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Volumn 5, Issue 12, 2010, Pages

Niclosamide prevents the formation of large ubiquitin-containing aggregates caused by proteasome inhibition

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; NICLOSAMIDE; PROTEASOME; PROTEIN P62; RAPAMYCIN; ANTINEMATODAL AGENT; GREEN FLUORESCENT PROTEIN; MTORC1 COMPLEX, HUMAN; PROTEIN; UBIQUITIN;

EID: 78650819064     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0014410     Document Type: Article
Times cited : (21)

References (62)
  • 1
    • 50149086108 scopus 로고    scopus 로고
    • Diversity of degradation signals in the ubiquitin-proteasome system
    • Ravid T, Hochstrasser M (2008) Diversity of degradation signals in the ubiquitin-proteasome system. Nat Rev Mol Cell Biol 9: 679-690.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 679-690
    • Ravid, T.1    Hochstrasser, M.2
  • 2
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert U, Anton LC, Gibbs J, Norbury CC, Yewdell JW, et al. (2000) Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404: 770-774.
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5
  • 3
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • Pickart CM, Eddins MJ (2004) Ubiquitin: structures, functions, mechanisms. Biochim Biophys Acta 1695: 55-72.
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 5
    • 33847705665 scopus 로고    scopus 로고
    • Role of ubiquitin- and Ubl-binding proteins in cell signaling
    • Kirkin V, Dikic I (2007) Role of ubiquitin- and Ubl-binding proteins in cell signaling. Curr Opin Cell Biol 19: 199-205.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 199-205
    • Kirkin, V.1    Dikic, I.2
  • 6
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu P, Duong DM, Seyfried NT, Cheng D, Xie Y, et al. (2009) Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 137: 133-145.
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3    Cheng, D.4    Xie, Y.5
  • 7
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau V, Tobias JW, Bachmair A, Marriott D, Ecker DJ, et al. (1989) A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243: 1576-1583.
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5
  • 8
    • 33847188168 scopus 로고    scopus 로고
    • Mechanisms of disease II: Cellular protein quality control
    • Outeiro TF, Tetzlaff J (2007) Mechanisms of disease II: cellular protein quality control. Semin Pediatr Neurol 14: 15-25.
    • (2007) Semin Pediatr Neurol , vol.14 , pp. 15-25
    • Outeiro, T.F.1    Tetzlaff, J.2
  • 9
    • 49549096453 scopus 로고    scopus 로고
    • Polyglutamine gene function and dysfunction in the ageing brain
    • Hands S, Sinadinos C, Wyttenbach A (2008) Polyglutamine gene function and dysfunction in the ageing brain. Biochim Biophys Acta 1779: 507-521.
    • (2008) Biochim Biophys Acta , vol.1779 , pp. 507-521
    • Hands, S.1    Sinadinos, C.2    Wyttenbach, A.3
  • 10
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl FU, Hayer-Hartl M (2009) Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol 16: 574-581.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 11
    • 0034646426 scopus 로고    scopus 로고
    • Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease
    • Wyttenbach A, Carmichael J, Swartz J, Furlong RA, Narain Y, et al. (2000) Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease. Proc Natl Acad Sci U S A 97: 2898-2903.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 2898-2903
    • Wyttenbach, A.1    Carmichael, J.2    Swartz, J.3    Furlong, R.A.4    Narain, Y.5
  • 12
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito RR (2000) Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 10: 524-530.
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 14
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431: 805-810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 15
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • Lansbury PT, Lashuel HA (2006) A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 443: 774-779.
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 16
    • 33745816760 scopus 로고    scopus 로고
    • Protein degradation by the ubiquitin-proteasome pathway in normal and disease states
    • Lecker SH, Goldberg AL, Mitch WE (2006) Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. J Am Soc Nephrol 17: 1807-1819.
    • (2006) J Am Soc Nephrol , vol.17 , pp. 1807-1819
    • Lecker, S.H.1    Goldberg, A.L.2    Mitch, W.E.3
  • 17
    • 68349108020 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neuropathology
    • Lehman NL (2009) The ubiquitin proteasome system in neuropathology. Acta Neuropathol 118: 329-347.
    • (2009) Acta Neuropathol , vol.118 , pp. 329-347
    • Lehman, N.L.1
  • 18
    • 0034884622 scopus 로고    scopus 로고
    • Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein-immunoreactive inclusions in PC12 cells
    • Rideout HJ, Larsen KE, Sulzer D, Stefanis L (2001) Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein-immunoreactive inclusions in PC12 cells. J Neurochem 78: 899-908.
    • (2001) J Neurochem , vol.78 , pp. 899-908
    • Rideout, H.J.1    Larsen, K.E.2    Sulzer, D.3    Stefanis, L.4
  • 19
    • 33747165263 scopus 로고    scopus 로고
    • Proteasome inhibitor MG-132 induces dopaminergic degeneration in cell culture and animal models
    • Sun F, Anantharam V, Zhang D, Latchoumycandane C, Kanthasamy A, et al. (2006) Proteasome inhibitor MG-132 induces dopaminergic degeneration in cell culture and animal models. Neurotoxicology 27: 807-815.
    • (2006) Neurotoxicology , vol.27 , pp. 807-815
    • Sun, F.1    Anantharam, V.2    Zhang, D.3    Latchoumycandane, C.4    Kanthasamy, A.5
  • 20
    • 3042794162 scopus 로고    scopus 로고
    • Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease
    • McNaught KS, Perl DP, Brownell AL, Olanow CW (2004) Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease. Ann Neurol 56: 149-162.
    • (2004) Ann Neurol , vol.56 , pp. 149-162
    • McNaught, K.S.1    Perl, D.P.2    Brownell, A.L.3    Olanow, C.W.4
  • 21
    • 33746851548 scopus 로고    scopus 로고
    • Reproducible nigral cell loss after systemic proteasomal inhibitor administration to rats
    • Zeng BY, Bukhatwa S, Hikima A, Rose S, Jenner P (2006) Reproducible nigral cell loss after systemic proteasomal inhibitor administration to rats. Ann Neurol 60: 248-252.
    • (2006) Ann Neurol , vol.60 , pp. 248-252
    • Zeng, B.Y.1    Bukhatwa, S.2    Hikima, A.3    Rose, S.4    Jenner, P.5
  • 22
    • 0035859226 scopus 로고    scopus 로고
    • Alpha-synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons
    • McLean PJ, Kawamata H, Hyman BT (2001) Alpha-synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons. Neuroscience 104: 901-912.
    • (2001) Neuroscience , vol.104 , pp. 901-912
    • McLean, P.J.1    Kawamata, H.2    Hyman, B.T.3
  • 23
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N, Levine B, Cuervo AM, Klionsky DJ (2008) Autophagy fights disease through cellular self-digestion. Nature 451: 1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 24
    • 77950487987 scopus 로고    scopus 로고
    • Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems
    • Korolchuk VI, Menzies FM, Rubinsztein DC (2010) Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems. FEBS Lett 584: 1393-1398.
    • (2010) FEBS Lett , vol.584 , pp. 1393-1398
    • Korolchuk, V.I.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 25
    • 42249106042 scopus 로고    scopus 로고
    • Novel targets for Huntington's disease in an mTOR-independent autophagy pathway
    • Williams A, Sarkar S, Cuddon P, Ttofi EK, Saiki S, et al. (2008) Novel targets for Huntington's disease in an mTOR-independent autophagy pathway. Nat Chem Biol 4: 295-305.
    • (2008) Nat Chem Biol , vol.4 , pp. 295-305
    • Williams, A.1    Sarkar, S.2    Cuddon, P.3    Ttofi, E.K.4    Saiki, S.5
  • 26
    • 34248994604 scopus 로고    scopus 로고
    • Small molecules enhance autophagy and reduce toxicity in Huntington's disease models
    • Sarkar S, Perlstein EO, Imarisio S, Pineau S, Cordenier A, et al. (2007) Small molecules enhance autophagy and reduce toxicity in Huntington's disease models. Nat Chem Biol 3: 331-338.
    • (2007) Nat Chem Biol , vol.3 , pp. 331-338
    • Sarkar, S.1    Perlstein, E.O.2    Imarisio, S.3    Pineau, S.4    Cordenier, A.5
  • 27
    • 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 (2010) 17- AAG induces cytoplasmic alpha-synuclein aggregate clearance by induction of autophagy. PLoS One 5: e8753.
    • (2010) PLoS One , vol.5
    • Riedel, M.1    Goldbaum, O.2    Schwarz, L.3    Schmitt, S.4    Richter-Landsberg, C.5
  • 28
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin V, McEwan DG, Novak I, Dikic I (2009) A role for ubiquitin in selective autophagy. Mol Cell 34: 259-269.
    • (2009) Mol Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 29
    • 56449094841 scopus 로고    scopus 로고
    • Autophagy and the ubiquitinproteasome system: Collaborators in neuroprotection
    • Nedelsky NB, Todd PK, Taylor JP (2008) Autophagy and the ubiquitinproteasome system: collaborators in neuroprotection. Biochim Biophys Acta 1782: 691-699.
    • (2008) Biochim Biophys Acta , vol.1782 , pp. 691-699
    • Nedelsky, N.B.1    Todd, P.K.2    Taylor, J.P.3
  • 30
    • 38949162988 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitin potentially partners with p62 to promote the clearance of protein inclusions by autophagy
    • Tan JM, Wong ES, Dawson VL, Dawson TM, Lim KL (2007) Lysine 63-linked polyubiquitin potentially partners with p62 to promote the clearance of protein inclusions by autophagy. Autophagy 4.
    • (2007) Autophagy , pp. 4
    • Tan, J.M.1    Wong, E.S.2    Dawson, V.L.3    Dawson, T.M.4    Lim, K.L.5
  • 31
    • 38349114036 scopus 로고    scopus 로고
    • Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases
    • Tan JM, Wong ES, Kirkpatrick DS, Pletnikova O, Ko HS, et al. (2008) Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases. Hum Mol Genet 17: 431-439.
    • (2008) Hum Mol Genet , vol.17 , pp. 431-439
    • Tan, J.M.1    Wong, E.S.2    Kirkpatrick, D.S.3    Pletnikova, O.4    Ko, H.S.5
  • 32
    • 33645731673 scopus 로고    scopus 로고
    • A dynamic ubiquitin equilibrium couples proteasomal activity to chromatin remodeling
    • Dantuma NP, Groothuis TA, Salomons FA, Neefjes J (2006) A dynamic ubiquitin equilibrium couples proteasomal activity to chromatin remodeling. J Cell Biol 173: 19-26.
    • (2006) J Cell Biol , vol.173 , pp. 19-26
    • Dantuma, N.P.1    Groothuis, T.A.2    Salomons, F.A.3    Neefjes, J.4
  • 33
    • 0033517032 scopus 로고    scopus 로고
    • Total synthesis of the potent proteasome inhibitor epoxomicin: A useful tool for understanding proteasome biology
    • Sin N, Kim KB, Elofsson M, Meng L, Auth H, et al. (1999) Total synthesis of the potent proteasome inhibitor epoxomicin: a useful tool for understanding proteasome biology. Bioorg Med Chem Lett 9: 2283-2288.
    • (1999) Bioorg Med Chem Lett , vol.9 , pp. 2283-2288
    • Sin, N.1    Kim, K.B.2    Elofsson, M.3    Meng, L.4    Auth, H.5
  • 34
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee DH, Goldberg AL (1998) Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol 8: 397-403.
    • (1998) Trends Cell Biol , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 35
    • 0036798685 scopus 로고    scopus 로고
    • Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components
    • Stenoien DL, Mielke M, Mancini MA (2002) Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components. Nat Cell Biol 4: 806-810.
    • (2002) Nat Cell Biol , vol.4 , pp. 806-810
    • Stenoien, D.L.1    Mielke, M.2    Mancini, M.A.3
  • 37
    • 34548851476 scopus 로고    scopus 로고
    • Parkinmediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6
    • Olzmann JA, Li L, Chudaev MV, Chen J, Perez FA, et al. (2007) Parkinmediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6. J Cell Biol 178: 1025-1038.
    • (2007) J Cell Biol , vol.178 , pp. 1025-1038
    • Olzmann, J.A.1    Li, L.2    Chudaev, M.V.3    Chen, J.4    Perez, F.A.5
  • 38
    • 34347260686 scopus 로고    scopus 로고
    • Assembly of lysine 63-linked ubiquitin conjugates by phosphorylated alpha-synuclein implies Lewy body biogenesis
    • Liu C, Fei E, Jia N, Wang H, Tao R, et al. (2007) Assembly of lysine 63-linked ubiquitin conjugates by phosphorylated alpha-synuclein implies Lewy body biogenesis. J Biol Chem 282: 14558-14566.
    • (2007) J Biol Chem , vol.282 , pp. 14558-14566
    • Liu, C.1    Fei, E.2    Jia, N.3    Wang, H.4    Tao, R.5
  • 39
    • 70350571135 scopus 로고    scopus 로고
    • On and around microtubules: An overview
    • Wade RH (2009) On and around microtubules: an overview. Mol Biotechnol 43: 177-191.
    • (2009) Mol Biotechnol , vol.43 , pp. 177-191
    • Wade, R.H.1
  • 40
    • 45949106557 scopus 로고    scopus 로고
    • The cytoskeleton in oligodendrocytes. Microtubule dynamics in health and disease
    • Richter-Landsberg C (2008) The cytoskeleton in oligodendrocytes. Microtubule dynamics in health and disease. J Mol Neurosci 35: 55-63.
    • (2008) J Mol Neurosci , vol.35 , pp. 55-63
    • Richter-Landsberg, C.1
  • 42
  • 43
    • 70349616273 scopus 로고    scopus 로고
    • Screen for chemical modulators of autophagy reveals novel therapeutic inhibitors of mTORC1 signaling
    • Balgi AD, Fonseca BD, Donohue E, Tsang TC, Lajoie P, et al. (2009) Screen for chemical modulators of autophagy reveals novel therapeutic inhibitors of mTORC1 signaling. PLoS One 4: e7124.
    • (2009) PLoS One , vol.4
    • Balgi, A.D.1    Fonseca, B.D.2    Donohue, E.3    Tsang, T.C.4    Lajoie, P.5
  • 44
    • 69449102545 scopus 로고    scopus 로고
    • A novel method for oral delivery of apolipoprotein mimetic peptides synthesized from all L-amino acids
    • Navab M, Ruchala P, Waring AJ, Lehrer RI, Hama S, et al. (2009) A novel method for oral delivery of apolipoprotein mimetic peptides synthesized from all L-amino acids. J Lipid Res 50: 1538-1547.
    • (2009) J Lipid Res , vol.50 , pp. 1538-1547
    • Navab, M.1    Ruchala, P.2    Waring, A.J.3    Lehrer, R.I.4    Hama, S.5
  • 45
    • 0017909527 scopus 로고
    • Chemotherapy of human intestinal parasitic diseases
    • Botero D (1978) Chemotherapy of human intestinal parasitic diseases. Annu Rev Pharmacol Toxicol 18: 1-15.
    • (1978) Annu Rev Pharmacol Toxicol , vol.18 , pp. 1-15
    • Botero, D.1
  • 47
    • 0342871691 scopus 로고    scopus 로고
    • Rapid deubiquitination of nucleosomal histones in human tumor cells caused by proteasome inhibitors and stress response inducers: Effects on replication, transcription, translation, and the cellular stress response
    • Mimnaugh EG, Chen HY, Davie JR, Celis JE, Neckers L (1997) Rapid deubiquitination of nucleosomal histones in human tumor cells caused by proteasome inhibitors and stress response inducers: effects on replication, transcription, translation, and the cellular stress response. Biochemistry 36: 14418-14429.
    • (1997) Biochemistry , vol.36 , pp. 14418-14429
    • Mimnaugh, E.G.1    Chen, H.Y.2    Davie, J.R.3    Celis, J.E.4    Neckers, L.5
  • 48
    • 0023576902 scopus 로고
    • Translocation and clustering of endosomes and lysosomes depends on microtubules
    • Matteoni R, Kreis TE (1987) Translocation and clustering of endosomes and lysosomes depends on microtubules. J Cell Biol 105: 1253-1265.
    • (1987) J Cell Biol , vol.105 , pp. 1253-1265
    • Matteoni, R.1    Kreis, T.E.2
  • 49
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • Iwata A, Riley BE, Johnston JA, Kopito RR (2005) HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J Biol Chem 280: 40282-40292.
    • (2005) J Biol Chem , vol.280 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 50
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger S, Loewith R, Hall MN (2006) TOR signaling in growth and metabolism. Cell 124: 471-484.
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 51
    • 35448938087 scopus 로고    scopus 로고
    • Essential role for autophagy protein Atg7 in the maintenance of axonal homeostasis and the prevention of axonal degeneration
    • Komatsu M, Wang QJ, Holstein GR, Friedrich VL, Jr., Iwata J, et al. (2007) Essential role for autophagy protein Atg7 in the maintenance of axonal homeostasis and the prevention of axonal degeneration. Proc Natl Acad Sci U S A 104: 14489-14494.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 14489-14494
    • Komatsu, M.1    Wang, Q.J.2    Holstein, G.R.3    Friedrich Jr., V.L.4    Iwata, J.5
  • 52
    • 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 (2001) Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells. Biochem Biophys Res Commun 280: 223-228.
    • (2001) Biochem Biophys Res Commun , vol.280 , pp. 223-228
    • Kuusisto, E.1    Suuronen, T.2    Salminen, A.3
  • 53
    • 43049138051 scopus 로고    scopus 로고
    • Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
    • Kraft C, Deplazes A, Sohrmann M, Peter M (2008) Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat Cell Biol 10: 602-610.
    • (2008) Nat Cell Biol , vol.10 , pp. 602-610
    • Kraft, C.1    Deplazes, A.2    Sohrmann, M.3    Peter, M.4
  • 54
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D, Tanaka A, Suen DF, Youle RJ (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 183: 795-803.
    • (2008) J Cell Biol , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 55
    • 38549110110 scopus 로고    scopus 로고
    • Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
    • Twig G, Elorza A, Molina AJ, Mohamed H, Wikstrom JD, et al. (2008) Fission and selective fusion govern mitochondrial segregation and elimination by autophagy. Embo J 27: 433-446.
    • (2008) Embo J , vol.27 , pp. 433-446
    • Twig, G.1    Elorza, A.2    Molina, A.J.3    Mohamed, H.4    Wikstrom, J.D.5
  • 57
    • 36749080327 scopus 로고    scopus 로고
    • Quantitative profiling of ubiquitylated proteins reveals proteasome substrates and the substrate repertoire influenced by the Rpn10 receptor pathway
    • Mayor T, Graumann J, Bryan J, MacCoss MJ, Deshaies RJ (2007) Quantitative profiling of ubiquitylated proteins reveals proteasome substrates and the substrate repertoire influenced by the Rpn10 receptor pathway. Mol Cell Proteomics 6: 1885-1895.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1885-1895
    • Mayor, T.1    Graumann, J.2    Bryan, J.3    McCoss, M.J.4    Deshaies, R.J.5
  • 58
    • 34547807613 scopus 로고    scopus 로고
    • Global changes to the ubiquitin system in Huntington's disease
    • Bennett EJ, Shaler TA, Woodman B, Ryu KY, Zaitseva TS, et al. (2007) Global changes to the ubiquitin system in Huntington's disease. Nature 448: 704-708.
    • (2007) Nature , vol.448 , pp. 704-708
    • Bennett, E.J.1    Shaler, T.A.2    Woodman, B.3    Ryu, K.Y.4    Zaitseva, T.S.5
  • 59
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitinproteasome system by protein aggregation
    • Bence NF, Sampat RM, Kopito RR (2001) Impairment of the ubiquitinproteasome system by protein aggregation. Science 292: 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 61
    • 65549145048 scopus 로고    scopus 로고
    • An ATPcompetitive mammalian target of rapamycin inhibitor reveals rapamycinresistant functions of mTORC1
    • Thoreen CC, Kang SA, Chang JW, Liu Q, Zhang J, et al. (2009) An ATPcompetitive mammalian target of rapamycin inhibitor reveals rapamycinresistant functions of mTORC1. J Biol Chem 284: 8023-8032.
    • (2009) J Biol Chem , vol.284 , pp. 8023-8032
    • Thoreen, C.C.1    Kang, S.A.2    Chang, J.W.3    Liu, Q.4    Zhang, J.5
  • 62
    • 20044386298 scopus 로고    scopus 로고
    • Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: Implications for Lewy body formation
    • Lim KL, Chew KC, Tan JM, Wang C, Chung KK, et al. (2005) Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation. J Neurosci 25: 2002-2009.
    • (2005) J Neurosci , vol.25 , pp. 2002-2009
    • Lim, K.L.1    Chew, K.C.2    Tan, J.M.3    Wang, C.4    Chung, K.K.5


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