitive determination of protein-nitrotyrosine by ELISA: Application to human plasma. Free Radic Res 2012; 46: 276-85.
    • (2012) Free Radic Res , vol.46 , pp. 276-285
    • Weber, D.1    Kneschke, N.2    Grimm, S.3    Bergheim, I.4    Breusing, N.5    Grune, T.6
  • 26
    • 64549097266 scopus 로고    scopus 로고
    • Thiol-based redox switches in eukaryotic proteins
    • Brandes N, Schmitt S, Jakob U. Thiol-based redox switches in eukaryotic proteins. Antioxid Redox Signal 2009; 11: 997-1014.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 997-1014
    • Brandes, N.1    Schmitt, S.2    Jakob, U.3
  • 27
    • 0041326831 scopus 로고    scopus 로고
    • Effects of age and caloric restriction on glutathione redox state in mice
    • Rebrin I, Kamzalov S, Sohal RS. Effects of age and caloric restriction on glutathione redox state in mice. Free Radic Biol Med 2003; 35: 626-35.
    • (2003) Free Radic Biol Med , vol.35 , pp. 626-635
    • Rebrin, I.1    Kamzalov, S.2    Sohal, R.S.3
  • 28
    • 34249672703 scopus 로고    scopus 로고
    • Biological aging is no longer an unsolved problem
    • Hayflick L. Biological aging is no longer an unsolved problem. Ann N Y Acad Sci 2007; 1100: 1-13.
    • (2007) Ann N Y Acad Sci , vol.1100 , pp. 1-13
    • Hayflick, L.1
  • 29
    • 34249028642 scopus 로고    scopus 로고
    • Mitochondrial dysfunction accounts for the stochastic heterogeneity in telomere-dependent senescence
    • doi: 10.1371/journal.pbio. 0050110
    • Passos JF, Saretzki G, Ahmed S, et al. Mitochondrial dysfunction accounts for the stochastic heterogeneity in telomere-dependent senescence. PLoS Biol 2007; 5: e110. doi: 10.1371/journal.pbio. 0050110
    • (2007) PLoS Biol , vol.5
    • Passos, J.F.1    Saretzki, G.2    Ahmed, S.3
  • 31
    • 0034117954 scopus 로고    scopus 로고
    • Protein oxidation and degradation during proliferative senescence of human MRC-5 fibroblasts
    • Sitte N, Merker K, Von ZT, Grune T. Protein oxidation and degradation during proliferative senescence of human MRC-5 fibroblasts. Free Radic Biol Med 2000; 28: 701-8.
    • (2000) Free Radic Biol Med , vol.28 , pp. 701-708
    • Sitte, N.1    Merker, K.2    Von, Z.T.3    Grune, T.4
  • 32
    • 0025943770 scopus 로고
    • Hydrogen peroxide production by mitochondria may be a biomarker of aging
    • Sohal RS. Hydrogen peroxide production by mitochondria may be a biomarker of aging. Mech Ageing Dev 1991; 60: 189-98.
    • (1991) Mech Ageing Dev , vol.60 , pp. 189-198
    • Sohal, R.S.1
  • 33
    • 75149165994 scopus 로고    scopus 로고
    • Update on the oxidative stress theory of aging: Does oxidative stress play a role in aging or healthy aging?
    • Salmon AB, Richardson A, Perez VI. Update on the oxidative stress theory of aging: does oxidative stress play a role in aging or healthy aging? Free Radic Biol Med 2010; 48: 642-55.
    • (2010) Free Radic Biol Med , vol.48 , pp. 642-655
    • Salmon, A.B.1    Richardson, A.2    Perez, V.I.3
  • 34
    • 13944262937 scopus 로고    scopus 로고
    • Understanding the odd science of aging
    • Kirkwood TB. Understanding the odd science of aging. Cell 2005; 120: 437-47.
    • (2005) Cell , vol.120 , pp. 437-447
    • Kirkwood, T.B.1
  • 35
    • 0025309791 scopus 로고
    • Mitochondrial mutations may increase oxidative stress: Implications for carcinogenesis and aging?
    • Bandy B, Davison AJ. Mitochondrial mutations may increase oxidative stress: implications for carcinogenesis and aging? Free Radic Biol Med 1990; 8: 523-39.
    • (1990) Free Radic Biol Med , vol.8 , pp. 523-539
    • Bandy, B.1    Davison, A.J.2
  • 36
    • 84855394783 scopus 로고    scopus 로고
    • Oxidative stress, mitochondrial dysfunction, and aging
    • doi: 10.1155/2012/646354
    • Cui H, Kong Y, Zhang H. Oxidative stress, mitochondrial dysfunction, and aging. J Signal Transduct 2012; 2012: 646354. doi: 10.1155/2012/646354.
    • (2012) J Signal Transduct , vol.2012 , pp. 646354
    • Cui, H.1    Kong, Y.2    Zhang, H.3
  • 37
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I. Superoxide radical and superoxide dismutases. Annu Rev Biochem 1995; 64: 97-112.
    • (1995) Annu Rev Biochem , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 38
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge W. Free radicals in the physiological control of cell function. Physiol Rev 2002; 82: 47-95.
    • (2002) Physiol Rev , vol.82 , pp. 47-95
    • Droge, W.1
  • 39
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • Nordberg J, Arner ES. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 2001; 31: 1287-312.
    • (2001) Free Radic Biol Med , vol.31 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.2
  • 41
    • 0029893851 scopus 로고    scopus 로고
    • Relationship between susceptibility to protein oxidation, aging, and maximum life span potential of different species
    • Agarwal S, Sohal RS. Relationship between susceptibility to protein oxidation, aging, and maximum life span potential of different species. Exp Gerontol 1996; 31: 365-72.
    • (1996) Exp Gerontol , vol.31 , pp. 365-372
    • Agarwal, S.1    Sohal, R.S.2
  • 43
    • 0037438869 scopus 로고    scopus 로고
    • Ectopic expression of catalase in Drosophila mitochondria increases stress resistance but not longevity
    • Mockett RJ, Bayne AC, Kwong LK, Orr WC, Sohal RS. Ectopic expression of catalase in Drosophila mitochondria increases stress resistance but not longevity. Free Radic Biol Med 2003; 34: 207-17.
    • (2003) Free Radic Biol Med , vol.34 , pp. 207-217
    • Mockett, R.J.1    Bayne, A.C.2    Kwong, L.K.3    Orr, W.C.4    Sohal, R.S.5
  • 44
    • 0025196557 scopus 로고
    • Slow mortality rate accelerations during aging in some animals approximate that of humans
    • Finch CE, Pike MC, Witten M. Slow mortality rate accelerations during aging in some animals approximate that of humans. Science 1990; 249: 902-5.
    • (1990) Science , vol.249 , pp. 902-905
    • Finch, C.E.1    Pike, M.C.2    Witten, M.3
  • 45
    • 84861865625 scopus 로고    scopus 로고
    • Age-Associated Proinflammatory Secretory Phenotype in Vascular Smooth Muscle Cells From the Non-human Primate Macaca mulatta: Reversal by Resveratrol Treatment
    • Csiszar A, Sosnowska D, Wang M, Lakatta EG, Sonntag WE, Ungvari Z. Age-Associated Proinflammatory Secretory Phenotype in Vascular Smooth Muscle Cells From the Non-human Primate Macaca mulatta: Reversal by Resveratrol Treatment. J Gerontol A Biol Sci Med Sci 2012; 67: 811-20.
    • (2012) J Gerontol A Biol Sci Med Sci , vol.67 , pp. 811-820
    • Csiszar, A.1    Sosnowska, D.2    Wang, M.3    Lakatta, E.G.4    Sonntag, W.E.5    Ungvari, Z.6
  • 46
    • 27144529182 scopus 로고    scopus 로고
    • Ubiquitylation and cell signaling
    • Haglund K, Dikic I. Ubiquitylation and cell signaling. EMBO J 2005; 24: 3353-9.
    • (2005) EMBO J , vol.24 , pp. 3353-3359
    • Haglund, K.1    Dikic, I.2
  • 47
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • Pickart CM, Fushman D. Polyubiquitin chains: polymeric protein signals. Curr Opin Chem Biol 2004; 8: 610-6.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 48
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: Biological regulation via destruction
    • Ciechanover A, Orian A, Schwartz AL. Ubiquitin-mediated proteolysis: biological regulation via destruction. Bioessays 2000; 22: 442-51.
    • (2000) Bioessays , vol.22 , pp. 442-451
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 49
    • 9744222883 scopus 로고    scopus 로고
    • Protein quality control in Alzheimer's disease by the ubiquitin proteasome system
    • de Vrij FM, Fischer DF, van Leeuwen FW, Hol EM. Protein quality control in Alzheimer's disease by the ubiquitin proteasome system. Prog Neurobiol 2004; 74: 249-70.
    • (2004) Prog Neurobiol , vol.74 , pp. 249-270
    • de Vrij, F.M.1    Fischer, D.F.2    van Leeuwen, F.W.3    Hol, E.M.4
  • 50
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O, Tanaka K, Goldberg AL. Structure and functions of the 20S and 26S proteasomes. Annu Rev Biochem 1996; 65: 801-47.
    • (1996) Annu Rev Biochem , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 51
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller JN, Hanni KB, Markesbery WR. Impaired proteasome function in Alzheimer's disease. J Neurochem 2000; 75: 436-9.
    • (2000) J Neurochem , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 52
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • Davies KJ. Degradation of oxidized proteins by the 20S proteasome. Biochimie 2001; 83: 301-10.
    • (2001) Biochimie , vol.83 , pp. 301-310
    • Davies, K.J.1
  • 53
    • 0029984892 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome
    • Grune T, Reinheckel T, Davies KJ. Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome. J Biol Chem 1996; 271: 15504-9.
    • (1996) J Biol Chem , vol.271 , pp. 15504-15509
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.3
  • 54
    • 78649848069 scopus 로고    scopus 로고
    • The immunoproteasome, the 20S proteasome and the PA28alphabeta proteasome regulator are oxidative-stress-adaptive proteolytic complexes
    • Pickering AM, Koop AL, Teoh CY, Ermak G, Grune T, Davies KJ. The immunoproteasome, the 20S proteasome and the PA28alphabeta proteasome regulator are oxidative-stress-adaptive proteolytic complexes. Biochem J 2010; 432: 585-94.
    • (2010) Biochem J , vol.432 , pp. 585-594
    • Pickering, A.M.1    Koop, A.L.2    Teoh, C.Y.3    Ermak, G.4    Grune, T.5    Davies, K.J.6
  • 55
  • 56
    • 0042346327 scopus 로고    scopus 로고
    • Central role of the proteasome in senescence and survival of human fibroblasts: Induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation
    • Chondrogianni N, Stratford FL, Trougakos IP, Friguet B, Rivett AJ, Gonos ES. Central role of the proteasome in senescence and survival of human fibroblasts: induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation. J Biol Chem 2003; 278: 28026-37.
    • (2003) J Biol Chem , vol.278 , pp. 28026-28037
    • Chondrogianni, N.1    Stratford, F.L.2    Trougakos, I.P.3    Friguet, B.4    Rivett, A.J.5    Gonos, E.S.6
  • 57
    • 0030982143 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in mammalian cells
    • Grune T, Reinheckel T, Davies KJ. Degradation of oxidized proteins in mammalian cells. FASEB J 1997; 11: 526-34.
    • (1997) FASEB J , vol.11 , pp. 526-534
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.3
  • 58
    • 0034769477 scopus 로고    scopus 로고
    • Removal of oxidatively damaged proteins from lens cells by the ubiquitin-proteasome pathway
    • Shang F, Nowell TR, Jr., Taylor A. Removal of oxidatively damaged proteins from lens cells by the ubiquitin-proteasome pathway. Exp Eye Res 2001; 73: 229-38.
    • (2001) Exp Eye Res , vol.73 , pp. 229-238
    • Shang, F.1    Nowell Jr., T.R.2    Taylor, A.3
  • 60
    • 80052265819 scopus 로고    scopus 로고
    • HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress
    • Grune T, Catalgol B, Licht A, et al. HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress. Free Radic Biol Med 2011; 51: 1355-64.
    • (2011) Free Radic Biol Med , vol.51 , pp. 1355-1364
    • Grune, T.1    Catalgol, B.2    Licht, A.3
  • 61
    • 78649980437 scopus 로고    scopus 로고
    • Regulation of the 26S proteasome complex during oxidative stress
    • doi: 10.1126/scisignal.2001232
    • Wang X, Yen J, Kaiser P, Huang L. Regulation of the 26S proteasome complex during oxidative stress. Sci Signal 2010; 3: ra88. doi: 10.1126/scisignal.2001232.
    • (2010) Sci Signal , vol.3 , pp. 88
    • Wang, X.1    Yen, J.2    Kaiser, P.3    Huang, L.4
  • 62
    • 84866389666 scopus 로고    scopus 로고
    • Chaperones, but not oxidized proteins, are ubiquitinated after oxidative stress
    • Kastle M, Reeg S, Rogowska-Wrzesinska A, Grune T. Chaperones, but not oxidized proteins, are ubiquitinated after oxidative stress. Free Radic Biol Med 2012; 53:1468-77.
    • (2012) Free Radic Biol Med , vol.53 , pp. 1468-1477
    • Kastle, M.1    Reeg, S.2    Rogowska-Wrzesinska, A.3    Grune, T.4
  • 64
    • 0019174693 scopus 로고
    • Ubiquitin is the ATPdependent proteolysis factor I of rabbit reticulocytes
    • Wilkinson KD, Urban MK, Haas AL. Ubiquitin is the ATPdependent proteolysis factor I of rabbit reticulocytes. J Biol Chem 1980; 255: 7529-32.
    • (1980) J Biol Chem , vol.255 , pp. 7529-7532
    • Wilkinson, K.D.1    Urban, M.K.2    Haas, A.L.3
  • 65
    • 77950487987 scopus 로고    scopus 로고
    • Mechanisms of cross-talk between the ubiquitin-proteasome and autophagylysosome systems
    • Korolchuk VI, Menzies FM, Rubinsztein DC. Mechanisms of cross-talk between the ubiquitin-proteasome and autophagylysosome systems. FEBS Lett 2010; 584: 1393-8.
    • (2010) FEBS Lett , vol.584 , pp. 1393-1398
    • Korolchuk, V.I.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 66
    • 77956410115 scopus 로고    scopus 로고
    • Selective autophagy: Ubiquitinmediated recognition and beyond
    • Kraft C, Peter M, Hofmann K. Selective autophagy: ubiquitinmediated recognition and beyond. Nat Cell Biol 2010; 12: 836-41.
    • (2010) Nat Cell Biol , vol.12 , pp. 836-841
    • Kraft, C.1    Peter, M.2    Hofmann, K.3
  • 67
    • 84857782898 scopus 로고    scopus 로고
    • Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling
    • Sims JJ, Scavone F, Cooper EM, et al. Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling. Nat Methods 2012; 9: 303-9.
    • (2012) Nat Methods , vol.9 , pp. 303-309
    • Sims, J.J.1    Scavone, F.2    Cooper, E.M.3
  • 68
    • 0020402944 scopus 로고
    • Uptake and degradation of proteins by isolated rat liver lysosomes. Suggestion of a microautophagic pathway of proteolysis
    • Ahlberg J, Marzella L, Glaumann H. Uptake and degradation of proteins by isolated rat liver lysosomes. Suggestion of a microautophagic pathway of proteolysis. Lab Invest 1982; 47: 523-32.
    • (1982) Lab Invest , vol.47 , pp. 523-532
    • Ahlberg, J.1    Marzella, L.2    Glaumann, H.3
  • 69
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice JF. Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem Sci 1990; 15: 305-9.
    • (1990) Trends Biochem Sci , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 70
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • Dice JF. Chaperone-mediated autophagy. Autophagy 2007; 3: 295-9.
    • (2007) Autophagy , vol.3 , pp. 295-299
    • Dice, J.F.1
  • 71
    • 79959999581 scopus 로고    scopus 로고
    • Microautophagy in mammalian cells: Revisiting a 40-year-old conundrum
    • Mijaljica D, Prescott M, Devenish RJ. Microautophagy in mammalian cells: revisiting a 40-year-old conundrum. Autophagy 2011; 7: 673-82.
    • (2011) Autophagy , vol.7 , pp. 673-682
    • Mijaljica, D.1    Prescott, M.2    Devenish, R.J.3
  • 72
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: Process and function
    • Mizushima N. Autophagy: process and function. Genes Dev 2007; 21: 2861-73.
    • (2007) Genes Dev , vol.21 , pp. 2861-2873
    • Mizushima, N.1
  • 73
    • 67649467294 scopus 로고    scopus 로고
    • Dynamics and diversity in autophagy mechanisms: Lessons from yeast
    • Nakatogawa H, Suzuki K, Kamada Y, Ohsumi Y. Dynamics and diversity in autophagy mechanisms: lessons from yeast. Nat Rev Mol Cell Biol 2009; 10: 458-67.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 458-467
    • Nakatogawa, H.1    Suzuki, K.2    Kamada, Y.3    Ohsumi, Y.4
  • 74
    • 79955588367 scopus 로고    scopus 로고
    • Cell sensitivity to oxidative stress is influenced by ferritin autophagy
    • Kurz T, Gustafsson B, Brunk UT. Cell sensitivity to oxidative stress is influenced by ferritin autophagy. Free Radic Biol Med 2011; 50: 1647-58.
    • (2011) Free Radic Biol Med , vol.50 , pp. 1647-1658
    • Kurz, T.1    Gustafsson, B.2    Brunk, U.T.3
  • 75
  • 76
    • 79952139698 scopus 로고    scopus 로고
    • Nrf2-mediated induction of p62 controls Toll-like receptor-4-driven aggresome-like induced structure formation and autophagic degradation
    • Fujita K, Maeda D, Xiao Q, Srinivasula SM. Nrf2-mediated induction of p62 controls Toll-like receptor-4-driven aggresome-like induced structure formation and autophagic degradation. Proc Natl Acad Sci USA 2011; 108: 1427-32.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 1427-1432
    • Fujita, K.1    Maeda, D.2    Xiao, Q.3    Srinivasula, S.M.4
  • 77
    • 22844436451 scopus 로고    scopus 로고
    • Dynein mutations impair autophagic clearance of aggregate-prone proteins
    • Ravikumar B, Acevedo-Arozena A, Imarisio S, et al. Dynein mutations impair autophagic clearance of aggregate-prone proteins. Nat Genet 2005; 37: 771-6.
    • (2005) Nat Genet , vol.37 , pp. 771-776
    • Ravikumar, B.1    Acevedo-Arozena, A.2    Imarisio, S.3
  • 78
    • 11244309014 scopus 로고    scopus 로고
    • Proteolysis: From the lysosome to ubiquitin and the proteasome
    • Ciechanover A. Proteolysis: from the lysosome to ubiquitin and the proteasome. Nat Rev Mol Cell Biol 2005; 6: 79-87.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 79-87
    • Ciechanover, A.1
  • 79
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: From phenomenology to molecular understanding in less than a decade
    • Klionsky DJ. Autophagy: from phenomenology to molecular understanding in less than a decade. Nat Rev Mol Cell Biol 2007; 8: 931-7.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 931-937
    • Klionsky, D.J.1
  • 80
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • Iwata A, Riley BE, Johnston JA, Kopito RR. HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J Biol Chem 2005; 280: 40282-92.
    • (2005) J Biol Chem , vol.280 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 81
    • 34250183177 scopus 로고    scopus 로고
    • HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS
    • Pandey UB, Nie Z, Batlevi Y, et al. HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature 2007; 447: 859-63.
    • (2007) Nature , vol.447 , pp. 859-863
    • Pandey, U.B.1    Nie, Z.2    Batlevi, Y.3
  • 82
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston JA, Ward CL, Kopito RR. Aggresomes: a cellular response to misfolded proteins. J Cell Biol 1998; 143: 1883-98.
    • (1998) J Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 83
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin V, McEwan DG, Novak I, Dikic I. A role for ubiquitin in selective autophagy. Mol Cell 2009; 34: 259-69.
    • (2009) Mol Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 84
    • 78650100616 scopus 로고    scopus 로고
    • Ubiquitin: Same molecule, different degradation pathways
    • Clague MJ, Urbe S. Ubiquitin: same molecule, different degradation pathways. Cell 2010; 143: 682-5.
    • (2010) Cell , vol.143 , pp. 682-685
    • Clague, M.J.1    Urbe, S.2
  • 85
    • 34548416641 scopus 로고    scopus 로고
    • HDAC6 controls major cell response pathways to cytotoxic accumulation of protein aggregates
    • Boyault C, Zhang Y, Fritah S, et al. HDAC6 controls major cell response pathways to cytotoxic accumulation of protein aggregates. Genes Dev 2007; 21: 2172-81.
    • (2007) Genes Dev , vol.21 , pp. 2172-2181
    • Boyault, C.1    Zhang, Y.2    Fritah, S.3
  • 86
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • Jakob U, Muse W, Eser M, Bardwell JC. Chaperone activity with a redox switch. Cell 1999; 96: 341-52.
    • (1999) Cell , vol.96 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.4
  • 87
    • 4944247868 scopus 로고    scopus 로고
    • Alfy, a novel FYVE-domain-containing protein associated with protein granules and autophagic membranes
    • Simonsen A, Birkeland HC, Gillooly DJ, et al. Alfy, a novel FYVE-domain-containing protein associated with protein granules and autophagic membranes. J Cell Sci 2004; 117: 4239-51.
    • (2004) J Cell Sci , vol.117 , pp. 4239-4251
    • Simonsen, A.1    Birkeland, H.C.2    Gillooly, D.J.3
  • 88
    • 77950903972 scopus 로고    scopus 로고
    • The selective macroautophagic degradation of aggregated proteins requires the PI3Pbinding protein Alfy
    • Filimonenko M, Isakson P, Finley KD, et al. The selective macroautophagic degradation of aggregated proteins requires the PI3Pbinding protein Alfy. Mol Cell 2010; 38: 265-79.
    • (2010) Mol Cell , vol.38 , pp. 265-279
    • Filimonenko, M.1    Isakson, P.2    Finley, K.D.3
  • 89
    • 36849089101 scopus 로고    scopus 로고
    • Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagydeficient mice
    • Komatsu M, Waguri S, Koike M, et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagydeficient mice. Cell 2007; 131: 1149-63.
    • (2007) Cell , vol.131 , pp. 1149-1163
    • Komatsu, M.1    Waguri, S.2    Koike, M.3
  • 90
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjorkoy G, Lamark T, Brech A, et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 2005; 171: 603-14.
    • (2005) J Cell Biol , vol.171 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3
  • 91
    • 34548259958 scopus 로고    scopus 로고
    • p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy
    • Pankiv S, Clausen TH, Lamark T, et al. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J Biol Chem 2007; 282: 24131-45.
    • (2007) J Biol Chem , vol.282 , pp. 24131-24145
    • Pankiv, S.1    Clausen, T.H.2    Lamark, T.3
  • 92
    • 4744349602 scopus 로고    scopus 로고
    • Increased expression of p62 in expanded polyglutamine-expressing cells and its association with polyglutamine inclusions
    • Nagaoka U, Kim K, Jana NR, et al. Increased expression of p62 in expanded polyglutamine-expressing cells and its association with polyglutamine inclusions. J Neurochem 2004; 91: 57-68.
    • (2004) J Neurochem , vol.91 , pp. 57-68
    • Nagaoka, U.1    Kim, K.2    Jana, N.R.3
  • 93
    • 0034805395 scopus 로고    scopus 로고
    • Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells
    • Kuusisto E, Suuronen T, Salminen A. Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells. Biochem Biophys Res Commun 2001; 280: 223-8.
    • (2001) Biochem Biophys Res Commun , vol.280 , pp. 223-228
    • Kuusisto, E.1    Suuronen, T.2    Salminen, A.3
  • 94
    • 0036144410 scopus 로고    scopus 로고
    • p62 Is a common component of cytoplasmic inclusions in protein aggregation diseases
    • Zatloukal K, Stumptner C, Fuchsbichler A, et al. p62 Is a common component of cytoplasmic inclusions in protein aggregation diseases. Am J Pathol 2002; 160: 255-63.
    • (2002) Am J Pathol , vol.160 , pp. 255-263
    • Zatloukal, K.1    Stumptner, C.2    Fuchsbichler, A.3
  • 95
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells
    • Zhao J, Brault JJ, Schild A, et al. FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab 2007; 6: 472-83.
    • (2007) Cell Metab , vol.6 , pp. 472-483
    • Zhao, J.1    Brault, J.J.2    Schild, A.3
  • 96
    • 33644662970 scopus 로고    scopus 로고
    • Proteasome function in aging and oxidative stress: Implications in protein maintenance failure
    • Farout L, Friguet B. Proteasome function in aging and oxidative stress: implications in protein maintenance failure. Antioxid Redox Signal 2006; 8: 205-16.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 205-216
    • Farout, L.1    Friguet, B.2
  • 97
    • 33646578189 scopus 로고    scopus 로고
    • Oxidized protein degradation and repair in ageing and oxidative stress
    • Friguet B. Oxidized protein degradation and repair in ageing and oxidative stress. FEBS Lett 2006; 580: 2910-6.
    • (2006) FEBS Lett , vol.580 , pp. 2910-2916
    • Friguet, B.1
  • 99
    • 27144441722 scopus 로고    scopus 로고
    • Oxidative modification of proteasome: Identification of an oxidation-sensitive subunit in 26 S proteasome
    • Ishii T, Sakurai T, Usami H, Uchida K. Oxidative modification of proteasome: identification of an oxidation-sensitive subunit in 26 S proteasome. Biochemistry 2005; 44: 13893-901.
    • (2005) Biochemistry , vol.44 , pp. 13893-13901
    • Ishii, T.1    Sakurai, T.2    Usami, H.3    Uchida, K.4
  • 100
    • 0033588087 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal-mediated impairment of intracellular proteolysis during oxidative stress. Identification of proteasomes as target molecules
    • Okada K, Wangpoengtrakul C, Osawa T, Toyokuni S, Tanaka K, Uchida K. 4-Hydroxy-2-nonenal-mediated impairment of intracellular proteolysis during oxidative stress. Identification of proteasomes as target molecules. J Biol Chem 1999; 274: 23787-93.
    • (1999) J Biol Chem , vol.274 , pp. 23787-23793
    • Okada, K.1    Wangpoengtrakul, C.2    Osawa, T.3    Toyokuni, S.4    Tanaka, K.5    Uchida, K.6
  • 101
    • 0032527963 scopus 로고    scopus 로고
    • Protection from oxidative inactivation of the 20S proteasome by heat-shock protein 90
    • Conconi M, Petropoulos I, Emod I, Turlin E, Biville F, Friguet B. Protection from oxidative inactivation of the 20S proteasome by heat-shock protein 90. Biochem J 1998; 333: 407-15.
    • (1998) Biochem J , vol.333 , pp. 407-415
    • Conconi, M.1    Petropoulos, I.2    Emod, I.3    Turlin, E.4    Biville, F.5    Friguet, B.6
  • 102
    • 0033712579 scopus 로고    scopus 로고
    • 4-Hydroxynonenalmodified amyloid-beta peptide inhibits the proteasome: Possible importance in Alzheimer's disease
    • Shringarpure R, Grune T, Sitte N, Davies KJ. 4-Hydroxynonenalmodified amyloid-beta peptide inhibits the proteasome: possible importance in Alzheimer's disease. Cell Mol Life Sci 2000; 57: 1802-9.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1802-1809
    • Shringarpure, R.1    Grune, T.2    Sitte, N.3    Davies, K.J.4
  • 103
    • 10044294918 scopus 로고    scopus 로고
    • Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal
    • Ferrington DA, Kapphahn RJ. Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal. FEBS Lett 2004; 578: 217-23.
    • (2004) FEBS Lett , vol.578 , pp. 217-223
    • Ferrington, D.A.1    Kapphahn, R.J.2
  • 104
    • 0030977793 scopus 로고    scopus 로고
    • Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein
    • Friguet B, Szweda LI. Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein. FEBS Lett 1997; 405: 21-5.
    • (1997) FEBS Lett , vol.405 , pp. 21-25
    • Friguet, B.1    Szweda, L.I.2
  • 105
    • 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
  • 106
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman KB, Ames BN. The free radical theory of aging matures. Physiol Rev 1998; 78: 547-81.
    • (1998) Physiol Rev , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 107
    • 49049106143 scopus 로고    scopus 로고
    • The proteasome: A target of oxidative damage in cultured human retina pigment epithelial cells
    • Zhang X, Zhou J, Fernandes AF, et al. The proteasome: a target of oxidative damage in cultured human retina pigment epithelial cells. Invest Ophthalmol Vis Sci 2008; 49: 3622-30.
    • (2008) Invest Ophthalmol Vis Sci , vol.49 , pp. 3622-3630
    • Zhang, X.1    Zhou, J.2    Fernandes, A.F.3
  • 108
    • 0042594473 scopus 로고    scopus 로고
    • Proteasome inhibition by chronic oxidative stress in human trabecular meshwork cells
    • Caballero M, Liton PB, Epstein DL, Gonzalez P. Proteasome inhibition by chronic oxidative stress in human trabecular meshwork cells. Biochem Biophys Res Commun 2003; 308: 346-52.
    • (2003) Biochem Biophys Res Commun , vol.308 , pp. 346-352
    • Caballero, M.1    Liton, P.B.2    Epstein, D.L.3    Gonzalez, P.4
  • 109
    • 0035006792 scopus 로고    scopus 로고
    • Proteasome inhibition in oxidative stress neurotoxicity: Implications for heat shock proteins
    • Ding Q, Keller JN. Proteasome inhibition in oxidative stress neurotoxicity: implications for heat shock proteins. J Neurochem 2001; 77: 1010-7.
    • (2001) J Neurochem , vol.77 , pp. 1010-1017
    • Ding, Q.1    Keller, J.N.2
  • 110
    • 0030881029 scopus 로고    scopus 로고
    • Activity of ubiquitin-dependent pathway in response to oxidative stress. Ubiquitin-activating enzyme is transiently up-regulated
    • Shang F, Gong X, Taylor A. Activity of ubiquitin-dependent pathway in response to oxidative stress. Ubiquitin-activating enzyme is transiently up-regulated. J Biol Chem 1997; 272: 23086-93.
    • (1997) J Biol Chem , vol.272 , pp. 23086-23093
    • Shang, F.1    Gong, X.2    Taylor, A.3
  • 111
    • 0028905549 scopus 로고
    • Oxidative stress and recovery from oxidative stress are associated with altered ubiquitin conjugating and proteolytic activities in bovine lens epithelial cells
    • Shang F, Taylor A. Oxidative stress and recovery from oxidative stress are associated with altered ubiquitin conjugating and proteolytic activities in bovine lens epithelial cells. Biochem J 1995; 307: 297-303.
    • (1995) Biochem J , vol.307 , pp. 297-303
    • Shang, F.1    Taylor, A.2
  • 112
    • 0028912676 scopus 로고
    • Proteolysis in cultured liver epithelial cells during oxidative stress. Role of the multicatalytic proteinase complex, proteasome
    • Grune T, Reinheckel T, Joshi M, Davies KJ. Proteolysis in cultured liver epithelial cells during oxidative stress. Role of the multicatalytic proteinase complex, proteasome. J Biol Chem 1995; 270: 2344-51.
    • (1995) J Biol Chem , vol.270 , pp. 2344-2351
    • Grune, T.1    Reinheckel, T.2    Joshi, M.3    Davies, K.J.4
  • 113
    • 0037098879 scopus 로고    scopus 로고
    • Increased proteolysis after single-dose exposure with hepatotoxins in HepG2 cells
    • Pirlich M, Muller C, Sandig G, et al. Increased proteolysis after single-dose exposure with hepatotoxins in HepG2 cells. Free Radic Biol Med 2002; 33: 283-91.
    • (2002) Free Radic Biol Med , vol.33 , pp. 283-291
    • Pirlich, M.1    Muller, C.2    Sandig, G.3
  • 114
    • 3242733689 scopus 로고    scopus 로고
    • Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity
    • Yao D, Gu Z, Nakamura T, et al. Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity. Proc Natl Acad Sci USA 2004; 101: 10810-4.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10810-10814
    • Yao, D.1    Gu, Z.2    Nakamura, T.3
  • 115
    • 0030724889 scopus 로고    scopus 로고
    • Regulation of ubiquitin-conjugating enzymes by glutathione following oxidative stress
    • Jahngen-Hodge J, Obin MS, Gong X, et al. Regulation of ubiquitin-conjugating enzymes by glutathione following oxidative stress. J Biol Chem 1997; 272: 28218-26.
    • (1997) J Biol Chem , vol.272 , pp. 28218-28226
    • Jahngen-Hodge, J.1    Obin, M.S.2    Gong, X.3
  • 116
    • 0031893232 scopus 로고    scopus 로고
    • Redox regulation of ubiquitin-conjugating enzymes: Mechanistic insights using the thiol-specific oxidant diamide
    • Obin M, Shang F, Gong X, Handelman G, Blumberg J, Taylor A. Redox regulation of ubiquitin-conjugating enzymes: mechanistic insights using the thiol-specific oxidant diamide. FASEB J 1998; 12: 561-9.
    • (1998) FASEB J , vol.12 , pp. 561-569
    • Obin, M.1    Shang, F.2    Gong, X.3    Handelman, G.4    Blumberg, J.5    Taylor, A.6
  • 117
    • 40149100476 scopus 로고    scopus 로고
    • Regulation of proteasome-mediated protein degradation during oxidative stress and aging
    • Breusing N, Grune T. Regulation of proteasome-mediated protein degradation during oxidative stress and aging. Biol Chem 2008; 389: 203-9.
    • (2008) Biol Chem , vol.389 , pp. 203-209
    • Breusing, N.1    Grune, T.2
  • 118
    • 57449104348 scopus 로고    scopus 로고
    • Sustained oxidative stress inhibits NFkappaB activation partially via inactivating the proteasome
    • Wu M, Bian Q, Liu Y, et al. Sustained oxidative stress inhibits NFkappaB activation partially via inactivating the proteasome. Free Radic Biol Med 2009; 46: 62-9.
    • (2009) Free Radic Biol Med , vol.46 , pp. 62-69
    • Wu, M.1    Bian, Q.2    Liu, Y.3
  • 119
    • 0031955732 scopus 로고    scopus 로고
    • Antiproliferative activity and phototoxicity of some methyl derivatives of 5-methoxypsoralen and 5-methoxyangelicin
    • Conconi MT, Montesi F, Parnigotto PP. Antiproliferative activity and phototoxicity of some methyl derivatives of 5-methoxypsoralen and 5-methoxyangelicin. Pharmacol Toxicol 1998; 82: 193-8.
    • (1998) Pharmacol Toxicol , vol.82 , pp. 193-198
    • Conconi, M.T.1    Montesi, F.2    Parnigotto, P.P.3
  • 120
    • 0034194227 scopus 로고    scopus 로고
    • Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress
    • Reinheckel T, Ullrich O, Sitte N, Grune T. Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress. Arch Biochem Biophys 2000; 377: 65-8.
    • (2000) Arch Biochem Biophys , vol.377 , pp. 65-68
    • Reinheckel, T.1    Ullrich, O.2    Sitte, N.3    Grune, T.4
  • 121
    • 0032538896 scopus 로고    scopus 로고
    • Calorie restriction, stress and the ubiquitin-dependent pathway in mouse livers
    • Scrofano MM, Shang F, Nowell TR, Jr., et al. Calorie restriction, stress and the ubiquitin-dependent pathway in mouse livers. Mech Ageing Dev 1998; 105: 273-90.
    • (1998) Mech Ageing Dev , vol.105 , pp. 273-290
    • Scrofano, M.M.1    Shang, F.2    Nowell Jr., T.R.3
  • 122
    • 0032055901 scopus 로고    scopus 로고
    • Aging, calorie restriction and ubiquitin-dependent proteolysis in the livers of Emory mice
    • Scrofano MM, Shang F, Nowell TR, Jr., et al. Aging, calorie restriction and ubiquitin-dependent proteolysis in the livers of Emory mice. Mech Ageing Dev 1998; 101: 277-96.
    • (1998) Mech Ageing Dev , vol.101 , pp. 277-296
    • Scrofano, M.M.1    Shang, F.2    Nowell Jr., T.R.3
  • 123
    • 26444577079 scopus 로고    scopus 로고
    • Selectivity of the ubiquitin pathway for oxidatively modified proteins: Relevance to protein precipitation diseases
    • Dudek EJ, Shang F, Valverde P, Liu Q, Hobbs M, Taylor A. Selectivity of the ubiquitin pathway for oxidatively modified proteins: relevance to protein precipitation diseases. FASEB J 2005; 19: 1707-9.
    • (2005) FASEB J , vol.19 , pp. 1707-1709
    • Dudek, E.J.1    Shang, F.2    Valverde, P.3    Liu, Q.4    Hobbs, M.5    Taylor, A.6
  • 124
    • 0037182751 scopus 로고    scopus 로고
    • Ubiquitination capabilities in response to neocarzinostatin and H(2)O(2) stress in cell lines from patients with ataxia-telangiectasia
    • Taylor A, Shang F, Nowell T, Galanty Y, Shiloh Y. Ubiquitination capabilities in response to neocarzinostatin and H(2)O(2) stress in cell lines from patients with ataxia-telangiectasia. Oncogene 2002; 21: 4363-73.
    • (2002) Oncogene , vol.21 , pp. 4363-4373
    • Taylor, A.1    Shang, F.2    Nowell, T.3    Galanty, Y.4    Shiloh, Y.5
  • 125
    • 44349160257 scopus 로고    scopus 로고
    • Proteasomal adaptation to environmental stress links resistance to proteotoxicity with longevity in Caenorhabditis elegans
    • Yun C, Stanhill A, Yang Y, et al. Proteasomal adaptation to environmental stress links resistance to proteotoxicity with longevity in Caenorhabditis elegans. Proc Natl Acad Sci USA 2008;105: 7094-9.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7094-7099
    • Yun, C.1    Stanhill, A.2    Yang, Y.3
  • 126
    • 34250882745 scopus 로고    scopus 로고
    • Regulation of Caenorhabditis elegans lifespan by a proteasomal E3 ligase complex
    • Ghazi A, Henis-Korenblit S, Kenyon C. Regulation of Caenorhabditis elegans lifespan by a proteasomal E3 ligase complex. Proc Natl Acad Sci USA 2007;104: 5947-52.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 5947-5952
    • Ghazi, A.1    Henis-Korenblit, S.2    Kenyon, C.3
  • 127
    • 84859164670 scopus 로고    scopus 로고
    • Immune and non-immune functions of the immunoproteasome
    • Angeles A, Fung G, Luo H. Immune and non-immune functions of the immunoproteasome. Front Biosci 2012; 17: 1904-16.
    • (2012) Front Biosci , vol.17 , pp. 1904-1916
    • Angeles, A.1    Fung, G.2    Luo, H.3
  • 130
    • 19444372708 scopus 로고    scopus 로고
    • IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted expression of immunosubunits of the proteasome
    • Namiki S, Nakamura T, Oshima S, et al. IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted expression of immunosubunits of the proteasome. FEBS Lett 2005; 579: 2781-7.
    • (2005) FEBS Lett , vol.579 , pp. 2781-2787
    • Namiki, S.1    Nakamura, T.2    Oshima, S.3
  • 131
    • 84857056178 scopus 로고    scopus 로고
    • Immunoproteasomes at the interface of innate and adaptive immune responses: Two faces of one enzyme
    • Kruger E, Kloetzel PM. Immunoproteasomes at the interface of innate and adaptive immune responses: two faces of one enzyme. Curr Opin Immunol 2012; 24: 77-83.
    • (2012) Curr Opin Immunol , vol.24 , pp. 77-83
    • Kruger, E.1    Kloetzel, P.M.2
  • 132
    • 77955596988 scopus 로고    scopus 로고
    • Immunoproteasomes preserve protein homeostasis upon interferon-induced oxidative stress
    • Seifert U, Bialy LP, Ebstein F, et al. Immunoproteasomes preserve protein homeostasis upon interferon-induced oxidative stress. Cell 2010; 142: 613-24.
    • (2010) Cell , vol.142 , pp. 613-624
    • Seifert, U.1    Bialy, L.P.2    Ebstein, F.3
  • 133
    • 84867757240 scopus 로고    scopus 로고
    • Advanced glycation end products-induced formation of immunoproteasomes: Involvement of the receptor for AGEs and Jak2/STAT1
    • Grimm S, Ott C, Horlacher M, Weber D, Hoehn A, Grune T. Advanced glycation end products-induced formation of immunoproteasomes: involvement of the receptor for AGEs and Jak2/STAT1. Biochem J 2012; 448: 127-39.
    • (2012) Biochem J , vol.448 , pp. 127-139
    • Grimm, S.1    Ott, C.2    Horlacher, M.3    Weber, D.4    Hoehn, A.5    Grune, T.6
  • 134
    • 34347327190 scopus 로고    scopus 로고
    • The road to advanced glycation end products: A mechanistic perspective
    • Cho SJ, Roman G, Yeboah F, Konishi Y. The road to advanced glycation end products: a mechanistic perspective. Curr Med Chem 2007; 14: 1653-71.
    • (2007) Curr Med Chem , vol.14 , pp. 1653-1671
    • Cho, S.J.1    Roman, G.2    Yeboah, F.3    Konishi, Y.4
  • 135
    • 77952243282 scopus 로고    scopus 로고
    • Deleterious effects of reactive aldehydes and glycated proteins on macrophage proteasomal function: Possible links between diabetes and atherosclerosis
    • Moheimani F, Morgan PE, van Reyk DM, Davies MJ. Deleterious effects of reactive aldehydes and glycated proteins on macrophage proteasomal function: possible links between diabetes and atherosclerosis. Biochim Biophys Acta 2010; 1802: 561-71.
    • (2010) Biochim Biophys Acta , vol.1802 , pp. 561-571
    • Moheimani, F.1    Morgan, P.E.2    van Reyk, D.M.3    Davies, M.J.4
  • 136
    • 0034614889 scopus 로고    scopus 로고
    • Efficient generation of a hepatitis B virus cytotoxic T lymphocyte epitope requires the structural features of immunoproteasomes
    • Sijts AJ, Ruppert T, Rehermann B, Schmidt M, Koszinowski U, Kloetzel PM. Efficient generation of a hepatitis B virus cytotoxic T lymphocyte epitope requires the structural features of immunoproteasomes. J Exp Med 2000; 191: 503-14.
    • (2000) J Exp Med , vol.191 , pp. 503-514
    • Sijts, A.J.1    Ruppert, T.2    Rehermann, B.3    Schmidt, M.4    Koszinowski, U.5    Kloetzel, P.M.6
  • 137
    • 0032542348 scopus 로고    scopus 로고
    • Antigen presentation. A protease draws first blood
    • Bogyo M, Ploegh HL. Antigen presentation. A protease draws first blood. Nature 1998; 396: 625-627.
    • (1998) Nature , vol.396 , pp. 625-627
    • Bogyo, M.1    Ploegh, H.L.2
  • 139
    • 2942610705 scopus 로고    scopus 로고
    • Agedependent protein modifications and declining proteasome activity in the human lens
    • Viteri G, Carrard G, Birlouez-Aragon I, Silva E, Friguet B. Agedependent protein modifications and declining proteasome activity in the human lens. Arch Biochem Biophys 2004; 427: 197-203.
    • (2004) Arch Biochem Biophys , vol.427 , pp. 197-203
    • Viteri, G.1    Carrard, G.2    Birlouez-Aragon, I.3    Silva, E.4    Friguet, B.5
  • 140
    • 0033870001 scopus 로고    scopus 로고
    • Proteasome inhibition by lipofuscin/ ceroid during postmitotic aging of fibroblasts
    • Sitte N, Huber M, Grune T, et al. Proteasome inhibition by lipofuscin/ ceroid during postmitotic aging of fibroblasts. FASEB J 2000; 14: 1490-8.
    • (2000) FASEB J , vol.14 , pp. 1490-1498
    • Sitte, N.1    Huber, M.2    Grune, T.3
  • 142
    • 80054026084 scopus 로고    scopus 로고
    • Distinct roles in vivo for the ubiquitin-proteasome system and the autophagylysosomal pathway in the degradation of alpha-synuclein
    • Ebrahimi-Fakhari D, Cantuti-Castelvetri I, Fan Z, et al. Distinct roles in vivo for the ubiquitin-proteasome system and the autophagylysosomal pathway in the degradation of alpha-synuclein. J Neurosci 2011; 31: 14508-20.
    • (2011) J Neurosci , vol.31 , pp. 14508-14520
    • Ebrahimi-Fakhari, D.1    Cantuti-Castelvetri, I.2    Fan, Z.3
  • 143
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer W, Przedborski S. Parkinson's disease: mechanisms and models. Neuron 2003; 39: 889-909.
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 144
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • Ciechanover A, Brundin P. The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 2003; 40: 427-46.
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 145
    • 51549086469 scopus 로고    scopus 로고
    • Neuroprotection of rapamycin in lactacystin-induced neurodegeneration via autophagy enhancement
    • Pan T, Kondo S, Zhu W, Xie W, Jankovic J, Le W. Neuroprotection of rapamycin in lactacystin-induced neurodegeneration via autophagy enhancement. Neurobiol Dis 2008; 32: 16-25.
    • (2008) Neurobiol Dis , vol.32 , pp. 16-25
    • Pan, T.1    Kondo, S.2    Zhu, W.3    Xie, W.4    Jankovic, J.5    Le, W.6
  • 146
    • 36549035313 scopus 로고    scopus 로고
    • Lipofuscin: Formation, distribution, and metabolic consequences
    • Jung T, Bader N, Grune T. Lipofuscin: formation, distribution, and metabolic consequences. Ann N Y Acad Sci 2007; 1119: 97-111.
    • (2007) Ann N Y Acad Sci , vol.1119 , pp. 97-111
    • Jung, T.1    Bader, N.2    Grune, T.3
  • 147
  • 148
    • 33744488281 scopus 로고    scopus 로고
    • Catabolic insufficiency and aging
    • Terman A. Catabolic insufficiency and aging. Ann N Y Acad Sci 2006; 1067: 27-36.
    • (2006) Ann N Y Acad Sci , vol.1067 , pp. 27-36
    • Terman, A.1
  • 149
    • 0037994340 scopus 로고    scopus 로고
    • p62 overexpression in breast tumors and regulation by prostate-derived Ets factor in breast cancer cells
    • Thompson HG, Harris JW, Wold BJ, Lin F, Brody JP. p62 overexpression in breast tumors and regulation by prostate-derived Ets factor in breast cancer cells. Oncogene 2003; 22: 2322-33.
    • (2003) Oncogene , vol.22 , pp. 2322-2333
    • Thompson, H.G.1    Harris, J.W.2    Wold, B.J.3    Lin, F.4    Brody, J.P.5
  • 150
    • 33846692198 scopus 로고    scopus 로고
    • Signal integration and diversification through the p62 scaffold protein
    • Moscat J, az-Meco MT, Wooten MW. Signal integration and diversification through the p62 scaffold protein. Trends Biochem Sci 2007; 32: 95-100.
    • (2007) Trends Biochem Sci , vol.32 , pp. 95-100
    • Moscat, J.1    az-Meco, M.T.2    Wooten, M.W.3
  • 151
    • 41549151641 scopus 로고    scopus 로고
    • Ref(2)P, the Drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain
    • Nezis IP, Simonsen A, Sagona AP, et al. Ref(2)P, the Drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain. J Cell Biol 2008; 180: 1065-71.
    • (2008) J Cell Biol , vol.180 , pp. 1065-1071
    • Nezis, I.P.1    Simonsen, A.2    Sagona, A.P.3
  • 152
    • 69449090071 scopus 로고    scopus 로고
    • A novel link between autophagy and the ubiquitin-proteasome system
    • Korolchuk VI, Menzies FM, Rubinsztein DC. A novel link between autophagy and the ubiquitin-proteasome system. Autophagy 2009; 5: 862-3.
    • (2009) Autophagy , vol.5 , pp. 862-863
    • Korolchuk, V.I.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 153
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • Korolchuk VI, Mansilla A, Menzies FM, Rubinsztein DC. Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Mol Cell 2009; 33: 517-27.
    • (2009) Mol Cell , vol.33 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2    Menzies, F.M.3    Rubinsztein, D.C.4
  • 154
    • 0031555892 scopus 로고    scopus 로고
    • Low micromolar levels of hydrogen peroxide and proteasome inhibitors induce the 60-kDa A170 stress protein in murine peritoneal macrophages
    • Ishii T, Yanagawa T, Yuki K, Kawane T, Yoshida H, Bannai S. Low micromolar levels of hydrogen peroxide and proteasome inhibitors induce the 60-kDa A170 stress protein in murine peritoneal macrophages. Biochem Biophys Res Commun 1997; 232: 33-7.
    • (1997) Biochem Biophys Res Commun , vol.232 , pp. 33-37
    • Ishii, T.1    Yanagawa, T.2    Yuki, K.3    Kawane, T.4    Yoshida, H.5    Bannai, S.6
  • 155
    • 34548259958 scopus 로고    scopus 로고
    • p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy
    • Pankiv S, Clausen TH, Lamark T, et al. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J Biol Chem 2007; 282: 24131-45.
    • (2007) J Biol Chem , vol.282 , pp. 24131-24145
    • Pankiv, S.1    Clausen, T.H.2    Lamark, T.3
  • 156
    • 53049103308 scopus 로고    scopus 로고
    • Structural basis for sorting mechanism of p62 in selective autophagy
    • Ichimura Y, Kumanomidou T, Sou YS, et al. Structural basis for sorting mechanism of p62 in selective autophagy. J Biol Chem 2008; 283: 22847-57.
    • (2008) J Biol Chem , vol.283 , pp. 22847-22857
    • Ichimura, Y.1    Kumanomidou, T.2    Sou, Y.S.3
  • 157
    • 77954599053 scopus 로고    scopus 로고
    • p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription
    • Jain A, Lamark T, Sjottem E, et al. p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription. J Biol Chem 2010; 285: 22576-91.
    • (2010) J Biol Chem , vol.285 , pp. 22576-22591
    • Jain, A.1    Lamark, T.2    Sjottem, E.3
  • 158
    • 0031577292 scopus 로고    scopus 로고
    • An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements
    • Itoh K, Chiba T, Takahashi S, et al. An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements. Biochem Biophys Res Commun 1997; 236: 313-22.
    • (1997) Biochem Biophys Res Commun , vol.236 , pp. 313-322
    • Itoh, K.1    Chiba, T.2    Takahashi, S.3
  • 160
    • 0034717329 scopus 로고    scopus 로고
    • Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages
    • Ishii T, Itoh K, Takahashi S, et al. Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages. J Biol Chem 2000; 275: 16023-9.
    • (2000) J Biol Chem , vol.275 , pp. 16023-16029
    • Ishii, T.1    Itoh, K.2    Takahashi, S.3
  • 161
    • 0035947654 scopus 로고    scopus 로고
    • Hemin-induced activation of the thioredoxin gene by Nrf2. A differential regulation of the antioxidant responsive element by a switch of its binding factors
    • Kim YC, Masutani H, Yamaguchi Y, Itoh K, Yamamoto M, Yodoi J. Hemin-induced activation of the thioredoxin gene by Nrf2. A differential regulation of the antioxidant responsive element by a switch of its binding factors. J Biol Chem 2001; 276: 18399-406.
    • (2001) J Biol Chem , vol.276 , pp. 18399-18406
    • Kim, Y.C.1    Masutani, H.2    Yamaguchi, Y.3    Itoh, K.4    Yamamoto, M.5    Yodoi, J.6
  • 163
    • 0033546686 scopus 로고    scopus 로고
    • Up-regulation of the human gammaglutamylcysteine synthetase regulatory subunit gene involves binding of Nrf-2 to an electrophile responsive element
    • Moinova HR, Mulcahy RT. Up-regulation of the human gammaglutamylcysteine synthetase regulatory subunit gene involves binding of Nrf-2 to an electrophile responsive element. Biochem Biophys Res Commun 1999; 261: 661-8.
    • (1999) Biochem Biophys Res Commun , vol.261 , pp. 661-668
    • Moinova, H.R.1    Mulcahy, R.T.2
  • 164
    • 0042330074 scopus 로고    scopus 로고
    • Identification of a novel Nrf2-regulated antioxidant response element (ARE) in the mouse NAD(P)H:Quinone oxidoreductase 1 gene: Reassessment of the ARE consensus sequence
    • Nioi P, McMahon M, Itoh K, Yamamoto M, Hayes JD. Identification of a novel Nrf2-regulated antioxidant response element (ARE) in the mouse NAD(P)H:quinone oxidoreductase 1 gene: reassessment of the ARE consensus sequence. Biochem J 2003; 374: 337-48.
    • (2003) Biochem J , vol.374 , pp. 337-348
    • Nioi, P.1    McMahon, M.2    Itoh, K.3    Yamamoto, M.4    Hayes, J.D.5
  • 165
    • 33845442925 scopus 로고    scopus 로고
    • Mechanistic studies of the Nrf2-Keap1 signaling pathway
    • Zhang DD. Mechanistic studies of the Nrf2-Keap1 signaling pathway. Drug Metab Rev 2006; 38:7 69-89.
    • (2006) Drug Metab Rev , vol.38 , pp. 769-789
    • Zhang, D.D.1
  • 166
    • 11144264663 scopus 로고    scopus 로고
    • BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase
    • Furukawa M, Xiong Y. BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase. Mol Cell Biol 2005; 25: 162-71.
    • (2005) Mol Cell Biol , vol.25 , pp. 162-171
    • Furukawa, M.1    Xiong, Y.2
  • 167
    • 4544294365 scopus 로고    scopus 로고
    • The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: Oxidative stress sensing by a Cul3-Keap1 ligase
    • Cullinan SB, Gordan JD, Jin J, Harper JW, Diehl JA. The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: oxidative stress sensing by a Cul3-Keap1 ligase. Mol Cell Biol 2004; 24: 8477-86.
    • (2004) Mol Cell Biol , vol.24 , pp. 8477-8486
    • Cullinan, S.B.1    Gordan, J.D.2    Jin, J.3    Harper, J.W.4    Diehl, J.A.5
  • 168
    • 33344469643 scopus 로고    scopus 로고
    • Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1
    • Kobayashi A, Kang MI, Watai Y, et al. Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1. Mol Cell Biol 2006; 26: 221-9.
    • (2006) Mol Cell Biol , vol.26 , pp. 221-229
    • Kobayashi, A.1    Kang, M.I.2    Watai, Y.3
  • 169
    • 12444257799 scopus 로고    scopus 로고
    • Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles
    • Itoh K, Wakabayashi N, Katoh Y, Ishii T, O'Connor T, Yamamoto M. Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles. Genes Cells 2003; 8: 379-91.
    • (2003) Genes Cells , vol.8 , pp. 379-391
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    O'Connor, T.5    Yamamoto, M.6
  • 170
    • 0037015035 scopus 로고    scopus 로고
    • Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants
    • Dinkova-Kostova AT, Holtzclaw WD, Cole RN, et al. Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc Natl Acad Sci USA 2002; 99: 11908-13.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11908-11913
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Cole, R.N.3
  • 171
    • 7244253081 scopus 로고    scopus 로고
    • Nrf2-Keap1 defines a physiologically important stress response mechanism
    • Motohashi H, Yamamoto M. Nrf2-Keap1 defines a physiologically important stress response mechanism. Trends Mol Med 2004; 10: 549-57.
    • (2004) Trends Mol Med , vol.10 , pp. 549-557
    • Motohashi, H.1    Yamamoto, M.2
  • 172
    • 9644272830 scopus 로고    scopus 로고
    • Protection against electrophile and oxidative stress by induction of phase 2 genes: The quest for the elusive sensor that responds to inducers
    • Holtzclaw WD, nkova-Kostova AT, Talalay P. Protection against electrophile and oxidative stress by induction of phase 2 genes: the quest for the elusive sensor that responds to inducers. Adv Enzyme Regul 2004; 44: 335-67.
    • (2004) Adv Enzyme Regul , vol.44 , pp. 335-367
    • Holtzclaw, W.D.1    Nkova-Kostova, A.T.2    Talalay, P.3
  • 173
    • 33748052967 scopus 로고    scopus 로고
    • Nrf2-Keap1 regulation of cellular defense mechanisms against lectrophiles and reactive oxygen species
    • Kobayashi M, Yamamoto M. Nrf2-Keap1 regulation of cellular defense mechanisms against lectrophiles and reactive oxygen species. Adv Enzyme Regul 2006; 46: 113-40.
    • (2006) Adv Enzyme Regul , vol.46 , pp. 113-140
    • Kobayashi, M.1    Yamamoto, M.2
  • 174
    • 82755197938 scopus 로고    scopus 로고
    • Metabolic contribution of hepatic autophagic proteolysis: Old wine in new bottles
    • Ueno T, Ezaki J, Kominami E. Metabolic contribution of hepatic autophagic proteolysis: old wine in new bottles. Biochim Biophys Acta 2012; 1824: 51-8.
    • (2012) Biochim Biophys Acta , vol.1824 , pp. 51-58
    • Ueno, T.1    Ezaki, J.2    Kominami, E.3
  • 175
    • 77649265091 scopus 로고    scopus 로고
    • The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1
    • Komatsu M, Kurokawa H, Waguri S, et al. The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1. Nat Cell Biol 2010; 12: 213-23.
    • (2010) Nat Cell Biol , vol.12 , pp. 213-223
    • Komatsu, M.1    Kurokawa, H.2    Waguri, S.3
  • 176
    • 77953366801 scopus 로고    scopus 로고
    • A noncanonical mechanism of Nrf2 activation by autophagy deficiency: Direct interaction between Keap1 and p62
    • Lau A, Wang XJ, Zhao F, et al. A noncanonical mechanism of Nrf2 activation by autophagy deficiency: direct interaction between Keap1 and p62. Mol Cell Biol 2010; 30: 3275-85.
    • (2010) Mol Cell Biol , vol.30 , pp. 3275-3285
    • Lau, A.1    Wang, X.J.2    Zhao, F.3
  • 177
    • 78649636576 scopus 로고    scopus 로고
    • Dietary isoflavones and vascular protection: Activation of cellular antioxidant defenses by SERMs or hormesis?
    • Siow RC, Mann GE. Dietary isoflavones and vascular protection: activation of cellular antioxidant defenses by SERMs or hormesis? Mol Aspects Med 2010; 31: 468-77.
    • (2010) Mol Aspects Med , vol.31 , pp. 468-477
    • Siow, R.C.1    Mann, G.E.2
  • 178
    • 78649635403 scopus 로고    scopus 로고
    • Nrf2, a guardian of healthspan and gatekeeper of species longevity
    • Lewis KN, Mele J, Hayes JD, Buffenstein R. Nrf2, a guardian of healthspan and gatekeeper of species longevity. Integr Comp Biol 2010; 50: 829-43.
    • (2010) Integr Comp Biol , vol.50 , pp. 829-843
    • Lewis, K.N.1    Mele, J.2    Hayes, J.D.3    Buffenstein, R.4
  • 179
    • 84861464050 scopus 로고    scopus 로고
    • Crosstalk between Nrf2 and the proteasome: Therapeutic potential of Nrf2 inducers in vascular disease and aging
    • Chapple SJ, Siow RC, Mann GE. Crosstalk between Nrf2 and the proteasome: therapeutic potential of Nrf2 inducers in vascular disease and aging. Int J Biochem Cell Biol 2012; 44: 1315-20.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 1315-1320
    • Chapple, S.J.1    Siow, R.C.2    Mann, G.E.3
  • 180
    • 77649242989 scopus 로고    scopus 로고
    • p62, an autophagy hero or culprit?
    • Rusten TE, Stenmark H. p62, an autophagy hero or culprit? Nat Cell Biol 2010; 12: 207-9.
    • (2010) Nat Cell Biol , vol.12 , pp. 207-209
    • Rusten, T.E.1    Stenmark, H.2
  • 181
    • 0344256510 scopus 로고    scopus 로고
    • Function of the ubiquitin proteolytic pathway in the eye
    • Shang F, Taylor A. Function of the ubiquitin proteolytic pathway in the eye. Exp Eye Res 2004; 78: 1-14.
    • (2004) Exp Eye Res , vol.78 , pp. 1-14
    • Shang, F.1    Taylor, A.2
  • 182
    • 0034613294 scopus 로고    scopus 로고
    • Age-related decline in chaperone-mediated autophagy
    • Cuervo AM, Dice JF. Age-related decline in chaperone-mediated autophagy. J Biol Chem 2000; 275: 31505-13.
    • (2000) J Biol Chem , vol.275 , pp. 31505-31513
    • Cuervo, A.M.1    Dice, J.F.2
  • 184
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • Iwata A, Riley BE, Johnston JA, Kopito RR. HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J Biol Chem 2005; 280: 40282-92.
    • (2005) J Biol Chem , vol.280 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 185
    • 79961023008 scopus 로고    scopus 로고
    • EGF signalling activates the ubiquitin proteasome system to modulate C. elegans lifespan
    • Liu G, Rogers J, Murphy CT, Rongo C. EGF signalling activates the ubiquitin proteasome system to modulate C. elegans lifespan. EMBO J 2011; 30: 2990-3003.
    • (2011) EMBO J , vol.30 , pp. 2990-3003
    • Liu, G.1    Rogers, J.2    Murphy, C.T.3    Rongo, C.4
  • 186
    • 46649083580 scopus 로고    scopus 로고
    • Aging and dietary restriction effects on ubiquitination, sumoylation, and the proteasome in the heart
    • Li F, Zhang L, Craddock J, et al. Aging and dietary restriction effects on ubiquitination, sumoylation, and the proteasome in the heart. Mech Ageing Dev 2008; 129: 515-21.
    • (2008) Mech Ageing Dev , vol.129 , pp. 515-521
    • Li, F.1    Zhang, L.2    Craddock, J.3
  • 187
    • 71849084532 scopus 로고    scopus 로고
    • Aging and dietary restriction alter proteasome biogenesis and composition in the brain and liver
    • Dasuri K, Zhang L, Ebenezer P, Liu Y, Fernandez-Kim SO, Keller JN. Aging and dietary restriction alter proteasome biogenesis and composition in the brain and liver. Mech Ageing Dev 2009; 130: 777-83.
    • (2009) Mech Ageing Dev , vol.130 , pp. 777-783
    • Dasuri, K.1    Zhang, L.2    Ebenezer, P.3    Liu, Y.4    Fernandez-Kim, S.O.5    Keller, J.N.6
  • 188
    • 43949117436 scopus 로고    scopus 로고
    • Early cellular changes after blockage of chaperone-mediated autophagy
    • Massey AC, Follenzi A, Kiffin R, Zhang C, Cuervo AM. Early cellular changes after blockage of chaperone-mediated autophagy. Autophagy 2008; 4: 442-56.
    • (2008) Autophagy , vol.4 , pp. 442-456
    • Massey, A.C.1    Follenzi, A.2    Kiffin, R.3    Zhang, C.4    Cuervo, A.M.5
  • 189
    • 34548851476 scopus 로고    scopus 로고
    • Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6
    • Olzmann JA, Li L, Chudaev MV, et al. Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6. J Cell Biol 2007; 178: 1025-38.
    • (2007) J Cell Biol , vol.178 , pp. 1025-1038
    • Olzmann, J.A.1    Li, L.2    Chudaev, M.V.3


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