메뉴 건너뛰기




Volumn 300, Issue , 2006, Pages 57-93

The role of the ubiquitination machinery in dislocation and degradation of endoplasmic reticulum proteins

Author keywords

[No Author keywords available]

Indexed keywords

UBIQUITIN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE;

EID: 30344434334     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Review
Times cited : (6)

References (198)
  • 1
    • 0028861418 scopus 로고
    • The PHD finger: Implications for chromatin-mediated transcriptional regulation
    • Aasland R, Gibson TJ, Stewart AF (1995) The PHD finger: implications for chromatin-mediated transcriptional regulation. Trends Biochem Sci 20:56-59
    • (1995) Trends Biochem Sci , vol.20 , pp. 56-59
    • Aasland, R.1    Gibson, T.J.2    Stewart, A.F.3
  • 2
    • 0037195907 scopus 로고    scopus 로고
    • Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome
    • Alberti S, Demand J, Esser C, Emmerich N, Schild H, Hohfeld J (2002) Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome. J Biol Chem 277:45920-45927
    • (2002) J Biol Chem , vol.277 , pp. 45920-45927
    • Alberti, S.1    Demand, J.2    Esser, C.3    Emmerich, N.4    Schild, H.5    Hohfeld, J.6
  • 5
    • 0037972167 scopus 로고    scopus 로고
    • Scores of RINGS but no PHDs in ubiquitin signaling
    • Aravind L, Iyer LM, Koonin EV (2003) Scores of RINGS but no PHDs in ubiquitin signaling. Cell Cycle 2:123-126
    • (2003) Cell Cycle , vol.2 , pp. 123-126
    • Aravind, L.1    Iyer, L.M.2    Koonin, E.V.3
  • 6
    • 0034708216 scopus 로고    scopus 로고
    • The U box is a modified RING finger - A common domain in ubiquitination
    • Aravind L, Koonin EV (2000) The U box is a modified RING finger - a common domain in ubiquitination. Curr Biol 10:R132-R134
    • (2000) Curr Biol , vol.10
    • Aravind, L.1    Koonin, E.V.2
  • 7
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY, Patterson C (1999) Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol Cell Biol 19:4535-4545
    • (1999) Mol Cell Biol , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7
  • 8
    • 0346373729 scopus 로고    scopus 로고
    • Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins
    • Bartee E, Mansouri M, Hovey Nerenberg BT, Gouveia K, Fruh K (2004) Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins. J Virol 78:1109-1120
    • (2004) J Virol , vol.78 , pp. 1109-1120
    • Bartee, E.1    Mansouri, M.2    Hovey Nerenberg, B.T.3    Gouveia, K.4    Fruh, K.5
  • 9
    • 0035144199 scopus 로고    scopus 로고
    • Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation
    • Bays NW, Gardner RG, Seelig LP, Joazeiro CA, Hampton RY (2001) Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat Cell Biol 3:24-29
    • (2001) Nat Cell Biol , vol.3 , pp. 24-29
    • Bays, N.W.1    Gardner, R.G.2    Seelig, L.P.3    Joazeiro, C.A.4    Hampton, R.Y.5
  • 10
    • 0029985369 scopus 로고    scopus 로고
    • Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway
    • Biederer T, Volkwein C, Sommer T (1996) Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO J 15:2069-2076
    • (1996) EMBO J , vol.15 , pp. 2069-2076
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 11
    • 0030666729 scopus 로고    scopus 로고
    • Role of Cue1p in ubiquitination and degradation at the ER surface
    • Biederer T, Volkwein C, Sommer T (1997) Role of Cue1p in ubiquitination and degradation at the ER surface. Science 278:1806-1809
    • (1997) Science , vol.278 , pp. 1806-1809
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 13
    • 1442313919 scopus 로고    scopus 로고
    • A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised
    • Blom D, Hirsch C, Stern P, Tortorella D, Ploegh HL (2004) A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised. EMBO J 23:650-658
    • (2004) EMBO J , vol.23 , pp. 650-658
    • Blom, D.1    Hirsch, C.2    Stern, P.3    Tortorella, D.4    Ploegh, H.L.5
  • 14
    • 0031885043 scopus 로고    scopus 로고
    • Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins
    • Bordallo J, Plemper RK, Finger A, Wolf DH (1998) Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins. Mol Biol Cell 9:209-222
    • (1998) Mol Biol Cell , vol.9 , pp. 209-222
    • Bordallo, J.1    Plemper, R.K.2    Finger, A.3    Wolf, D.H.4
  • 15
    • 0032960581 scopus 로고    scopus 로고
    • A RING-H2 finger motif is essential for the function of Der3/Hrd1 in endoplasmic reticulum associated protein degradation in the yeast Saccharomyces cerevisiae
    • Bordallo J, Wolf DH (1999) A RING-H2 finger motif is essential for the function of Der3/Hrd1 in endoplasmic reticulum associated protein degradation in the yeast Saccharomyces cerevisiae. FEBS Lett 448:244-248
    • (1999) FEBS Lett , vol.448 , pp. 244-248
    • Bordallo, J.1    Wolf, D.H.2
  • 16
    • 0036715341 scopus 로고    scopus 로고
    • Ubc6p and ubc7p are required for normal and substrate-induced endoplasmic reticulum-associated degradation of the human selenoprotein type 2 iodothyronine monodeiodinase
    • Bolero D, Gereben B, Goncalves C, De Jesus LA, Harney JW, Bianco AC (2002) Ubc6p and ubc7p are required for normal and substrate-induced endoplasmic reticulum-associated degradation of the human selenoprotein type 2 iodothyronine monodeiodinase. Mol Endocrinol 16:1999-2007
    • (2002) Mol Endocrinol , vol.16 , pp. 1999-2007
    • Bolero, D.1    Gereben, B.2    Goncalves, C.3    De Jesus, L.A.4    Harney, J.W.5    Bianco, A.C.6
  • 17
    • 0035844173 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCP-mediated degradation of Ikappa B
    • Bour S, Perrin C, Akari H, Strebel K (2001) The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCP-mediated degradation of Ikappa B. J Biol Chem 276:15920-15928
    • (2001) J Biol Chem , vol.276 , pp. 15920-15928
    • Bour, S.1    Perrin, C.2    Akari, H.3    Strebel, K.4
  • 18
    • 3943102116 scopus 로고    scopus 로고
    • Unraveling the mechanisms involved in motor neuron degeneration in ALS
    • Bruijn LI, Miller TM, Cleveland DW (2004) Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu Rev Neurosci 27:723-749
    • (2004) Annu Rev Neurosci , vol.27 , pp. 723-749
    • Bruijn, L.I.1    Miller, T.M.2    Cleveland, D.W.3
  • 20
    • 0347948145 scopus 로고    scopus 로고
    • Identification of a region within SEL1L protein required for tumour growth inhibition
    • Cattaneo M, Canton C, Albertini A, Biunno I (2004) Identification of a region within SEL1L protein required for tumour growth inhibition. Gene 326:149-156
    • (2004) Gene , vol.326 , pp. 149-156
    • Cattaneo, M.1    Canton, C.2    Albertini, A.3    Biunno, I.4
  • 25
    • 0034617224 scopus 로고    scopus 로고
    • Rsp5 WW domains interact directly with the carboxyl-terminal domain of RNA polymerase II
    • Chang A, Cheang S, Espanel X, Sudol M (2000) Rsp5 WW domains interact directly with the carboxyl-terminal domain of RNA polymerase II. J Biol Chem 275:20562-20571
    • (2000) J Biol Chem , vol.275 , pp. 20562-20571
    • Chang, A.1    Cheang, S.2    Espanel, X.3    Sudol, M.4
  • 26
    • 0036277299 scopus 로고    scopus 로고
    • Rad23 promotes the targeting of proteolytic substrates to the proteasome
    • Chen L, Madura K (2002) Rad23 promotes the targeting of proteolytic substrates to the proteasome. Mol Cell Biol 22:4902-4913
    • (2002) Mol Cell Biol , vol.22 , pp. 4902-4913
    • Chen, L.1    Madura, K.2
  • 27
    • 0034776095 scopus 로고    scopus 로고
    • Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: Implications for Lewy-body formation in Parkinson disease
    • Chung KK, Zhang Y, Lim KL, Tanaka Y, Huang H, Gao J, Ross CA, Dawson VL, Dawson TM (2001) Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. Nat Med 7:1144-1150
    • (2001) Nat Med , vol.7 , pp. 1144-1150
    • Chung, K.K.1    Zhang, Y.2    Lim, K.L.3    Tanaka, Y.4    Huang, H.5    Gao, J.6    Ross, C.A.7    Dawson, V.L.8    Dawson, T.M.9
  • 30
    • 0034608951 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus encodes two proteins that block cell surface display of MHC class I chains by enhancing their endocytosis
    • Coscoy L, Ganem D (2000) Kaposi's sarcoma-associated herpesvirus encodes two proteins that block cell surface display of MHC class I chains by enhancing their endocytosis. Proc Natl Acad Sci U S A 97:8051-8056
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8051-8056
    • Coscoy, L.1    Ganem, D.2
  • 31
    • 0034971266 scopus 로고    scopus 로고
    • A viral protein that selectively downregulates ICAM-1 and B7-2 and modulates T cell costimulation
    • Coscoy L, Ganem D (2001) A viral protein that selectively downregulates ICAM-1 and B7-2 and modulates T cell costimulation. J Clin Invest 107:1599-1606
    • (2001) J Clin Invest , vol.107 , pp. 1599-1606
    • Coscoy, L.1    Ganem, D.2
  • 32
    • 0035945349 scopus 로고    scopus 로고
    • A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition
    • Coscoy L, Sanchez DJ, Ganem D (2001) A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition. J Cell Biol 155:1265-1273
    • (2001) J Cell Biol , vol.155 , pp. 1265-1273
    • Coscoy, L.1    Sanchez, D.J.2    Ganem, D.3
  • 33
    • 0032540384 scopus 로고    scopus 로고
    • Ubiquitination is required for the retrotranslocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome
    • De Virgilio M, Weninger H, Ivessa NE (1998) Ubiquitination is required for the retrotranslocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome. J Biol Chem 273:9734-9743
    • (1998) J Biol Chem , vol.273 , pp. 9734-9743
    • De Virgilio, M.1    Weninger, H.2    Ivessa, N.E.3
  • 34
    • 0035815754 scopus 로고    scopus 로고
    • Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation
    • Deak PM, Wolf DH (2001) Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation. J Biol Chem 276:10663-10669
    • (2001) J Biol Chem , vol.276 , pp. 10663-10669
    • Deak, P.M.1    Wolf, D.H.2
  • 35
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
    • Demand J, Alberti S, Patterson C, Hohfeld J (2001) Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr Biol 11:1569-1577
    • (2001) Curr Biol , vol.11 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 37
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies RJ (1999) SCF and Cullin/Ring H2-based ubiquitin ligases. Annu Rev Cell Dev Biol 15:435-467
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 38
    • 1042278180 scopus 로고    scopus 로고
    • Distinct steps in dislocation of luminal endoplasmic reticulum-associated degradation substrates: Roles of endoplasmic reticulum-bound p97/Cdc48p and proteasome
    • Elkabetz Y, Shapira I, Rabinovich E, Bar-Nun S (2004) Distinct steps in dislocation of luminal endoplasmic reticulum-associated degradation substrates: roles of endoplasmic reticulum-bound p97/Cdc48p and proteasome. J Biol Chem 279:3980-3989
    • (2004) J Biol Chem , vol.279 , pp. 3980-3989
    • Elkabetz, Y.1    Shapira, I.2    Rabinovich, E.3    Bar-Nun, S.4
  • 39
    • 3042677641 scopus 로고    scopus 로고
    • Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome
    • Elsasser S, Chandler-Militello D, Muller B, Hanna J, Finley D (2004) Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. J Biol Chem 279:26817-26822
    • (2004) J Biol Chem , vol.279 , pp. 26817-26822
    • Elsasser, S.1    Chandler-Militello, D.2    Muller, B.3    Hanna, J.4    Finley, D.5
  • 40
    • 0035807839 scopus 로고    scopus 로고
    • The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum
    • Fang S, Ferrone M, Yang C, Jensen JP, Tiwari S, Weissman AM (2001) The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc Natl Acad Sci U S A 98:14422-14427
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14422-14427
    • Fang, S.1    Ferrone, M.2    Yang, C.3    Jensen, J.P.4    Tiwari, S.5    Weissman, A.M.6
  • 41
    • 3242671372 scopus 로고    scopus 로고
    • A field guide to ubiquitylation
    • Fang S, Weissman AM (2004) A field guide to ubiquitylation. Cell Mol Life Sci 61:1546-1561
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1546-1561
    • Fang, S.1    Weissman, A.M.2
  • 42
    • 0038121031 scopus 로고    scopus 로고
    • The cellular protein level of Parkin is regulated by its ubiquitin-like domain
    • Finney N, Walther F, Mantel PY, Stauffer D, Rovelli G, Dev KK (2003) The cellular protein level of Parkin is regulated by its ubiquitin-like domain. J Biol Chem 278:16054-16058
    • (2003) J Biol Chem , vol.278 , pp. 16054-16058
    • Finney, N.1    Walther, F.2    Mantel, P.Y.3    Stauffer, D.4    Rovelli, G.5    Dev, K.K.6
  • 43
    • 0033780610 scopus 로고    scopus 로고
    • A regulatory link between ER-associated protein degradation and the unfolded-protein response
    • Friedlander R, Jarosch E, Urban J, Volkwein C, Sommer T (2000) A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat Cell Biol 2:379-384
    • (2000) Nat Cell Biol , vol.2 , pp. 379-384
    • Friedlander, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4    Sommer, T.5
  • 44
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • Galan JM, Moreau V, Andre B, Volland C, Haguenauer-Tsapis R (1996) Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J Biol Chem 271:10946-10952
    • (1996) J Biol Chem , vol.271 , pp. 10946-10952
    • Galan, J.M.1    Moreau, V.2    Andre, B.3    Volland, C.4    Haguenauer-Tsapis, R.5
  • 45
    • 0034971386 scopus 로고    scopus 로고
    • In vivo action of the HRD ubiquitin ligase complex: Mechanisms of endoplasmic reticulum quality control and sterol regulation
    • Gardner RG, Shearer AG, Hampton RY (2001) In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation. Mol Cell Biol 21:4276-4291
    • (2001) Mol Cell Biol , vol.21 , pp. 4276-4291
    • Gardner, R.G.1    Shearer, A.G.2    Hampton, R.Y.3
  • 48
    • 4344560565 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast
    • Gnann A, Riordan JR, Wolf DH (2004) Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast. Mol Biol Cell 15:4125-4135
    • (2004) Mol Biol Cell , vol.15 , pp. 4125-4135
    • Gnann, A.1    Riordan, J.R.2    Wolf, D.H.3
  • 51
    • 0036437316 scopus 로고    scopus 로고
    • Proteolysis and sterol regulation
    • Hampton RY (2002) Proteolysis and sterol regulation. Annu Rev Cell Dev Biol 18:345-378
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 345-378
    • Hampton, R.Y.1
  • 52
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • Hampton RY, Gardner RG, Rine J (1996) Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol Biol Cell 7:2029-2044
    • (1996) Mol Biol Cell , vol.7 , pp. 2029-2044
    • Hampton, R.Y.1    Gardner, R.G.2    Rine, J.3
  • 53
    • 0027550821 scopus 로고
    • The cystic fibrosis gene and its product CFTR
    • Harris A, Argent BE (1993) The cystic fibrosis gene and its product CFTR. Semin Cell Biol 4:37-44
    • (1993) Semin Cell Biol , vol.4 , pp. 37-44
    • Harris, A.1    Argent, B.E.2
  • 56
    • 5444239863 scopus 로고    scopus 로고
    • U-box protein carboxyl terminus of Hsc70- Interacting protein (CHIP) mediates poly-ubiquitylation preferentially on four-repeat Tau and is involved in neurodegeneration of tauopathy
    • Hatakeyama S, Matsumoto M, Kamura T, Murayama M, Chui DH, Planel E, Takahashi R, Nakayama KI, Takashima A (2004a) U-box protein carboxyl terminus of Hsc70- interacting protein (CHIP) mediates poly-ubiquitylation preferentially on four-repeat Tau and is involved in neurodegeneration of tauopathy. J Neurochem 91:299-307
    • (2004) J Neurochem , vol.91 , pp. 299-307
    • Hatakeyama, S.1    Matsumoto, M.2    Kamura, T.3    Murayama, M.4    Chui, D.H.5    Planel, E.6    Takahashi, R.7    Nakayama, K.I.8    Takashima, A.9
  • 57
    • 3042856481 scopus 로고    scopus 로고
    • Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones
    • Hatakeyama S, Matsumoto M, Yada M, Nakayama KI (2004b) Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones. Genes Cells 9:533-548
    • (2004) Genes Cells , vol.9 , pp. 533-548
    • Hatakeyama, S.1    Matsumoto, M.2    Yada, M.3    Nakayama, K.I.4
  • 58
    • 0037043340 scopus 로고    scopus 로고
    • An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport
    • Haynes CM, Caldwell S, Cooper AA (2002) An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport. J Cell Biol 158:91-101
    • (2002) J Cell Biol , vol.158 , pp. 91-101
    • Haynes, C.M.1    Caldwell, S.2    Cooper, A.A.3
  • 59
    • 0028971506 scopus 로고
    • NPl1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase
    • Hein C, Springael JY, Volland C, Haguenauer-Tsapis R, Andre B (1995) NPl1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase. Mol Microbiol 18:77-87
    • (1995) Mol Microbiol , vol.18 , pp. 77-87
    • Hein, C.1    Springael, J.Y.2    Volland, C.3    Haguenauer-Tsapis, R.4    Andre, B.5
  • 62
    • 0037093467 scopus 로고    scopus 로고
    • Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation
    • Hewitt EW, Duncan L, Mufti D, Baker J, Stevenson PG, Lehner PJ (2002) Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation. EMBO J 21:2418-2429
    • (2002) EMBO J , vol.21 , pp. 2418-2429
    • Hewitt, E.W.1    Duncan, L.2    Mufti, D.3    Baker, J.4    Stevenson, P.G.5    Lehner, P.J.6
  • 63
    • 0033106369 scopus 로고    scopus 로고
    • Gettin' down with ubiquitin: Turning off cell-surface receptors, transporters and channels
    • Hicke L (1999) Gettin' down with ubiquitin: turning off cell-surface receptors, transporters and channels. Trends Cell Biol 9:107-112
    • (1999) Trends Cell Biol , vol.9 , pp. 107-112
    • Hicke, L.1
  • 64
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke L, Dunn R (2003) Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 19:141-172
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 65
    • 0034651604 scopus 로고    scopus 로고
    • Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system
    • Hill K, Cooper AA (2000) Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system. EMBO J 19:550-561
    • (2000) EMBO J , vol.19 , pp. 550-561
    • Hill, K.1    Cooper, A.A.2
  • 66
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Killer MM, Finger A, Schweiger M, Wolf DH (1996) ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273:1725-1728
    • (1996) Science , vol.273 , pp. 1725-1728
    • Killer, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 67
    • 0030469819 scopus 로고    scopus 로고
    • Expression of autocrine motility factor receptor correlates with disease progression in human gastric cancer
    • Hirono Y, Fushida S, Yonemura Y, Yamamoto H, Watanabe H, Raz A (1996) Expression of autocrine motility factor receptor correlates with disease progression in human gastric cancer. Br J Cancer 74:2003-2007
    • (1996) Br J Cancer , vol.74 , pp. 2003-2007
    • Hirono, Y.1    Fushida, S.2    Yonemura, Y.3    Yamamoto, H.4    Watanabe, H.5    Raz, A.6
  • 68
    • 0037416196 scopus 로고    scopus 로고
    • A role for N-glycanase in the cytosolic turnover of glycoproteins
    • Hirsch C, Blom D, Ploegh HL (2003) A role for N-glycanase in the cytosolic turnover of glycoproteins. EMBO J 22:1036-1046
    • (2003) EMBO J , vol.22 , pp. 1036-1046
    • Hirsch, C.1    Blom, D.2    Ploegh, H.L.3
  • 69
    • 9644300910 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated protein degradation - One model fits all?
    • Hirsch C, Jarosch E, Sommer T, Wolf DH (2004) Endoplasmic reticulum-associated protein degradation - one model fits all? Biochim Biophys Acta 1695:215-223
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 215-223
    • Hirsch, C.1    Jarosch, E.2    Sommer, T.3    Wolf, D.H.4
  • 70
    • 0242300110 scopus 로고    scopus 로고
    • A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery
    • Hitchcock AL, Auld K, Gygi SP, Silver PA (2003) A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery. Proc Natl Acad Sci U S A 100:12735-12740
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 12735-12740
    • Hitchcock, A.L.1    Auld, K.2    Gygi, S.P.3    Silver, P.A.4
  • 71
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
    • Hoppe T, Matuschewski K, Rape M, Schlenker S, Ulrich HD, Jentsch S (2000) Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102:577-586
    • (2000) Cell , vol.102 , pp. 577-586
    • Hoppe, T.1    Matuschewski, K.2    Rape, M.3    Schlenker, S.4    Ulrich, H.D.5    Jentsch, S.6
  • 73
    • 0141816772 scopus 로고    scopus 로고
    • A nonconserved Ala401 in the yeast Rsp5 ubiquitin ligase is involved in degradation of Gap1 permease and stress-induced abnormal proteins
    • Hoshikawa C, Shichiri M, Nakamori S, Takagi H (2003) A nonconserved Ala401 in the yeast Rsp5 ubiquitin ligase is involved in degradation of Gap1 permease and stress-induced abnormal proteins. Proc Natl Acad Sci U S A 100:11505-11510
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 11505-11510
    • Hoshikawa, C.1    Shichiri, M.2    Nakamori, S.3    Takagi, H.4
  • 74
    • 4744348809 scopus 로고    scopus 로고
    • Notch-induced E2A degradation requires CHIP and Hsc70 as novel facilitators of ubiquitination
    • Huang Z, Nie L, Xu M, Sun XH (2004) Notch-induced E2A degradation requires CHIP and Hsc70 as novel facilitators of ubiquitination. Mol Cell Biol 24:8951-8962
    • (2004) Mol Cell Biol , vol.24 , pp. 8951-8962
    • Huang, Z.1    Nie, L.2    Xu, M.3    Sun, X.H.4
  • 75
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse JM, Scheffner M, Beaudenon S, Howley PM (1995) A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc Natl Acad Sci U S A 92:2563-2567
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 76
    • 0141995596 scopus 로고    scopus 로고
    • The autosomal recessive juvenile Parkinson disease gene product, Parkin, interacts with and ubiquitinates synaptotagmin XI
    • Huynh DP, Scoles DR, Nguyen D, Pulst SM (2003) The autosomal recessive juvenile Parkinson disease gene product, Parkin, interacts with and ubiquitinates synaptotagmin XI. Hum Mol Genet 12:2587-2597
    • (2003) Hum Mol Genet , vol.12 , pp. 2587-2597
    • Huynh, D.P.1    Scoles, D.R.2    Nguyen, D.3    Pulst, S.M.4
  • 77
    • 0036345454 scopus 로고    scopus 로고
    • CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity
    • Imai Y, Soda M, Hatakeyama S, Akagi T, Hashikawa T, Nakayama KI, Takahashi R (2002) CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol Cell 10:55-67
    • (2002) Mol Cell , vol.10 , pp. 55-67
    • Imai, Y.1    Soda, M.2    Hatakeyama, S.3    Akagi, T.4    Hashikawa, T.5    Nakayama, K.I.6    Takahashi, R.7
  • 78
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai Y, Soda M, Inoue H, Hattori N, Mizuno Y, Takahashi R (2001) An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105:891-902
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 79
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • Imai Y, Soda M, Takahashi R (2000) Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J Biol Chem 275:35661-35664
    • (2000) J Biol Chem , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 80
    • 0033667743 scopus 로고    scopus 로고
    • Inhibition of natural killer cell-mediated cytotoxicity by Kaposi's sarcoma-associated herpesvirus K5 protein
    • Ishido S, Choi JK, Lee BS, Wang C, DeMaria M, Johnson RP, Cohen GB, Jung JU (2000a) Inhibition of natural killer cell-mediated cytotoxicity by Kaposi's sarcoma-associated herpesvirus K5 protein. Immunity 13:365-374
    • (2000) Immunity , vol.13 , pp. 365-374
    • Ishido, S.1    Choi, J.K.2    Lee, B.S.3    Wang, C.4    DeMaria, M.5    Johnson, R.P.6    Cohen, G.B.7    Jung, J.U.8
  • 81
    • 0034068631 scopus 로고    scopus 로고
    • Downregulation of major histocompatibility complex class I molecules by Kaposi's sarcoma-associated herpesvirus K3 and K5 proteins
    • Ishido S, Wang C, Lee BS, Cohen GB, Jung JU (2000b) Downregulation of major histocompatibility complex class I molecules by Kaposi's sarcoma-associated herpesvirus K3 and K5 proteins. J Virol 74:5300-5309
    • (2000) J Virol , vol.74 , pp. 5300-5309
    • Ishido, S.1    Wang, C.2    Lee, B.S.3    Cohen, G.B.4    Jung, J.U.5
  • 85
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
    • Jiang J, Ballinger CA, Wu Y, Dai Q, Cyr DM, Hohfeld J, Patterson C (2001) CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J Biol Chem 276:42938-42944
    • (2001) J Biol Chem , vol.276 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Hohfeld, J.6    Patterson, C.7
  • 87
    • 0037021416 scopus 로고    scopus 로고
    • Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
    • Kaneko M, Ishiguro M, Niinuma Y, Uesugi M, Nomura Y (2002) Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation. FEBS Lett 532:147-152
    • (2002) FEBS Lett , vol.532 , pp. 147-152
    • Kaneko, M.1    Ishiguro, M.2    Niinuma, Y.3    Uesugi, M.4    Nomura, Y.5
  • 88
    • 0242321271 scopus 로고    scopus 로고
    • ER signaling in unfolded protein response
    • Kaneko M, Nomura Y (2003) ER signaling in unfolded protein response. Life Sci 74:199-205
    • (2003) Life Sci , vol.74 , pp. 199-205
    • Kaneko, M.1    Nomura, Y.2
  • 89
    • 10944247152 scopus 로고    scopus 로고
    • Protective effects of HRD1 and 4-phenylbutyric acid against neuronal cell death
    • Kaneko M, Nomura Y (2004) Protective effects of HRD1 and 4-phenylbutyric acid against neuronal cell death. Nippon Yakurigaku Zasshi 124:391-398
    • (2004) Nippon Yakurigaku Zasshi , vol.124 , pp. 391-398
    • Kaneko, M.1    Nomura, Y.2
  • 90
    • 4644318292 scopus 로고    scopus 로고
    • A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins
    • Katiyar S, Li G, Lennarz WJ (2004) A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins. Proc Natl Acad Sci U S A 101:13774-13779
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 13774-13779
    • Katiyar, S.1    Li, G.2    Lennarz, W.J.3
  • 91
    • 0742288063 scopus 로고    scopus 로고
    • Multivesicular body sorting: Ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S
    • Katzmann DJ, Sarkar S, Chu T, Audhya A, Emr SD (2004) Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S. Mol Biol Cell 15:468-480
    • (2004) Mol Biol Cell , vol.15 , pp. 468-480
    • Katzmann, D.J.1    Sarkar, S.2    Chu, T.3    Audhya, A.4    Emr, S.D.5
  • 93
    • 0035448296 scopus 로고    scopus 로고
    • Ubiquitination is essential for human cytomegalovirus US11-mediated dislocation of MHC class I molecules from the endoplasmic reticulum to the cytosol
    • Kikkert M, Hassink G, Barel M, Hirsch C, van der Wal FJ, Wiertz E (2001) Ubiquitination is essential for human cytomegalovirus US11-mediated dislocation of MHC class I molecules from the endoplasmic reticulum to the cytosol. Biochem J 358:369-377
    • (2001) Biochem J , vol.358 , pp. 369-377
    • Kikkert, M.1    Hassink, G.2    Barel, M.3    Hirsch, C.4    Van Der Wal, F.J.5    Wiertz, E.6
  • 94
    • 0347480259 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation of the human type 2 iodothyronine deiodinase (D2) is mediated via an association between mammalian UBC7 and the carboxyl region of D2
    • Kim BW, Zavacki AM, Curcio-Morelli C, Dentice M, Harney JW, Larsen PR, Bianco AC (2003) Endoplasmic reticulum-associated degradation of the human type 2 iodothyronine deiodinase (D2) is mediated via an association between mammalian UBC7 and the carboxyl region of D2. Mol Endocrinol 17:2603-2612
    • (2003) Mol Endocrinol , vol.17 , pp. 2603-2612
    • Kim, B.W.1    Zavacki, A.M.2    Curcio-Morelli, C.3    Dentice, M.4    Harney, J.W.5    Larsen, P.R.6    Bianco, A.C.7
  • 95
    • 0034568688 scopus 로고    scopus 로고
    • The F-box protein family
    • REVIEWS3002
    • Kipreos ET, Pagano M (2000) The F-box protein family. Genome Biol 1:REVIEWS3002
    • (2000) Genome Biol , vol.1
    • Kipreos, E.T.1    Pagano, M.2
  • 96
    • 27244462469 scopus 로고    scopus 로고
    • Expression and degradation of the cystic fibrosis transmembrane conductance regulator in Saccharomyces cerevisiae
    • Kiser GL, Gentzsch M, Kloser AK, Balzi E, Wolf DH, Goffeau A, Riordan JR (2001) Expression and degradation of the cystic fibrosis transmembrane conductance regulator in Saccharomyces cerevisiae. Arch Biochem Biophys 390:195-205
    • (2001) Arch Biochem Biophys , vol.390 , pp. 195-205
    • Kiser, G.L.1    Gentzsch, M.2    Kloser, A.K.3    Balzi, E.4    Wolf, D.H.5    Goffeau, A.6    Riordan, J.R.7
  • 98
    • 0034044667 scopus 로고    scopus 로고
    • Molecular cloning, gene expression, and identification of a splicing variant of the mouse Parkin gene
    • Kitada T, Asakawa S, Minoshima S, Mizuno Y, Shimizu N (2000) Molecular cloning, gene expression, and identification of a splicing variant of the mouse Parkin gene. Mamm Genome 11:417-421
    • (2000) Mamm Genome , vol.11 , pp. 417-421
    • Kitada, T.1    Asakawa, S.2    Minoshima, S.3    Mizuno, Y.4    Shimizu, N.5
  • 99
    • 0034693217 scopus 로고    scopus 로고
    • Herp, a newubiquitin-like membrane protein induced by endoplasmic reticulum stress
    • Kokame K, Agarwala KL, Kato H, Miyata T (2000) Herp, a newubiquitin-like membrane protein induced by endoplasmic reticulum stress. J Biol Chem 275:32846-32853
    • (2000) J Biol Chem , vol.275 , pp. 32846-32853
    • Kokame, K.1    Agarwala, K.L.2    Kato, H.3    Miyata, T.4
  • 100
    • 17544404364 scopus 로고    scopus 로고
    • Evaluation and classification of RING-finger domains encoded by the Arabidopsis genome
    • RESEARCH0016
    • Kosarev P, Mayer KF, Hardtke CS (2002) Evaluation and classification of RING-finger domains encoded by the Arabidopsis genome. Genome Biol 3:RESEARCH0016
    • (2002) Genome Biol , vol.3
    • Kosarev, P.1    Mayer, K.F.2    Hardtke, C.S.3
  • 102
    • 0037929972 scopus 로고    scopus 로고
    • Overexpression of the tumor autocrine motility factor receptor Gp78, a ubiquitin protein ligase, results in increased ubiquitinylation and decreased secretion of apolipoprotein B100 in HepG2 cells
    • Liang JS, Kim T, Fang S, Yamaguchi J, Weissman AM, Fisher EA, Ginsberg HN (2003) Overexpression of the tumor autocrine motility factor receptor Gp78, a ubiquitin protein ligase, results in increased ubiquitinylation and decreased secretion of apolipoprotein B100 in HepG2 cells. J Biol Chem 278:23984-23988
    • (2003) J Biol Chem , vol.278 , pp. 23984-23988
    • Liang, J.S.1    Kim, T.2    Fang, S.3    Yamaguchi, J.4    Weissman, A.M.5    Fisher, E.A.6    Ginsberg, H.N.7
  • 103
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley BN, Ploegh HL (2004) A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429:834-840
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 104
    • 0033034120 scopus 로고    scopus 로고
    • Beta-Trcp couples beta-catenin phosphorylation-degradation and regulates Xenopus axis formation
    • Liu C, Kato Y, Zhang Z, Do VM, Yankner BA, He X (1999) beta-Trcp couples beta-catenin phosphorylation-degradation and regulates Xenopus axis formation. Proc Natl Acad Sci U S A 96:6273-6278
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 6273-6278
    • Liu, C.1    Kato, Y.2    Zhang, Z.3    Do, V.M.4    Yankner, B.A.5    He, X.6
  • 106
    • 0036091854 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus K3 utilizes the ubiquitin-proteasome system in routing class major histocompatibility complexes to late endocytic compartments
    • Lorenzo ME, Jung JU, Ploegh HL (2002) Kaposi's sarcoma-associated herpesvirus K3 utilizes the ubiquitin-proteasome system in routing class major histocompatibility complexes to late endocytic compartments. J Virol 76:5522-5531
    • (2002) J Virol , vol.76 , pp. 5522-5531
    • Lorenzo, M.E.1    Jung, J.U.2    Ploegh, H.L.3
  • 108
    • 0039172708 scopus 로고    scopus 로고
    • The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
    • Luders J, Demand J, Hohfeld J (2000) The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J Biol Chem 275:4613-4617
    • (2000) J Biol Chem , vol.275 , pp. 4613-4617
    • Luders, J.1    Demand, J.2    Hohfeld, J.3
  • 109
    • 0034714280 scopus 로고    scopus 로고
    • Interaction between the transcription factor SPBP and the positive cofactor RNF4. An interplay between protein binding zinc fingers
    • Lyngso C, Bouteiller G, Damgaard CK, Ryom D, Sanchez-Munoz S, Norby PL, Bonven BJ, Jorgensen P (2000) Interaction between the transcription factor SPBP and the positive cofactor RNF4. An interplay between protein binding zinc fingers. J Biol Chem 275:26144-26149
    • (2000) J Biol Chem , vol.275 , pp. 26144-26149
    • Lyngso, C.1    Bouteiller, G.2    Damgaard, C.K.3    Ryom, D.4    Sanchez-Munoz, S.5    Norby, P.L.6    Bonven, B.J.7    Jorgensen, P.8
  • 110
    • 1842791361 scopus 로고    scopus 로고
    • Herp is dually regulated by both the endoplasmic reticulum stress-specific branch of the unfolded protein response and a branch that is shared with other cellular stress pathways
    • Ma Y, Hendershot LM (2004) Herp is dually regulated by both the endoplasmic reticulum stress-specific branch of the unfolded protein response and a branch that is shared with other cellular stress pathways. J Biol Chem 279:13792-13799
    • (2004) J Biol Chem , vol.279 , pp. 13792-13799
    • Ma, Y.1    Hendershot, L.M.2
  • 111
    • 0032012456 scopus 로고    scopus 로고
    • A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif
    • Margottin F, Bour SP, Durand H, Selig L, Benichou S, Richard V, Thomas D, Strebel K, Benarous R (1998) A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Mol Cell 1:565-574
    • (1998) Mol Cell , vol.1 , pp. 565-574
    • Margottin, F.1    Bour, S.P.2    Durand, H.3    Selig, L.4    Benichou, S.5    Richard, V.6    Thomas, D.7    Strebel, K.8    Benarous, R.9
  • 112
    • 0037534899 scopus 로고    scopus 로고
    • Prophase destruction of Emil by the SCF(betaTrCP/Slimb) ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase
    • Margottin-Goguet F, Hsu JY, Loktev A, Hsieh HM, Reimann JD, Jackson PK (2003) Prophase destruction of Emil by the SCF(betaTrCP/Slimb) ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase. Dev Cell 4:813-826
    • (2003) Dev Cell , vol.4 , pp. 813-826
    • Margottin-Goguet, F.1    Hsu, J.Y.2    Loktev, A.3    Hsieh, H.M.4    Reimann, J.D.5    Jackson, P.K.6
  • 113
    • 1842591231 scopus 로고    scopus 로고
    • Role of protein ubiquitylation in regulating endocytosis of receptor tyrosine kinases
    • Marmor MD, Yarden Y (2004) Role of protein ubiquitylation in regulating endocytosis of receptor tyrosine kinases. Oncogene 23:2057-2070
    • (2004) Oncogene , vol.23 , pp. 2057-2070
    • Marmor, M.D.1    Yarden, Y.2
  • 115
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: A link between the chaperone and proteasome systems
    • McDonough H, Patterson C (2003) CHIP: a link between the chaperone and proteasome systems. Cell Stress Chaperones 8:303-308
    • (2003) Cell Stress Chaperones , vol.8 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 116
    • 0037378898 scopus 로고    scopus 로고
    • Proteolytic stress: A unifying concept for the etiopathogenesis of Parkinson's disease
    • McNaught KS, Olanow CW (2003) Proteolytic stress: a unifying concept for the etiopathogenesis of Parkinson's disease. Ann Neurol 53 [Suppl 3]:S73-S84
    • (2003) Ann Neurol , vol.53 , Issue.SUPPL. 3
    • McNaught, K.S.1    Olanow, C.W.2
  • 117
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham GC, Patterson C, Zhang W, Younger JM, Cyr DM (2001) The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol 3:100-105
    • (2001) Nat Cell Biol , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 118
    • 0036845476 scopus 로고    scopus 로고
    • Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Np14
    • Meyer HH, Wang Y, Warren G (2002) Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Np14. EMBO J 21:5645-5652
    • (2002) EMBO J , vol.21 , pp. 5645-5652
    • Meyer, H.H.1    Wang, Y.2    Warren, G.3
  • 119
    • 0036365674 scopus 로고    scopus 로고
    • Progressive myoclonus epilepsy with polyglucosan bodies: Lafora disease
    • Minassian BA (2002) Progressive myoclonus epilepsy with polyglucosan bodies: Lafora disease. Adv Neurol 89:199-210
    • (2002) Adv Neurol , vol.89 , pp. 199-210
    • Minassian, B.A.1
  • 124
    • 0025134024 scopus 로고
    • Identification of B16-F1 melanoma autocrine motility-like factor receptor
    • Nabi IR, Watanabe H, Raz A (1990) Identification of B16-F1 melanoma autocrine motility-like factor receptor. Cancer Res. 50:409-414
    • (1990) Cancer Res , vol.50 , pp. 409-414
    • Nabi, I.R.1    Watanabe, H.2    Raz, A.3
  • 125
    • 0026572472 scopus 로고
    • Autocrine motility factor and its receptor: Role in cell locomotion and metastasis
    • Nabi IR, Watanabe H, Raz A (1992) Autocrine motility factor and its receptor: role in cell locomotion and metastasis. Cancer Metastasis Rev 11:5-20
    • (1992) Cancer Metastasis Rev , vol.11 , pp. 5-20
    • Nabi, I.R.1    Watanabe, H.2    Raz, A.3
  • 129
    • 0037217949 scopus 로고    scopus 로고
    • Overexpression of autocrine motility factor receptor (AMFR) in NIH3T3 fibroblasts induces cell transformation
    • Onishi Y, Tsukada K, Yokota J, Raz A (2003) Overexpression of autocrine motility factor receptor (AMFR) in NIH3T3 fibroblasts induces cell transformation. Clin Exp Metastasis 20:51-58
    • (2003) Clin Exp Metastasis , vol.20 , pp. 51-58
    • Onishi, Y.1    Tsukada, K.2    Yokota, J.3    Raz, A.4
  • 131
    • 0030909233 scopus 로고    scopus 로고
    • Improved prognosis assessment for patients with bladder carcinoma
    • Otto T, Bex A, Schmidt U, Raz A, Rubben H (1997) Improved prognosis assessment for patients with bladder carcinoma. Am J Pathol 150:1919-1923
    • (1997) Am J Pathol , vol.150 , pp. 1919-1923
    • Otto, T.1    Bex, A.2    Schmidt, U.3    Raz, A.4    Rubben, H.5
  • 134
    • 0037756789 scopus 로고    scopus 로고
    • Emi1 proteolysis: How SCF(beta-Trcp1) helps to activate the anaphase-promoting complex
    • Peters JM (2003) Emi1 proteolysis: how SCF(beta-Trcp1) helps to activate the anaphase-promoting complex. Mol Cell 11:1420-1421
    • (2003) Mol Cell , vol.11 , pp. 1420-1421
    • Peters, J.M.1
  • 135
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski MD, Deshaies RJ (2005) Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol 6:9-20
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 136
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper RK, Bohmler S, Bordallo J, Sommer T, Wolf DH (1997) Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388:891-895
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Bohmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 137
    • 0034667598 scopus 로고    scopus 로고
    • Proteins of the endoplasmic-reticulum-associated degradation pathway: Domain detection and function prediction
    • Ponting CP (2000) Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction. Biochem J 351:527-535
    • (2000) Biochem J , vol.351 , pp. 527-535
    • Ponting, C.P.1
  • 139
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich E, Kerem A, Frohlich KU, Diamant N, Bar-Nun S (2002) AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol Cell Biol 22:626-634
    • (2002) Mol Cell Biol , vol.22 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Frohlich, K.U.3    Diamant, N.4    Bar-Nun, S.5
  • 140
    • 0037738525 scopus 로고    scopus 로고
    • Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation
    • Ren Y, Zhao J, Feng J (2003) Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation. J Neurosci 23:3316-3324
    • (2003) J Neurosci , vol.23 , pp. 3316-3324
    • Ren, Y.1    Zhao, J.2    Feng, J.3
  • 141
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly H, Rape M, Braun S, Rumpf S, Hoege C, Jentsch S (2005) A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120:73-84
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 142
    • 0042812051 scopus 로고    scopus 로고
    • The HECT ubiquitin ligase Rsp5p is required for proper nuclear export of mRNA in Saccharomyces cerevisiae
    • Rodriguez MS, Gwizdek C, Haguenauer-Tsapis R, Dargemont C (2003) The HECT ubiquitin ligase Rsp5p is required for proper nuclear export of mRNA in Saccharomyces cerevisiae. Traffic. 4:566-575
    • (2003) Traffic , vol.4 , pp. 566-575
    • Rodriguez, M.S.1    Gwizdek, C.2    Haguenauer-Tsapis, R.3    Dargemont, C.4
  • 143
    • 0028857948 scopus 로고
    • The leukemia-associated-protein (LAP) domain, a cysteine-rich motif, is present in a wide range of proteins, including MLL, AF10, and MLLT6 proteins
    • Saha V, Chaplin T, Gregorini A, Ayton P, Young BD (1995) The leukemia-associated-protein (LAP) domain, a cysteine-rich motif, is present in a wide range of proteins, including MLL, AF10, and MLLT6 proteins. Proc Natl Acad Sci U S A 92:9737-9741
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 9737-9741
    • Saha, V.1    Chaplin, T.2    Gregorini, A.3    Ayton, P.4    Young, B.D.5
  • 145
    • 0027630839 scopus 로고
    • HAT3.1, a novel Arabidopsis homeodomain protein containing a conserved cysteine-rich region
    • Schindler U, Beckmann H, Cashmore AR (1993) HAT3.1, a novel Arabidopsis homeodomain protein containing a conserved cysteine-rich region. Plant J 4:137-150
    • (1993) Plant J , vol.4 , pp. 137-150
    • Schindler, U.1    Beckmann, H.2    Cashmore, A.R.3
  • 146
    • 0035167960 scopus 로고    scopus 로고
    • Polyubiquitination is required for US 11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol
    • Shamu CE, Flierman D, Ploegh HL, Rapoport TA, Chau V (2001) Polyubiquitination is required for US 11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol. Mol Biol Cell 12:2546-2555
    • (2001) Mol Biol Cell , vol.12 , pp. 2546-2555
    • Shamu, C.E.1    Flierman, D.2    Ploegh, H.L.3    Rapoport, T.A.4    Chau, V.5
  • 147
    • 0033523771 scopus 로고    scopus 로고
    • The pathway of US11-dependent degradation of MHC class I heavy chains involves a ubiquitin-conjugated intermediate
    • Shamu CE, Story CM, Rapoport TA, Ploegh HL (1999) The pathway of US11-dependent degradation of MHC class I heavy chains involves a ubiquitin-conjugated intermediate. J Cell Biol 147:45-58
    • (1999) J Cell Biol , vol.147 , pp. 45-58
    • Shamu, C.E.1    Story, C.M.2    Rapoport, T.A.3    Ploegh, H.L.4
  • 149
    • 0345616428 scopus 로고    scopus 로고
    • A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain
    • Shih SC, Prag G, Francis SA, Sutanto MA, Hurley JH, Hicke L (2003) A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain. EMBO J 22:1273-1281
    • (2003) EMBO J , vol.22 , pp. 1273-1281
    • Shih, S.C.1    Prag, G.2    Francis, S.A.3    Sutanto, M.A.4    Hurley, J.H.5    Hicke, L.6
  • 153
    • 0032410209 scopus 로고    scopus 로고
    • A novel repeat domain that is often associated with RING finger and B-box motifs
    • Slack FJ, Ruvkun G (1998) A novel repeat domain that is often associated with RING finger and B-box motifs. Trends Biochem Sci 23:474-475
    • (1998) Trends Biochem Sci , vol.23 , pp. 474-475
    • Slack, F.J.1    Ruvkun, G.2
  • 154
    • 0027327659 scopus 로고
    • A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
    • Sommer T, Jentsch S (1993) A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 365:176-179
    • (1993) Nature , vol.365 , pp. 176-179
    • Sommer, T.1    Jentsch, S.2
  • 155
    • 0030700576 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation: Reverse protein flow of no return
    • Sommer T, Wolf DH (1997) Endoplasmic reticulum degradation: reverse protein flow of no return. FASEB J 11:1227-1233
    • (1997) FASEB J , vol.11 , pp. 1227-1233
    • Sommer, T.1    Wolf, D.H.2
  • 156
    • 12544250585 scopus 로고    scopus 로고
    • Multivesicular bodies and multivesicular endosomes: The "ins and outs" of endosomal traffic
    • Stahl PD, Barbieri MA (2002) Multivesicular bodies and multivesicular endosomes: the "ins and outs" of endosomal traffic. Sci STKE 2002:E32
    • (2002) Sci STKE , vol.2002
    • Stahl, P.D.1    Barbieri, M.A.2
  • 157
    • 0037422010 scopus 로고    scopus 로고
    • Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity
    • Staropoli JF, McDermott C, Martinat C, Schulman B, Demireva E, Abeliovich A (2003) Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity. Neuron 37:735-749
    • (2003) Neuron , vol.37 , pp. 735-749
    • Staropoli, J.F.1    McDermott, C.2    Martinat, C.3    Schulman, B.4    Demireva, E.5    Abeliovich, A.6
  • 158
    • 0037195510 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and the regulation of growth hormone receptor availability
    • Strous GJ, van Kerkhof P (2002) The ubiquitin-proteasome pathway and the regulation of growth hormone receptor availability. Mol Cell Endocrinol 197:143-151
    • (2002) Mol Cell Endocrinol , vol.197 , pp. 143-151
    • Strous, G.J.1    Van Kerkhof, P.2
  • 159
    • 0032555648 scopus 로고    scopus 로고
    • Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity
    • Suzuki T, Park H, Kitajima K, Lennarz WJ (1998) Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity. J Biol Chem 273:21526-21530
    • (1998) J Biol Chem , vol.273 , pp. 21526-21530
    • Suzuki, T.1    Park, H.2    Kitajima, K.3    Lennarz, W.J.4
  • 160
    • 0035887277 scopus 로고    scopus 로고
    • A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation
    • Swanson R, Locher M, Hochstrasser M (2001) A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes Dev 15:2660-2674
    • (2001) Genes Dev , vol.15 , pp. 2660-2674
    • Swanson, R.1    Locher, M.2    Hochstrasser, M.3
  • 161
    • 0142093671 scopus 로고    scopus 로고
    • Pael receptor, endoplasmic reticulum stress, and Parkinson's disease
    • Takahashi R, Imai Y (2003) Pael receptor, endoplasmic reticulum stress, and Parkinson's disease. J Neurol 250 [Suppl 3]:III25-III29
    • (2003) J Neurol , vol.250 , Issue.SUPPL. 3
    • Takahashi, R.1    Imai, Y.2
  • 163
    • 0141592584 scopus 로고    scopus 로고
    • Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD
    • Taxis C, Hitt R, Park SH, Deak PM, Kostova Z, Wolf DH (2003) Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD. J Biol Chem 278:35903-35913
    • (2003) J Biol Chem , vol.278 , pp. 35903-35913
    • Taxis, C.1    Hitt, R.2    Park, S.H.3    Deak, P.M.4    Kostova, Z.5    Wolf, D.H.6
  • 164
    • 0035844139 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s)
    • Tiwari S, Weissman AM (2001) Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s). J Biol Chem 276:16193-16200
    • (2001) J Biol Chem , vol.276 , pp. 16193-16200
    • Tiwari, S.1    Weissman, A.M.2
  • 165
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Tsai YC, Fishman PS, Thakor NV, Oyler GA (2003) Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. J Biol Chem 278:22044-22055
    • (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
  • 167
    • 0034598991 scopus 로고    scopus 로고
    • The novel MMS-inducible gene Mif1/KIAA0025 is a target of the unfolded protein response pathway
    • Van Laar T, Schouten T, Hoogervorst E, van Eck M, van der Eb AJ, Terleth C (2000) The novel MMS-inducible gene Mif1/KIAA0025 is a target of the unfolded protein response pathway. FEBS Lett 469:123-131
    • (2000) FEBS Lett , vol.469 , pp. 123-131
    • Van Laar, T.1    Schouten, T.2    Hoogervorst, E.3    Van Eck, M.4    Van Der Eb, A.J.5    Terleth, C.6
  • 168
    • 2442451126 scopus 로고    scopus 로고
    • Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control
    • Vashist S, Ng DT (2004) Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control. J Cell Biol 165:41-52
    • (2004) J Cell Biol , vol.165 , pp. 41-52
    • Vashist, S.1    Ng, D.T.2
  • 169
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • Verma R, Oania R, Graumann J, Deshaies RJ (2004) Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell 118:99-110
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 170
    • 0035875921 scopus 로고    scopus 로고
    • Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
    • Walter J, Urban J, Volkwein C, Sommer T (2001) Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p. EMBO J 20:3124-3131
    • (2001) EMBO J , vol.20 , pp. 3124-3131
    • Walter, J.1    Urban, J.2    Volkwein, C.3    Sommer, T.4
  • 171
    • 0032907946 scopus 로고    scopus 로고
    • Functional domains of the Rsp5 ubiquitin-protein ligase
    • Wang G, Yang J, Huibregtse JM (1999) Functional domains of the Rsp5 ubiquitin-protein ligase. Mol Cell Biol 19:342-352
    • (1999) Mol Cell Biol , vol.19 , pp. 342-352
    • Wang, G.1    Yang, J.2    Huibregtse, J.M.3
  • 172
    • 0034967244 scopus 로고    scopus 로고
    • Developmental changes in the expression of Parkin and UbcR7, a Parkin-interacting and ubiquitin-conjugating enzyme, in rat brain
    • Wang M, Suzuki T, Kitada T, Asakawa S, Minoshima S, Shimizu N, Tanaka K, Mizuno Y, Hattori N (2001) Developmental changes in the expression of Parkin and UbcR7, a Parkin-interacting and ubiquitin-conjugating enzyme, in rat brain. J Neurochem 77:1561-1568
    • (2001) J Neurochem , vol.77 , pp. 1561-1568
    • Wang, M.1    Suzuki, T.2    Kitada, T.3    Asakawa, S.4    Minoshima, S.5    Shimizu, N.6    Tanaka, K.7    Mizuno, Y.8    Hattori, N.9
  • 173
    • 0043026909 scopus 로고    scopus 로고
    • Substrate recognition in ER-associated degradation mediated by Eps1, a member of the protein disulfide isomerase family
    • Wang Q, Chang A (2003) Substrate recognition in ER-associated degradation mediated by Eps1, a member of the protein disulfide isomerase family. EMBO J 22:3792-3802
    • (2003) EMBO J , vol.22 , pp. 3792-3802
    • Wang, Q.1    Chang, A.2
  • 174
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward CL, Omura S, Kopito RR (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83:121-127
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 175
    • 0025769292 scopus 로고
    • The relationship between motility factor receptor internalization and the lung colonization capacity of murine melanoma cells
    • Watanabe H, Nabi IR, Raz A (1991) The relationship between motility factor receptor internalization and the lung colonization capacity of murine melanoma cells. Cancer Res 51:2699-2705
    • (1991) Cancer Res , vol.51 , pp. 2699-2705
    • Watanabe, H.1    Nabi, I.R.2    Raz, A.3
  • 176
    • 0141532211 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptor ubiquitination is mediated by mammalian Ubc7, a component of the endoplasmic reticulum-associated degradation pathway, and is inhibited by chelation of intracellular Zn2+
    • Webster JM, Tiwari S, Weissman AM, Wojcikiewicz RJ (2003) Inositol 1,4,5-trisphosphate receptor ubiquitination is mediated by mammalian Ubc7, a component of the endoplasmic reticulum-associated degradation pathway, and is inhibited by chelation of intracellular Zn2+. J Biol Chem 278:38238-38246
    • (2003) J Biol Chem , vol.278 , pp. 38238-38246
    • Webster, J.M.1    Tiwari, S.2    Weissman, A.M.3    Wojcikiewicz, R.J.4
  • 177
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman AM (2001) Themes and variations on ubiquitylation. Nat Rev Mol Cell Biol 2:169-178
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 179
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
    • Wiertz EJ, Jones TR, Sun L, Bogyo M, Geuze HJ, Ploegh HL (1996a) The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84:769-779
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5    Ploegh, H.L.6
  • 180
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz EJ, Tortorella D, Bogyo M, Yu J, Mothes W, Jones TR, Rapoport TA, Ploegh HL (1996b) Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384:432-438
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4    Mothes, W.5    Jones, T.R.6    Rapoport, T.A.7    Ploegh, H.L.8
  • 181
    • 0034108089 scopus 로고    scopus 로고
    • HRD gene dependence of endoplasmic reticulum-associated degradation
    • Wilhovsky S, Gardner R, Hampton R (2000) HRD gene dependence of endoplasmic reticulum-associated degradation. Mol Biol Cell 11:1697-1708
    • (2000) Mol Biol Cell , vol.11 , pp. 1697-1708
    • Wilhovsky, S.1    Gardner, R.2    Hampton, R.3
  • 185
    • 9144228073 scopus 로고    scopus 로고
    • Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II
    • Yamamoto K, Yoshida H, Kokame K, Kaufman RJ, Mori K (2004) Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II. J Biochem (Tokyo) 136:343-350
    • (2004) J Biochem (Tokyo) , vol.136 , pp. 343-350
    • Yamamoto, K.1    Yoshida, H.2    Kokame, K.3    Kaufman, R.J.4    Mori, K.5
  • 186
    • 0030006865 scopus 로고    scopus 로고
    • Bull, a new protein that binds to the Rsp5 ubiquitin ligase in Saccharomyces cerevisiae
    • Yashiroda H, Oguchi T, Yasuda Y, Toh E, Kikuchi Y (1996) Bull, a new protein that binds to the Rsp5 ubiquitin ligase in Saccharomyces cerevisiae. Mol Cell Biol 16:3255-3263
    • (1996) Mol Cell Biol , vol.16 , pp. 3255-3263
    • Yashiroda, H.1    Oguchi, T.2    Yasuda, Y.3    Toh, E.4    Kikuchi, Y.5
  • 187
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye Y, Meyer HH, Rapoport TA (2001) The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414:652-656
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 188
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye Y, Meyer HH, Rapoport TA (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162:71-84
    • (2003) J Cell Biol , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 189
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Ye Y, Shibata Y, Yun C, Ron D, Rapoport TA (2004) A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429:841-847
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 191
    • 0242321836 scopus 로고    scopus 로고
    • Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains
    • Yoshida Y, Tokunaga F, Chiba T, Iwai K, Tanaka K, Tai T (2003) Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains. J Biol Chem 278:43877-43884
    • (2003) J Biol Chem , vol.278 , pp. 43877-43884
    • Yoshida, Y.1    Tokunaga, F.2    Chiba, T.3    Iwai, K.4    Tanaka, K.5    Tai, T.6
  • 192
    • 0030817978 scopus 로고    scopus 로고
    • Cytosolic degradation of T-cell receptor alpha chains by the proteasome
    • Yu H, Kaung G, Kobayashi S, Kopito RR (1997) Cytosolic degradation of T-cell receptor alpha chains by the proteasome. J Biol Chem 272:20800-20804
    • (1997) J Biol Chem , vol.272 , pp. 20800-20804
    • Yu, H.1    Kaung, G.2    Kobayashi, S.3    Kopito, R.R.4
  • 193
    • 0033601349 scopus 로고    scopus 로고
    • The role of multiubiquitination in dislocation and degradation of the alpha subunit of the T cell antigen receptor
    • Yu H, Kopito RR (1999) The role of multiubiquitination in dislocation and degradation of the alpha subunit of the T cell antigen receptor. J Biol Chem 274:36852-36858
    • (1999) J Biol Chem , vol.274 , pp. 36852-36858
    • Yu, H.1    Kopito, R.R.2
  • 194
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin- Protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • Zhang Y, Gao J, Chung KK, Huang H, Dawson VL, Dawson TM (2000) Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc Natl Acad Sci U S A 97:13354-13359
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6
  • 195
    • 0142074728 scopus 로고    scopus 로고
    • Parkin is recruited to the centrosome in response to inhibition of proteasomes
    • Zhao J, Ren Y, Jiang Q, Feng J (2003) Parkin is recruited to the centrosome in response to inhibition of proteasomes. J Cell Sci 116:4011-4019
    • (2003) J Cell Sci , vol.116 , pp. 4011-4019
    • Zhao, J.1    Ren, Y.2    Jiang, Q.3    Feng, J.4
  • 197
    • 15744369806 scopus 로고    scopus 로고
    • RING finger ubiquitin-protein isopeptide ligase Nrdp1/FLRF regulates Parkin stability and activity
    • Zhong L, Tan Y, Zhou A, Yu Q, Zhou J (2005) RING finger ubiquitin-protein isopeptide ligase Nrdp1/FLRF regulates Parkin stability and activity. J Biol Chem 280:9425-9430
    • (2005) J Biol Chem , vol.280 , pp. 9425-9430
    • Zhong, L.1    Tan, Y.2    Zhou, A.3    Yu, Q.4    Zhou, J.5
  • 198
    • 8544263881 scopus 로고    scopus 로고
    • AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation
    • Zhong X, Shen Y, Ballar P, Apostolou A, Agami R, Fang S (2004) AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation. J Biol Chem 279:45676-45684
    • (2004) J Biol Chem , vol.279 , pp. 45676-45684
    • Zhong, X.1    Shen, Y.2    Ballar, P.3    Apostolou, A.4    Agami, R.5    Fang, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.