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Volumn 10, Issue 3, 2011, Pages 1062-1072

Proteomic characterization of aggregating proteins after the inhibition of the ubiquitin proteasome system

Author keywords

aggregation; neurodegenerative disease; proteasome; proteomics; ubiquitin

Indexed keywords

CHAPERONE; NBR1 UBIQUITIN BINDING PROTEIN; PROTEASOME; PROTEIN P62; SEQUESTOSOME 1; SUCROSE; UBIQUITIN; UBIQUITIN ASSOCIATED PROTEIN 2 LIKE; UNCLASSIFIED DRUG;

EID: 79952376730     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr1008543     Document Type: Article
Times cited : (49)

References (78)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti, F.; Dobson, C. M. Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 2006, 75, 333-66 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C. A.; Poirier, M. A. Protein aggregation and neurodegenerative disease Nat. Med. 2004, 10 Suppl) S10-7
    • (2004) Nat. Med. , Issue.10 SUPPL. , pp. 10-7
    • Ross, C.A.1    Poirier, M.A.2
  • 3
    • 0023927981 scopus 로고
    • Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinsons disease, Picks disease, and Alzheimers disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease
    • Lowe, J.; Blanchard, A.; Morrell, K.; Lennox, G.; Reynolds, L.; Billett, M.; Landon, M.; Mayer, R. J. Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinsons disease, Picks disease, and Alzheimers disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease J. Pathol. 1988, 155 (1) 9-15
    • (1988) J. Pathol. , vol.155 , Issue.1 , pp. 9-15
    • Lowe, J.1    Blanchard, A.2    Morrell, K.3    Lennox, G.4    Reynolds, L.5    Billett, M.6    Landon, M.7    Mayer, R.J.8
  • 4
    • 0032402298 scopus 로고    scopus 로고
    • Ubiquitin, cellular inclusions and their role in neurodegeneration
    • DOI 10.1016/S0166-2236(98)01276-4
    • Alves-Rodrigues, A.; Gregori, L.; Figueiredo-Pereira, M. E. Ubiquitin, cellular inclusions and their role in neurodegeneration Trends Neurosci. 1998, 21 (12) 516-20 (Pubitemid 28555693)
    • (1998) Trends in Neurosciences , vol.21 , Issue.12 , pp. 516-520
    • Alves-Rodrigues, A.1    Gregori, L.2    Figueiredo-Pereira, M.E.3
  • 5
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • DOI 10.1038/35056563
    • Weissman, A. M. Themes and variations on ubiquitylation Nat. Rev. Mol. Cell. Biol. 2001, 2 (3) 169-78 (Pubitemid 33675741)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.3 , pp. 169-178
    • Weissman, A.M.1
  • 6
    • 33745816760 scopus 로고    scopus 로고
    • Protein degradation by the ubiquitin-proteasome pathway in normal and disease states
    • DOI 10.1681/ASN.2006010083
    • Lecker, S. H.; Goldberg, A. L.; Mitch, W. E. Protein degradation by the ubiquitin-proteasome pathway in normal and disease states J. Am. Soc. Nephrol. 2006, 17 (7) 1807-19 (Pubitemid 44036165)
    • (2006) Journal of the American Society of Nephrology , vol.17 , Issue.7 , pp. 1807-1819
    • Lecker, S.H.1    Goldberg, A.L.2    Mitch, W.E.3
  • 7
    • 0038155130 scopus 로고    scopus 로고
    • Proteasomal inhibition causes the formation of protein aggregates containing a wide range of proteins, including nitrated proteins
    • DOI 10.1046/j.1471-4159.2003.01841.x
    • Hyun, D. H.; Lee, M.; Halliwell, B.; Jenner, P. Proteasomal inhibition causes the formation of protein aggregates containing a wide range of proteins, including nitrated proteins J. Neurochem. 2003, 86 (2) 363-73 (Pubitemid 36842435)
    • (2003) Journal of Neurochemistry , vol.86 , Issue.2 , pp. 363-373
    • Hyun, D.-H.1    Lee, M.2    Halliwell, B.3    Jenner, P.4
  • 9
    • 13844300068 scopus 로고    scopus 로고
    • L-dopa and dopamine enhance the formation of aggregates under proteasome inhibition in PC12 cells
    • DOI 10.1016/j.febslet.2004.12.091
    • Yoshimoto, Y.; Nakaso, K.; Nakashima, K. L-dopa and dopamine enhance the formation of aggregates under proteasome inhibition in PC12 cells FEBS Lett. 2005, 579 (5) 1197-202 (Pubitemid 40248687)
    • (2005) FEBS Letters , vol.579 , Issue.5 , pp. 1197-1202
    • Yoshimoto, Y.1    Nakaso, K.2    Nakashima, K.3
  • 10
    • 33747165263 scopus 로고    scopus 로고
    • Proteasome inhibitor MG-132 induces dopaminergic degeneration in cell culture and animal models
    • DOI 10.1016/j.neuro.2006.06.006, PII S0161813X06001689
    • Sun, F.; Anantharam, V.; Zhang, D.; Latchoumycandane, C.; Kanthasamy, A.; Kanthasamy, A. G. Proteasome inhibitor MG-132 induces dopaminergic degeneration in cell culture and animal models Neurotoxicology 2006, 27 (5) 807-15 (Pubitemid 44232996)
    • (2006) NeuroToxicology , vol.27 , Issue.5 , pp. 807-815
    • Sun, F.1    Anantharam, V.2    Zhang, D.3    Latchoumycandane, C.4    Kanthasamy, A.5    Kanthasamy, A.G.6
  • 11
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley, D. Recognition and processing of ubiquitin-protein conjugates by the proteasome Annu. Rev. Biochem. 2009, 78, 477-513
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 12
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • DOI 10.1016/j.bbamcr.2004.09.019, PII S0167488904002356, The Ubiquitin-Proteasome System
    • Pickart, C. M.; Eddins, M. J. Ubiquitin: structures, functions, mechanisms Biochim. Biophys. Acta 2004, 1695 (1-3) 55-72 (Pubitemid 39585154)
    • (2004) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1695 , Issue.1-3 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 15
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • DOI 10.1038/35008096
    • Schubert, U.; Anton, L. C.; Gibbs, J.; Norbury, C. C.; Yewdell, J. W.; Bennink, J. R. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes Nature 2000, 404 (6779) 770-4 (Pubitemid 30212405)
    • (2000) Nature , vol.404 , Issue.6779 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 17
    • 33646578189 scopus 로고    scopus 로고
    • Oxidized protein degradation and repair in ageing and oxidative stress
    • DOI 10.1016/j.febslet.2006.03.028, PII S0014579306003309
    • Friguet, B. Oxidized protein degradation and repair in ageing and oxidative stress FEBS Lett. 2006, 580 (12) 2910-6 (Pubitemid 43729157)
    • (2006) FEBS Letters , vol.580 , Issue.12 , pp. 2910-2916
    • Friguet, B.1
  • 18
    • 69549103145 scopus 로고    scopus 로고
    • Recent advances in our understanding of neurodegeneration
    • Jellinger, K. A. Recent advances in our understanding of neurodegeneration J. Neural Transm. 2009, 116 (9) 1111-62
    • (2009) J. Neural Transm. , vol.116 , Issue.9 , pp. 1111-62
    • Jellinger, K.A.1
  • 20
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • DOI 10.1126/science.292.5521.1552
    • Bence, N. F.; Sampat, R. M.; Kopito, R. R. Impairment of the ubiquitin-proteasome system by protein aggregation Science 2001, 292 (5521) 1552-5 (Pubitemid 32493425)
    • (2001) Science , vol.292 , Issue.5521 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 21
    • 0038413759 scopus 로고    scopus 로고
    • Aggregated and monomeric α-synuclein bind to the S6′ proteasomal protein and inhibit proteasomal function
    • DOI 10.1074/jbc.M208641200
    • Snyder, H.; Mensah, K.; Theisler, C.; Lee, J.; Matouschek, A.; Wolozin, B. Aggregated and monomeric alpha-synuclein bind to the S6′ proteasomal protein and inhibit proteasomal function J. Biol. Chem. 2003, 278 (14) 11753-9 (Pubitemid 36800143)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 11753-11759
    • Snyder, H.1    Mensah, K.2    Theisler, C.3    Lee, J.4    Matouschek, A.5    Wolozin, B.6
  • 22
    • 77951976610 scopus 로고    scopus 로고
    • Cell-produced alpha-synuclein oligomers are targeted to, and impair, the 26S proteasome
    • Emmanouilidou, E.; Stefanis, L.; Vekrellis, K. Cell-produced alpha-synuclein oligomers are targeted to, and impair, the 26S proteasome Neurobiol. Aging 2010, 31 (6) 953-68
    • (2010) Neurobiol. Aging , vol.31 , Issue.6 , pp. 953-68
    • Emmanouilidou, E.1    Stefanis, L.2    Vekrellis, K.3
  • 23
    • 51449096696 scopus 로고    scopus 로고
    • Abeta inhibits the proteasome and enhances amyloid and tau accumulation
    • Tseng, B. P.; Green, K. N.; Chan, J. L.; Blurton-Jones, M.; LaFerla, F. M. Abeta inhibits the proteasome and enhances amyloid and tau accumulation Neurobiol. Aging 2008, 29 (11) 1607-18
    • (2008) Neurobiol. Aging , vol.29 , Issue.11 , pp. 1607-18
    • Tseng, B.P.1    Green, K.N.2    Chan, J.L.3    Blurton-Jones, M.4    Laferla, F.M.5
  • 24
    • 3042857991 scopus 로고    scopus 로고
    • Proteolytic stress causes heat shock protein induction, tau ubiquitination, and the recruitment of ubiquitin to tau-positive aggregates in oligodendrocytes in culture
    • DOI 10.1523/JNEUROSCI.1307-04.2004
    • Goldbaum, O.; Richter-Landsberg, C. Proteolytic stress causes heat shock protein induction, tau ubiquitination, and the recruitment of ubiquitin to tau-positive aggregates in oligodendrocytes in culture J. Neurosci. 2004, 24 (25) 5748-57 (Pubitemid 38857229)
    • (2004) Journal of Neuroscience , vol.24 , Issue.25 , pp. 5748-5757
    • Goldbaum, O.1    Richter-Landsberg, C.2
  • 25
    • 70450220221 scopus 로고    scopus 로고
    • The small heat shock protein HSP25 protects astrocytes against stress induced by proteasomal inhibition
    • Goldbaum, O.; Riedel, M.; Stahnke, T.; Richter-Landsberg, C. The small heat shock protein HSP25 protects astrocytes against stress induced by proteasomal inhibition Glia 2009, 57 (14) 1566-77
    • (2009) Glia , vol.57 , Issue.14 , pp. 1566-77
    • Goldbaum, O.1    Riedel, M.2    Stahnke, T.3    Richter-Landsberg, C.4
  • 26
    • 0036239489 scopus 로고    scopus 로고
    • Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and αB-crystallin to aggresomes
    • Ito, H.; Kamei, K.; Iwamoto, I.; Inaguma, Y.; Garcia-Mata, R.; Sztul, E.; Kato, K. Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and alphaB-Crystallin to aggresomes J. Biochem. 2002, 131 (4) 593-603 (Pubitemid 34456616)
    • (2002) Journal of Biochemistry , vol.131 , Issue.4 , pp. 593-603
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3    Inaguma, Y.4    Garcia-Mata, R.5    Sztul, E.6    Kato, K.7
  • 28
    • 0037728958 scopus 로고    scopus 로고
    • Proteasome inhibitors induce intracellular protein aggregation and cell death by an oxygen-dependent mechanism
    • DOI 10.1016/S0014-5793(03)00353-3
    • Demasi, M.; Davies, K. J. Proteasome inhibitors induce intracellular protein aggregation and cell death by an oxygen-dependent mechanism FEBS Lett. 2003, 542 (1-3) 89-94 (Pubitemid 36555720)
    • (2003) FEBS Letters , vol.542 , Issue.1-3 , pp. 89-94
    • Demasi, M.1    Davies, K.J.A.2
  • 30
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong, S. E.; Mann, M. A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC) Nat. Protoc. 2006, 1 (6) 2650-60
    • (2006) Nat. Protoc. , vol.1 , Issue.6 , pp. 2650-60
    • Ong, S.E.1    Mann, M.2
  • 31
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel, D.; Flugge, U. I. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids Anal. Biochem. 1984, 138 (1) 141-3 (Pubitemid 14146660)
    • (1984) Analytical Biochemistry , vol.138 , Issue.1 , pp. 141-143
    • Wessel, D.1    Flugge, U.I.2
  • 32
    • 0037317228 scopus 로고    scopus 로고
    • Stop And Go Extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • DOI 10.1021/ac026117i
    • Rappsilber, J.; Ishihama, Y.; Mann, M. Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics Anal. Chem. 2003, 75 (3) 663-70 (Pubitemid 36176744)
    • (2003) Analytical Chemistry , vol.75 , Issue.3 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 33
    • 56449127251 scopus 로고    scopus 로고
    • Changes in protein expression during honey bee larval development
    • Chan, Q. W.; Foster, L. J. Changes in protein expression during honey bee larval development Genome Biol. 2008, 9 (10) R156
    • (2008) Genome Biol. , vol.9 , Issue.10 , pp. 156
    • Chan, Q.W.1    Foster, L.J.2
  • 34
    • 70349581497 scopus 로고    scopus 로고
    • Cytoscape: A community-based framework for network modeling
    • Killcoyne, S.; Carter, G. W.; Smith, J.; Boyle, J. Cytoscape: a community-based framework for network modeling Methods Mol. Biol. 2009, 563, 219-39
    • (2009) Methods Mol. Biol. , vol.563 , pp. 219-39
    • Killcoyne, S.1    Carter, G.W.2    Smith, J.3    Boyle, J.4
  • 36
    • 36749080327 scopus 로고    scopus 로고
    • Quantitative profiling of ubiquitylated proteins reveals proteasome substrates and the substrate repertoire influenced by the Rpn10 receptor pathway
    • DOI 10.1074/mcp.M700264-MCP200
    • Mayor, T.; Graumann, J.; Bryan, J.; MacCoss, M. J.; Deshaies, R. J. Quantitative profiling of ubiquitylated proteins reveals proteasome substrates and the substrate repertoire influenced by the Rpn10 receptor pathway Mol. Cell. Proteomics 2007, 6 (11) 1885-95 (Pubitemid 350201866)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.11 , pp. 1885-1895
    • Mayor, T.1    Graumann, J.2    Bryan, J.3    MacCoss, M.J.4    Deshaies, R.J.5
  • 37
    • 34547535639 scopus 로고    scopus 로고
    • The functions of UCH-L1 and its relation to neurodegenerative diseases
    • DOI 10.1016/j.neuint.2007.05.007, PII S0197018607001246
    • Setsuie, R.; Wada, K. The functions of UCH-L1 and its relation to neurodegenerative diseases Neurochem. Int. 2007, 51 (2-4) 105-11 (Pubitemid 47179898)
    • (2007) Neurochemistry International , vol.51 , Issue.2-4 SPEC. ISSUE , pp. 105-111
    • Setsuie, R.1    Wada, K.2
  • 40
    • 3142724742 scopus 로고    scopus 로고
    • UCH-L1 aggresome formation in response to proteasome impairment indicates a role in inclusion formation in Parkinson's disease
    • DOI 10.1111/j.1471-4159.2004.02485.x
    • Ardley, H. C.; Scott, G. B.; Rose, S. A.; Tan, N. G.; Robinson, P. A. UCH-L1 aggresome formation in response to proteasome impairment indicates a role in inclusion formation in Parkinsons disease J. Neurochem. 2004, 90 (2) 379-91 (Pubitemid 38938224)
    • (2004) Journal of Neurochemistry , vol.90 , Issue.2 , pp. 379-391
    • Ardley, H.C.1    Scott, G.B.2    Rose, S.A.3    Tan, N.G.S.4    Robinson, P.A.5
  • 42
    • 4143119185 scopus 로고    scopus 로고
    • Ataxin-10, the spinocerebellar ataxia type 10 neurodegenerative disorder protein, is essential for survival of cerebellar neurons
    • DOI 10.1074/jbc.M405865200
    • Marz, P.; Probst, A.; Lang, S.; Schwager, M.; Rose-John, S.; Otten, U.; Ozbek, S. Ataxin-10, the spinocerebellar ataxia type 10 neurodegenerative disorder protein, is essential for survival of cerebellar neurons J. Biol. Chem. 2004, 279 (34) 35542-50 (Pubitemid 39100555)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35542-35550
    • Marz, P.1    Probst, A.2    Lang, S.3    Schwager, M.4    Rose-John, S.5    Otten, U.6    Ozbek, S.7
  • 44
    • 55949136614 scopus 로고    scopus 로고
    • Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry
    • Meierhofer, D.; Wang, X.; Huang, L.; Kaiser, P. Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry J. Proteome Res. 2008, 7 (10) 4566-76
    • (2008) J. Proteome Res. , vol.7 , Issue.10 , pp. 4566-76
    • Meierhofer, D.1    Wang, X.2    Huang, L.3    Kaiser, P.4
  • 45
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • Xu, G.; Paige, J. S.; Jaffrey, S. R. Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling Nat. Biotechnol. 2010, 28 (8) 868-73
    • (2010) Nat. Biotechnol. , vol.28 , Issue.8 , pp. 868-73
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 46
    • 29144505073 scopus 로고    scopus 로고
    • Proteomic analysis of ubiquitinated proteins from human MCF-7 breast cancer cells by immunoaffinity purification and mass spectrometry
    • DOI 10.1021/pr050265i
    • Vasilescu, J.; Smith, J. C.; Ethier, M.; Figeys, D. Proteomic analysis of ubiquitinated proteins from human MCF-7 breast cancer cells by immunoaffinity purification and mass spectrometry J. Proteome Res. 2005, 4 (6) 2192-200 (Pubitemid 41814287)
    • (2005) Journal of Proteome Research , vol.4 , Issue.6 , pp. 2192-2200
    • Vasilescu, J.1    Smith, J.C.2    Ethier, M.3    Figeys, D.4
  • 48
    • 55849136903 scopus 로고    scopus 로고
    • Global protein stability profiling in mammalian cells
    • Yen, H. C.; Xu, Q.; Chou, D. M.; Zhao, Z.; Elledge, S. J. Global protein stability profiling in mammalian cells Science 2008, 322 (5903) 918-23
    • (2008) Science , vol.322 , Issue.5903 , pp. 918-23
    • Yen, H.C.1    Xu, Q.2    Chou, D.M.3    Zhao, Z.4    Elledge, S.J.5
  • 49
    • 34249679116 scopus 로고    scopus 로고
    • P62 accumulates and enhances aggregate formation in model systems of familial amyotrophic lateral sclerosis
    • DOI 10.1074/jbc.M608787200
    • Gal, J.; Strom, A. L.; Kilty, R.; Zhang, F.; Zhu, H. p62 accumulates and enhances aggregate formation in model systems of familial amyotrophic lateral sclerosis J. Biol. Chem. 2007, 282 (15) 11068-77 (Pubitemid 47100749)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.15 , pp. 11068-11077
    • Gal, J.1    Strom, A.-L.2    Kilty, R.3    Zhang, F.4    Zhu, H.5
  • 52
    • 67650234499 scopus 로고    scopus 로고
    • NBR1 cooperates with p62 in selective autophagy of ubiquitinated targets
    • Kirkin, V.; Lamark, T.; Johansen, T.; Dikic, I. NBR1 cooperates with p62 in selective autophagy of ubiquitinated targets Autophagy 2009, 5 (5) 732-3
    • (2009) Autophagy , vol.5 , Issue.5 , pp. 732-3
    • Kirkin, V.1    Lamark, T.2    Johansen, T.3    Dikic, I.4
  • 53
    • 0034805395 scopus 로고    scopus 로고
    • Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells
    • DOI 10.1006/bbrc.2000.4107
    • 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 (1) 223-8 (Pubitemid 32917500)
    • (2001) Biochemical and Biophysical Research Communications , vol.280 , Issue.1 , pp. 223-228
    • Kuusisto, E.1    Suuronen, T.2    Salminen, A.3
  • 54
    • 77953108542 scopus 로고    scopus 로고
    • The diversity of ubiquitin recognition: Hot spots and varied specificity
    • Winget, J. M.; Mayor, T. The diversity of ubiquitin recognition: hot spots and varied specificity Mol. Cell 2010, 38 (5) 627-35
    • (2010) Mol. Cell , vol.38 , Issue.5 , pp. 627-35
    • Winget, J.M.1    Mayor, T.2
  • 57
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da, W.; Sherman, B. T.; Lempicki, R. A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources Nat. Protoc. 2009, 4 (1) 44-57
    • (2009) Nat. Protoc. , vol.4 , Issue.1 , pp. 44-57
    • Huang Da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 58
    • 33645074670 scopus 로고    scopus 로고
    • Alterations in degradative pathways and protein aggregation in a neuropathy model based on PMP22 overexpression
    • Fortun, J.; Go, J. C.; Li, J.; Amici, S. A.; Dunn, W. A., Jr.; Notterpek, L. Alterations in degradative pathways and protein aggregation in a neuropathy model based on PMP22 overexpression Neurobiol. Dis. 2006, 22 (1) 153-64
    • (2006) Neurobiol. Dis. , vol.22 , Issue.1 , pp. 153-64
    • Fortun, J.1    Go, J.C.2    Li, J.3    Amici, S.A.4    Dunn Jr., W.A.5    Notterpek, L.6
  • 59
    • 78149456945 scopus 로고    scopus 로고
    • WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins
    • Pashkova, N.; Gakhar, L.; Winistorfer, S. C.; Yu, L.; Ramaswamy, S.; Piper, R. C. WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins Mol. Cell 2010, 40 (3) 433-43
    • (2010) Mol. Cell , vol.40 , Issue.3 , pp. 433-43
    • Pashkova, N.1    Gakhar, L.2    Winistorfer, S.C.3    Yu, L.4    Ramaswamy, S.5    Piper, R.C.6
  • 60
    • 2942552459 scopus 로고    scopus 로고
    • An automated method for finding molecular complexes in large protein interaction networks
    • Bader, G. D.; Hogue, C. W. An automated method for finding molecular complexes in large protein interaction networks BMC Bioinform. 2003, 4, 2
    • (2003) BMC Bioinform. , vol.4 , pp. 2
    • Bader, G.D.1    Hogue, C.W.2
  • 61
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance
    • DOI 10.1074/jbc.272.14.9086
    • Bush, K. T.; Goldberg, A. L.; Nigam, S. K. Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance J. Biol. Chem. 1997, 272 (14) 9086-92 (Pubitemid 27154911)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 9086-9092
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 62
    • 77649305375 scopus 로고    scopus 로고
    • 17-AAG induces cytoplasmic alpha-synuclein aggregate clearance by induction of autophagy
    • Riedel, M.; Goldbaum, O.; Schwarz, L.; Schmitt, S.; Richter-Landsberg, C. 17-AAG induces cytoplasmic alpha-synuclein aggregate clearance by induction of autophagy PLoS One 2010, 5 (1 e8753
    • (2010) PLoS One , vol.5 , Issue.1
    • Riedel, M.1    Goldbaum, O.2    Schwarz, L.3    Schmitt, S.4    Richter-Landsberg, C.5
  • 63
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
    • Waelter, S.; Boeddrich, A.; Lurz, R.; Scherzinger, E.; Lueder, G.; Lehrach, H.; Wanker, E. E. Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation Mol. Biol. Cell 2001, 12 (5) 1393-407 (Pubitemid 33044419)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.5 , pp. 1393-1407
    • Waelter, S.1    Boeddrich, A.2    Lurz, R.3    Scherzinger, E.4    Lueder, G.5    Lehrach, H.6    Wanker, E.E.7
  • 64
    • 0037073747 scopus 로고    scopus 로고
    • Characterization of cytoplasmic alpha-synuclein aggregates. Fibril formation is tightly linked to the inclusion-forming process in cells
    • Lee, H. J.; Lee, S. J. Characterization of cytoplasmic alpha-synuclein aggregates. Fibril formation is tightly linked to the inclusion-forming process in cells J. Biol. Chem. 2002, 277 (50) 48976-83
    • (2002) J. Biol. Chem. , vol.277 , Issue.50 , pp. 48976-83
    • Lee, H.J.1    Lee, S.J.2
  • 65
    • 77955053465 scopus 로고    scopus 로고
    • Hsp105 reduces the protein aggregation and cytotoxicity by expanded-polyglutamine proteins through the induction of Hsp70
    • Yamagishi, N.; Goto, K.; Nakagawa, S.; Saito, Y.; Hatayama, T. Hsp105 reduces the protein aggregation and cytotoxicity by expanded-polyglutamine proteins through the induction of Hsp70 Exp. Cell Res. 2010, 316 (15) 2424-33
    • (2010) Exp. Cell Res. , vol.316 , Issue.15 , pp. 2424-33
    • Yamagishi, N.1    Goto, K.2    Nakagawa, S.3    Saito, Y.4    Hatayama, T.5
  • 66
    • 0042591262 scopus 로고    scopus 로고
    • Hsp105α Suppresses the Aggregation of Truncated Androgen Receptor with Expanded CAG Repeats and Cell Toxicity
    • DOI 10.1074/jbc.M302975200
    • Ishihara, K.; Yamagishi, N.; Saito, Y.; Adachi, H.; Kobayashi, Y.; Sobue, G.; Ohtsuka, K.; Hatayama, T. Hsp105alpha suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity J. Biol. Chem. 2003, 278 (27) 25143-50 (Pubitemid 37548678)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.27 , pp. 25143-25150
    • Ishihara, K.1    Yamagishi, N.2    Saito, Y.3    Adachi, H.4    Kobayashi, Y.5    Sobue, G.6    Ohtsuka, K.7    Hatayama, T.8
  • 67
    • 1542373742 scopus 로고    scopus 로고
    • The Role of Heat Shock Transcription Factor 1 in the Genome-wide Regulation of the Mammalian Heat Shock Response
    • DOI 10.1091/mbc.E03-10-0738
    • Trinklein, N. D.; Murray, J. I.; Hartman, S. J.; Botstein, D.; Myers, R. M. The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response Mol. Biol. Cell 2004, 15 (3) 1254-61 (Pubitemid 38316232)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.3 , pp. 1254-1261
    • Trinklein, N.D.1    Murray, J.I.2    Hartman, S.J.3    Botstein, D.4    Myers, R.M.5
  • 68
    • 33645803596 scopus 로고    scopus 로고
    • Differential effects of Hsc70 and Hsp70 on the intracellular trafficking and functional expression of epithelial sodium channels
    • Goldfarb, S. B.; Kashlan, O. B.; Watkins, J. N.; Suaud, L.; Yan, W.; Kleyman, T. R.; Rubenstein, R. C. Differential effects of Hsc70 and Hsp70 on the intracellular trafficking and functional expression of epithelial sodium channels Proc. Natl. Acad. Sci. U.S.A. 2006, 103 (15) 5817-22
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , Issue.15 , pp. 5817-22
    • Goldfarb, S.B.1    Kashlan, O.B.2    Watkins, J.N.3    Suaud, L.4    Yan, W.5    Kleyman, T.R.6    Rubenstein, R.C.7
  • 70
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: Emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne, C.; Polymenidou, M.; Cleveland, D. W. TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration Hum. Mol. Genet. 2010, 19 (R1) R46-64
    • (2010) Hum. Mol. Genet. , vol.19 , Issue.R1 , pp. 46-64
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 71
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • DOI 10.1083/jcb.143.7.1883
    • Johnston, J. A.; Ward, C. L.; Kopito, R. R. Aggresomes: a cellular response to misfolded proteins J. Cell Biol. 1998, 143 (7) 1883-98 (Pubitemid 29022611)
    • (1998) Journal of Cell Biology , vol.143 , Issue.7 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 72
    • 0032771080 scopus 로고    scopus 로고
    • The Emery-Dreifuss muscular dystrophy phonotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane
    • Fairley, E. A.; Kendrick-Jones, J.; Ellis, J. A. The Emery-Dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane J. Cell Sci. 1999, 112 (Pt 15) 2571-82 (Pubitemid 29401680)
    • (1999) Journal of Cell Science , vol.112 , Issue.15 , pp. 2571-2582
    • Fairley, E.A.L.1    Kendrick-Jones, J.2    Ellis, J.A.3
  • 73
    • 0037447893 scopus 로고    scopus 로고
    • Effects of expressing lamin A mutant protein causing Emery-Dreifuss muscular dystrophy and familial partial lipodystrophy in HeLa cells
    • DOI 10.1016/S0014-4827(03)00104-6
    • Bechert, K.; Lagos-Quintana, M.; Harborth, J.; Weber, K.; Osborn, M. Effects of expressing lamin A mutant protein causing Emery-Dreifuss muscular dystrophy and familial partial lipodystrophy in HeLa cells Exp. Cell Res. 2003, 286 (1) 75-86 (Pubitemid 36506860)
    • (2003) Experimental Cell Research , vol.286 , Issue.1 , pp. 75-86
    • Bechert, K.1    Lagos-Quintana, M.2    Harborth, J.3    Weber, K.4    Osborn, M.5
  • 76
    • 50249147874 scopus 로고    scopus 로고
    • Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation
    • Shao, J.; Welch, W. J.; Diprospero, N. A.; Diamond, M. I. Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation Mol. Cell. Biol. 2008, 28 (17) 5196-208
    • (2008) Mol. Cell. Biol. , vol.28 , Issue.17 , pp. 5196-208
    • Shao, J.1    Welch, W.J.2    Diprospero, N.A.3    Diamond, M.I.4


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