메뉴 건너뛰기




Volumn 60, Issue 5, 2012, Pages 443-447

Protein homeostasis and aging: Role of ubiquitin protein ligases

Author keywords

Aging; Oxidative stress; Proteasome; Protein homeostasis; Ubiquitin; Ubiquitin ligase

Indexed keywords

UBIQUITIN PROTEIN LIGASE;

EID: 84857703860     PISSN: 01970186     EISSN: 18729754     Source Type: Journal    
DOI: 10.1016/j.neuint.2012.02.009     Document Type: Short Survey
Times cited : (49)

References (89)
  • 1
    • 34248327285 scopus 로고    scopus 로고
    • CHIP overexpression reduces mutant androgen receptor protein and ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model
    • H. Adachi, M. Waza, K. Tokui, M. Katsuno, M. Minamiyama, F. Tanaka, M. Doyu, and G. Sobue CHIP overexpression reduces mutant androgen receptor protein and ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model J. Neurosci. 27 2007 5115 5126
    • (2007) J. Neurosci. , vol.27 , pp. 5115-5126
    • Adachi, H.1    Waza, M.2    Tokui, K.3    Katsuno, M.4    Minamiyama, M.5    Tanaka, F.6    Doyu, M.7    Sobue, G.8
  • 2
    • 79954571967 scopus 로고    scopus 로고
    • Amyloid-binding compounds maintain protein homeostasis during ageing and extend lifespan
    • S. Alavez, M.C. Vantipalli, D.J. Zucker, I.M. Klang, and G.J. Lithgow Amyloid-binding compounds maintain protein homeostasis during ageing and extend lifespan Nature 472 2011 226 229
    • (2011) Nature , vol.472 , pp. 226-229
    • Alavez, S.1    Vantipalli, M.C.2    Zucker, D.J.3    Klang, I.M.4    Lithgow, G.J.5
  • 3
    • 84859164670 scopus 로고    scopus 로고
    • Immune and non-immune functions of the immunoproteasome
    • A. Angeles, G. Fung, and H. Luo Immune and non-immune functions of the immunoproteasome Front. Biosci. 17 2012 1904 1916
    • (2012) Front. Biosci. , vol.17 , pp. 1904-1916
    • Angeles, A.1    Fung, G.2    Luo, H.3
  • 4
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • N.F. Bence, R.M. Sampat, and R.R. Kopito Impairment of the ubiquitin-proteasome system by protein aggregation Science 292 2001 1552 1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 6
    • 33645926989 scopus 로고    scopus 로고
    • P62/SQSTM1: A missing link between protein aggregates and the autophagy machinery
    • G. Bjorkoy, T. Lamark, and T. Johansen P62/SQSTM1: a missing link between protein aggregates and the autophagy machinery Autophagy 2 2006 138 139
    • (2006) Autophagy , vol.2 , pp. 138-139
    • Bjorkoy, G.1    Lamark, T.2    Johansen, T.3
  • 7
    • 26844505808 scopus 로고    scopus 로고
    • Toxin-induced models of Parkinson's disease
    • J. Bove, D. Prou, C. Perier, and S. Przedborski Toxin-induced models of Parkinson's disease NeuroRx. 2 2005 484 494
    • (2005) NeuroRx. , vol.2 , pp. 484-494
    • Bove, J.1    Prou, D.2    Perier, C.3    Przedborski, S.4
  • 8
    • 59849091257 scopus 로고    scopus 로고
    • Insulin/IGF-like signalling, the central nervous system and aging
    • S. Broughton, and L. Partridge Insulin/IGF-like signalling, the central nervous system and aging Biochem. J. 418 2009 1 12
    • (2009) Biochem. J. , vol.418 , pp. 1-12
    • Broughton, S.1    Partridge, L.2
  • 9
    • 67651004289 scopus 로고    scopus 로고
    • A conserved ubiquitination pathway determines longevity in response to diet restriction
    • A.C. Carrano, Z. Liu, A. Dillin, and T. Hunter A conserved ubiquitination pathway determines longevity in response to diet restriction Nature 460 2009 396 399
    • (2009) Nature , vol.460 , pp. 396-399
    • Carrano, A.C.1    Liu, Z.2    Dillin, A.3    Hunter, T.4
  • 12
    • 67149107430 scopus 로고    scopus 로고
    • HIF-1 modulates dietary restriction-mediated lifespan extension via IRE-1 in Caenorhabditis elegans
    • D. Chen, E.L. Thomas, and P. Kapahi HIF-1 modulates dietary restriction-mediated lifespan extension via IRE-1 in Caenorhabditis elegans PLoS Genet. 5 2009 e1000486
    • (2009) PLoS Genet. , vol.5 , pp. 1000486
    • Chen, D.1    Thomas, E.L.2    Kapahi, P.3
  • 13
    • 66349105688 scopus 로고    scopus 로고
    • The WD40 repeat protein WDR-23 functions with the CUL4/DDB1 ubiquitin ligase to regulate nuclear abundance and activity of SKN-1 in Caenorhabditis elegans
    • K.P. Choe, A.J. Przybysz, and K. Strange The WD40 repeat protein WDR-23 functions with the CUL4/DDB1 ubiquitin ligase to regulate nuclear abundance and activity of SKN-1 in Caenorhabditis elegans Mol. Cell. Biol. 29 2009 2704 2715
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2704-2715
    • Choe, K.P.1    Przybysz, A.J.2    Strange, K.3
  • 14
    • 11244309014 scopus 로고    scopus 로고
    • Proteolysis: From the lysosome to ubiquitin and the proteasome
    • A. Ciechanover Proteolysis: from the lysosome to ubiquitin and the proteasome Nat. Rev. Mol. Cell Biol. 6 2005 79 87
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 79-87
    • Ciechanover, A.1
  • 15
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • A. Ciechanover, and P. Brundin The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg Neuron 40 2003 427 446
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 16
    • 0030586350 scopus 로고    scopus 로고
    • Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90
    • M. Conconi, L.I. Szweda, R.L. Levine, E.R. Stadtman, and B. Friguet Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90 Arch. Biochem. Biophys. 331 1996 232 240
    • (1996) Arch. Biochem. Biophys. , vol.331 , pp. 232-240
    • Conconi, M.1    Szweda, L.I.2    Levine, R.L.3    Stadtman, E.R.4    Friguet, B.5
  • 17
    • 0033391428 scopus 로고    scopus 로고
    • Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice
    • C.J. Cummings, E. Reinstein, Y. Sun, B. Antalffy, Y. Jiang, A. Ciechanover, H.T. Orr, A.L. Beaudet, and H.Y. Zoghbi Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice Neuron 24 1999 879 892
    • (1999) Neuron , vol.24 , pp. 879-892
    • Cummings, C.J.1    Reinstein, E.2    Sun, Y.3    Antalffy, B.4    Jiang, Y.5    Ciechanover, A.6    Orr, H.T.7    Beaudet, A.L.8    Zoghbi, H.Y.9
  • 18
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • D.M. Cyr, J. Hohfeld, and C. Patterson Protein quality control: U-box-containing E3 ubiquitin ligases join the fold Trends Biochem. Sci. 27 2002 368 375
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 368-375
    • Cyr, D.M.1    Hohfeld, J.2    Patterson, C.3
  • 19
    • 80053578494 scopus 로고    scopus 로고
    • Proteasome alterations during adipose differentiation and aging: Links to impaired adipocyte differentiation and development of oxidative stress
    • K. Dasuri, L. Zhang, P. Ebenezer, S.O. Fernandez-Kim, A.J. Bruce-Keller, L.I. Szweda, and J.N. Keller Proteasome alterations during adipose differentiation and aging: links to impaired adipocyte differentiation and development of oxidative stress Free Radical Biol. Med. 51 2011 1727 1735
    • (2011) Free Radical Biol. Med. , vol.51 , pp. 1727-1735
    • Dasuri, K.1    Zhang, L.2    Ebenezer, P.3    Fernandez-Kim, S.O.4    Bruce-Keller, A.J.5    Szweda, L.I.6    Keller, J.N.7
  • 20
    • 71849084532 scopus 로고    scopus 로고
    • Aging and dietary restriction alter proteasome biogenesis and composition in the brain and liver
    • K. Dasuri, L. Zhang, P. Ebenezer, Y. Liu, S.O. Fernandez-Kim, and J.N. Keller Aging and dietary restriction alter proteasome biogenesis and composition in the brain and liver Mech. Ageing Dev. 130 2009 777 783
    • (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
  • 21
    • 38449083555 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias
    • J.E. Davies, S. Sarkar, and D.C. Rubinsztein The ubiquitin proteasome system in Huntington's disease and the spinocerebellar ataxias BMC Biochem. 8 Suppl 1 2007 S2
    • (2007) BMC Biochem. , vol.8 , Issue.SUPPL. 1 , pp. 2
    • Davies, J.E.1    Sarkar, S.2    Rubinsztein, D.C.3
  • 22
    • 41049117758 scopus 로고    scopus 로고
    • Role of ubiquitin protein ligases in the pathogenesis of polyglutamine diseases
    • P. Dikshit, and N.R. Jana Role of ubiquitin protein ligases in the pathogenesis of polyglutamine diseases Neurochem. Res. 33 2008 945 951
    • (2008) Neurochem. Res. , vol.33 , pp. 945-951
    • Dikshit, P.1    Jana, N.R.2
  • 23
    • 33644652951 scopus 로고    scopus 로고
    • Proteasome regulation of oxidative stress in aging and age-related diseases of the CNS
    • Q. Ding, E. Dimayuga, and J.N. Keller Proteasome regulation of oxidative stress in aging and age-related diseases of the CNS Antioxid. Redox Signaling 8 2006 163 172
    • (2006) Antioxid. Redox Signaling , vol.8 , pp. 163-172
    • Ding, Q.1    Dimayuga, E.2    Keller, J.N.3
  • 24
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • M.L. Duennwald, and S. Lindquist Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity Genes Dev. 22 2008 3308 3319
    • (2008) Genes Dev. , vol.22 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 25
    • 33644662970 scopus 로고    scopus 로고
    • Proteasome function in aging and oxidative stress: Implications in protein maintenance failure
    • L. Farout, and B. Friguet Proteasome function in aging and oxidative stress: implications in protein maintenance failure Antioxid. Redox Signaling 8 2006 205 216
    • (2006) Antioxid. Redox Signaling , vol.8 , pp. 205-216
    • Farout, L.1    Friguet, B.2
  • 26
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • D. Finley Recognition and processing of ubiquitin-protein conjugates by the proteasome Annu. Rev. Biochem. 78 2009 477 513
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 27
    • 0035050618 scopus 로고    scopus 로고
    • Caretaker or undertaker? the role of the proteasome in aging
    • M. Gaczynska, P.A. Osmulski, and W.F. Ward Caretaker or undertaker? The role of the proteasome in aging Mech. Ageing Dev. 122 2001 235 254
    • (2001) Mech. Ageing Dev. , vol.122 , pp. 235-254
    • Gaczynska, M.1    Osmulski, P.A.2    Ward, W.F.3
  • 28
    • 58949098465 scopus 로고    scopus 로고
    • The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system
    • P. Garyali, P. Siwach, P.K. Singh, R. Puri, S. Mittal, S. Sengupta, R. Parihar, and S. Ganesh The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system Hum. Mol. Genet. 18 2009 688 700
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 688-700
    • Garyali, P.1    Siwach, P.2    Singh, P.K.3    Puri, R.4    Mittal, S.5    Sengupta, S.6    Parihar, R.7    Ganesh, S.8
  • 30
    • 66749126389 scopus 로고    scopus 로고
    • Antioxidant defense and aging in C. elegans: Is the oxidative damage theory of aging wrong?
    • D. Gems, and R. Doonan Antioxidant defense and aging in C. elegans: is the oxidative damage theory of aging wrong? Cell Cycle 8 2009 1681 1687
    • (2009) Cell Cycle , vol.8 , pp. 1681-1687
    • Gems, D.1    Doonan, R.2
  • 31
    • 34250882745 scopus 로고    scopus 로고
    • Regulation of Caenorhabditis elegans lifespan by a proteasomal E3 ligase complex
    • A. Ghazi, S. Henis-Korenblit, and C. Kenyon Regulation of Caenorhabditis elegans lifespan by a proteasomal E3 ligase complex Proc. Nat. Acad. Sci. U.S.A. 104 2007 5947 5952
    • (2007) Proc. Nat. Acad. Sci. U.S.A. , vol.104 , pp. 5947-5952
    • Ghazi, A.1    Henis-Korenblit, S.2    Kenyon, C.3
  • 32
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • M.H. Glickman, and A. Ciechanover The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction Physiol. Rev. 82 2002 373 428
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 33
    • 32644481227 scopus 로고    scopus 로고
    • Oxidative stress promotes mutant huntingtin aggregation and mutant huntingtin-dependent cell death by mimicking proteasomal malfunction
    • A. Goswami, P. Dikshit, A. Mishra, S. Mulherkar, N. Nukina, and N.R. Jana Oxidative stress promotes mutant huntingtin aggregation and mutant huntingtin-dependent cell death by mimicking proteasomal malfunction Biochem. Biophys. Res. Commun. 342 2006 184 190
    • (2006) Biochem. Biophys. Res. Commun. , vol.342 , pp. 184-190
    • Goswami, A.1    Dikshit, P.2    Mishra, A.3    Mulherkar, S.4    Nukina, N.5    Jana, N.R.6
  • 36
    • 77953020414 scopus 로고    scopus 로고
    • A photoconvertible reporter of the ubiquitin-proteasome system in vivo
    • G. Hamer, O. Matilainen, and C.I. Holmberg A photoconvertible reporter of the ubiquitin-proteasome system in vivo Nat. Methods 7 2010 473 478
    • (2010) Nat. Methods , vol.7 , pp. 473-478
    • Hamer, G.1    Matilainen, O.2    Holmberg, C.I.3
  • 38
    • 0029870836 scopus 로고    scopus 로고
    • Protein degradation or regulation: Ub the judge
    • M. Hochstrasser Protein degradation or regulation: Ub the judge Cell 84 1996 813 815
    • (1996) Cell , vol.84 , pp. 813-815
    • Hochstrasser, M.1
  • 40
    • 15744387323 scopus 로고    scopus 로고
    • Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes
    • N.R. Jana, P. Dikshit, A. Goswami, S. Kotliarova, S. Murata, K. Tanaka, and N. Nukina Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes J. Biol. Chem. 280 2005 11635 11640
    • (2005) J. Biol. Chem. , vol.280 , pp. 11635-11640
    • Jana, N.R.1    Dikshit, P.2    Goswami, A.3    Kotliarova, S.4    Murata, S.5    Tanaka, K.6    Nukina, N.7
  • 41
    • 1642564603 scopus 로고    scopus 로고
    • Inhibition of proteasomal function by curcumin induces apoptosis through mitochondrial pathway
    • N.R. Jana, P. Dikshit, A. Goswami, and N. Nukina Inhibition of proteasomal function by curcumin induces apoptosis through mitochondrial pathway J. Biol. Chem. 279 2004 11680 11685
    • (2004) J. Biol. Chem. , vol.279 , pp. 11680-11685
    • Jana, N.R.1    Dikshit, P.2    Goswami, A.3    Nukina, N.4
  • 42
    • 0242289453 scopus 로고    scopus 로고
    • Recent advances in understanding the pathogenesis of polyglutamine diseases: Involvement of molecular chaperones and ubiquitin-proteasome pathway
    • N.R. Jana, and N. Nukina Recent advances in understanding the pathogenesis of polyglutamine diseases: involvement of molecular chaperones and ubiquitin-proteasome pathway J. Chem. Neuroanat. 26 2003 95 101
    • (2003) J. Chem. Neuroanat. , vol.26 , pp. 95-101
    • Jana, N.R.1    Nukina, N.2
  • 44
    • 0032192481 scopus 로고    scopus 로고
    • Mutation of the Angelman ubiquitin ligase in mice causes increased cytoplasmic p53 and deficits of contextual learning and long-term potentiation
    • Y.H. Jiang, D. Armstrong, U. Albrecht, C.M. Atkins, J.L. Noebels, G. Eichele, J.D. Sweatt, and A.L. Beaudet Mutation of the Angelman ubiquitin ligase in mice causes increased cytoplasmic p53 and deficits of contextual learning and long-term potentiation Neuron 21 1998 799 811
    • (1998) Neuron , vol.21 , pp. 799-811
    • Jiang, Y.H.1    Armstrong, D.2    Albrecht, U.3    Atkins, C.M.4    Noebels, J.L.5    Eichele, G.6    Sweatt, J.D.7    Beaudet, A.L.8
  • 48
    • 0033972037 scopus 로고    scopus 로고
    • Possible involvement of proteasome inhibition in aging: Implications for oxidative stress
    • J.N. Keller, K.B. Hanni, and W.R. Markesbery Possible involvement of proteasome inhibition in aging: implications for oxidative stress Mech. Ageing Dev. 113 2000 61 70
    • (2000) Mech. Ageing Dev. , vol.113 , pp. 61-70
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 49
    • 0034087369 scopus 로고    scopus 로고
    • Decreased levels of proteasome activity and proteasome expression in aging spinal cord
    • J.N. Keller, F.F. Huang, and W.R. Markesbery Decreased levels of proteasome activity and proteasome expression in aging spinal cord Neuroscience 98 2000 149 156
    • (2000) Neuroscience , vol.98 , pp. 149-156
    • Keller, J.N.1    Huang, F.F.2    Markesbery, W.R.3
  • 50
    • 77950200010 scopus 로고    scopus 로고
    • The genetics of ageing
    • C.J. Kenyon The genetics of ageing Nature 464 2010 504 512
    • (2010) Nature , vol.464 , pp. 504-512
    • Kenyon, C.J.1
  • 52
    • 0031012849 scopus 로고    scopus 로고
    • UBE3A/E6-AP mutations cause Angelman syndrome
    • T. Kishino, M. Lalande, and J. Wagstaff UBE3A/E6-AP mutations cause Angelman syndrome Nat. Genet. 15 1997 70 73
    • (1997) Nat. Genet. , vol.15 , pp. 70-73
    • Kishino, T.1    Lalande, M.2    Wagstaff, J.3
  • 55
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
    • Y.A. Lam, T.G. Lawson, M. Velayutham, J.L. Zweier, and C.M. Pickart A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal Nature 416 2002 763 767
    • (2002) Nature , vol.416 , pp. 763-767
    • Lam, Y.A.1    Lawson, T.G.2    Velayutham, M.3    Zweier, J.L.4    Pickart, C.M.5
  • 56
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • J.D. Laney, and M. Hochstrasser Substrate targeting in the ubiquitin system Cell 97 1999 427 430
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.D.1    Hochstrasser, M.2
  • 57
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • P.T. Lansbury, and H.A. Lashuel A century-old debate on protein aggregation and neurodegeneration enters the clinic Nature 443 2006 774 779
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 58
    • 0033610079 scopus 로고    scopus 로고
    • Gene expression profile of aging and its retardation by caloric restriction
    • C.K. Lee, R.G. Klopp, R. Weindruch, and T.A. Prolla Gene expression profile of aging and its retardation by caloric restriction Science 285 1999 1390 1393
    • (1999) Science , vol.285 , pp. 1390-1393
    • Lee, C.K.1    Klopp, R.G.2    Weindruch, R.3    Prolla, T.A.4
  • 59
    • 0000847978 scopus 로고    scopus 로고
    • Gene-expression profile of the ageing brain in mice
    • C.K. Lee, R. Weindruch, and T.A. Prolla Gene-expression profile of the ageing brain in mice Nat. Genet. 25 2000 294 297
    • (2000) Nat. Genet. , vol.25 , pp. 294-297
    • Lee, C.K.1    Weindruch, R.2    Prolla, T.A.3
  • 61
    • 46649083580 scopus 로고    scopus 로고
    • Aging and dietary restriction effects on ubiquitination, sumoylation, and the proteasome in the heart
    • F. Li, L. Zhang, J. Craddock, A.J. Bruce-Keller, K. Dasuri, A. Nguyen, and J.N. Keller Aging and dietary restriction effects on ubiquitination, sumoylation, and the proteasome in the heart Mech. Ageing Dev. 129 2008 515 521
    • (2008) Mech. Ageing Dev. , vol.129 , pp. 515-521
    • Li, F.1    Zhang, L.2    Craddock, J.3    Bruce-Keller, A.J.4    Dasuri, K.5    Nguyen, A.6    Keller, J.N.7
  • 62
    • 33846596646 scopus 로고    scopus 로고
    • RLE-1, an E3 ubiquitin ligase, regulates C. elegans aging by catalyzing DAF-16 polyubiquitination
    • W. Li, B. Gao, S.M. Lee, K. Bennett, and D. Fang RLE-1, an E3 ubiquitin ligase, regulates C. elegans aging by catalyzing DAF-16 polyubiquitination Dev. Cell 12 2007 235 246
    • (2007) Dev. Cell , vol.12 , pp. 235-246
    • Li, W.1    Gao, B.2    Lee, S.M.3    Bennett, K.4    Fang, D.5
  • 63
    • 79961023008 scopus 로고    scopus 로고
    • EGF signalling activates the ubiquitin proteasome system to modulate C. elegans lifespan
    • G. Liu, J. Rogers, C.T. Murphy, and C. Rongo EGF signalling activates the ubiquitin proteasome system to modulate C. elegans lifespan EMBO J. 30 2011 2990 3003
    • (2011) EMBO J. , vol.30 , pp. 2990-3003
    • Liu, G.1    Rogers, J.2    Murphy, C.T.3    Rongo, C.4
  • 67
    • 44949127204 scopus 로고    scopus 로고
    • CHIP deficiency decreases longevity, with accelerated aging phenotypes accompanied by altered protein quality control
    • J.N. Min, R.A. Whaley, N.E. Sharpless, P. Lockyer, A.L. Portbury, and C. Patterson CHIP deficiency decreases longevity, with accelerated aging phenotypes accompanied by altered protein quality control Mol. Cell. Biol. 28 2008 4018 4025
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4018-4025
    • Min, J.N.1    Whaley, R.A.2    Sharpless, N.E.3    Lockyer, P.4    Portbury, A.L.5    Patterson, C.6
  • 68
    • 43149120469 scopus 로고    scopus 로고
    • E6-AP promotes misfolded polyglutamine proteins for proteasomal degradation and suppresses polyglutamine protein aggregation and toxicity
    • A. Mishra, P. Dikshit, S. Purkayastha, J. Sharma, N. Nukina, and N.R. Jana E6-AP promotes misfolded polyglutamine proteins for proteasomal degradation and suppresses polyglutamine protein aggregation and toxicity J. Biol. Chem. 283 2008 7648 7656
    • (2008) J. Biol. Chem. , vol.283 , pp. 7648-7656
    • Mishra, A.1    Dikshit, P.2    Purkayastha, S.3    Sharma, J.4    Nukina, N.5    Jana, N.R.6
  • 69
    • 67449107793 scopus 로고    scopus 로고
    • The ubiquitin ligase E6-AP is induced and recruited to aggresomes in response to proteasome inhibition and may be involved in the ubiquitination of Hsp70-bound misfolded proteins
    • A. Mishra, S.K. Godavarthi, M. Maheshwari, A. Goswami, and N.R. Jana The ubiquitin ligase E6-AP is induced and recruited to aggresomes in response to proteasome inhibition and may be involved in the ubiquitination of Hsp70-bound misfolded proteins J. Biol. Chem. 284 2009 10537 10545
    • (2009) J. Biol. Chem. , vol.284 , pp. 10537-10545
    • Mishra, A.1    Godavarthi, S.K.2    Maheshwari, M.3    Goswami, A.4    Jana, N.R.5
  • 71
    • 77956324028 scopus 로고    scopus 로고
    • Loss of dopaminergic neurons and resulting behavioural deficits in mouse model of Angelman syndrome
    • S.A. Mulherkar, and N.R. Jana Loss of dopaminergic neurons and resulting behavioural deficits in mouse model of Angelman syndrome Neurobiol. Dis. 40 2010 586 592
    • (2010) Neurobiol. Dis. , vol.40 , pp. 586-592
    • Mulherkar, S.A.1    Jana, N.R.2
  • 72
    • 48649085488 scopus 로고    scopus 로고
    • P97 homologs from Caenorhabditis elegans, CDC-48.1 and CDC-48.2, suppress the aggregate formation of huntingtin exon1 containing expanded polyQ repeat
    • S. Nishikori, K. Yamanaka, T. Sakurai, M. Esaki, and T. Ogura P97 homologs from Caenorhabditis elegans, CDC-48.1 and CDC-48.2, suppress the aggregate formation of huntingtin exon1 containing expanded polyQ repeat Genes Cells 13 2008 827 838
    • (2008) Genes Cells , vol.13 , pp. 827-838
    • Nishikori, S.1    Yamanaka, K.2    Sakurai, T.3    Esaki, M.4    Ogura, T.5
  • 73
    • 0029154502 scopus 로고
    • Age-related accumulation of high-molecular-weight ubiquitin protein conjugates in mouse brains
    • H. Ohtsuka, R. Takahashi, and S. Goto Age-related accumulation of high-molecular-weight ubiquitin protein conjugates in mouse brains J. Gerontol. A Biol. Sci. Med. Sci. 50 1995 B277 B281
    • (1995) J. Gerontol. A Biol. Sci. Med. Sci. , vol.50
    • Ohtsuka, H.1    Takahashi, R.2    Goto, S.3
  • 74
    • 0032919345 scopus 로고    scopus 로고
    • The role of the ubiquitin-proteasome pathway in apoptosis
    • R.Z. Orlowski The role of the ubiquitin-proteasome pathway in apoptosis Cell Death Differ. 6 1999 303 313
    • (1999) Cell Death Differ. , vol.6 , pp. 303-313
    • Orlowski, R.Z.1
  • 76
    • 0030772933 scopus 로고    scopus 로고
    • Targeting of substrates to the 26S proteasome
    • C.M. Pickart Targeting of substrates to the 26S proteasome FASEB J. 11 1997 1055 1066
    • (1997) FASEB J. , vol.11 , pp. 1055-1066
    • Pickart, C.M.1
  • 77
    • 78149272475 scopus 로고    scopus 로고
    • Sequestration of chaperones and proteasome into Lafora bodies and proteasomal dysfunction induced by Lafora disease-associated mutations of malin
    • S.N. Rao, R. Maity, J. Sharma, P. Dey, S.K. Shankar, P. Satishchandra, and N.R. Jana Sequestration of chaperones and proteasome into Lafora bodies and proteasomal dysfunction induced by Lafora disease-associated mutations of malin Hum. Mol. Genet. 19 2010 4726 4734
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 4726-4734
    • Rao, S.N.1    Maity, R.2    Sharma, J.3    Dey, P.4    Shankar, S.K.5    Satishchandra, P.6    Jana, N.R.7
  • 80
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • D.C. Rubinsztein The roles of intracellular protein-degradation pathways in neurodegeneration Nature 443 2006 780 786
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 81
    • 79955366725 scopus 로고    scopus 로고
    • A screenable in vivo assay to study proteostasis networks in Caenorhabditis elegans
    • A. Segref, S. Torres, and T. Hoppe A screenable in vivo assay to study proteostasis networks in Caenorhabditis elegans Genetics 187 2011 1235 1240
    • (2011) Genetics , vol.187 , pp. 1235-1240
    • Segref, A.1    Torres, S.2    Hoppe, T.3
  • 82
    • 79957684292 scopus 로고    scopus 로고
    • CHIP E3 ligase regulates mammalian senescence by modulating the levels of oxidized proteins
    • C. Sisoula, and E.S. Gonos CHIP E3 ligase regulates mammalian senescence by modulating the levels of oxidized proteins Mech. Ageing Dev. 132 2011 269 272
    • (2011) Mech. Ageing Dev. , vol.132 , pp. 269-272
    • Sisoula, C.1    Gonos, E.S.2
  • 83
    • 59449095881 scopus 로고    scopus 로고
    • Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process
    • A. Tonoki, E. Kuranaga, T. Tomioka, J. Hamazaki, S. Murata, K. Tanaka, and M. Miura Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process Mol. Cell. Biol. 29 2009 1095 1106
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1095-1106
    • Tonoki, A.1    Kuranaga, E.2    Tomioka, T.3    Hamazaki, J.4    Murata, S.5    Tanaka, K.6    Miura, M.7
  • 84
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Y.C. Tsai, P.S. Fishman, N.V. Thakor, and G.A. Oyler Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function J. Biol. Chem. 278 2003 22044 22055
    • (2003) J. Biol. Chem. , vol.278 , pp. 22044-22055
    • Tsai, Y.C.1    Fishman, P.S.2    Thakor, N.V.3    Oyler, G.A.4
  • 87
    • 60849119525 scopus 로고    scopus 로고
    • In vivo suppression of polyglutamine neurotoxicity by C-terminus of Hsp70-interacting protein (CHIP) supports an aggregation model of pathogenesis
    • A.J. Williams, T.M. Knutson, V.F. Colomer Gould, and H.L. Paulson In vivo suppression of polyglutamine neurotoxicity by C-terminus of Hsp70-interacting protein (CHIP) supports an aggregation model of pathogenesis Neurobiol. Dis. 33 2009 342 353
    • (2009) Neurobiol. Dis. , vol.33 , pp. 342-353
    • Williams, A.J.1    Knutson, T.M.2    Colomer Gould, V.F.3    Paulson, H.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.