메뉴 건너뛰기




Volumn 25, Issue 9, 2003, Pages 868-877

Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; AQUAPORIN 2; BETA N ACETYLHEXOSAMINIDASE; CD4 ANTIGEN; CELL PROTEIN; COLLAGEN; FIBRINOGEN; GAP JUNCTION PROTEIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; INSULIN RECEPTOR; LOW DENSITY LIPOPROTEIN RECEPTOR; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MONOPHENOL MONOOXYGENASE; MUTANT PROTEIN; MYELOPEROXIDASE; PARATHYROID HORMONE RELATED PROTEIN; PROTEASOME; RHODOPSIN; THYROGLOBULIN; TRANSMEMBRANE CONDUCTANCE REGULATOR; UNCLASSIFIED DRUG; UNFOLDED PROTEIN;

EID: 0042318739     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.10320     Document Type: Review
Times cited : (198)

References (107)
  • 1
    • 0035370949 scopus 로고    scopus 로고
    • Intracellular signaling from the endoplasmic reticulum to the nucleus: The unfolded protein response in yeast and mammals
    • Patil C, Walter P. Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr Opin Cell Biol 2001;13:349-355.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 349-355
    • Patil, C.1    Walter, P.2
  • 3
    • 0030070704 scopus 로고    scopus 로고
    • Assembly of ER-associated protein degradation in vitro: Dependence on cytosol, calnexin, and ATP
    • McCracken AA, Brodsky JL. Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J Cell Biol 1996;132:291-298.
    • (1996) J Cell Biol , vol.132 , pp. 291-298
    • McCracken, A.A.1    Brodsky, J.L.2
  • 4
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B, Horwich AL. The Hsp70 and Hsp60 chaperone machines. Cell 1998;92:351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 5
    • 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. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 1997;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
  • 6
    • 0033525198 scopus 로고    scopus 로고
    • The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct
    • Brodsky JL, Werner ED, Dubas ME, Goeckeler JL, Kruse KB, McCracken AA. The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J Biol Chem 1999;274:3453-3460.
    • (1999) J Biol Chem , vol.274 , pp. 3453-3460
    • Brodsky, J.L.1    Werner, E.D.2    Dubas, M.E.3    Goeckeler, J.L.4    Kruse, K.B.5    McCracken, A.A.6
  • 7
    • 0033611127 scopus 로고    scopus 로고
    • Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase
    • Gillece P, Luz JM, Lennarz WJ, de La Cruz FJ, Romisch K. Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase. J Cell Biol 1999;147:1443-1456.
    • (1999) J Cell Biol , vol.147 , pp. 1443-1456
    • Gillece, P.1    Luz, J.M.2    Lennarz, W.J.3    De La Cruz, F.J.4    Romisch, K.5
  • 8
    • 0037157856 scopus 로고    scopus 로고
    • Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER
    • Molinari M, Galli C, Piccaluga V, Pieren M, Paganetti P. Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER. J Cell Biol 2002;158:247-257.
    • (2002) J Cell Biol , vol.158 , pp. 247-257
    • Molinari, M.1    Galli, C.2    Piccaluga, V.3    Pieren, M.4    Paganetti, P.5
  • 9
    • 0032539619 scopus 로고    scopus 로고
    • The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP
    • Skowronek MH, Hendershot LM, Haas IG. The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP. Proc Natl Acad Sci USA 1998;95:1574-1578.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1574-1578
    • Skowronek, M.H.1    Hendershot, L.M.2    Haas, I.G.3
  • 10
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner S, Maurizi MR, Gottesman S. Posttranslational quality control: folding, refolding, and degrading proteins. Science 1999;286:1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 11
    • 0035947773 scopus 로고    scopus 로고
    • Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation
    • Nishikawa SI, Fewell SW, Kato Y, Brodsky JL, Endo T. Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J Cell Biol 2001;153:1061-1070.
    • (2001) J Cell Biol , vol.153 , pp. 1061-1070
    • Nishikawa, S.I.1    Fewell, S.W.2    Kato, Y.3    Brodsky, J.L.4    Endo, T.5
  • 13
    • 0034896499 scopus 로고    scopus 로고
    • Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release
    • Vanhove M, Usherwood YK, Hendershot LM. Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release. Immunity 2001;15:105-114.
    • (2001) Immunity , vol.15 , pp. 105-114
    • Vanhove, M.1    Usherwood, Y.K.2    Hendershot, L.M.3
  • 14
    • 0035478934 scopus 로고    scopus 로고
    • Dissecting glycoprotein quality control in the secretory pathway
    • Cabral CM, Liu Y, Sifers RN. Dissecting glycoprotein quality control in the secretory pathway. Trends Biochem Sci 2001;26:619-624.
    • (2001) Trends Biochem Sci , vol.26 , pp. 619-624
    • Cabral, C.M.1    Liu, Y.2    Sifers, R.N.3
  • 15
    • 0037422614 scopus 로고    scopus 로고
    • Inaugural Article: UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates
    • Caramelo JJ, Castro OA, Alonso LG, De Prat-Gay G, Parodi AJ. Inaugural Article: UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates. Proc Natl Acad Sci USA 2003;100:86-89.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 86-89
    • Caramelo, J.J.1    Castro, O.A.2    Alonso, L.G.3    De Prat-Gay, G.4    Parodi, A.J.5
  • 16
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • Parodi AJ. Protein glucosylation and its role in protein folding. Annu Rev Biochem 2000;69:69-93.
    • (2000) Annu Rev Biochem , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 17
    • 0034872726 scopus 로고    scopus 로고
    • A novel lectin in the secretory pathway. An elegant mechanism for glycoprotein elimination
    • Braakman I. A novel lectin in the secretory pathway. An elegant mechanism for glycoprotein elimination. EMBO Rep 2001;2:666-668.
    • (2001) EMBO Rep , vol.2 , pp. 666-668
    • Braakman, I.1
  • 18
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda Y, Hosokawa N, Wada I, Nagata K. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 2003;299:1394-1397.
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 19
    • 0037470410 scopus 로고    scopus 로고
    • Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle
    • Molinari M, Calanca V, Galli C, Lucca P, Paganetti P. Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science 2003;299:1397-1400.
    • (2003) Science , vol.299 , pp. 1397-1400
    • Molinari, M.1    Calanca, V.2    Galli, C.3    Lucca, P.4    Paganetti, P.5
  • 20
    • 0033197741 scopus 로고    scopus 로고
    • Calnexin discriminate between protein conformational states and functions as a molecular chaperone in vitro
    • Ihara Y, Cohen-Doyle MF, Saito Y, Williams DB. Calnexin discriminate between protein conformational states and functions as a molecular chaperone in vitro. Mol Cell 1999;4:331-341.
    • (1999) Mol Cell , vol.4 , pp. 331-341
    • Ihara, Y.1    Cohen-Doyle, M.F.2    Saito, Y.3    Williams, D.B.4
  • 21
    • 0034646876 scopus 로고    scopus 로고
    • Chaperone selection during glycoprotein translocation into the endoplasmic reticulum
    • Molinari M, Helenius A. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. Science 2000;288:331-333.
    • (2000) Science , vol.288 , pp. 331-333
    • Molinari, M.1    Helenius, A.2
  • 22
    • 0031084807 scopus 로고    scopus 로고
    • Viruses use stealth technology to escape from the host immune system
    • Wiertz EJ, Mukherjee S, Ploegh HL. Viruses use stealth technology to escape from the host immune system. Mol Med Today 1997;3:116-123.
    • (1997) Mol Med Today , vol.3 , pp. 116-123
    • Wiertz, E.J.1    Mukherjee, S.2    Ploegh, H.L.3
  • 23
    • 0030789680 scopus 로고    scopus 로고
    • Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
    • Pilon M, Schekman R, Römisch K. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J 1997;16:4540-4548.
    • (1997) EMBO J , vol.16 , pp. 4540-4548
    • Pilon, M.1    Schekman, R.2    Römisch, K.3
  • 24
    • 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. A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat Cell Biol 2000;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
  • 25
    • 0037148535 scopus 로고    scopus 로고
    • A new role for BiP: Closing the aqueous translocon pore during protein integration into the ER membrane
    • Haigh NG, Johnson AE. A new role for BiP: closing the aqueous translocon pore during protein integration into the ER membrane. J Cell Biol 2002;156:261-270.
    • (2002) J Cell Biol , vol.156 , pp. 261-270
    • Haigh, N.G.1    Johnson, A.E.2
  • 26
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocation pore before and early in translocation
    • Hamman BD, Hendershot LM, Johnson AE. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocation pore before and early in translocation. Cell 1998;92:747-758.
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 27
    • 0026644816 scopus 로고
    • Bidirectional movement of a nascent polypeptide across microsomal membranes reveals requirements for vectorial translocation of proteins
    • Ooi CE, Weiss J. Bidirectional movement of a nascent polypeptide across microsomal membranes reveals requirements for vectorial translocation of proteins. Cell 1992;71:87-96.
    • (1992) Cell , vol.71 , pp. 87-96
    • Ooi, C.E.1    Weiss, J.2
  • 28
    • 0033031194 scopus 로고    scopus 로고
    • Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species
    • Plemper RK, Deak PM, Otto RT, Wolf DH. Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. FEBS Lett 1999;443:241-245.
    • (1999) FEBS Lett , vol.443 , pp. 241-245
    • Plemper, R.K.1    Deak, P.M.2    Otto, R.T.3    Wolf, D.H.4
  • 29
    • 0035968205 scopus 로고    scopus 로고
    • Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi
    • Caldwell SR, Hill KJ, Cooper AA. Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi. J Biol Chem 2001;276:23296-23303.
    • (2001) J Biol Chem , vol.276 , pp. 23296-23303
    • Caldwell, S.R.1    Hill, K.J.2    Cooper, A.A.3
  • 30
    • 0035851911 scopus 로고    scopus 로고
    • Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding
    • Vashist S, Kim W, Belden WJ, Spear ED, Barlowe C, Ng DTW. Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding. J Cell Biol 2001;155:355-367.
    • (2001) J Cell Biol , vol.155 , pp. 355-367
    • Vashist, S.1    Kim, W.2    Belden, W.J.3    Spear, E.D.4    Barlowe, C.5    Ng, D.T.W.6
  • 31
    • 0035985150 scopus 로고    scopus 로고
    • ER-Golgi traffic is a prerequisite for efficient ER degradation
    • Taxis C, Vogel F, Wolf DH. ER-Golgi traffic is a prerequisite for efficient ER degradation. Mol Biol Cell 2002;13:1806-1818.
    • (2002) Mol Biol Cell , vol.13 , pp. 1806-1818
    • Taxis, C.1    Vogel, F.2    Wolf, D.H.3
  • 32
    • 0035845484 scopus 로고    scopus 로고
    • Immunolocalization of UDP-glucose-: Glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control
    • Zuber C, Fan J, Guhl B, Parodi A, Fessler JH, Parker C, Roth J. Immunolocalization of UDP-glucose-: glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality control. Proc Natl Acad Sci USA 2001;98:10710-10715.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10710-10715
    • Zuber, C.1    Fan, J.2    Guhl, B.3    Parodi, A.4    Fessler, J.H.5    Parker, C.6    Roth, J.7
  • 33
    • 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. An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport. J Cell Biol 2002;158:91-101.
    • (2002) J Cell Biol , vol.158 , pp. 91-101
    • Haynes, C.M.1    Caldwell, S.2    Cooper, A.A.3
  • 34
    • 0034710889 scopus 로고    scopus 로고
    • Furin-mediated processing in the early secretory pathway: Sequential cleavage and degradation of misfolded insulin receptors
    • Bass J, Turck C, Rouard M, Steiner DF. Furin-mediated processing in the early secretory pathway: Sequential cleavage and degradation of misfolded insulin receptors. Proc Natl Acad Sci USA 2000;97:11905-11909.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11905-11909
    • Bass, J.1    Turck, C.2    Rouard, M.3    Steiner, D.F.4
  • 35
    • 0036843023 scopus 로고    scopus 로고
    • Secretory pathway quality control operating in Golgi, plasmalemmal and endosomal systems
    • Arvan P, Zhao X, Ramos-Castaneda J, Chang A. Secretory pathway quality control operating in Golgi, plasmalemmal and endosomal systems. Traffic 2002;3:771-780.
    • (2002) Traffic , vol.3 , pp. 771-780
    • Arvan, P.1    Zhao, X.2    Ramos-Castaneda, J.3    Chang, A.4
  • 36
    • 0037769904 scopus 로고    scopus 로고
    • Stress tolerance of misfolded carboxypeptidase Y requires maintenance of protein trafficking and degradative pathways
    • Spear ED, Ng DTW. Stress tolerance of misfolded carboxypeptidase Y requires maintenance of protein trafficking and degradative pathways. Mol Biol Cell 2003;14:2756-2767.
    • (2003) Mol Biol Cell , vol.14 , pp. 2756-2767
    • Spear, E.D.1    Ng, D.T.W.2
  • 37
    • 0032977841 scopus 로고    scopus 로고
    • Sec61 complex is located in both the ER and the ER-Golgi intermediate compartment
    • Greenfield JJ, High S. Sec61 complex is located in both the ER and the ER-Golgi intermediate compartment. J Cell Sci 1999;112:1477-1486.
    • (1999) J Cell Sci , vol.112 , pp. 1477-1486
    • Greenfield, J.J.1    High, S.2
  • 38
    • 0035947777 scopus 로고    scopus 로고
    • COOH-terminal truncations promote proteasome-dependent degradation of mature cystic fibrosis transmembrane conductance regulator from post-Golgi compartments
    • Benharouga M, Haardt M, Kartner N, Lukacs GL. COOH-terminal truncations promote proteasome-dependent degradation of mature cystic fibrosis transmembrane conductance regulator from post-Golgi compartments. J Cell Biol 2001;153:957-970.
    • (2001) J Cell Biol , vol.153 , pp. 957-970
    • Benharouga, M.1    Haardt, M.2    Kartner, N.3    Lukacs, G.L.4
  • 39
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston JA, Ward CL, Kopito RR. Aggresomes: a cellular response to misfolded proteins. J Cell Biol 1998;143:1883-1898.
    • (1998) J Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 40
    • 0034651604 scopus 로고    scopus 로고
    • Degradation of unassembled Vphlp reveals novel aspects of the yeast ER quality control system
    • Hill K, Cooper AA. Degradation of unassembled Vphlp reveals novel aspects of the yeast ER quality control system. EMBO J 2000;19:550-561.
    • (2000) EMBO J , vol.19 , pp. 550-561
    • Hill, K.1    Cooper, A.A.2
  • 41
    • 0035816574 scopus 로고    scopus 로고
    • Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70
    • Gusarova V, Caplan AJ, Brodsky JL, Fisher EA. Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70. J Biol Chem 2001;276:24891-2900.
    • (2001) J Biol Chem , vol.276 , pp. 24891-24900
    • Gusarova, V.1    Caplan, A.J.2    Brodsky, J.L.3    Fisher, E.A.4
  • 42
    • 0034757165 scopus 로고    scopus 로고
    • The Hsp70 molecular chaperone facilitates the ER associated protein degradation of the cystic fibrosis transmembrane conductance regulator in yeast
    • Zhang Y, Nijbroek G, Sullivan ML, McCracken AA, Watkins SC, Michaelis S, Brodsky JL. The Hsp70 molecular chaperone facilitates the ER associated protein degradation of the cystic fibrosis transmembrane conductance regulator in yeast, Mol Cell Biol 2001;12:1303-1314.
    • (2001) Mol Cell Biol , vol.12 , pp. 1303-1314
    • Zhang, Y.1    Nijbroek, G.2    Sullivan, M.L.3    McCracken, A.A.4    Watkins, S.C.5    Michaelis, S.6    Brodsky, J.L.7
  • 43
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart CM. Mechanisms underlying ubiquitination. Annu Rev Biochem 2001;70:503-533.
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 46
    • 0032540384 scopus 로고    scopus 로고
    • Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome
    • de Virgilio M, Weninger H, Ivessa NE. Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome. J Biol Chem 1998;273:9734-9743.
    • (1998) J Biol Chem , vol.273 , pp. 9734-9743
    • De Virgilio, M.1    Weninger, H.2    Ivessa, N.E.3
  • 47
    • 0035167960 scopus 로고    scopus 로고
    • Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol
    • Shamu CE, Flierman D, Ploegh HL, Rapoport TA, Chau V. Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol. Mol Biol Cell 2001;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
  • 49
    • 0032526433 scopus 로고    scopus 로고
    • Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein
    • Mayer TU, Braun T, Jentsch S. Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein. EMBO J 1998;17:3251-3257.
    • (1998) EMBO J , vol.17 , pp. 3251-3257
    • Mayer, T.U.1    Braun, T.2    Jentsch, S.3
  • 50
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D, Zwickl P, Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 1999;68:1015-1068.
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 51
    • 0031973716 scopus 로고    scopus 로고
    • The AAA team: Related ATPases with diverse functions
    • Patel S, Latterich M. The AAA team: related ATPases with diverse functions. Trends Cell Biol 1998;8:65-71.
    • (1998) Trends Cell Biol , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 53
    • 0030447659 scopus 로고    scopus 로고
    • Proteasome-dependent ER-associated protein degradation: An unconventional route to a familiar fate
    • Werner ED, Brodsky JL, McCracken AA, Proteasome-dependent ER-associated protein degradation: an unconventional route to a familiar fate. Proc Natl Acad Sci USA 1996;93:13797-13801.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13797-13801
    • Werner, E.D.1    Brodsky, J.L.2    McCracken, A.A.3
  • 54
    • 0037076507 scopus 로고    scopus 로고
    • Cdc48-Ufd1-Npl4; Stuck in the middle with Ub
    • Bays NW, Hampton RY, Cdc48-Ufd1-Npl4; stuck in the middle with Ub. Curr Biol 2002;12:R366-R371.
    • (2002) Curr Biol , vol.12
    • Bays, N.W.1    Hampton, R.Y.2
  • 55
    • 0033791447 scopus 로고    scopus 로고
    • Proteasomel proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity purified proteasome
    • Verma R, Chen S, Feldman R, Schieltz D, Yates J, Dohmen J, Deshaies RJ. Proteasomel proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity purified proteasome. Mol Biol Cell 2000;11:3425-3439.
    • (2000) Mol Biol Cell , vol.11 , pp. 3425-3439
    • Verma, R.1    Chen, S.2    Feldman, R.3    Schieltz, D.4    Yates, J.5    Dohmen, J.6    Deshaies, R.J.7
  • 56
    • 0037084028 scopus 로고    scopus 로고
    • Role of the ubiquitin-selective CDC48 (UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates
    • Braun S, Matuschewski K, Rape M, Thoms S, Jentsch S. Role of the ubiquitin-selective CDC48 (UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J 2002;21:615-621.
    • (2002) EMBO J , vol.21 , pp. 615-621
    • Braun, S.1    Matuschewski, K.2    Rape, M.3    Thoms, S.4    Jentsch, S.5
  • 57
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
    • Lam YA, Lawson TG, Velayutham M, Zweier JL, Pickart CM. A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal. Nature 2002;416:763-767.
    • (2002) Nature , vol.416 , pp. 763-767
    • Lam, Y.A.1    Lawson, T.G.2    Velayutham, M.3    Zweier, J.L.4    Pickart, C.M.5
  • 58
    • 0033963160 scopus 로고    scopus 로고
    • Role of ubiquitin in proteasomal degradation of mutant alpha(1)-antitrypsin Z in the endoplasmic reticulum
    • Teckman JH, Gilmore R, Perlmutter DH. Role of ubiquitin in proteasomal degradation of mutant alpha(1)-antitrypsin Z in the endoplasmic reticulum. Am J Physiol Gastrointest Liver Physiol 2000;278:G39-G48.
    • (2000) Am J Physiol Gastrointest Liver Physiol , vol.278
    • Teckman, J.H.1    Gilmore, R.2    Perlmutter, D.H.3
  • 59
    • 0035977095 scopus 로고    scopus 로고
    • Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone
    • Rape M, Hoppe T, Gorr I, Kalocay M, Richly H, Jentsch S. Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 2001;107:667-677.
    • (2001) Cell , vol.107 , pp. 667-677
    • Rape, M.1    Hoppe, T.2    Gorr, I.3    Kalocay, M.4    Richly, H.5    Jentsch, S.6
  • 60
    • 0034746779 scopus 로고    scopus 로고
    • The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation
    • Hitchcock AL, Krebber H, Frietze S, Lin A, Latterich M, Silver PA. The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation. Mol Biol Cell 2001;12:3226-3241.
    • (2001) Mol Biol Cell , vol.12 , pp. 3226-3241
    • Hitchcock, A.L.1    Krebber, H.2    Frietze, S.3    Lin, A.4    Latterich, M.5    Silver, P.A.6
  • 61
    • 0035875921 scopus 로고    scopus 로고
    • Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
    • Walter J, Urban J, Volkwein C, Sommer T. Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p. EMBO J 2001;20:3124-3131.
    • (2001) EMBO J , vol.20 , pp. 3124-3131
    • Walter, J.1    Urban, J.2    Volkwein, C.3    Sommer, T.4
  • 63
    • 0037144567 scopus 로고    scopus 로고
    • Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel
    • Lee C, Prakash S, Matouschek A. Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel. J Biol Chem 2002;277:34760-34765.
    • (2002) J Biol Chem , vol.277 , pp. 34760-34765
    • Lee, C.1    Prakash, S.2    Matouschek, A.3
  • 64
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • Weihofen A, Binns K, Lemberg MK, Ashman K, Martoglio B, Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 2002;296:2215-2218.
    • (2002) Science , vol.296 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 65
    • 0029146856 scopus 로고
    • A mutation affecting signal peptidase inhibits degradation of an abnormal membrane protein in Saccharomyces cerevisiae
    • Mullins C, Lu Y, Campbell A, Fang H, Green N. A mutation affecting signal peptidase inhibits degradation of an abnormal membrane protein in Saccharomyces cerevisiae. J Biol Chem 1995;270:17139-17147.
    • (1995) J Biol Chem , vol.270 , pp. 17139-17147
    • Mullins, C.1    Lu, Y.2    Campbell, A.3    Fang, H.4    Green, N.5
  • 66
    • 0036437316 scopus 로고    scopus 로고
    • Proteolysis and sterol regulation
    • Hampton RY. Proteolysis and sterol regulation. Annu Rev Cell Dev Biol 2002;18:345-378.
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 345-378
    • Hampton, R.Y.1
  • 67
    • 0033546303 scopus 로고    scopus 로고
    • Oligomerization state influences the degradation rate of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Cheng HH, Xu L, Kumagai H, Simoni RD. Oligomerization state influences the degradation rate of 3-hydroxy-3-methylglutaryl-CoA reductase. J Biol Chem 1999;274:17171-17178.
    • (1999) J Biol Chem , vol.274 , pp. 17171-17178
    • Cheng, H.H.1    Xu, L.2    Kumagai, H.3    Simoni, R.D.4
  • 69
    • 1842832344 scopus 로고    scopus 로고
    • Two distinctly localized p-type ATPases collaborate to maintain organelle homeostasis required for glycoprotein processing and quality control
    • Vashist S, Frank CG, Jakob CA, Ng DT. Two distinctly localized p-type ATPases collaborate to maintain organelle homeostasis required for glycoprotein processing and quality control. Mol Biol Cell 2002;13:3955-3966.
    • (2002) Mol Biol Cell , vol.13 , pp. 3955-3966
    • Vashist, S.1    Frank, C.G.2    Jakob, C.A.3    Ng, D.T.4
  • 70
  • 71
    • 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. Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation. J Biol Chem 2001;276:10663-10669.
    • (2001) J Biol Chem , vol.276 , pp. 10663-10669
    • Deak, P.M.1    Wolf, D.H.2
  • 72
    • 0037124084 scopus 로고    scopus 로고
    • Complexity in the secretory pathway: The assembly and secretion of apolipoprotein B-containing lipoproteins
    • Fisher EA, Ginsberg HN. Complexity in the secretory pathway: the assembly and secretion of apolipoprotein B-containing lipoproteins. J Biol Chem 2002;277:17377-17380.
    • (2002) J Biol Chem , vol.277 , pp. 17377-17380
    • Fisher, E.A.1    Ginsberg, H.N.2
  • 73
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma J, Wollmann R, Lindquist S. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 2003;298:1781-1785.
    • (2003) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 75
    • 0037099080 scopus 로고    scopus 로고
    • The cellular fate of mutant rhodopsin: Quality control, degradation and aggresome formation
    • Saliba RS, Munro PM, Luthert PJ, Cheetham ME. The cellular fate of mutant rhodopsin: quality control, degradation and aggresome formation. J Cell Sci 2002;115:2907-2918.
    • (2002) J Cell Sci , vol.115 , pp. 2907-2918
    • Saliba, R.S.1    Munro, P.M.2    Luthert, P.J.3    Cheetham, M.E.4
  • 76
    • 0037072934 scopus 로고    scopus 로고
    • A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system
    • Illing ME, Rajan RS, Bence NF, Kopito RR. A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system. J Biol Chem 2002;277:34150-34160.
    • (2002) J Biol Chem , vol.277 , pp. 34150-34160
    • Illing, M.E.1    Rajan, R.S.2    Bence, N.F.3    Kopito, R.R.4
  • 77
    • 0034813890 scopus 로고    scopus 로고
    • Chaperoning the maturation of the cystic fibrosis transmembrane conductance regulator
    • Brodsky JL. Chaperoning the maturation of the cystic fibrosis transmembrane conductance regulator. Am J Physiol Lung Cell Mol Physiol 2001;281:L39-L42.
    • (2001) Am J Physiol Lung Cell Mol Physiol , vol.281
    • Brodsky, J.L.1
  • 79
    • 85047684827 scopus 로고    scopus 로고
    • α1-antitrypsin polymerization and the serpinopathies: Pathobiology and prospects for therapy
    • Lomas DA, Mahadev R. α1-Antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy. J Clin Invest 2002;110:1585-1590.
    • (2002) J Clin Invest , vol.110 , pp. 1585-1590
    • Lomas, D.A.1    Mahadev, R.2
  • 80
    • 0028593988 scopus 로고
    • A lag in intracellular degradation of mutant alpha 1-antitrypsin correlates with the liver disease phenotype in homozygous PiZZ alpha 1-antitrypsin deficiency
    • Wu Y, Whitman I, Molmenti E, Moore K, Hippenmeyer P, Perlmutter DH. A lag in intracellular degradation of mutant alpha 1-antitrypsin correlates with the liver disease phenotype in homozygous PiZZ alpha 1-antitrypsin deficiency. Proc Natl Acad Sci USA 1994;91:9014-9018.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9014-9018
    • Wu, Y.1    Whitman, I.2    Molmenti, E.3    Moore, K.4    Hippenmeyer, P.5    Perlmutter, D.H.6
  • 81
    • 0028947440 scopus 로고
    • Mutations which impede loop/sheet polymerization enhance the secretion of human alpha 1-antitrypsin deficiency variants
    • Sidhar SK, Lomas DA, Carrell RW, Foreman RC. Mutations which impede loop/sheet polymerization enhance the secretion of human alpha 1-antitrypsin deficiency variants. J Biol Chem 1995;270:8393-8396.
    • (1995) J Biol Chem , vol.270 , pp. 8393-8396
    • Sidhar, S.K.1    Lomas, D.A.2    Carrell, R.W.3    Foreman, R.C.4
  • 82
    • 0036510604 scopus 로고    scopus 로고
    • 6-Mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization. Implications for the prevention of Z alpha(1)-antitrypsin-related cirrhosis
    • Mahadeva R, Dafforn TR, Carrell RW, Lomas DA. 6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization. Implications for the prevention of Z alpha(1)-antitrypsin-related cirrhosis. J Biol Chem 2002;277:6771-6774.
    • (2002) J Biol Chem , vol.277 , pp. 6771-6774
    • Mahadeva, R.1    Dafforn, T.R.2    Carrell, R.W.3    Lomas, D.A.4
  • 83
    • 0033882702 scopus 로고    scopus 로고
    • Fibrinogen brescia: Hepatic endoplasmic reticulum storage and hypofibrinogenemia because of a gamma284 Gly → Arg mutation
    • Brennan SO, Wyatt J, Medicina D, Callea F, George PM. Fibrinogen brescia: hepatic endoplasmic reticulum storage and hypofibrinogenemia because of a gamma284 Gly → Arg mutation. Am J Pathol 2000;157:189-196.
    • (2000) Am J Pathol , vol.157 , pp. 189-196
    • Brennan, S.O.1    Wyatt, J.2    Medicina, D.3    Callea, F.4    George, P.M.5
  • 84
    • 0036707542 scopus 로고    scopus 로고
    • Novel fibrinogen gamma 375 Arg → Trp mutation (fibrinogen aguadilla) causes hepatic endoplasmic reticulum storage and hypofibrinogenemia
    • Brennan SO, Maghzal G, Shneider BL, Gordon R, Magid MS, George PM. Novel fibrinogen gamma 375 Arg → Trp mutation (fibrinogen aguadilla) causes hepatic endoplasmic reticulum storage and hypofibrinogenemia. Hepatology 2002;36:652-658.
    • (2002) Hepatology , vol.36 , pp. 652-658
    • Brennan, S.O.1    Maghzal, G.2    Shneider, B.L.3    Gordon, R.4    Magid, M.S.5    George, P.M.6
  • 85
    • 0036839616 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum-associated degradation in CHO cells resistant to cholera toxin. Pseudomonas aeruginosa exotoxin A, and ricin
    • Teter K, Holmes RK. Inhibition of endoplasmic reticulum-associated degradation in CHO cells resistant to cholera toxin, Pseudomonas aeruginosa exotoxin A, and ricin. Infect Immun 2002;70:6172-6179.
    • (2002) Infect Immun , vol.70 , pp. 6172-6179
    • Teter, K.1    Holmes, R.K.2
  • 86
    • 0037066109 scopus 로고    scopus 로고
    • The low lysine content of ricin A chain reduces the risk of proteolytic degradation after translocation from the endoplasmic reticulum to the cytosol
    • Deeks ED, Cook JP, Day PJ, Smith DC, Roberts LM, Lord JM. The low lysine content of ricin A chain reduces the risk of proteolytic degradation after translocation from the endoplasmic reticulum to the cytosol. Biochemistry 2002;41:3405-3413.
    • (2002) Biochemistry , vol.41 , pp. 3405-3413
    • Deeks, E.D.1    Cook, J.P.2    Day, P.J.3    Smith, D.C.4    Roberts, L.M.5    Lord, J.M.6
  • 87
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai B, Rodighiero C, Lencer WI, Rapoport TA. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 2001;104:937-948.
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 88
    • 0033607688 scopus 로고    scopus 로고
    • Dependence of ricin toxicity on translocation of the toxin A-chain from the endoplasmic reticulum to the cytosol
    • Wesche J, Rapak A, Olsnes S. Dependence of ricin toxicity on translocation of the toxin A-chain from the endoplasmic reticulum to the cytosol. J Biol Chem 1999;274:34443-34449.
    • (1999) J Biol Chem , vol.274 , pp. 34443-34449
    • Wesche, J.1    Rapak, A.2    Olsnes, S.3
  • 90
    • 0036479140 scopus 로고    scopus 로고
    • Membrane-specific, host-derived factors are required for US2- and US11-mediated degradation of major histocompatibility complex class I molecules
    • Furman MH, Ploegh HL, Tortorella D. Membrane-specific, host-derived factors are required for US2- and US11-mediated degradation of major histocompatibility complex class I molecules. J Biol Chem 2002;277:3258-3267.
    • (2002) J Biol Chem , vol.277 , pp. 3258-3267
    • Furman, M.H.1    Ploegh, H.L.2    Tortorella, D.3
  • 91
    • 0035463587 scopus 로고    scopus 로고
    • Ssh1p determines the translocation and dislocation capacities of the yeast endoplasmic reticulum
    • Wilkinson BM, Tyson JR, Stirling CJ. Ssh1p determines the translocation and dislocation capacities of the yeast endoplasmic reticulum. Dev Cell 2001;1:401-409.
    • (2001) Dev Cell , vol.1 , pp. 401-409
    • Wilkinson, B.M.1    Tyson, J.R.2    Stirling, C.J.3
  • 92
    • 0029788023 scopus 로고    scopus 로고
    • Degradation of a mutant secretory protein, alphal-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity
    • Qu D, Teckman JH, Omura S, Perlmutter DH. Degradation of a mutant secretory protein, alphal-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J Biol Chem 1996;271:22791-22795.
    • (1996) J Biol Chem , vol.271 , pp. 22791-22795
    • Qu, D.1    Teckman, J.H.2    Omura, S.3    Perlmutter, D.H.4
  • 94
    • 0024788009 scopus 로고    scopus 로고
    • A frameshift mutation in a patient with Tay-Sachs disease causes premature termination and defective intracellular transport of the alpha-subunit of beta-hexosaminidase
    • Lau MM, Neufeld EF. A frameshift mutation in a patient with Tay-Sachs disease causes premature termination and defective intracellular transport of the alpha-subunit of beta-hexosaminidase. J Biol Chem 1998;264:21376-21380.
    • (1998) J Biol Chem , vol.264 , pp. 21376-21380
    • Lau, M.M.1    Neufeld, E.F.2
  • 95
    • 0030069139 scopus 로고    scopus 로고
    • The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domains
    • Schubert U, Bour S, Ferrer-Montiel AV, Montal M, Maldarell F, Strebel K. The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domains. J Virol 1996;70:809-819.
    • (1996) J Virol , vol.70 , pp. 809-819
    • Schubert, U.1    Bour, S.2    Ferrer-Montiel, A.V.3    Montal, M.4    Maldarell, F.5    Strebel, K.6
  • 96
    • 0033600789 scopus 로고    scopus 로고
    • Proteasomal degradation of unassembled mutant type I collagen pro-alpha1(1) chains
    • Fitzgerald J, Lamande SR, Bateman JF. Proteasomal degradation of unassembled mutant type I collagen pro-alpha1(1) chains. J Biol Chem 1999;274:27392-27398.
    • (1999) J Biol Chem , vol.274 , pp. 27392-27398
    • Fitzgerald, J.1    Lamande, S.R.2    Bateman, J.F.3
  • 97
    • 0034047183 scopus 로고    scopus 로고
    • Intracellular transport, assembly, and degradation of wild-type and disease-linked mutant gap junction proteins
    • VanSlyke JK, Deschenes SM, Musil LS. Intracellular transport, assembly, and degradation of wild-type and disease-linked mutant gap junction proteins. Mol Biol Cell 2000;11:1933-1946.
    • (2000) Mol Biol Cell , vol.11 , pp. 1933-1946
    • VanSlyke, J.K.1    Deschenes, S.M.2    Musil, L.S.3
  • 98
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein JL, Brown MS. Regulation of the mevalonate pathway. Nature 1990;343:425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 100
    • 0023720346 scopus 로고    scopus 로고
    • Transport-deficient mutations in the low density lipoprotein receptor. Alterations in the cysteine-rich and cysteine-poor regions of the protein block intracellular transport
    • Esser V, Russell DW. Transport-deficient mutations in the low density lipoprotein receptor. Alterations in the cysteine-rich and cysteine-poor regions of the protein block intracellular transport. J Biol Chem 1998;263:13276-13281.
    • (1998) J Biol Chem , vol.263 , pp. 13276-13281
    • Esser, V.1    Russell, D.W.2
  • 101
    • 0038701031 scopus 로고    scopus 로고
    • A single viral protein HCMV US2 affects antigen presentation and intracellular iron homeostasis by degradation of classical HLA class I and HFE molecules
    • Vahdati-Ben Arieh S, Laham N, Schechter C, Yewdell JW, Coligan JE, Ehrlich R. A single viral protein HCMV US2 affects antigen presentation and intracellular iron homeostasis by degradation of classical HLA class I and HFE molecules. Blood 2002;101:2858-2864.
    • (2002) Blood , vol.101 , pp. 2858-2864
    • Vahdati-Ben Arieh, S.1    Laham, N.2    Schechter, C.3    Yewdell, J.W.4    Coligan, J.E.5    Ehrlich, R.6
  • 102
    • 0032526264 scopus 로고    scopus 로고
    • A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation
    • DeLeo FR, Goedken M, McCormick SJ, Nauseef WM. A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/ proteasome degradation. J Clin Invest 1998;101:2900-2909.
    • (1998) J Clin Invest , vol.101 , pp. 2900-2909
    • DeLeo, F.R.1    Goedken, M.2    McCormick, S.J.3    Nauseef, W.M.4
  • 103
    • 0036345454 scopus 로고    scopus 로고
    • CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity
    • lmai Y, Soda M, Hatakeyama S, Akagi T, Hashikawa T, Nakayama KI, Takahashi R. CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol Cell 2002;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
  • 104
    • 0032516924 scopus 로고    scopus 로고
    • Proparathyroid hormone-related protein is associated with the chaperone protein BIP and undergoes proteasome-mediated degradation
    • Meerovitch K, Wing S, Goltzman D. Proparathyroid Hormone-related Protein Is Associated with the Chaperone Protein BiP and Undergoes Proteasome-mediated Degradation. J Biol Chem 1998;273:21025-21030.
    • (1998) J Biol Chem , vol.273 , pp. 21025-21030
    • Meerovitch, K.1    Wing, S.2    Goltzman, D.3
  • 105
    • 0030481624 scopus 로고    scopus 로고
    • Congenital hypothyroid goiter with deficient thyroglobulin. Identification of an endoplasmic reticulum storage disease with induction of molecular chaperones
    • Medeiros-Neto G, Kim PS, Yoo SE, Vono J, Targovnik HM, Camargo R, Hossain SA, Arvan P. Congenital hypothyroid goiter with deficient thyroglobulin. Identification of an endoplasmic reticulum storage disease with induction of molecular chaperones. J Clin Invest 1996;98:2838-2844.
    • (1996) J Clin Invest , vol.98 , pp. 2838-2844
    • Medeiros-Neto, G.1    Kim, P.S.2    Yoo, S.E.3    Vono, J.4    Targovnik, H.M.5    Camargo, R.6    Hossain, S.A.7    Arvan, P.8
  • 106
    • 0030912157 scopus 로고    scopus 로고
    • Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells
    • Halaban R, Cheng E, Zhang Y, Moellmann G, Hanlon D, Michalak M, Setaluri V, Hebert DN. Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proc Natl Acad Sci USA 1997;94:6210-6215.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6210-6215
    • Halaban, R.1    Cheng, E.2    Zhang, Y.3    Moellmann, G.4    Hanlon, D.5    Michalak, M.6    Setaluri, V.7    Hebert, D.N.8
  • 107
    • 0032167856 scopus 로고    scopus 로고
    • Functional expression of the Wilson disease protein reveals mislocalization and impaired copper-dependent trafficking of the common H1069Q mutation
    • Payne AS, Kelly EJ, Gitlin JD. Functional expression of the Wilson disease protein reveals mislocalization and impaired copper-dependent trafficking of the common H1069Q mutation. Proc Natl Acad Sci USA 1998;95:10854-10859.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10854-10859
    • Payne, A.S.1    Kelly, E.J.2    Gitlin, J.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.