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Volumn 416, Issue 1-2, 2011, Pages 75-85

Ion channel activity of HIV-1 Vpu is dispensable for counteraction of CD317

Author keywords

CD317; Ion channel; Tetherin; Virus release; Vpu

Indexed keywords

ALANINE; ASPARAGINE; CALNEXIN; CD137 ANTIGEN; CD4 ANTIGEN; ION CHANNEL; VPU PROTEIN;

EID: 79958026081     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2011.04.009     Document Type: Article
Times cited : (32)

References (58)
  • 1
    • 0022495870 scopus 로고
    • Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone
    • Adachi A., Gendelman H.E., Koenig S., Folks T., Willey R., Rabson A., Martin M.A. Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone. J. Virol. 1986, 59(2):284-291.
    • (1986) J. Virol. , vol.59 , Issue.2 , pp. 284-291
    • Adachi, A.1    Gendelman, H.E.2    Koenig, S.3    Folks, T.4    Willey, R.5    Rabson, A.6    Martin, M.A.7
  • 3
    • 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. 1995, 69(3):1510-1520.
    • (1995) J. Virol. , vol.69 , Issue.3 , pp. 1510-1520
    • Bour, S.1    Schubert, U.2    Strebel, K.3
  • 4
    • 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. 1993, 67(7):3877-3884.
    • (1993) J. Virol. , vol.67 , Issue.7 , pp. 3877-3884
    • Chen, M.Y.1    Maldarelli, F.2    Karczewski, M.K.3    Willey, R.L.4    Strebel, K.5
  • 5
    • 0023729963 scopus 로고
    • Identification of a protein encoded by the vpu gene of HIV-1
    • Cohen E.A., Terwilliger E.F., Sodroski J.G., Haseltine W.A. Identification of a protein encoded by the vpu gene of HIV-1. Nature 1988, 334(6182):532-534.
    • (1988) Nature , vol.334 , Issue.6182 , pp. 532-534
    • Cohen, E.A.1    Terwilliger, E.F.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 6
    • 67749095196 scopus 로고    scopus 로고
    • Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2/Tetherin via a {beta}TrCP-dependent mechanism
    • Douglas J.L., Viswanathan K., McCarroll M.N., Gustin J.K., Fruh K., Moses A.V. Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2/Tetherin via a {beta}TrCP-dependent mechanism. J. Virol. 2009, 83(16):7931-7947.
    • (2009) J. Virol. , vol.83 , Issue.16 , pp. 7931-7947
    • Douglas, J.L.1    Viswanathan, K.2    McCarroll, M.N.3    Gustin, J.K.4    Fruh, K.5    Moses, A.V.6
  • 7
    • 77954055324 scopus 로고    scopus 로고
    • Antagonism of tetherin restriction of HIV-1 release by Vpu involves binding and sequestration of the restriction factor in a perinuclear compartment
    • Dube M., Roy B.B., Guiot-Guillain P., Binette J., Mercier J., Chiasson A., Cohen E.A. Antagonism of tetherin restriction of HIV-1 release by Vpu involves binding and sequestration of the restriction factor in a perinuclear compartment. PLoS Pathog. 2010, 6(4):e1000856.
    • (2010) PLoS Pathog. , vol.6 , Issue.4
    • Dube, M.1    Roy, B.B.2    Guiot-Guillain, P.3    Binette, J.4    Mercier, J.5    Chiasson, A.6    Cohen, E.A.7
  • 8
    • 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. 1996, 70(10):7108-7115.
    • (1996) J. Virol. , vol.70 , Issue.10 , pp. 7108-7115
    • Ewart, G.D.1    Sutherland, T.2    Gage, P.W.3    Cox, G.B.4
  • 11
    • 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. U.S.A. 1993, 90(15):7381-7385.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , Issue.15 , pp. 7381-7385
    • Gottlinger, H.G.1    Dorfman, T.2    Cohen, E.A.3    Haseltine, W.A.4
  • 12
    • 21644454519 scopus 로고    scopus 로고
    • Analysis of human immunodeficiency virus type 1 Gag ubiquitination
    • Gottwein E., Krausslich H.G. Analysis of human immunodeficiency virus type 1 Gag ubiquitination. J. Virol. 2005, 79(14):9134-9144.
    • (2005) J. Virol. , vol.79 , Issue.14 , pp. 9134-9144
    • Gottwein, E.1    Krausslich, H.G.2
  • 13
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill O.P., Marty A. Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflugers Arch 1981, 391(2):85-100.
    • (1981) Pflugers Arch , vol.391 , Issue.2 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2
  • 15
    • 33646231733 scopus 로고    scopus 로고
    • A single amino acid substitution within the transmembrane domain of the human immunodeficiency virus type 1 Vpu protein renders simian-human immunodeficiency virus (SHIV(KU-1bMC33)) susceptible to rimantadine
    • Hout D.R., Gomez L.M., Pacyniak E., Miller J.M., Hill M.S., Stephens E.B. A single amino acid substitution within the transmembrane domain of the human immunodeficiency virus type 1 Vpu protein renders simian-human immunodeficiency virus (SHIV(KU-1bMC33)) susceptible to rimantadine. Virology 2006, 348(2):449-461.
    • (2006) Virology , vol.348 , Issue.2 , pp. 449-461
    • Hout, D.R.1    Gomez, L.M.2    Pacyniak, E.3    Miller, J.M.4    Hill, M.S.5    Stephens, E.B.6
  • 16
    • 20244374809 scopus 로고
    • Molecular cloning and chromosomal mapping of a bone marrow stromal cell surface gene, BST2, that may be involved in pre-B-cell growth
    • Ishikawa J., Kaisho T., Tomizawa H., Lee B.O., Kobune Y., Inazawa J., Oritani K., Itoh M., Ochi T., Ishihara K., et al. Molecular cloning and chromosomal mapping of a bone marrow stromal cell surface gene, BST2, that may be involved in pre-B-cell growth. Genomics 1995, 26(3):527-534.
    • (1995) Genomics , vol.26 , Issue.3 , pp. 527-534
    • Ishikawa, J.1    Kaisho, T.2    Tomizawa, H.3    Lee, B.O.4    Kobune, Y.5    Inazawa, J.6    Oritani, K.7    Itoh, M.8    Ochi, T.9    Ishihara, K.10
  • 17
    • 71749086904 scopus 로고    scopus 로고
    • HIV-1 accessory protein Vpu internalizes cell-surface BST-2/tetherin through transmembrane interactions leading to lysosomes
    • Iwabu Y., Fujita H., Kinomoto M., Kaneko K., Ishizaka Y., Tanaka Y., Sata T., Tokunaga K. HIV-1 accessory protein Vpu internalizes cell-surface BST-2/tetherin through transmembrane interactions leading to lysosomes. J. Biol. Chem. 2009, 284(50):35060-35072.
    • (2009) J. Biol. Chem. , vol.284 , Issue.50 , pp. 35060-35072
    • Iwabu, Y.1    Fujita, H.2    Kinomoto, M.3    Kaneko, K.4    Ishizaka, Y.5    Tanaka, Y.6    Sata, T.7    Tokunaga, K.8
  • 18
    • 62449106199 scopus 로고    scopus 로고
    • Tetherin-mediated restriction of filovirus budding is antagonized by the Ebola glycoprotein
    • Kaletsky R.L., Francica J.R., Agrawal-Gamse C., Bates P. Tetherin-mediated restriction of filovirus budding is antagonized by the Ebola glycoprotein. Proc. Natl. Acad. Sci. U.S.A. 2009, 106(8):2886-2891.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , Issue.8 , pp. 2886-2891
    • Kaletsky, R.L.1    Francica, J.R.2    Agrawal-Gamse, C.3    Bates, P.4
  • 19
    • 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. 1990, 64(2):621-629.
    • (1990) J. Virol. , vol.64 , Issue.2 , pp. 621-629
    • Klimkait, T.1    Strebel, K.2    Hoggan, M.D.3    Martin, M.A.4    Orenstein, J.M.5
  • 20
    • 0141494290 scopus 로고    scopus 로고
    • Bst-2/HM1.24 is a raft-associated apical membrane protein with an unusual topology
    • Kupzig S., Korolchuk V., Rollason R., Sugden A., Wilde A., Banting G. Bst-2/HM1.24 is a raft-associated apical membrane protein with an unusual topology. Traffic 2003, 4(10):694-709.
    • (2003) Traffic , vol.4 , Issue.10 , pp. 694-709
    • Kupzig, S.1    Korolchuk, V.2    Rollason, R.3    Sugden, A.4    Wilde, A.5    Banting, G.6
  • 21
    • 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. 2002, 83(3):1259-1267.
    • (2002) Biophys. J. , vol.83 , Issue.3 , pp. 1259-1267
    • Lopez, C.F.1    Montal, M.2    Blasie, J.K.3    Klein, M.L.4    Moore, P.B.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. 1993, 67(8):5056-5061.
    • (1993) J. Virol. , vol.67 , Issue.8 , pp. 5056-5061
    • Maldarelli, F.1    Chen, M.Y.2    Willey, R.L.3    Strebel, K.4
  • 23
    • 70349663496 scopus 로고    scopus 로고
    • HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation
    • Mangeat B., Gers-Huber G., Lehmann M., Zufferey M., Luban J., Piguet V. HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation. PLoS Pathog. 2009, 5(9):e1000574.
    • (2009) PLoS Pathog. , vol.5 , Issue.9
    • Mangeat, B.1    Gers-Huber, G.2    Lehmann, M.3    Zufferey, M.4    Luban, J.5    Piguet, V.6
  • 24
    • 70349267563 scopus 로고    scopus 로고
    • Molecular mechanism of BST2/tetherin downregulation by K5/MIR2 of Kaposi's sarcoma-associated herpesvirus
    • Mansouri M., Viswanathan K., Douglas J.L., Hines J., Gustin J., Moses A.V., Fruh K. Molecular mechanism of BST2/tetherin downregulation by K5/MIR2 of Kaposi's sarcoma-associated herpesvirus. J. Virol. 2009, 83(19):9672-9681.
    • (2009) J. Virol. , vol.83 , Issue.19 , pp. 9672-9681
    • Mansouri, M.1    Viswanathan, K.2    Douglas, J.L.3    Hines, J.4    Gustin, J.5    Moses, A.V.6    Fruh, K.7
  • 25
    • 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., 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(4):565-574.
    • (1998) Mol. Cell , vol.1 , Issue.4 , 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
  • 26
    • 39749180320 scopus 로고    scopus 로고
    • Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism
    • Mehnert T., Routh A., Judge P.J., Lam Y.H., Fischer D., Watts A., Fischer W.B. Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism. Proteins 2008, 70(4):1488-1497.
    • (2008) Proteins , vol.70 , Issue.4 , pp. 1488-1497
    • Mehnert, T.1    Routh, A.2    Judge, P.J.3    Lam, Y.H.4    Fischer, D.5    Watts, A.6    Fischer, W.B.7
  • 28
    • 77956939580 scopus 로고    scopus 로고
    • Inhibition of lipid antigen presentation in dendritic cells by HIV-1 Vpu interference with CD1d recycling from endosomal compartments
    • Moll M., Andersson S.K., Smed-Sorensen A., Sandberg J.K. Inhibition of lipid antigen presentation in dendritic cells by HIV-1 Vpu interference with CD1d recycling from endosomal compartments. Blood 2010, 116(11):1876-1884.
    • (2010) Blood , vol.116 , Issue.11 , pp. 1876-1884
    • Moll, M.1    Andersson, S.K.2    Smed-Sorensen, A.3    Sandberg, J.K.4
  • 29
    • 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. 1998, 431(2):143-148.
    • (1998) FEBS Lett. , vol.431 , Issue.2 , pp. 143-148
    • Moore, P.B.1    Zhong, Q.2    Husslein, T.3    Klein, M.L.4
  • 30
    • 34548392739 scopus 로고    scopus 로고
    • An interferon-alpha-induced tethering mechanism inhibits HIV-1 and Ebola virus particle release but is counteracted by the HIV-1 Vpu protein
    • Neil S.J., Sandrin V., Sundquist W.I., Bieniasz P.D. An interferon-alpha-induced tethering mechanism inhibits HIV-1 and Ebola virus particle release but is counteracted by the HIV-1 Vpu protein. Cell Host Microbe 2007, 2(3):193-203.
    • (2007) Cell Host Microbe , vol.2 , Issue.3 , pp. 193-203
    • Neil, S.J.1    Sandrin, V.2    Sundquist, W.I.3    Bieniasz, P.D.4
  • 31
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • Neil S.J., Zang T., Bieniasz P.D. Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 2008, 451(7177):425-430.
    • (2008) Nature , vol.451 , Issue.7177 , pp. 425-430
    • Neil, S.J.1    Zang, T.2    Bieniasz, P.D.3
  • 32
    • 20444372631 scopus 로고    scopus 로고
    • Identification of a region within the cytoplasmic domain of the subtype B Vpu protein of human immunodeficiency virus type 1 (HIV-1) that is responsible for retention in the golgi complex and its absence in the Vpu protein from a subtype C HIV-1
    • Pacyniak E., Gomez M.L., Gomez L.M., Mulcahy E.R., Jackson M., Hout D.R., Wisdom B.J., Stephens E.B. Identification of a region within the cytoplasmic domain of the subtype B Vpu protein of human immunodeficiency virus type 1 (HIV-1) that is responsible for retention in the golgi complex and its absence in the Vpu protein from a subtype C HIV-1. AIDS Res. Hum. Retroviruses 2005, 21(5):379-394.
    • (2005) AIDS Res. Hum. Retroviruses , vol.21 , Issue.5 , pp. 379-394
    • Pacyniak, E.1    Gomez, M.L.2    Gomez, L.M.3    Mulcahy, E.R.4    Jackson, M.5    Hout, D.R.6    Wisdom, B.J.7    Stephens, E.B.8
  • 33
    • 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. 1998, 72(2):1270-1279.
    • (1998) J. Virol. , vol.72 , Issue.2 , pp. 1270-1279
    • Paul, M.1    Mazumder, S.2    Raja, N.3    Jabbar, M.A.4
  • 35
    • 36549052593 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis of a lipid-raft-associated protein is mediated through a dual tyrosine motif
    • Rollason R., Korolchuk V., Hamilton C., Schu P., Banting G. Clathrin-mediated endocytosis of a lipid-raft-associated protein is mediated through a dual tyrosine motif. J. Cell Sci. 2007, 120(Pt 21):3850-3858.
    • (2007) J. Cell Sci. , vol.120 , Issue.PART 21 , pp. 3850-3858
    • Rollason, R.1    Korolchuk, V.2    Hamilton, C.3    Schu, P.4    Banting, G.5
  • 36
    • 67650860393 scopus 로고    scopus 로고
    • The transmembrane domain of BST-2 determines its sensitivity to down-modulation by human immunodeficiency virus type 1 Vpu
    • Rong L., Zhang J., Lu J., Pan Q., Lorgeoux R.P., Aloysius C., Guo F., Liu S.L., Wainberg M.A., Liang C. The transmembrane domain of BST-2 determines its sensitivity to down-modulation by human immunodeficiency virus type 1 Vpu. J. Virol. 2009, 83(15):7536-7546.
    • (2009) J. Virol. , vol.83 , Issue.15 , pp. 7536-7546
    • Rong, L.1    Zhang, J.2    Lu, J.3    Pan, Q.4    Lorgeoux, R.P.5    Aloysius, C.6    Guo, F.7    Liu, S.L.8    Wainberg, M.A.9    Liang, C.10
  • 37
    • 60049094369 scopus 로고    scopus 로고
    • Inhibition of Lassa and Marburg virus production by tetherin
    • Sakuma T., Noda T., Urata S., Kawaoka Y., Yasuda J. Inhibition of Lassa and Marburg virus production by tetherin. J. Virol. 2009, 83(5):2382-2385.
    • (2009) J. Virol. , vol.83 , Issue.5 , pp. 2382-2385
    • Sakuma, T.1    Noda, T.2    Urata, S.3    Kawaoka, Y.4    Yasuda, J.5
  • 40
    • 0141521574 scopus 로고    scopus 로고
    • Down-modulation of mature major histocompatibility complex class II and up-regulation of invariant chain cell surface expression are well-conserved functions of human and simian immunodeficiency virus nef alleles
    • Schindler M., Wurfl S., Benaroch P., Greenough T.C., Daniels R., Easterbrook P., Brenner M., Munch J., Kirchhoff F. Down-modulation of mature major histocompatibility complex class II and up-regulation of invariant chain cell surface expression are well-conserved functions of human and simian immunodeficiency virus nef alleles. J. Virol. 2003, 77(19):10548-10556.
    • (2003) J. Virol. , vol.77 , Issue.19 , pp. 10548-10556
    • Schindler, M.1    Wurfl, S.2    Benaroch, P.3    Greenough, T.C.4    Daniels, R.5    Easterbrook, P.6    Brenner, M.7    Munch, J.8    Kirchhoff, F.9
  • 41
    • 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. 1996, 70(2):809-819.
    • (1996) J. Virol. , vol.70 , Issue.2 , pp. 809-819
    • Schubert, U.1    Bour, S.2    Ferrer-Montiel, A.V.3    Montal, M.4    Maldarell, F.5    Strebel, K.6
  • 42
    • 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
    • Schubert U., Clouse K.A., 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(12):7699-7711.
    • (1995) J. Virol. , vol.69 , Issue.12 , pp. 7699-7711
    • Schubert, U.1    Clouse, K.A.2    Strebel, K.3
  • 43
    • 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. 1996, 398(1):12-18.
    • (1996) FEBS Lett. , vol.398 , Issue.1 , pp. 12-18
    • Schubert, U.1    Ferrer-Montiel, A.V.2    Oblatt-Montal, M.3    Henklein, P.4    Strebel, K.5    Montal, M.6
  • 44
    • 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. 1994, 236(1):16-25.
    • (1994) J. Mol. Biol. , vol.236 , Issue.1 , pp. 16-25
    • Schubert, U.1    Henklein, P.2    Boldyreff, B.3    Wingender, E.4    Strebel, K.5    Porstmann, T.6
  • 46
    • 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. 1994, 68(4):2260-2271.
    • (1994) J. Virol. , vol.68 , Issue.4 , pp. 2260-2271
    • Schubert, U.1    Strebel, K.2
  • 47
    • 78349264184 scopus 로고    scopus 로고
    • Degranulation of natural killer cells following interaction with HIV-1-infected cells is hindered by downmodulation of NTB-A by Vpu
    • Shah A.H., Sowrirajan B., Davis Z.B., Ward J.P., Campbell E.M., Planelles V., Barker E. Degranulation of natural killer cells following interaction with HIV-1-infected cells is hindered by downmodulation of NTB-A by Vpu. Cell Host Microbe 2010, 8(5):397-409.
    • (2010) Cell Host Microbe , vol.8 , Issue.5 , pp. 397-409
    • Shah, A.H.1    Sowrirajan, B.2    Davis, Z.B.3    Ward, J.P.4    Campbell, E.M.5    Planelles, V.6    Barker, E.7
  • 48
    • 79551682881 scopus 로고    scopus 로고
    • BST-2 is rapidly down-regulated from the cell surface by the HIV-1 protein Vpu: evidence for a post-ER mechanism of Vpu-action
    • Skasko M., Tokarev A., Chen C.C., Fischer W.B., Pillai S.K., Guatelli J. BST-2 is rapidly down-regulated from the cell surface by the HIV-1 protein Vpu: evidence for a post-ER mechanism of Vpu-action. Virology 2011, 411(1):65-77.
    • (2011) Virology , vol.411 , Issue.1 , pp. 65-77
    • Skasko, M.1    Tokarev, A.2    Chen, C.C.3    Fischer, W.B.4    Pillai, S.K.5    Guatelli, J.6
  • 49
    • 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 1988, 241(4870):1221-1223.
    • (1988) Science , vol.241 , Issue.4870 , pp. 1221-1223
    • Strebel, K.1    Klimkait, T.2    Martin, M.A.3
  • 50
    • 0032506276 scopus 로고    scopus 로고
    • Structural and functional analysis of the membrane-spanning domain of the human immunodeficiency virus type 1 Vpu protein
    • Tiganos E., Friborg J., Allain B., Daniel N.G., Yao X.J., Cohen E.A. Structural and functional analysis of the membrane-spanning domain of the human immunodeficiency virus type 1 Vpu protein. Virology 1998, 251(1):96-107.
    • (1998) Virology , vol.251 , Issue.1 , pp. 96-107
    • Tiganos, E.1    Friborg, J.2    Allain, B.3    Daniel, N.G.4    Yao, X.J.5    Cohen, E.A.6
  • 51
    • 78650038839 scopus 로고    scopus 로고
    • Serine-threonine ubiquitination mediates downregulation of BST-2/tetherin and relief of restricted virion release by HIV-1 Vpu
    • Tokarev A.A., Munguia J., Guatelli J.C. Serine-threonine ubiquitination mediates downregulation of BST-2/tetherin and relief of restricted virion release by HIV-1 Vpu. J. Virol. 2011, 85(1):51-63.
    • (2011) J. Virol. , vol.85 , Issue.1 , pp. 51-63
    • Tokarev, A.A.1    Munguia, J.2    Guatelli, J.C.3
  • 52
    • 41849116366 scopus 로고    scopus 로고
    • The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein
    • Van Damme N., Goff D., Katsura C., Jorgenson R.L., Mitchell R., Johnson M.C., Stephens E.B., Guatelli J. The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein. Cell Host Microbe 2008, 3(4):245-252.
    • (2008) Cell Host Microbe , vol.3 , Issue.4 , pp. 245-252
    • Van Damme, N.1    Goff, D.2    Katsura, C.3    Jorgenson, R.L.4    Mitchell, R.5    Johnson, M.C.6    Stephens, E.B.7    Guatelli, J.8
  • 53
    • 33644654306 scopus 로고    scopus 로고
    • The pericentriolar recycling endosome plays a key role in Vpu-mediated enhancement of HIV-1 particle release
    • Varthakavi V., Smith R.M., Martin K.L., Derdowski A., Lapierre L.A., Goldenring J.R., Spearman P. The pericentriolar recycling endosome plays a key role in Vpu-mediated enhancement of HIV-1 particle release. Traffic 2006, 7(3):298-307.
    • (2006) Traffic , vol.7 , Issue.3 , pp. 298-307
    • Varthakavi, V.1    Smith, R.M.2    Martin, K.L.3    Derdowski, A.4    Lapierre, L.A.5    Goldenring, J.R.6    Spearman, P.7
  • 54
    • 78649401965 scopus 로고    scopus 로고
    • Determinants of tetherin antagonism in the transmembrane domain of the human immunodeficiency virus type 1 Vpu protein
    • Vigan R., Neil S.J. Determinants of tetherin antagonism in the transmembrane domain of the human immunodeficiency virus type 1 Vpu protein. J. Virol. 2010, 84(24):12958-12970.
    • (2010) J. Virol. , vol.84 , Issue.24 , pp. 12958-12970
    • Vigan, R.1    Neil, S.J.2
  • 55
    • 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. 1992, 66(12):7193-7200.
    • (1992) J. Virol. , vol.66 , Issue.12 , pp. 7193-7200
    • Willey, R.L.1    Maldarelli, F.2    Martin, M.A.3    Strebel, K.4
  • 56
    • 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. 1992, 66(1):226-234.
    • (1992) J. Virol. , vol.66 , Issue.1 , pp. 226-234
    • Willey, R.L.1    Maldarelli, F.2    Martin, M.A.3    Strebel, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.