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Volumn 4, Issue , 2007, Pages

Requirements for the selective degradation of CD4 receptor molecules by the human immunodeficiency virus type 1 Vpu protein in the endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ARGININE; CD4 ANTIGEN; CELL CYCLE PROTEIN; CELL CYCLE PROTEIN 48; LYSINE; PROTEIN P97; SODIUM CARBONATE; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; VPU PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS PROTEIN; UBIQUITIN; VIRUS PROTEIN; VPU PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 37749032764     PISSN: None     EISSN: 17424690     Source Type: Journal    
DOI: 10.1186/1742-4690-4-75     Document Type: Article
Times cited : (82)

References (57)
  • 2
    • 2342503325 scopus 로고    scopus 로고
    • Role of CD4 receptor down-regulation during HIV-1 infection
    • 10.2174/1570162043485086 15053340
    • Levesque K Finzi A Binette J Cohen EA Role of CD4 receptor down-regulation during HIV-1 infection Curr HIV Res 2004, 2:51:59 10.2174/1570162043485086 15053340
    • (2004) Curr HIV Res , vol.2 , pp. 51-59
    • Levesque, K.1    Finzi, A.2    Binette, J.3    Cohen, E.A.4
  • 3
    • 0042346262 scopus 로고    scopus 로고
    • Vpu exerts a positive effect on HIV-1 infectivity by down-modulating CD4 receptor molecules at the surface of HIV-1-producing cells
    • 10.1074/jbc.M300327200 12746459
    • Levesque K Zhao YS Cohen EA Vpu exerts a positive effect on HIV-1 infectivity by down-modulating CD4 receptor molecules at the surface of HIV-1-producing cells J Biol Chem 2003, 278:28346-28353 10.1074/ jbc.M300327200 12746459
    • (2003) J Biol Chem , vol.278 , pp. 28346-28353
    • Levesque, K.1    Zhao, Y.S.2    Cohen, E.A.3
  • 4
    • 33746799703 scopus 로고    scopus 로고
    • Contribution of Vpu, Env, and Nef to CD4 down-modulation and resistance of human immunodeficiency virus type 1-infected T cells to superinfection
    • 1563805 16873261 10.1128/JVI.00252-06
    • Wildum S Schindler M Munch J Kirchhoff F Contribution of Vpu, Env, and Nef to CD4 down-modulation and resistance of human immunodeficiency virus type 1-infected T cells to superinfection J Virol 2006, 80:8047-8059 1563805 16873261 10.1128/JVI.00252-06
    • (2006) J Virol , vol.80 , pp. 8047-8059
    • Wildum, S.1    Schindler, M.2    Munch, J.3    Kirchhoff, F.4
  • 5
    • 0028924785 scopus 로고
    • Human immunodeficiency virus type 1 Nef induces accumulation of CD4 in early endosomes
    • 188604 7983750
    • Schwartz O Dautry-Varsat A Goud B Marechal V Subtil A Heard JM Danos O Human immunodeficiency virus type 1 Nef induces accumulation of CD4 in early endosomes J Virol 1995, 69:528-533 188604 7983750
    • (1995) J Virol , vol.69 , pp. 528-533
    • Schwartz, O.1    Dautry-Varsat, A.2    Goud, B.3    Marechal, V.4    Subtil, A.5    Heard, J.M.6    Danos, O.7
  • 6
    • 0010296944 scopus 로고
    • Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160
    • 282803 2849111 10.1073/pnas.85.24.9580
    • Willey RL Bonifacino JS Potts BJ Martin MA Klausner RD Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160 Proc Natl Acad Sci USA 1988, 85:9580-9584 282803 2849111 10.1073/pnas.85.24.9580
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 9580-9584
    • Willey, R.L.1    Bonifacino, J.S.2    Potts, B.J.3    Martin, M.A.4    Klausner, R.D.5
  • 7
    • 0025183723 scopus 로고
    • CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor
    • 248611 2214026
    • Crise B Buonocore L Rose JK CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor J Virol 1990, 64:5585-5593 248611 2214026
    • (1990) J Virol , vol.64 , pp. 5585-5593
    • Crise, B.1    Buonocore, L.2    Rose, J.K.3
  • 8
    • 0026567269 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein regulates the formation of intracellular gp160-CD4 complexes
    • 238279 1727486
    • Willey RL Maldarelli F Martin MA Strebel K Human immunodeficiency virus type 1 Vpu protein regulates the formation of intracellular gp160-CD4 complexes J Virol 1992, 66:226-234 238279 1727486
    • (1992) J Virol , vol.66 , pp. 226-234
    • Willey, R.L.1    Maldarelli, F.2    Martin, M.A.3    Strebel, K.4
  • 9
    • 0023729963 scopus 로고
    • Identification of a protein encoded by the vpu gene of HIV-1
    • 10.1038/334532a0 3043230
    • Cohen EA Terwilliger EF Sodroski JG Haseltine WA Identification of a protein encoded by the vpu gene of HIV-1 Nature 1988, 334:532-534 10.1038/334532a0 3043230
    • (1988) Nature , vol.334 , pp. 532-534
    • Cohen, E.A.1    Terwilliger, E.F.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 10
    • 0023677668 scopus 로고
    • A novel gene of HIV-1, vpu, and its 16-kilodalton product
    • 10.1126/science.3261888 3261888
    • Strebel K Klimkait T Martin MA A novel gene of HIV-1, vpu, and its 16-kilodalton product Science 1988, 241:1221-1223 10.1126/ science.3261888 3261888
    • (1988) Science , vol.241 , pp. 1221-1223
    • Strebel, K.1    Klimkait, T.2    Martin, M.A.3
  • 11
    • 0025343127 scopus 로고
    • Genetic organization of a chimpanzee lentivirus related to HIV-1
    • 10.1038/345356a0 2188136
    • Huet T Cheynier R Meyerhans A Roelants G Wain-Hobson S Genetic organization of a chimpanzee lentivirus related to HIV-1 Nature 1990, 345:356-359 10.1038/345356a0 2188136
    • (1990) Nature , vol.345 , pp. 356-359
    • Huet, T.1    Cheynier, R.2    Meyerhans, A.3    Roelants, G.4    Wain-Hobson, S.5
  • 12
    • 7444258608 scopus 로고    scopus 로고
    • Recent advances in the understanding of HIV-1 Vpu accessory protein functions
    • 10.2174/1568008043339695 15578980
    • Binette J Cohen EA Recent advances in the understanding of HIV-1 Vpu accessory protein functions Curr Drug Targets Immune Endocr Metabol Disord 2004, 4:297-307 10.2174/1568008043339695 15578980
    • (2004) Curr Drug Targets Immune Endocr Metabol Disord , vol.4 , pp. 297-307
    • Binette, J.1    Cohen, E.A.2
  • 13
    • 0027209705 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein is an oligomeric type I integral membrane protein
    • 237897 8331740
    • Maldarelli F Chen MY Willey RL Strebel K Human immunodeficiency virus type 1 Vpu protein is an oligomeric type I integral membrane protein J Virol 1993, 67:5056-5061 237897 8331740
    • (1993) J Virol , vol.67 , pp. 5056-5061
    • Maldarelli, F.1    Chen, M.Y.2    Willey, R.L.3    Strebel, K.4
  • 14
    • 0026595974 scopus 로고
    • Human-immunodeficiency-virus-type-1-encoded Vpu protein is phosphorylated by casein kinase II
    • 10.1111/j.1432-1033.1992.tb16707.x 1541298
    • Schubert U Schneider T Henklein P Hoffmann K Berthold E Hauser H Pauli G Porstmann T Human-immunodeficiency-virus-type-1-encoded Vpu protein is phosphorylated by casein kinase II Eur J Biochem 1992, 204:875-883 10.1111/j.1432-1033.1992.tb16707.x 1541298
    • (1992) Eur J Biochem , vol.204 , pp. 875-883
    • Schubert, U.1    Schneider, T.2    Henklein, P.3    Hoffmann, K.4    Berthold, E.5    Hauser, H.6    Pauli, G.7    Porstmann, T.8
  • 17
    • 0025139857 scopus 로고
    • The human immunodeficiency virus type 1-specific protein vpu is required for efficient virus maturation and release
    • 249152 2404139
    • Klimkait T Strebel K Hoggan MD Martin MA Orenstein JM The human immunodeficiency virus type 1-specific protein vpu is required for efficient virus maturation and release J Virol 1990, 64:621-629 249152 2404139
    • (1990) J Virol , vol.64 , pp. 621-629
    • Klimkait, T.1    Strebel, K.2    Hoggan, M.D.3    Martin, M.A.4    Orenstein, J.M.5
  • 18
    • 0344303622 scopus 로고    scopus 로고
    • Viral protein U counteracts a human host cell restriction that inhibits HIV-1 particle production
    • 299932 14657387 10.1073/pnas.2433165100
    • Varthakavi V Smith RM Bour SP Strebel K Spearman P Viral protein U counteracts a human host cell restriction that inhibits HIV-1 particle production Proc Natl Acad Sci USA 2003, 100:15154-15159 299932 14657387 10.1073/pnas.2433165100
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15154-15159
    • Varthakavi, V.1    Smith, R.M.2    Bour, S.P.3    Strebel, K.4    Spearman, P.5
  • 19
    • 0028857927 scopus 로고
    • Augmentation of virus secretion by the human immunodeficiency virus type 1 Vpu protein is cell type independent and occurs in cultured human primary macrophages and lymphocytes
    • 189711 7494279
    • Schubert U Clouse KA Strebel K Augmentation of virus secretion by the human immunodeficiency virus type 1 Vpu protein is cell type independent and occurs in cultured human primary macrophages and lymphocytes J Virol 1995, 69:7699-7711 189711 7494279
    • (1995) J Virol , vol.69 , pp. 7699-7711
    • Schubert, U.1    Clouse, K.A.2    Strebel, K.3
  • 20
    • 0026452726 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4
    • 240416 1433512
    • Willey RL Maldarelli F Martin MA Strebel K Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4 J Virol 1992, 66:7193-7200 240416 1433512
    • (1992) J Virol , vol.66 , pp. 7193-7200
    • Willey, R.L.1    Maldarelli, F.2    Martin, M.A.3    Strebel, K.4
  • 21
    • 0028816432 scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: Implications for the mechanism of degradation
    • 188742 7853484
    • Bour S Schubert U Strebel K The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradation J Virol 1995, 69:1510-1520 188742 7853484
    • (1995) J Virol , vol.69 , pp. 1510-1520
    • Bour, S.1    Schubert, U.2    Strebel, K.3
  • 22
    • 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
    • 10.1016/S1097-2765(00)80056-8 9660940
    • Margottin F Bour SP Durand H Selig L Benichou S Richard V Thomas D Strebel K Benarous R 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 1998, 1:565-574 10.1016/ S1097-2765(00)80056-8 9660940
    • (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
  • 23
    • 1942502180 scopus 로고    scopus 로고
    • The many faces of beta-TrCP E3 ubiquitin ligases: Reflections in the magic mirror of cancer
    • 10.1038/sj.onc.1207389 15021890
    • Fuchs SY Spiegelman VS Kumar KG The many faces of beta-TrCP E3 ubiquitin ligases: Reflections in the magic mirror of cancer Oncogene 2004, 23:2028-2036 10.1038/sj.onc.1207389 15021890
    • (2004) Oncogene , vol.23 , pp. 2028-2036
    • Fuchs, S.Y.1    Spiegelman, V.S.2    Kumar, K.G.3
  • 24
    • 0031935031 scopus 로고    scopus 로고
    • CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway
    • 109526 9499087
    • Schubert U Anton LC Bacik I Cox JH Bour S Bennink JR Orlowski M Strebel K Yewdell JW CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway J Virol 1998, 72:2280-2288 109526 9499087
    • (1998) J Virol , vol.72 , pp. 2280-2288
    • Schubert, U.1    Anton, L.C.2    Bacik, I.3    Cox, J.H.4    Bour, S.5    Bennink, J.R.6    Orlowski, M.7    Strebel, K.8    Yewdell, J.W.9
  • 25
    • 23144451257 scopus 로고    scopus 로고
    • ERAD: The long road to destruction
    • 10.1038/ncb0805-766 16056268
    • Meusser B Hirsch C Jarosch E Sommer T ERAD: The long road to destruction Nat Cell Biol 2005, 7:766-772 10.1038/ncb0805-766 16056268
    • (2005) Nat Cell Biol , vol.7 , pp. 766-772
    • Meusser, B.1    Hirsch, C.2    Jarosch, E.3    Sommer, T.4
  • 26
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • 10.1038/nature02592 15215855
    • Lilley BN Ploegh HL A membrane protein required for dislocation of misfolded proteins from the ER Nature 2004, 429:834-840 10.1038/ nature02592 15215855
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 27
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • 10.1038/nature02656 15215856
    • Ye Y Shibata Y Yun C Ron D Rapoport TA A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol Nature 2004, 429:841-847 10.1038/nature02656 15215856
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 28
    • 33646552435 scopus 로고    scopus 로고
    • The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment
    • 1456945 16619026 10.1038/sj.emboj.7601088
    • Gauss R Sommer T Jarosch E The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment EMBO J 2006, 25:1827-1835 1456945 16619026 10.1038/sj.emboj.7601088
    • (2006) EMBO J , vol.25 , pp. 1827-1835
    • Gauss, R.1    Sommer, T.2    Jarosch, E.3
  • 29
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • 10.1038/384432a0 8945469
    • Wiertz EJHJ Tortorella D Bogyo M Yu J Mothes W Jones TR Rapoport TA Ploegh HL Sec61-mediated transfer of membrane protein from the endoplasmic reticulum to the proteasome for destruction Nature 1996, 384:432-438 10.1038/384432a0 8945469
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.H.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
  • 30
    • 0029915568 scopus 로고    scopus 로고
    • The Human Cytomegalovirus US11 Gene Product Dislocates MHC Class I Heavy Chains from the Endoplasmic Reticulum to the Cytosol
    • 10.1016/S0092-8674(00)81054-5 8625414
    • Wiertz EJHJ Jones TR Sun L Bogyo M Geuze HJ Ploegh HL The Human Cytomegalovirus US11 Gene Product Dislocates MHC Class I Heavy Chains from the Endoplasmic Reticulum to the Cytosol Cell 1996, 84:769-779 10.1016/S0092-8674(00)81054-5 8625414
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.H.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5    Ploegh, H.L.6
  • 31
    • 0032536903 scopus 로고    scopus 로고
    • Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: Importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes
    • 10.1084/jem.187.6.835 9500786
    • Yang M Omura S Bonifacino JS Weissman AM Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes J Exp Med 1998, 187:835-846 10.1084/jem.187.6.835 9500786
    • (1998) J Exp Med , vol.187 , pp. 835-846
    • Yang, M.1    Omura, S.2    Bonifacino, J.S.3    Weissman, A.M.4
  • 32
    • 0041816452 scopus 로고    scopus 로고
    • Ubiquitinylation of the cytosolic domain of a type I membrane protein is not required to initiate its dislocation from the endoplasmic reticulum
    • 10.1074/jbc.M300913200 12832421
    • Furman MH Loureiro J Ploegh HL Tortorella D Ubiquitinylation of the cytosolic domain of a type I membrane protein is not required to initiate its dislocation from the endoplasmic reticulum J Biol Chem 2003, 278:34804-34811 10.1074/jbc.M300913200 12832421
    • (2003) J Biol Chem , vol.278 , pp. 34804-34811
    • Furman, M.H.1    Loureiro, J.2    Ploegh, H.L.3    Tortorella, D.4
  • 33
    • 0035167960 scopus 로고    scopus 로고
    • Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol
    • 58612 11514634
    • 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 58612 11514634
    • (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
  • 34
    • 1942534656 scopus 로고    scopus 로고
    • Vpu-mediated degradation of CD4 reconstituted in yeast reveals mechanistic differences to cellular ER-associated protein degradation
    • 10.1016/S1097-2765(04)00212-6 15099523
    • Meusser B Sommer T Vpu-mediated degradation of CD4 reconstituted in yeast reveals mechanistic differences to cellular ER-associated protein degradation Mol Cell 2004, 14:247-258 10.1016/S1097-2765(04)00212-6 15099523
    • (2004) Mol Cell , vol.14 , pp. 247-258
    • Meusser, B.1    Sommer, T.2
  • 35
    • 0031057925 scopus 로고    scopus 로고
    • Rapid degradation of CD4 in cells expressing human immunodeficiency virus type 1 Env and Vpu is blocked by proteasome inhibitors
    • 9049413
    • Fujita K Omura S Silver J Rapid degradation of CD4 in cells expressing human immunodeficiency virus type 1 Env and Vpu is blocked by proteasome inhibitors J Gen Virol 1997, 78(Pt 3):619-625 9049413
    • (1997) J Gen Virol , vol.78 , Issue.PART 3 , pp. 619-625
    • Fujita, K.1    Omura, S.2    Silver, J.3
  • 36
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • 10.1126/science.2538923 2538923
    • Chau V Tobias JW Bachmair A Marriott D Ecker DJ Gonda DK Varshavsky A A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein Science 1989, 243:1576-1583 10.1126/science.2538923 2538923
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6    Varshavsky, A.7
  • 37
    • 0025838227 scopus 로고
    • Epitope-tagged ubiquitin. A new probe for analyzing ubiquitin function
    • 1718971
    • Ellison MJ Hochstrasser M Epitope-tagged ubiquitin. A new probe for analyzing ubiquitin function J Biol Chem 1991, 266:21150-21157 1718971
    • (1991) J Biol Chem , vol.266 , pp. 21150-21157
    • Ellison, M.J.1    Hochstrasser, M.2
  • 38
    • 4644243461 scopus 로고    scopus 로고
    • Ubiquitin is conjugated by membrane ubiquitin ligase to three sites, including the N terminus, in transmembrane region of mammalian 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • 10.1074/jbc.M405935200 15247208
    • Doolman R Leichner GS Avner R Roitelman J Ubiquitin is conjugated by membrane ubiquitin ligase to three sites, including the N terminus, in transmembrane region of mammalian 3-hydroxy-3-methylglutaryl coenzyme A reductase J Biol Chem 2004, 279:38184-38193 10.1074/jbc.M405935200 15247208
    • (2004) J Biol Chem , vol.279 , pp. 38184-38193
    • Doolman, R.1    Leichner, G.S.2    Avner, R.3    Roitelman, J.4
  • 39
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • 384367 10811609 10.1093/emboj/19.10.2181
    • Meyer HH Shorter JG Seemann J Pappin D Warren G A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways EMBO J 2000, 19:2181-2192 384367 10811609 10.1093/ emboj/19.10.2181
    • (2000) EMBO J , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 40
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • 10.1038/414652a 11740563
    • Ye Y Meyer HH Rapoport TA The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol Nature 2001, 414:652-656 10.1038/414652a 11740563
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 41
    • 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
    • 10.1083/jcb.200302169 12847084
    • Ye Y Meyer HH Rapoport TA 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 2003, 162:71-84 10.1083/jcb.200302169 12847084
    • (2003) J Cell Biol , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 42
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • 10.1074/jbc.M313093200 14672928
    • Mehle A Strack B Ancuta P Zhang C McPike M Gabuzda D Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway J Biol Chem 2004, 279:7792-7798 10.1074/ jbc.M313093200 14672928
    • (2004) J Biol Chem , vol.279 , pp. 7792-7798
    • Mehle, A.1    Strack, B.2    Ancuta, P.3    Zhang, C.4    McPike, M.5    Gabuzda, D.6
  • 43
    • 33749569154 scopus 로고    scopus 로고
    • Ubiquitination of MHC class I heavy chains is essential for dislocation by human cytomegalovirus-encoded US2 but not US11
    • 10.1074/jbc.M602248200 16877758
    • Hassink GC Barel MT Van Voorden SB Kikkert M Wiertz EJ Ubiquitination of MHC class I heavy chains is essential for dislocation by human cytomegalovirus-encoded US2 but not US11 J Biol Chem 2006, 281:30063-30071 10.1074/jbc.M602248200 16877758
    • (2006) J Biol Chem , vol.281 , pp. 30063-30071
    • Hassink, G.C.1    Barel, M.T.2    Van Voorden, S.B.3    Kikkert, M.4    Wiertz, E.J.5
  • 44
    • 34249042608 scopus 로고    scopus 로고
    • Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3
    • 10.1083/jcb.200611063 17502423
    • Wang X Herr RA Chua WJ Lybarger L Wiertz EJ Hansen TH Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3 J Cell Biol 2007, 177:613-624 10.1083/jcb.200611063 17502423
    • (2007) J Cell Biol , vol.177 , pp. 613-624
    • Wang, X.1    Herr, R.A.2    Chua, W.J.3    Lybarger, L.4    Wiertz, E.J.5    Hansen, T.H.6
  • 45
    • 21744433861 scopus 로고    scopus 로고
    • Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase
    • 10.1126/science.1110340 15994556
    • Cadwell K Coscoy L Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase Science 2005, 309:127-130 10.1126/science.1110340 15994556
    • (2005) Science , vol.309 , pp. 127-130
    • Cadwell, K.1    Coscoy, L.2
  • 46
    • 4444355303 scopus 로고    scopus 로고
    • Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein
    • 10.1074/jbc.M402468200 15252059
    • Huyer G Piluek WF Fansler Z Kreft SG Hochstrasser M Brodsky JL Michaelis S Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein J Biol Chem 2004, 279:38369-38378 10.1074/jbc.M402468200 15252059
    • (2004) J Biol Chem , vol.279 , pp. 38369-38378
    • Huyer, G.1    Piluek, W.F.2    Fansler, Z.3    Kreft, S.G.4    Hochstrasser, M.5    Brodsky, J.L.6    Michaelis, S.7
  • 47
    • 2442451126 scopus 로고    scopus 로고
    • Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control
    • 10.1083/jcb.200309132 15078901
    • Vashist S Ng DT Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control J Cell Biol 2004, 165:41-52 10.1083/ jcb.200309132 15078901
    • (2004) J Cell Biol , vol.165 , pp. 41-52
    • Vashist, S.1    Ng, D.T.2
  • 48
    • 33746228127 scopus 로고    scopus 로고
    • Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins
    • 10.1016/j.cell.2006.05.043 16873066
    • Carvalho P Goder V Rapoport TA Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins Cell 2006, 126:361-373 10.1016/j.cell.2006.05.043 16873066
    • (2006) Cell , vol.126 , pp. 361-373
    • Carvalho, P.1    Goder, V.2    Rapoport, T.A.3
  • 49
    • 33746253687 scopus 로고    scopus 로고
    • Have you HRD? Understanding ERAD is DOAble!
    • 10.1016/j.cell.2006.07.001 16873052
    • Ismail N Ng DT Have you HRD? Understanding ERAD is DOAble! Cell 2006, 126:237-239 10.1016/j.cell.2006.07.001 16873052
    • (2006) Cell , vol.126 , pp. 237-239
    • Ismail, N.1    Ng, D.T.2
  • 50
    • 0029044110 scopus 로고
    • Degradation of CD4 induced by human immunodeficiency virus type 1 Vpu protein: A predicted alpha-helix structure in the proximal cytoplasmic region of CD4 contributes to Vpu sensitivity
    • 10.1006/viro.1995.1293 7778293
    • Yao XJ Friborg J Checroune F Gratton S Boisvert F Sekaly RP Cohen EA Degradation of CD4 induced by human immunodeficiency virus type 1 Vpu protein: A predicted alpha-helix structure in the proximal cytoplasmic region of CD4 contributes to Vpu sensitivity Virology 1995 209 615 623 10.1006/viro.1995.1293 7778293
    • (1995) Virology , vol.209 , pp. 615-623
    • Yao, X.J.1    Friborg, J.2    Checroune, F.3    Gratton, S.4    Boisvert, F.5    Sekaly, R.P.6    Cohen, E.A.7
  • 51
    • 0022356559 scopus 로고
    • The isolation and nucleotide sequence of a cDNA encoding the T cell surface protein T4: A new member of the immunoglobulin gene family
    • 10.1016/S0092-8674(85)80105-7 2990730
    • Maddon PJ Littman DR Godfrey M Maddon DE Chess L Axel R The isolation and nucleotide sequence of a cDNA encoding the T cell surface protein T4: A new member of the immunoglobulin gene family Cell 1985, 42:93-104 10.1016/S0092-8674(85)80105-7 2990730
    • (1985) Cell , vol.42 , pp. 93-104
    • Maddon, P.J.1    Littman, D.R.2    Godfrey, M.3    Maddon, D.E.4    Chess, L.5    Axel, R.6
  • 52
    • 0026715929 scopus 로고
    • Envelope glycoprotein and CD4 independence of vpu-facilitated human immunodeficiency virus type 1 capsid export
    • 241384 1629967
    • Yao XJ Gottlinger H Haseltine WA Cohen EA Envelope glycoprotein and CD4 independence of vpu-facilitated human immunodeficiency virus type 1 capsid export J Virol 1992, 66:5119-5126 241384 1629967
    • (1992) J Virol , vol.66 , pp. 5119-5126
    • Yao, X.J.1    Gottlinger, H.2    Haseltine, W.A.3    Cohen, E.A.4
  • 53
    • 0032506276 scopus 로고    scopus 로고
    • Structural and functional analysis of the membrane-spanning domain of the human immunodeficiency virus type 1 Vpu protein
    • 10.1006/viro.1998.9368 9813206
    • Tiganos E Friborg J Allain B Daniel NG Yao XJ Cohen EA Structural and functional analysis of the membrane-spanning domain of the human immunodeficiency virus type 1 Vpu protein Virology 1998, 251:96-107 10.1006/viro.1998.9368 9813206
    • (1998) Virology , vol.251 , pp. 96-107
    • Tiganos, E.1    Friborg, J.2    Allain, B.3    Daniel, N.G.4    Yao, X.J.5    Cohen, E.A.6
  • 54
    • 0027306176 scopus 로고
    • Vpu protein of human immunodeficiency virus type 1 enhances the release of capsids produced by gag gene constructs of widely divergent retroviruses
    • 47141 8346259 10.1073/pnas.90.15.7381
    • Gottlinger HG Dorfman T Cohen EA Haseltine WA Vpu protein of human immunodeficiency virus type 1 enhances the release of capsids produced by gag gene constructs of widely divergent retroviruses Proc Natl Acad Sci USA 1993, 90:7381-7385 47141 8346259 10.1073/pnas.90.15.7381
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7381-7385
    • Gottlinger, H.G.1    Dorfman, T.2    Cohen, E.A.3    Haseltine, W.A.4
  • 55
    • 0028388662 scopus 로고
    • Requirement of the Pr55gag precursor for incorporation of the Vpr product into human immunodeficiency virus type 1 viral particles
    • 236654 8107252
    • Lavallee C Yao XJ Ladha A Gottlinger H Haseltine WA Cohen EA Requirement of the Pr55gag precursor for incorporation of the Vpr product into human immunodeficiency virus type 1 viral particles J Virol 1994, 68:1926-1934 236654 8107252
    • (1994) J Virol , vol.68 , pp. 1926-1934
    • Lavallee, C.1    Yao, X.J.2    Ladha, A.3    Gottlinger, H.4    Haseltine, W.A.5    Cohen, E.A.6
  • 56
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • 10.1016/0092-8674(95)90240-6 7553863
    • Ward CL Omura S Kopito RR Degradation of CFTR by the ubiquitin-proteasome pathway Cell 1995, 83:121-127 10.1016/ 0092-8674(95)90240-6 7553863
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 57
    • 0030962174 scopus 로고    scopus 로고
    • Putative alpha-helical structures in the human immunodeficiency virus type 1 Vpu protein and CD4 are involved in binding and degradation of the CD4 molecule
    • 191664 9151836
    • Tiganos E Yao XJ Friborg J Daniel N Cohen EA Putative alpha-helical structures in the human immunodeficiency virus type 1 Vpu protein and CD4 are involved in binding and degradation of the CD4 molecule J Virol 1997, 71:4452-4460 191664 9151836
    • (1997) J Virol , vol.71 , pp. 4452-4460
    • Tiganos, E.1    Yao, X.J.2    Friborg, J.3    Daniel, N.4    Cohen, E.A.5


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