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Volumn 1, Issue 4, 1998, Pages 565-574

A novel human WD protein, h-βTrCP, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif

Author keywords

[No Author keywords available]

Indexed keywords

BETA TRANSDUCIN REPEAT CONTAINING PROTEIN; BTRC PROTEIN, HUMAN; CD4 ANTIGEN; CELL CYCLE PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; S PHASE KINASE ASSOCIATED PROTEIN; SERINE; UBIQUITIN; VPU PROTEIN;

EID: 0032012456     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80056-8     Document Type: Article
Times cited : (588)

References (50)
  • 1
    • 0030602813 scopus 로고    scopus 로고
    • SKP1P connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box
    • Bai, C., Sen, P., Hofmann, K., Ma, L., Goebl, M., Harper, J.W., and Elledge, S.J. (1996). SKP1P connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 86, 263-274.
    • (1996) Cell , vol.86 , pp. 263-274
    • Bai, C.1    Sen, P.2    Hofmann, K.3    Ma, L.4    Goebl, M.5    Harper, J.W.6    Elledge, S.J.7
  • 2
    • 0028062729 scopus 로고
    • Physical interaction of the HIV-1 Nef protein with β-COP, a component of nonclathrin-coated vesicles essential for membrane traffic
    • Benichou, S., Bomsel, M., Bodeus, M., Durand, H., Doute, M., Letourneur, F., Camonis, J., and Benarous, R. (1994). Physical interaction of the HIV-1 Nef protein with β-COP, a component of nonclathrin-coated vesicles essential for membrane traffic. J. Biol. Chem. 269, 30073-30076.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30073-30076
    • Benichou, S.1    Bomsel, M.2    Bodeus, M.3    Durand, H.4    Doute, M.5    Letourneur, F.6    Camonis, J.7    Benarous, R.8
  • 4
    • 0025789624 scopus 로고
    • Inhibition of gp 160 and CD4 maturation in U937 cells after both defective and productive infections by human immunodeficiency virus type 1
    • Bour, S., Boulerice, F., and Wainberg, M.A. (1991). Inhibition of gp 160 and CD4 maturation in U937 cells after both defective and productive infections by human immunodeficiency virus type 1. J. Virol. 65, 6387-6396.
    • (1991) J. Virol. , vol.65 , pp. 6387-6396
    • Bour, S.1    Boulerice, F.2    Wainberg, M.A.3
  • 5
    • 0028913817 scopus 로고
    • The human immunodeficiency virus type 1 (HIV-1) CD4 receptor and its central role in promotion of HIV-1 infection
    • Bour, S., Geleziunas, R., and Wainberg, M.A. (1995a). The human immunodeficiency virus type 1 (HIV-1) CD4 receptor and its central role in promotion of HIV-1 infection. Microbiol. Rev. 59, 63-93.
    • (1995) Microbiol. Rev. , vol.59 , pp. 63-93
    • Bour, S.1    Geleziunas, R.2    Wainberg, M.A.3
  • 6
    • 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
    • Bour, S., Schubert, U., and Strebel, K. (1995b).The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradation. J. Virol. 69, 1510-1520.
    • (1995) J. Virol. , vol.69 , pp. 1510-1520
    • Bour, S.1    Schubert, U.2    Strebel, K.3
  • 7
    • 0031128320 scopus 로고    scopus 로고
    • ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together
    • Brodsky, J.L., and McCracken, A.A. (1997). ER-associated and proteasome-mediated protein degradation: how two topologically restricted events came together. Trends Cell Biol. 7, 151-156.
    • (1997) Trends Cell Biol. , vol.7 , pp. 151-156
    • Brodsky, J.L.1    McCracken, A.A.2
  • 8
    • 0027174989 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein induces degradation of CD4 in vitro: The cytoplasmic domain of CD4 contributes to Vpu sensitivity
    • Chen, M.Y., Maldarelli, F., Karczewski, M.K., Willey, R.L., and Strebel, K. (1993). Human immunodeficiency virus type 1 Vpu protein induces degradation of CD4 in vitro: the cytoplasmic domain of CD4 contributes to Vpu sensitivity. J. Virol. 67, 3877-3884.
    • (1993) J. Virol. , vol.67 , pp. 3877-3884
    • Chen, M.Y.1    Maldarelli, F.2    Karczewski, M.K.3    Willey, R.L.4    Strebel, K.5
  • 9
    • 0029793620 scopus 로고    scopus 로고
    • CD4 down-modulation during infection of human T cells with human immunodeficiency virus type 1 involves independent activities of vpu, env, and nef
    • Chen, B.K., Gandhi, R.T., and Baltimore, D. (1996). CD4 down-modulation during infection of human T cells with human immunodeficiency virus type 1 involves independent activities of vpu, env, and nef. J. Virol. 70, 6044-6053.
    • (1996) J. Virol. , vol.70 , pp. 6044-6053
    • Chen, B.K.1    Gandhi, R.T.2    Baltimore, D.3
  • 10
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover, A. (1994). The ubiquitin-proteasome proteolytic pathway. Cell 79, 13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 11
    • 0023729963 scopus 로고
    • Identification of a protein encoded by the vpu gene of HIV-1
    • Cohen, E.A., Terwilliger, E.F., Sodroski, J.G., and Haseltine, W.A. (1988). Identification of a protein encoded by the vpu gene of HIV-1. Nature 334, 532-534.
    • (1988) Nature , vol.334 , pp. 532-534
    • Cohen, E.A.1    Terwilliger, E.F.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 12
    • 0030602823 scopus 로고    scopus 로고
    • Budding yeast SKP1P encodes an evolutionarily conserved kinetochore protein required for cell cycle progression
    • Connelly, C., and Hieter, P. (1996). Budding yeast SKP1P encodes an evolutionarily conserved kinetochore protein required for cell cycle progression. Cell 86, 275-285.
    • (1996) Cell , vol.86 , pp. 275-285
    • Connelly, C.1    Hieter, P.2
  • 13
    • 0025183723 scopus 로고
    • CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor
    • Crise, B., Buonocore, L., and Rose, J.K. (1990). CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor. J. Virol. 64, 5585-5593.
    • (1990) J. Virol. , vol.64 , pp. 5585-5593
    • Crise, B.1    Buonocore, L.2    Rose, J.K.3
  • 14
    • 0030695025 scopus 로고    scopus 로고
    • A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p
    • Feldman, R.M.R., Correll, C.C., Kaplan, K.B., and Deshaies, R.J. (1997). A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91, 221-230.
    • (1997) Cell , vol.91 , pp. 221-230
    • Feldman, R.M.R.1    Correll, C.C.2    Kaplan, K.B.3    Deshaies, R.J.4
  • 16
    • 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
    • Fujita, K., Omura, S., and Silver, J. (1997). Rapid degradation of CD4 in cells expressing human immunodeficiency virus type 1 Env and Vpu is blocked by proteasome inhibitors. J. Gen. Virol. 78, 619-625.
    • (1997) J. Gen. Virol. , vol.78 , pp. 619-625
    • Fujita, K.1    Omura, S.2    Silver, J.3
  • 17
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller, M.M., Finger, A., Schweiger, M., and Wolf, D.H. (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
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 18
    • 0029844373 scopus 로고    scopus 로고
    • Identification of new localized RNAs in the Xenopus oocyte by differential display PCR
    • Hudson, J.W., Vernadeth, B.A., and Elinson, R.P. (1996). Identification of new localized RNAs in the Xenopus oocyte by differential display PCR. Dev. Genet. 19, 190-198.
    • (1996) Dev. Genet. , vol.19 , pp. 190-198
    • Hudson, J.W.1    Vernadeth, B.A.2    Elinson, R.P.3
  • 19
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen, T.J., Loo, M.A., Pind, S., Williams, D.B., Goldberg, A.L., and Riordan, J.R. (1995). Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83, 129-135.
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 20
    • 0030940154 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 (HIV-1) Vpu protein interferes with an early step in the biosynthesis of majorhistocompatibilitycomplex (MHC)class I molecules
    • Kerkau, T., Bacik, I., Bennink, J.R., Yewdell, J.W., Hunig, T., Schimpl, A., and Schubert, U. (1997). The human immunodeficiency virus type 1 (HIV-1) Vpu protein interferes with an early step in the biosynthesis of majorhistocompatibilitycomplex (MHC)class I molecules. J. Exp. Med. 185, 1295-1305.
    • (1997) J. Exp. Med. , vol.185 , pp. 1295-1305
    • Kerkau, T.1    Bacik, I.2    Bennink, J.R.3    Yewdell, J.W.4    Hunig, T.5    Schimpl, A.6    Schubert, U.7
  • 22
    • 0025041029 scopus 로고
    • Protein degradation in the endoplasmic reticulum
    • Klausner, R.D., and Sitia, R. (1990). Protein degradation in the endoplasmic reticulum. Cell 62, 611-614.
    • (1990) Cell , vol.62 , pp. 611-614
    • Klausner, R.D.1    Sitia, R.2
  • 23
    • 0030950644 scopus 로고    scopus 로고
    • Fission yeast WD-repeat protein Pop1 regulates genome ploidy through ubiquitin-proteasome-mediated degradation of theCDK inhibitor Rum1 and the S-phase initiator Cdc18
    • Kominami, K., and Toda, T. (1997). Fission yeast WD-repeat protein Pop1 regulates genome ploidy through ubiquitin-proteasome-mediated degradation of theCDK inhibitor Rum1 and the S-phase initiator Cdc18. Genes Dev. 11, 1548-1560.
    • (1997) Genes Dev. , vol.11 , pp. 1548-1560
    • Kominami, K.1    Toda, T.2
  • 24
    • 0027517186 scopus 로고
    • Vpu-induced degradation of CD4: Requirement for specific amino acid residues in the cytoplasmic domain of CD4
    • Lenburg, M.E., and Landau, N.R. (1993). Vpu-induced degradation of CD4: requirement for specific amino acid residues in the cytoplasmic domain of CD4. J. Virol. 67, 7238-7245.
    • (1993) J. Virol. , vol.67 , pp. 7238-7245
    • Lenburg, M.E.1    Landau, N.R.2
  • 25
    • 0030874516 scopus 로고    scopus 로고
    • Grr1 of Saccharomycescerevisiae is connected to the ubiquitin proteolysis machinery through Skp1: Coupling glucose sensing to gene expression and the cell cycle
    • Li, F.N., and Johnston, M. (1997). Grr1 of Saccharomycescerevisiae is connected to the ubiquitin proteolysis machinery through Skp1: coupling glucose sensing to gene expression and the cell cycle. EMBO J. 16, 5629-5638.
    • (1997) EMBO J. , vol.16 , pp. 5629-5638
    • Li, F.N.1    Johnston, M.2
  • 26
    • 0027209705 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein is an oligomeric type 1 integral membrane protein
    • Maldarelli, F., Chen, M.Y., Willey, R.L., and Strebel, K. (1993). Human immunodeficiency virus type 1 Vpu protein is an oligomeric type 1 integral membrane protein. J. Virol. 67, 5056-5061.
    • (1993) J. Virol. , vol.67 , pp. 5056-5061
    • Maldarelli, F.1    Chen, M.Y.2    Willey, R.L.3    Strebel, K.4
  • 27
    • 0030587419 scopus 로고    scopus 로고
    • Interaction between the cytoplasmic domains of HIV-1 vpu and CD4: Role of Vpu residues involved in CD4 interaction and in vitro CD4 degradation
    • Margottin F., Benichou, S., Durand, H., Richard, V., Liu, L.X., Gomas, E., and Benarous, R. (1996). Interaction between the cytoplasmic domains of HIV-1 vpu and CD4: role of Vpu residues involved in CD4 interaction and in vitro CD4 degradation. Virology 223, 381-386.
    • (1996) Virology , vol.223 , pp. 381-386
    • Margottin, F.1    Benichou, S.2    Durand, H.3    Richard, V.4    Liu, L.X.5    Gomas, E.6    Benarous, R.7
  • 28
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer, E.J., Schmidt, C.J., Nambudripad, R., and Smith, T.F. (1994). The ancient regulatory-protein family of WD-repeat proteins. Nature 377, 297-300.
    • (1994) Nature , vol.377 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 29
    • 0030921020 scopus 로고    scopus 로고
    • Phosphorylation of both phosphoacceptor sites in the HIV-1 vpu cytoplasmic domain is essential for vpu-mediated ER degradation of CD4
    • Paul, M., and Jabbar, M.A. (1997). Phosphorylation of both phosphoacceptor sites in the HIV-1 vpu cytoplasmic domain is essential for vpu-mediated ER degradation of CD4. Virology 232, 207-216.
    • (1997) Virology , vol.232 , pp. 207-216
    • Paul, M.1    Jabbar, M.A.2
  • 30
    • 0027516156 scopus 로고
    • Proteasomes: Multicatalytic proteinase complexes
    • Rivett, A.J. (1993). Proteasomes: multicatalytic proteinase complexes. Biochem. J. 291, 1-10.
    • (1993) Biochem. J. , vol.291 , pp. 1-10
    • Rivett, A.J.1
  • 31
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner, M., Huibregtse, J.M., Vierstra, R.D., and Howley, P.M. (1993). The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75, 495-505.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 32
    • 0028349047 scopus 로고
    • Differential activities of the human immunodeficiency virus type 1-encoded vpu protein are regulated by phosphorylation and occur in different cellular compartments
    • Schubert, U., and Strebel, K. (1994). Differential activities of the human immunodeficiency virus type 1-encoded vpu protein are regulated by phosphorylation and occur in different cellular compartments. J. Virol. 68, 2260-2271.
    • (1994) J. Virol. , vol.68 , pp. 2260-2271
    • Schubert, U.1    Strebel, K.2
  • 33
    • 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
    • in press
    • Schubert, U., Anton, L.C., Bacik, I., Cox, J.H., Bour, S., Bennink, J.R., Orlowski, M., Strebel, K., and Yewdell, J.W. (1998). CD4 glycoprotein degradation induced by human immunodeficiency virus type-1 Vpu protein requires the function of proteasomes and the ubiquitin conjugating pathway. J. Virol., in press.
    • (1998) J. Virol.
    • 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
  • 35
    • 0030662523 scopus 로고    scopus 로고
    • F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
    • Skowyra, D., Craig, K.L., Tyers, M., Elledge, S.J., and Harper, J.W. (1997). F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 91, 209-219.
    • (1997) Cell , vol.91 , pp. 209-219
    • Skowyra, D.1    Craig, K.L.2    Tyers, M.3    Elledge, S.J.4    Harper, J.W.5
  • 36
    • 0027237551 scopus 로고
    • Saccharomyces cerevisiae cdc 15 mutants arrested at a late stage in anaphase are rescued by Xenopus cDNAs encoding N-ras or a protein with β-transducin repeats
    • Spevak, W., Keiper, B.D., Stratowa, C., and Castanon, M.J. (1993). Saccharomyces cerevisiae cdc 15 mutants arrested at a late stage in anaphase are rescued by Xenopus cDNAs encoding N-ras or a protein with β-transducin repeats. Mol. Cell. Biol. 13, 4953-4966.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4953-4966
    • Spevak, W.1    Keiper, B.D.2    Stratowa, C.3    Castanon, M.J.4
  • 37
    • 0023677668 scopus 로고
    • A novel gene product of HIV-1, vpu, and its 16-kilodalton product
    • Strebel, K., Klimkait, T., and Martin, M.A. (1988). A novel gene product of HIV-1, vpu, and its 16-kilodalton product. Science 2, 1221-1223.
    • (1988) Science , vol.2 , pp. 1221-1223
    • Strebel, K.1    Klimkait, T.2    Martin, M.A.3
  • 38
    • 0022648673 scopus 로고
    • Characterization of foot-and-mouth disease virus gene products with anti-sera against bacterially synthesized fusion proteins
    • Strebel, K., Beck, E., Strohmaier, K., and Schaller, H. (1986). Characterization of foot-and-mouth disease virus gene products with anti-sera against bacterially synthesized fusion proteins. J. Virol. 57, 983-991.
    • (1986) J. Virol. , vol.57 , pp. 983-991
    • Strebel, K.1    Beck, E.2    Strohmaier, K.3    Schaller, H.4
  • 39
    • 0028806055 scopus 로고
    • Met30p, a yeast transcriptional inhibitor that responds to S-adenosylmethionine, is an essential protein with WD40 repeats
    • Thomas, D., Kuras, L., Barbey, R., Cherest, H., Blaiseau, P.L., and Surdin-Kerjan, Y. (1995). Met30p, a yeast transcriptional inhibitor that responds to S-adenosylmethionine, is an essential protein with WD40 repeats. Mol. Cell. Biol. 15, 6526-6534.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6526-6534
    • Thomas, D.1    Kuras, L.2    Barbey, R.3    Cherest, H.4    Blaiseau, P.L.5    Surdin-Kerjan, Y.6
  • 40
    • 0029150052 scopus 로고
    • HIV accessory proteins: Leading roles for the supporting cast
    • Trono, D. (1995). HIV accessory proteins: leading roles for the supporting cast. Cell 82, 189-192.
    • (1995) Cell , vol.82 , pp. 189-192
    • Trono, D.1
  • 41
    • 0030612012 scopus 로고    scopus 로고
    • Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase
    • Verma, R., Annan, R.S., Huddleston, M.J., Carr, S.A., Reynard, G., and Deshaies, R.J. (1997). Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase. Science 278, 455-460.
    • (1997) Science , vol.278 , pp. 455-460
    • Verma, R.1    Annan, R.S.2    Huddleston, M.J.3    Carr, S.A.4    Reynard, G.5    Deshaies, R.J.6
  • 42
    • 0027261551 scopus 로고
    • Human immunodeficiency virus type 1 vpu protein induces degradation of chimeric envelope glycoproteins bearing the cytoplasmic and anchor domains of CD4: Role of the cytoplasmic domain in vpu-induced degradation in the endoplasmic reticulum
    • Vincent, M.J., Raja, N.U., and Abdul Jabbar, M. (1993). Human immunodeficiency virus type 1 vpu protein induces degradation of chimeric envelope glycoproteins bearing the cytoplasmic and anchor domains of CD4: role of the cytoplasmic domain in vpu-induced degradation in the endoplasmic reticulum. J. Virol. 67, 5538-5549.
    • (1993) J. Virol. , vol.67 , pp. 5538-5549
    • Vincent, M.J.1    Raja, N.U.2    Abdul Jabbar, M.3
  • 43
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C.L., Omura, S., and Kopito, R.R. (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
  • 44
    • 0030997067 scopus 로고    scopus 로고
    • Regulating protein degradation by ubiquitination
    • Weissman, A.M. (1997). Regulating protein degradation by ubiquitination. Immunol. Today 18, 189-198.
    • (1997) Immunol. Today , vol.18 , pp. 189-198
    • Weissman, A.M.1
  • 45
    • 0030447659 scopus 로고    scopus 로고
    • Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate
    • Werner, E.D., Brodsky, J.L., and McCracken, A.A. (1996). Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proc. Natl. Acad. Sci. USA 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
  • 46
    • 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, E.J.H.J., Jones, T.R., Sun, L., Bogyo, M., Geuze, H.J., and Ploegh, H.L. (1996). 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.H.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5    Ploegh, H.L.6
  • 48
    • 0026452726 scopus 로고
    • Human immunodeficiency virus type 1 vpu protein induces rapid degradation of CD4
    • Willey, R.L., Maldarelli, F., Martin, M.A., and Strebel, K., (1992). Human immunodeficiency virus type 1 vpu protein induces rapid degradation of CD4. J. Virol. 66, 7193-7200.
    • (1992) J. Virol. , vol.66 , pp. 7193-7200
    • Willey, R.L.1    Maldarelli, F.2    Martin, M.A.3    Strebel, K.4
  • 49
    • 0023268147 scopus 로고
    • Structural comparison of yeast cell division cycle gene CDC4 and a related pseudogene
    • Yochem, J., and Byers, B. (1987). Structural comparison of yeast cell division cycle gene CDC4 and a related pseudogene. J. Mol. Biol. 195, 233-245.
    • (1987) J. Mol. Biol. , vol.195 , pp. 233-245
    • Yochem, J.1    Byers, B.2


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