메뉴 건너뛰기




Volumn 5, Issue 11, 2003, Pages 1029-1039

The HIV-1 Vpu protein: A multifunctional enhancer of viral particle release

Author keywords

Accessory genes; HIV; Vpu

Indexed keywords

CD4 RECEPTOR; ION CHANNEL; RECEPTOR; UNCLASSIFIED DRUG; VPU PROTEIN;

EID: 0041570003     PISSN: 12864579     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1286-4579(03)00191-6     Document Type: Review
Times cited : (87)

References (93)
  • 1
    • 0026786712 scopus 로고
    • Cell-free transmission of Vif mutants of HIV-1
    • Fan L., Peden K. Cell-free transmission of Vif mutants of HIV-1. Virology. 190:1992;19-29.
    • (1992) Virology , vol.190 , pp. 19-29
    • Fan, L.1    Peden, K.2
  • 2
    • 0023677668 scopus 로고
    • A novel gene of HIV-1, vpu, and its 16-kilodalton product
    • Strebel K., Klimkait T., Martin M.A. A novel gene of HIV-1, vpu, and its 16-kilodalton product. Science. 241:1988;1221-1223.
    • (1988) Science , vol.241 , pp. 1221-1223
    • Strebel, K.1    Klimkait, T.2    Martin, M.A.3
  • 3
    • 0034564274 scopus 로고    scopus 로고
    • HIV accessory proteins: Multifunctional components of a complex system
    • Bour S., Strebel K. HIV accessory proteins: multifunctional components of a complex system. Adv. Pharmacol. 48:2000;75-120.
    • (2000) Adv. Pharmacol. , vol.48 , pp. 75-120
    • Bour, S.1    Strebel, K.2
  • 4
    • 0025343127 scopus 로고
    • Genetic organization of a chimpanzee lentivirus related to HIV-1
    • Huet T., Cheynier R., Meyerhans A., Roelants G., Wain-Hobson S. Genetic organization of a chimpanzee lentivirus related to HIV-1. Nature. 345:1990;356-359.
    • (1990) Nature , vol.345 , pp. 356-359
    • Huet, T.1    Cheynier, R.2    Meyerhans, A.3    Roelants, G.4    Wain-Hobson, S.5
  • 5
    • 0036319292 scopus 로고    scopus 로고
    • Characterization of a novel simian immunodeficiency virus with a vpu gene from greater spot-nosed monkeys (Cercopithecus nictitans) provides new insights into simian/human immunodeficiency virus phylogeny
    • Courgnaud V., Salemi M., Pourrut X., Mpoudi-Ngole E., Abela B., Auzel P., Bibollet-Ruche F., Hahn B., Vandamme A.M., Delaporte E., Peeters M. Characterization of a novel simian immunodeficiency virus with a vpu gene from greater spot-nosed monkeys (Cercopithecus nictitans) provides new insights into simian/human immunodeficiency virus phylogeny. J. Virol. 76:2002;8298-8309.
    • (2002) J. Virol. , vol.76 , pp. 8298-8309
    • Courgnaud, V.1    Salemi, M.2    Pourrut, X.3    Mpoudi-Ngole, E.4    Abela, B.5    Auzel, P.6    Bibollet-Ruche, F.7    Hahn, B.8    Vandamme, A.M.9    Delaporte, E.10    Peeters, M.11
  • 6
    • 0029918147 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 2 glycoprotein enhancement of particle budding: Role of the cytoplasmic domain
    • Ritter G.D. Jr., Yamshchikov G., Cohen S.J., Mulligan M.J. Human immunodeficiency virus type 2 glycoprotein enhancement of particle budding: role of the cytoplasmic domain. J. Virol. 70:1996;2669-2673.
    • (1996) J. Virol. , vol.70 , pp. 2669-2673
    • Ritter G.D., Jr.1    Yamshchikov, G.2    Cohen, S.J.3    Mulligan, M.J.4
  • 7
    • 0030052467 scopus 로고    scopus 로고
    • The envelope glycoprotein of human immunodeficiency virus type 2 enhances viral particle release: A Vpu-like factor?
    • Bour S., Schubert U., Peden K., Strebel K. The envelope glycoprotein of human immunodeficiency virus type 2 enhances viral particle release: a Vpu-like factor? J. Virol. 70:1996;820-829.
    • (1996) J. Virol. , vol.70 , pp. 820-829
    • Bour, S.1    Schubert, U.2    Peden, K.3    Strebel, K.4
  • 8
    • 0029956763 scopus 로고    scopus 로고
    • The human immunodeficiency virus (HIV) type 2 envelope protein is a functional complement to HIV type 1 Vpu that enhances particle release of heterologous retroviruses
    • Bour S., Strebel K. The human immunodeficiency virus (HIV) type 2 envelope protein is a functional complement to HIV type 1 Vpu that enhances particle release of heterologous retroviruses. J. Virol. 70:1996;8285-8300.
    • (1996) J. Virol. , vol.70 , pp. 8285-8300
    • Bour, S.1    Strebel, K.2
  • 9
    • 0025131891 scopus 로고
    • Env and Vpu proteins of human immunodeficiency virus type 1 are produced from multiple bicistronic mRNAs
    • Schwartz S., Felber B.K., Fenyo E.M., Pavlakis G.N. Env and Vpu proteins of human immunodeficiency virus type 1 are produced from multiple bicistronic mRNAs. J. Virol. 64:1990;5448-5456.
    • (1990) J. Virol. , vol.64 , pp. 5448-5456
    • Schwartz, S.1    Felber, B.K.2    Fenyo, E.M.3    Pavlakis, G.N.4
  • 11
    • 0032923614 scopus 로고    scopus 로고
    • Regulation of virus release by the macrophage-tropic human immunodeficiency virus type 1 AD8 isolate is redundant and can be controlled by either Vpu or Env
    • Schubert U., Bour S., Willey R.L., Strebel K. Regulation of virus release by the macrophage-tropic human immunodeficiency virus type 1 AD8 isolate is redundant and can be controlled by either Vpu or Env. J. Virol. 73:1999;887-896.
    • (1999) J. Virol. , vol.73 , pp. 887-896
    • Schubert, U.1    Bour, S.2    Willey, R.L.3    Strebel, K.4
  • 12
  • 13
    • 0028348370 scopus 로고
    • The human immunodeficiency virus type 1 encoded Vpu protein is phosphorylated by casein kinase-2 (CK-2) at positions Ser52 and Ser56 within a predicted alpha-helix-turn-alpha-helix-motif
    • Schubert U., Henklein P., Boldyreff B., Wingender E., Strebel K., Porstmann T. The human immunodeficiency virus type 1 encoded Vpu protein is phosphorylated by casein kinase-2 (CK-2) at positions Ser52 and Ser56 within a predicted alpha-helix-turn-alpha-helix-motif. J. Mol. Biol. 236:1994;16-25.
    • (1994) J. Mol. Biol. , vol.236 , pp. 16-25
    • Schubert, U.1    Henklein, P.2    Boldyreff, B.3    Wingender, E.4    Strebel, K.5    Porstmann, T.6
  • 14
    • 0027568142 scopus 로고
    • Synthesis and characterization of the hydrophilic C-terminal domain of the human immunodeficiency virus type 1-encoded virus protein U (Vpu)
    • Henklein P., Schubert U., Kunert O., Klabunde S., Wray V., Kloppel K. D., Kiess M., Portsmann T., Schomburg D. Synthesis and characterization of the hydrophilic C-terminal domain of the human immunodeficiency virus type 1-encoded virus protein U (Vpu). Pept. Res. 6:1993;79-87.
    • (1993) Pept. Res. , vol.6 , pp. 79-87
    • Henklein, P.1    Schubert, U.2    Kunert, O.3    Klabunde, S.4    Wray, V.5    Kloppel K., D.6    Kiess, M.7    Portsmann, T.8    Schomburg, D.9
  • 15
    • 0029977571 scopus 로고    scopus 로고
    • Solution structure of the cytoplasmic domain of the human immunodeficiency virus type 1 encoded virus protein U (Vpu)
    • Federau T., Schubert U., Flossdorf J., Henklein P., Schomburg D., Wray V. Solution structure of the cytoplasmic domain of the human immunodeficiency virus type 1 encoded virus protein U (Vpu). Int. J. Pept. Protein Res. 47:1996;297-310.
    • (1996) Int. J. Pept. Protein Res. , vol.47 , pp. 297-310
    • Federau, T.1    Schubert, U.2    Flossdorf, J.3    Henklein, P.4    Schomburg, D.5    Wray, V.6
  • 17
    • 0030943906 scopus 로고    scopus 로고
    • Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution
    • Willbold D., Hoffmann S., Rosch P. Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution. Eur. J. Biochem. 245:1997;581-588.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 581-588
    • Willbold, D.1    Hoffmann, S.2    Rosch, P.3
  • 19
    • 0033586794 scopus 로고    scopus 로고
    • Solution structure and orientation of the transmembrane anchor domain of the HIV-1-encoded virus protein U by high-resolution and solid-state NMR spectroscopy
    • Wray V., Kinder R., Federau T., Henklein P., Bechinger B., Schubert U. Solution structure and orientation of the transmembrane anchor domain of the HIV-1-encoded virus protein U by high-resolution and solid-state NMR spectroscopy. Biochemistry. 38:1999;5272-5282.
    • (1999) Biochemistry , vol.38 , pp. 5272-5282
    • Wray, V.1    Kinder, R.2    Federau, T.3    Henklein, P.4    Bechinger, B.5    Schubert, U.6
  • 20
    • 0034613058 scopus 로고    scopus 로고
    • Membrane interactions and alignment of structures within the HIV-1 Vpu cytoplasmic domain: Effect of phosphorylation of serines 52 and 56
    • Henklein P., Kinder R., Schubert U., Bechinger B. Membrane interactions and alignment of structures within the HIV-1 Vpu cytoplasmic domain: effect of phosphorylation of serines 52 and 56. FEBS Lett. 482:2000;220-224.
    • (2000) FEBS Lett. , vol.482 , pp. 220-224
    • Henklein, P.1    Kinder, R.2    Schubert, U.3    Bechinger, B.4
  • 21
    • 0037040363 scopus 로고    scopus 로고
    • HIV-1 encoded virus protein U (Vpu) solution structure of the 41-62 hydrophilic region containing the phosphorylated sites Ser52 and Ser56
    • Coadou G., Evrard-Todeschi N., Gharbi-Benarous J., Benarous R., Girault J.P. HIV-1 encoded virus protein U (Vpu) solution structure of the 41-62 hydrophilic region containing the phosphorylated sites Ser52 and Ser56. Int. J. Biol. Macromol. 30:2002;23-40.
    • (2002) Int. J. Biol. Macromol. , vol.30 , pp. 23-40
    • Coadou, G.1    Evrard-Todeschi, N.2    Gharbi-Benarous, J.3    Benarous, R.4    Girault, J.P.5
  • 22
    • 0027209705 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein is an oligomeric type I integral membrane protein
    • Maldarelli F., Chen M.Y., Willey R.L., Strebel K. Human immunodeficiency virus type 1 Vpu protein is an oligomeric type I integral membrane protein. J. Virol. 67:1993;5056-5061.
    • (1993) J. Virol. , vol.67 , pp. 5056-5061
    • Maldarelli, F.1    Chen, M.Y.2    Willey, R.L.3    Strebel, K.4
  • 23
    • 0028913817 scopus 로고
    • The human immunodeficiency virus type 1 (HIV-1) CD4 receptor and its central role in the promotion of HIV-1 infection
    • Bour S., Geleziunas R., Wainberg M.A. The human immunodeficiency virus type 1 (HIV-1) CD4 receptor and its central role in the promotion of HIV-1 infection. Microbiol. Rev. 59:1995;63-93.
    • (1995) Microbiol. Rev. , vol.59 , pp. 63-93
    • Bour, S.1    Geleziunas, R.2    Wainberg, M.A.3
  • 24
    • 0025183723 scopus 로고
    • CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor
    • Crise B., Buonocore L., Rose J.K. CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor. J. Virol. 64:1990;5585-5593.
    • (1990) J. Virol. , vol.64 , pp. 5585-5593
    • Crise, B.1    Buonocore, L.2    Rose, J.K.3
  • 25
    • 0025244369 scopus 로고
    • Intracellular interaction of human immunodeficiency virus type 1 (ARV-2) envelope glycoprotein gp160 with CD4 blocks the movement and maturation of CD4 to the plasma membrane
    • Jabbar M.A., Nayak D.P. Intracellular interaction of human immunodeficiency virus type 1 (ARV-2) envelope glycoprotein gp160 with CD4 blocks the movement and maturation of CD4 to the plasma membrane. J. Virol. 64:1990;6297-6304.
    • (1990) J. Virol. , vol.64 , pp. 6297-6304
    • Jabbar, M.A.1    Nayak, D.P.2
  • 26
    • 0025789624 scopus 로고
    • Inhibition of gp160 and CD4 maturation in U937 cells after both defective and productive infections by human immunodeficiency virus type 1
    • Bour S., Boulerice F., Wainberg M.A. Inhibition of gp160 and CD4 maturation in U937 cells after both defective and productive infections by human immunodeficiency virus type 1. J. Virol. 65:1991;6387-6396.
    • (1991) J. Virol. , vol.65 , pp. 6387-6396
    • Bour, S.1    Boulerice, F.2    Wainberg, M.A.3
  • 27
    • 0027526286 scopus 로고
    • Blockade of human immunodeficiency virus type 1 production in CD4+ T cells by an intracellular CD4 expressed under control of the viral long terminal repeat
    • Buonocore L., Rose J.K. Blockade of human immunodeficiency virus type 1 production in CD4+ T cells by an intracellular CD4 expressed under control of the viral long terminal repeat. Proc. Natl. Acad. Sci. USA. 90:1993;2695-2699.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2695-2699
    • Buonocore, L.1    Rose, J.K.2
  • 28
    • 0025299912 scopus 로고
    • Prevention of HIV-1 glycoprotein transport by soluble CD4 retained in the endoplasmic reticulum
    • (see comments)
    • Buonocore L., Rose J.K. Prevention of HIV-1 glycoprotein transport by soluble CD4 retained in the endoplasmic reticulum. Nature. 345:1990;625-628. (see comments).
    • (1990) Nature , vol.345 , pp. 625-628
    • Buonocore, L.1    Rose, J.K.2
  • 29
    • 0026567269 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein regulates the formation of intracellular gp160-CD4 complexes
    • Willey R.L., Maldarelli F., Martin M.A., Strebel K. Human immunodeficiency virus type 1 Vpu protein regulates the formation of intracellular gp160-CD4 complexes. J. Virol. 66:1992;226-234.
    • (1992) J. Virol. , vol.66 , pp. 226-234
    • Willey, R.L.1    Maldarelli, F.2    Martin, M.A.3    Strebel, K.4
  • 30
    • 0026452726 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4
    • Willey R.L., Maldarelli F., Martin M.A., Strebel K. Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4. J. Virol. 66:1992;7193-7200.
    • (1992) J. Virol. , vol.66 , pp. 7193-7200
    • Willey, R.L.1    Maldarelli, F.2    Martin, M.A.3    Strebel, K.4
  • 31
    • 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., Strebel K. Human immunodeficiency virus type 1 Vpu protein induces degradation of CD4 in vitro: the cytoplasmic domain of CD4 contributes to Vpu sensitivity. J. Virol. 67:1993;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
  • 32
    • 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., 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. 69:1995;1510-1520.
    • (1995) J. Virol. , vol.69 , pp. 1510-1520
    • Bour, S.1    Schubert, U.2    Strebel, K.3
  • 33
    • 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
    • Yao X.J., Friborg J., Checroune F., Gratton S., Boisvert F., Sekaly R.P., Cohen E.A. 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. 209:1995;615-623.
    • (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
  • 34
    • 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., Jabbar M.A. 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. 67:1993;5538-5549.
    • (1993) J. Virol. , vol.67 , pp. 5538-5549
    • Vincent, M.J.1    Raja, N.U.2    Jabbar, M.A.3
  • 35
    • 0027517186 scopus 로고
    • Vpu-induced degradation of CD4: Requirement for specific amino acid residues in the cytoplasmic domain of CD4
    • Lenburg M.E., Landau N.R. Vpu-induced degradation of CD4: requirement for specific amino acid residues in the cytoplasmic domain of CD4. J. Virol. 67:1993;7238-7245.
    • (1993) J. Virol. , vol.67 , pp. 7238-7245
    • Lenburg, M.E.1    Landau, N.R.2
  • 36
    • 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., Strebel K. Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartments. J. Virol. 68:1994;2260-2271.
    • (1994) J. Virol. , vol.68 , pp. 2260-2271
    • Schubert, U.1    Strebel, K.2
  • 37
    • 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., Jabbar M.A. Phosphorylation of both phosphoacceptor sites in the HIV-1 Vpu cytoplasmic domain is essential for Vpu-mediated ER degradation of CD4. Virology. 232:1997;207-216.
    • (1997) Virology , vol.232 , pp. 207-216
    • Paul, M.1    Jabbar, M.A.2
  • 38
    • 0032012456 scopus 로고    scopus 로고
    • A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif
    • Margottin F., Bour S.P., Durand H., Selig L., Benichou S., Richard V., Thomas D., Strebel K. A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Mol. Cell. 1:1998;565-574.
    • (1998) Mol. Cell , vol.1 , pp. 565-574
    • Margottin, F.1    Bour, S.P.2    Durand, H.3    Selig, L.4    Benichou, S.5    Richard, V.6    Thomas, D.7    Strebel, K.8
  • 39
    • 0027237551 scopus 로고
    • Saccharomyces cerevisiae cdc15 mutants arrested at a late stage in anaphase are rescued by Xenopus cDNAs encoding N-ras or a protein with beta-transducin repeats
    • Spevak W., Keiper B.D., Stratowa C., Castanon M.J. Saccharomyces cerevisiae cdc15 mutants arrested at a late stage in anaphase are rescued by Xenopus cDNAs encoding N-ras or a protein with beta-transducin repeats. Mol. Cell. Biol. 13:1993;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
  • 40
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • [published erratum appears in Nature 371 (6500) (1994) 812]
    • Neer E.J., Schmidt C.J., Nambudripad R., Smith T.F. The ancient regulatory-protein family of WD-repeat proteins. Nature. 371:1994;297-300. [published erratum appears in Nature 371 (6500) (1994) 812].
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 41
    • 0030602813 scopus 로고    scopus 로고
    • SKP1 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., Elledge S.J. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell. 86:1996;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
  • 42
    • 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
    • Schubert U., Anton L.C., Bacik I., Cox J.H., Bour S., Bennink J.R., Orlowski M., Strebel K., Yewdell J.W. CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway. J. Virol. 72:1998;2280-2288.
    • (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
  • 43
    • 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
    • [published erratum appears in J. Gen. Virol. 78 (Pt 8) (1997) 2129-2130]
    • 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. 78:1997;619-625. [published erratum appears in J. Gen. Virol. 78 (Pt 8) (1997) 2129-2130].
    • (1997) J. Gen. Virol. , vol.78 , pp. 619-625
    • Fujita, K.1    Omura, S.2    Silver, J.3
  • 45
    • 0033068154 scopus 로고    scopus 로고
    • The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitro
    • Winston J.T., Strack P., Beer-Romero P., Chu C.Y., Elledge S.J., Harper J.W. The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitro. Genes Dev. 13:1999;270-283.
    • (1999) Genes Dev. , vol.13 , pp. 270-283
    • Winston, J.T.1    Strack, P.2    Beer-Romero, P.3    Chu, C.Y.4    Elledge, S.J.5    Harper, J.W.6
  • 46
    • 0033083158 scopus 로고    scopus 로고
    • Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP
    • Spencer E., Jiang J., Chen Z.J. Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP. Genes Dev. 13:1999;284-294.
    • (1999) Genes Dev. , vol.13 , pp. 284-294
    • Spencer, E.1    Jiang, J.2    Chen, Z.J.3
  • 48
    • 0029870836 scopus 로고    scopus 로고
    • Protein degradation or regulation: Ub the judge
    • Hochstrasser M. Protein degradation or regulation: Ub the judge. Cell. 84:1996;813-815.
    • (1996) Cell , vol.84 , pp. 813-815
    • Hochstrasser, M.1
  • 50
    • 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., Jones T.R., Sun L., Bogyo M., Geuze H.J., Ploegh H.L. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell. 84:1996;769-779.
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5    Ploegh, H.L.6
  • 51
    • 0035844173 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCP-mediated degradation of Ikappa B
    • Bour S., Perrin C., Akari H., Strebel K. The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCP-mediated degradation of Ikappa B. J. Biol. Chem. 276:2001;15920-15928.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15920-15928
    • Bour, S.1    Perrin, C.2    Akari, H.3    Strebel, K.4
  • 52
    • 0033596127 scopus 로고    scopus 로고
    • Control of apoptosis by Rel/NF-kappaB transcription factors
    • Barkett M., Gilmore T.D. Control of apoptosis by Rel/NF-kappaB transcription factors. Oncogene. 18:1999;6910-6924.
    • (1999) Oncogene , vol.18 , pp. 6910-6924
    • Barkett, M.1    Gilmore, T.D.2
  • 53
    • 0033596121 scopus 로고    scopus 로고
    • Activators and target genes of Rel/NF-kappaB transcription factors
    • Pahl H.L. Activators and target genes of Rel/NF-kappaB transcription factors. Oncogene. 18:1999;6853-6866.
    • (1999) Oncogene , vol.18 , pp. 6853-6866
    • Pahl, H.L.1
  • 54
    • 0034329318 scopus 로고    scopus 로고
    • Mechanisms of HIV-associated lymphocyte apoptosis
    • Badley A.D., Pilon A.A., Landay A., Lynch D.H. Mechanisms of HIV-associated lymphocyte apoptosis. Blood. 96:2000;2951-2964.
    • (2000) Blood , vol.96 , pp. 2951-2964
    • Badley, A.D.1    Pilon, A.A.2    Landay, A.3    Lynch, D.H.4
  • 55
    • 0032889036 scopus 로고    scopus 로고
    • Vpu increases susceptibility of human immunodeficiency virus type 1-infected cells to fas killing
    • Casella C.R., Rapaport E.L., Finkel T.H. Vpu increases susceptibility of human immunodeficiency virus type 1-infected cells to fas killing. J. Virol. 73:1999;92-100.
    • (1999) J. Virol. , vol.73 , pp. 92-100
    • Casella, C.R.1    Rapaport, E.L.2    Finkel, T.H.3
  • 56
    • 0035163739 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 accessory protein Vpu induces apoptosis by suppressing the nuclear factor kappaB-dependent expression of antiapoptotic factors
    • Akari H., Bour S., Kao S., Adachi A., Strebel K. The human immunodeficiency virus type 1 accessory protein Vpu induces apoptosis by suppressing the nuclear factor kappaB-dependent expression of antiapoptotic factors. J. Exp. M. 194:2001;1299-1311.
    • (2001) J. Exp. M , vol.194 , pp. 1299-1311
    • Akari, H.1    Bour, S.2    Kao, S.3    Adachi, A.4    Strebel, K.5
  • 57
    • 0025139857 scopus 로고
    • The human immunodeficiency virus type 1-specific protein vpu is required for efficient virus maturation and release
    • Klimkait T., Strebel K., Hoggan M.D., Martin M.A., Orenstein J.M. The human immunodeficiency virus type 1-specific protein vpu is required for efficient virus maturation and release. J. Virol. 64:1990;621-629.
    • (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
  • 58
    • 0024381228 scopus 로고
    • Molecular and biochemical analyses of human immunodeficiency virus type 1 vpu protein
    • Strebel K., Klimkait T., Maldarelli F., Martin M.A. Molecular and biochemical analyses of human immunodeficiency virus type 1 vpu protein. J. Virol. 63:1989;3784-3791.
    • (1989) J. Virol. , vol.63 , pp. 3784-3791
    • Strebel, K.1    Klimkait, T.2    Maldarelli, F.3    Martin, M.A.4
  • 61
    • 0026715929 scopus 로고
    • Envelope glycoprotein and CD4 independence of vpu-facilitated human immunodeficiency virus type 1 capsid export
    • Yao X.J., Gottlinger H., Haseltine W.A., Cohen E.A. Envelope glycoprotein and CD4 independence of vpu-facilitated human immunodeficiency virus type 1 capsid export. J. Virol. 66:1992;5119-5126.
    • (1992) J. Virol. , vol.66 , pp. 5119-5126
    • Yao, X.J.1    Gottlinger, H.2    Haseltine, W.A.3    Cohen, E.A.4
  • 62
    • 0027207952 scopus 로고
    • Human immunodeficiency virus type 1 Vpu has a CD4- and an envelope glycoprotein-independent function
    • Geraghty R.J., Panganiban A.T. Human immunodeficiency virus type 1 Vpu has a CD4- and an envelope glycoprotein-independent function. J. Virol. 67:1993;4190-4194.
    • (1993) J. Virol. , vol.67 , pp. 4190-4194
    • Geraghty, R.J.1    Panganiban, A.T.2
  • 63
    • 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 A.V., 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. 70:1996;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
  • 64
    • 0031908685 scopus 로고    scopus 로고
    • Mutational analysis of the human immunodeficiency virus type 1 Vpu transmembrane domain that promotes the enhanced release of virus-like particles from the plasma membrane of mammalian cells
    • Paul M., Mazumder S., Raja N., Jabbar M.A. Mutational analysis of the human immunodeficiency virus type 1 Vpu transmembrane domain that promotes the enhanced release of virus-like particles from the plasma membrane of mammalian cells. J. Virol. 72:1998;1270-1279.
    • (1998) J. Virol. , vol.72 , pp. 1270-1279
    • Paul, M.1    Mazumder, S.2    Raja, N.3    Jabbar, M.A.4
  • 65
    • 0029794387 scopus 로고    scopus 로고
    • The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels
    • Ewart G.D., Sutherland T., Gage P.W., Cox G.B. The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels. J. Virol. 70:1996;7108-7115.
    • (1996) J. Virol. , vol.70 , pp. 7108-7115
    • Ewart, G.D.1    Sutherland, T.2    Gage, P.W.3    Cox, G.B.4
  • 66
    • 0031954778 scopus 로고    scopus 로고
    • Functional interaction of human immunodeficiency virus type 1 Vpu and Gag with a novel member of the tetratricopeptide repeat protein family
    • [Erratum appears in J. Virol. 72:8461]
    • Callahan M.A., Handley M.A., Lee Y.H., Talbot K.J., Harper J.W., Panganiban A.T. Functional interaction of human immunodeficiency virus type 1 Vpu and Gag with a novel member of the tetratricopeptide repeat protein family. J. Virol. 72:1998;5189-5197. [Erratum appears in J. Virol. 72:8461].
    • (1998) J. Virol. , vol.72 , pp. 5189-5197
    • Callahan, M.A.1    Handley, M.A.2    Lee, Y.H.3    Talbot, K.J.4    Harper, J.W.5    Panganiban, A.T.6
  • 67
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5: Implications for TPR-mediated protein-protein interactions
    • Das A.K., Cohen P.W., Barford D. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 17:1998;1192-1199.
    • (1998) EMBO J. , vol.17 , pp. 1192-1199
    • Das, A.K.1    Cohen, P.W.2    Barford, D.3
  • 68
    • 0035694564 scopus 로고    scopus 로고
    • Association of Vpu-binding protein with microtubules and Vpu-dependent redistribution of HIV-1 Gag protein
    • Handley M.A., Paddock S., Dall A., Panganiban A.T. Association of Vpu-binding protein with microtubules and Vpu-dependent redistribution of HIV-1 Gag protein. Virology. 291:2001;198-207.
    • (2001) Virology , vol.291 , pp. 198-207
    • Handley, M.A.1    Paddock, S.2    Dall, A.3    Panganiban, A.T.4
  • 69
    • 0034991502 scopus 로고    scopus 로고
    • Viral protein U (Vpu)-mediated enhancement of human immunodeficiency virus type 1 particle release depends on the rate of cellular proliferation
    • Deora A., Ratner L. Viral protein U (Vpu)-mediated enhancement of human immunodeficiency virus type 1 particle release depends on the rate of cellular proliferation. J. Virol. 75:2001;6714-6718.
    • (2001) J. Virol. , vol.75 , pp. 6714-6718
    • Deora, A.1    Ratner, L.2
  • 70
    • 0030602182 scopus 로고    scopus 로고
    • Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells
    • Schubert U., Ferrer-Montiel A.V., Oblatt-Montal M., Henklein P., Strebel K., Montal M. Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells. FEBS Lett. 398:1996;12-18.
    • (1996) FEBS Lett. , vol.398 , pp. 12-18
    • Schubert, U.1    Ferrer-Montiel, A.V.2    Oblatt-Montal, M.3    Henklein, P.4    Strebel, K.5    Montal, M.6
  • 72
    • 0032540881 scopus 로고    scopus 로고
    • Simulation of the HIV-1 Vpu transmembrane domain as a pentameric bundle
    • Moore P.B., Zhong Q., Husslein T., Klein M.L. Simulation of the HIV-1 Vpu transmembrane domain as a pentameric bundle. FEBS Lett. 431:1998;143-148.
    • (1998) FEBS Lett. , vol.431 , pp. 143-148
    • Moore, P.B.1    Zhong, Q.2    Husslein, T.3    Klein, M.L.4
  • 73
    • 0030891182 scopus 로고    scopus 로고
    • Ion channels formed by HIV-1 Vpu: A modelling and simulation study
    • Grice A.L., Kerr I.D., Sansom M.S. Ion channels formed by HIV-1 Vpu: a modelling and simulation study. FEBS Lett. 405:1997;299-304.
    • (1997) FEBS Lett. , vol.405 , pp. 299-304
    • Grice, A.L.1    Kerr, I.D.2    Sansom, M.S.3
  • 74
    • 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
    • Gottlinger H.G., Dorfman T., Cohen E.A., Haseltine W.A. 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. 90:1993;7381-7385.
    • (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
  • 75
    • 0032889496 scopus 로고    scopus 로고
    • Lack of effect of cytoplasmic tail truncations on human immunodeficiency virus type 2 ROD env particle release activity
    • Bour S.P., Aberham C., Perrin C., Strebel K. Lack of effect of cytoplasmic tail truncations on human immunodeficiency virus type 2 ROD env particle release activity. J. Virol. 73:1999;778-782.
    • (1999) J. Virol. , vol.73 , pp. 778-782
    • Bour, S.P.1    Aberham, C.2    Perrin, C.3    Strebel, K.4
  • 76
    • 0023026104 scopus 로고
    • Molecular cloning and polymorphism of the human immune deficiency virus type 2
    • Clavel F., Guyader M., Guetard D., Salle M., Montagnier L., Alizon M. Molecular cloning and polymorphism of the human immune deficiency virus type 2. Nature. 324:1986;691-695.
    • (1986) Nature , vol.324 , pp. 691-695
    • Clavel, F.1    Guyader, M.2    Guetard, D.3    Salle, M.4    Montagnier, L.5    Alizon, M.6
  • 77
    • 0037466524 scopus 로고    scopus 로고
    • Naturally occurring amino acid substitutions in the HIV-2 ROD envelope glycoprotein regulate its ability to augment viral particle release
    • Bour S., Akari H., Miyagi E., Strebel K. Naturally occurring amino acid substitutions in the HIV-2 ROD envelope glycoprotein regulate its ability to augment viral particle release. Virology. 309:2003;85-98.
    • (2003) Virology , vol.309 , pp. 85-98
    • Bour, S.1    Akari, H.2    Miyagi, E.3    Strebel, K.4
  • 78
    • 0034691653 scopus 로고    scopus 로고
    • Comparison of Vpu sequences from diverse geographical isolates of HIV type 1 identifies the presence of highly variable domains, additional invariant amino acids, and a signature sequence motif common to subtype C isolates
    • McCormick-Davis C., Dalton S.B., Singh D.K., Stephens E.B. Comparison of Vpu sequences from diverse geographical isolates of HIV type 1 identifies the presence of highly variable domains, additional invariant amino acids, and a signature sequence motif common to subtype C isolates. AIDS Res. Hum. Retroviruses. 16:2000;1089-1095.
    • (2000) AIDS Res. Hum. Retroviruses , vol.16 , pp. 1089-1095
    • McCormick-Davis, C.1    Dalton, S.B.2    Singh, D.K.3    Stephens, E.B.4
  • 79
    • 0027470193 scopus 로고
    • Mapping of a new immunodominant human linear B-cell epitope on the vpu protein of the human immunodeficiency virus type 1
    • Kusk P., Lindhardt B.O., Bugge T.H., Holmback K., Hulgaard E.F. Mapping of a new immunodominant human linear B-cell epitope on the vpu protein of the human immunodeficiency virus type 1. J. Acquired Immune Defic. Syndr. 6:1993;334-338.
    • (1993) J. Acquired Immune Defic. Syndr. , vol.6 , pp. 334-338
    • Kusk, P.1    Lindhardt, B.O.2    Bugge, T.H.3    Holmback, K.4    Hulgaard, E.F.5
  • 80
    • 0025074572 scopus 로고
    • The antibody response to the HIV-1 specific "out" (vpu) protein: Identification of an immunodominant epitope and correlation of antibody detectability to clinical stages
    • Schneider T., Hildebrandt P., Ronspeck W., Weigelt W., Pauli G. The antibody response to the HIV-1 specific "out" (vpu) protein: identification of an immunodominant epitope and correlation of antibody detectability to clinical stages. AIDS Res. Hum. Retroviruses. 6:1990;943-950.
    • (1990) AIDS Res. Hum. Retroviruses , vol.6 , pp. 943-950
    • Schneider, T.1    Hildebrandt, P.2    Ronspeck, W.3    Weigelt, W.4    Pauli, G.5
  • 83
    • 0036340475 scopus 로고    scopus 로고
    • Clustering patterns of cytotoxic T-lymphocyte epitopes in human immunodeficiency virus type 1 (HIV-1) proteins reveal imprints of immune evasion on HIV-1 global variation
    • Yusim K., Kesmir C., Gaschen B., Addo M.M., Altfeld M., Brunak S., Chigaev A., Detours V., Korber B.T. Clustering patterns of cytotoxic T-lymphocyte epitopes in human immunodeficiency virus type 1 (HIV-1) proteins reveal imprints of immune evasion on HIV-1 global variation. J. Virol. 76:2002;8757-8768.
    • (2002) J. Virol. , vol.76 , pp. 8757-8768
    • Yusim, K.1    Kesmir, C.2    Gaschen, B.3    Addo, M.M.4    Altfeld, M.5    Brunak, S.6    Chigaev, A.7    Detours, V.8    Korber, B.T.9
  • 84
    • 0030976282 scopus 로고    scopus 로고
    • A cell-free stock of simian-human immunodeficiency virus that causes AIDS in pig-tailed macaques has a limited number of amino acid substitutions in both SIVmac and HIV-1 regions of the genome and has offered cytotropism
    • Stephens E.B., Mukherjee S., Sahni M., Zhuge W., Raghavan R., Singh D.K., Leung K., Atkinson B., Li Z., Joag S.V., Liu Z.Q., Narayan O. A cell-free stock of simian-human immunodeficiency virus that causes AIDS in pig-tailed macaques has a limited number of amino acid substitutions in both SIVmac and HIV-1 regions of the genome and has offered cytotropism. Virology. 231:1997;313-321.
    • (1997) Virology , vol.231 , pp. 313-321
    • Stephens, E.B.1    Mukherjee, S.2    Sahni, M.3    Zhuge, W.4    Raghavan, R.5    Singh, D.K.6    Leung, K.7    Atkinson, B.8    Li, Z.9    Joag, S.V.10    Liu, Z.Q.11    Narayan, O.12
  • 85
    • 0032169152 scopus 로고    scopus 로고
    • Chronology of genetic changes in the vpu, env, and Nef genes of chimeric simian-human immunodeficiency virus (strain HXB2) during acquisition of virulence for pig-tailed macaques
    • McCormick-Davis C., Zhao L.J., Mukherjee S., Leung K., Sheffer D., Joag S.V., Narayan O., Stephens E.B. Chronology of genetic changes in the vpu, env, and Nef genes of chimeric simian-human immunodeficiency virus (strain HXB2) during acquisition of virulence for pig-tailed macaques. Virology. 248:1998;275-283.
    • (1998) Virology , vol.248 , pp. 275-283
    • McCormick-Davis, C.1    Zhao, L.J.2    Mukherjee, S.3    Leung, K.4    Sheffer, D.5    Joag, S.V.6    Narayan, O.7    Stephens, E.B.8
  • 87
    • 0035995683 scopus 로고    scopus 로고
    • Presence of Intact vpu and nef genes in nonpathogenic SHIV is essential for acquisition of pathogenicity of this virus by serial passage in macaques
    • Mackay G.A., Niu Y., Liu Z.Q., Mukherjee S., Li Z., Adany I., Buch S., Zhuge W., McClure H.M., Narayan O., Smith M.S. Presence of Intact vpu and nef genes in nonpathogenic SHIV is essential for acquisition of pathogenicity of this virus by serial passage in macaques. Virology. 295:2002;133-146.
    • (2002) Virology , vol.295 , pp. 133-146
    • Mackay, G.A.1    Niu, Y.2    Liu, Z.Q.3    Mukherjee, S.4    Li, Z.5    Adany, I.6    Buch, S.7    Zhuge, W.8    McClure, H.M.9    Narayan, O.10    Smith, M.S.11
  • 88
    • 0036059017 scopus 로고    scopus 로고
    • Deletion of the vpu sequences prior to the env in a simian-human immunodeficiency virus results in enhanced Env precursor synthesis but is less pathogenic for pig-tailed macaques
    • Stephens E.B., McCormick C., Pacyniak E., Griffin D., Pinson D.M., Sun F., Nothnick W., Wong S.W., Gunderson R., Berman N.E., Singh D.K. Deletion of the vpu sequences prior to the env in a simian-human immunodeficiency virus results in enhanced Env precursor synthesis but is less pathogenic for pig-tailed macaques. Virology. 293:2002;252-261.
    • (2002) Virology , vol.293 , pp. 252-261
    • Stephens, E.B.1    McCormick, C.2    Pacyniak, E.3    Griffin, D.4    Pinson, D.M.5    Sun, F.6    Nothnick, W.7    Wong, S.W.8    Gunderson, R.9    Berman, N.E.10    Singh, D.K.11
  • 89
    • 0034691032 scopus 로고    scopus 로고
    • A molecular clone of simian-human immunodeficiency virus (DeltavpuSHIV(KU-1bMC33)) with a truncated, non-membrane-bound vpu results in rapid CD4(+) T cell loss and neuro-AIDS in pig-tailed macaques
    • McCormick-Davis C., Dalton S.B., Hout D.R., Singh D.K., Berman N.E., Yong C., Pinson D.M., Foresman L., Stephens E.B. A molecular clone of simian-human immunodeficiency virus (DeltavpuSHIV(KU-1bMC33)) with a truncated, non-membrane-bound vpu results in rapid CD4(+) T cell loss and neuro-AIDS in pig-tailed macaques. Virology. 272:2000;112-126.
    • (2000) Virology , vol.272 , pp. 112-126
    • McCormick-Davis, C.1    Dalton, S.B.2    Hout, D.R.3    Singh, D.K.4    Berman, N.E.5    Yong, C.6    Pinson, D.M.7    Foresman, L.8    Stephens, E.B.9
  • 90
    • 0035970306 scopus 로고    scopus 로고
    • A simian human immunodeficiency virus with a nonfunctional Vpu (deltavpuSHIV(KU-1bMC33)) isolated from a macaque with neuroAIDS has selected for mutations in env and nef that contributed to its pathogenic phenotype
    • Singh D.K., McCormick C., Pacyniak E., Lawrence K., Dalton S.B., Pinson D.M., Sun F., Berman N.E., Calvert M., Gunderson R.S., Wong S.W., Stephens E.B. A simian human immunodeficiency virus with a nonfunctional Vpu (deltavpuSHIV(KU-1bMC33)) isolated from a macaque with neuroAIDS has selected for mutations in env and nef that contributed to its pathogenic phenotype. Virology. 282:2001;123-140.
    • (2001) Virology , vol.282 , pp. 123-140
    • Singh, D.K.1    McCormick, C.2    Pacyniak, E.3    Lawrence, K.4    Dalton, S.B.5    Pinson, D.M.6    Sun, F.7    Berman, N.E.8    Calvert, M.9    Gunderson, R.S.10    Wong, S.W.11    Stephens, E.B.12
  • 91
    • 0033585117 scopus 로고    scopus 로고
    • Cell surface CD4 inhibits HIV-1 particle release by interfering with Vpu activity
    • Bour S., Perrin C., Strebel K. Cell surface CD4 inhibits HIV-1 particle release by interfering with Vpu activity. J. Biol. Chem. 274:1999;33800-33806.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33800-33806
    • Bour, S.1    Perrin, C.2    Strebel, K.3
  • 93
    • 0036708437 scopus 로고    scopus 로고
    • Molecular dynamics investigation of membrane-bound bundles of the channel-forming transmembrane domain of viral protein U from the human immunodeficiency virus HIV-1
    • Lopez C.F., Montal M., Blasie J.K., Klein M.L., Moore P.B. Molecular dynamics investigation of membrane-bound bundles of the channel-forming transmembrane domain of viral protein U from the human immunodeficiency virus HIV-1. Biophys. J. 83:2002;1259-1267.
    • (2002) Biophys. J. , vol.83 , pp. 1259-1267
    • Lopez, C.F.1    Montal, M.2    Blasie, J.K.3    Klein, M.L.4    Moore, P.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.