메뉴 건너뛰기




Volumn 424, Issue 1, 2012, Pages 33-44

HIV-1 Vpu's lipid raft association is dispensable for counteraction of the particle release restriction imposed by CD317/Tetherin

Author keywords

CD317; CRAC motif; DRM; HIV 1 release; Lipid rafts; Vpu

Indexed keywords

CD137 ANTIGEN; CHOLESTEROL; PROTEIN; TYROSINE; VALINE;

EID: 84856223412     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2011.12.008     Document Type: Article
Times cited : (19)

References (60)
  • 1
    • 79952424915 scopus 로고    scopus 로고
    • Differential effects of human immunodeficiency virus type 1 Vpu on the stability of BST-2/Tetherin
    • Andrew A.J., Miyagi E., Strebel K. Differential effects of human immunodeficiency virus type 1 Vpu on the stability of BST-2/Tetherin. J. Virol. 2011, 85:2611-2619.
    • (2011) J. Virol. , vol.85 , pp. 2611-2619
    • Andrew, A.J.1    Miyagi, E.2    Strebel, K.3
  • 3
    • 33748325741 scopus 로고    scopus 로고
    • Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER
    • Browman D.T., Resek M.E., Zajchowski L.D., Robbins S.M. Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER. J. Cell Sci. 2006, 119:3149-3160.
    • (2006) J. Cell Sci. , vol.119 , pp. 3149-3160
    • Browman, D.T.1    Resek, M.E.2    Zajchowski, L.D.3    Robbins, S.M.4
  • 4
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown D.A., Rose J.K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 1992, 68:533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 5
    • 66149099203 scopus 로고    scopus 로고
    • Suppression of Tetherin-restricting activity upon human immunodeficiency virus type 1 particle release correlates with localization of Vpu in the trans-Golgi network
    • Dube M., Roy B.B., Guiot-Guillain P., Mercier J., Binette J., Leung G., Cohen E.A. Suppression of Tetherin-restricting activity upon human immunodeficiency virus type 1 particle release correlates with localization of Vpu in the trans-Golgi network. J. Virol. 2009, 83:4574-4590.
    • (2009) J. Virol. , vol.83 , pp. 4574-4590
    • Dube, M.1    Roy, B.B.2    Guiot-Guillain, P.3    Mercier, J.4    Binette, J.5    Leung, G.6    Cohen, E.A.7
  • 6
    • 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:e1000856.
    • (2010) PLoS Pathog. , vol.6
    • 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
    • 33750614324 scopus 로고    scopus 로고
    • Specific and distinct determinants mediate membrane binding and lipid raft incorporation of HIV-1(SF2) Nef
    • Giese S.I., Woerz I., Homann S., Tibroni N., Geyer M., Fackler O.T. Specific and distinct determinants mediate membrane binding and lipid raft incorporation of HIV-1(SF2) Nef. Virology 2006, 355:175-191.
    • (2006) Virology , vol.355 , pp. 175-191
    • Giese, S.I.1    Woerz, I.2    Homann, S.3    Tibroni, N.4    Geyer, M.5    Fackler, O.T.6
  • 10
    • 77950495072 scopus 로고    scopus 로고
    • Antagonism of CD317 restriction of human immunodeficiency virus type 1 (HIV-1) particle release and depletion of CD317 are separable activities of HIV-1 Vpu
    • Goffinet C., Homann S., Ambiel I., Tibroni N., Rupp D., Keppler O.T., Fackler O.T. Antagonism of CD317 restriction of human immunodeficiency virus type 1 (HIV-1) particle release and depletion of CD317 are separable activities of HIV-1 Vpu. J. Virol. 2010, 84:4089-4094.
    • (2010) J. Virol. , vol.84 , pp. 4089-4094
    • Goffinet, C.1    Homann, S.2    Ambiel, I.3    Tibroni, N.4    Rupp, D.5    Keppler, O.T.6    Fackler, O.T.7
  • 11
    • 67249100279 scopus 로고    scopus 로고
    • Mutation of a single residue renders human Tetherin resistant to HIV-1 Vpu-mediated depletion
    • Gupta R.K., Hue S., Schaller T., Verschoor E., Pillay D., Towers G.J. Mutation of a single residue renders human Tetherin resistant to HIV-1 Vpu-mediated depletion. PLoS Pathog. 2009, 5:e1000443.
    • (2009) PLoS Pathog. , vol.5
    • Gupta, R.K.1    Hue, S.2    Schaller, T.3    Verschoor, E.4    Pillay, D.5    Towers, G.J.6
  • 14
    • 0037384986 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 assembly and lipid rafts: Pr55(gag) associates with membrane domains that are largely resistant to Brij98 but sensitive to Triton X-100
    • Holm K., Weclewicz K., Hewson R., Suomalainen M. Human immunodeficiency virus type 1 assembly and lipid rafts: Pr55(gag) associates with membrane domains that are largely resistant to Brij98 but sensitive to Triton X-100. J. Virol. 2003, 77:4805-4817.
    • (2003) J. Virol. , vol.77 , pp. 4805-4817
    • Holm, K.1    Weclewicz, K.2    Hewson, R.3    Suomalainen, M.4
  • 15
    • 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, 26:527-534.
    • (1995) Genomics , vol.26 , 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
  • 16
    • 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, 284:35060-35072.
    • (2009) J. Biol. Chem. , vol.284 , 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, 106:2886-2891.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 2886-2891
    • Kaletsky, R.L.1    Francica, J.R.2    Agrawal-Gamse, C.3    Bates, P.4
  • 19
    • 13744259226 scopus 로고    scopus 로고
    • Rodent cells support key functions of the human immunodeficiency virus type 1 pathogenicity factor Nef
    • Keppler O.T., Allespach I., Schuller L., Fenard D., Greene W.C., Fackler O.T. Rodent cells support key functions of the human immunodeficiency virus type 1 pathogenicity factor Nef. J. Virol. 2005, 79:1655-1665.
    • (2005) J. Virol. , vol.79 , pp. 1655-1665
    • Keppler, O.T.1    Allespach, I.2    Schuller, L.3    Fenard, D.4    Greene, W.C.5    Fackler, O.T.6
  • 20
    • 78650636704 scopus 로고    scopus 로고
    • Identification of amino acids in the human Tetherin transmembrane domain responsible for HIV-1 Vpu interaction and susceptibility
    • Kobayashi T., Ode H., Yoshida T., Sato K., Gee P., Yamamoto S.P., Ebina H., Strebel K., Sato H., Koyanagi Y. Identification of amino acids in the human Tetherin transmembrane domain responsible for HIV-1 Vpu interaction and susceptibility. J. Virol. 2011, 85:932-945.
    • (2011) J. Virol. , vol.85 , pp. 932-945
    • Kobayashi, T.1    Ode, H.2    Yoshida, T.3    Sato, K.4    Gee, P.5    Yamamoto, S.P.6    Ebina, H.7    Strebel, K.8    Sato, H.9    Koyanagi, Y.10
  • 21
    • 12144291075 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef activates p21-activated kinase via recruitment into lipid rafts
    • Krautkramer E., Giese S.I., Gasteier J.E., Muranyi W., Fackler O.T. Human immunodeficiency virus type 1 Nef activates p21-activated kinase via recruitment into lipid rafts. J. Virol. 2004, 78:4085-4097.
    • (2004) J. Virol. , vol.78 , pp. 4085-4097
    • Krautkramer, E.1    Giese, S.I.2    Gasteier, J.E.3    Muranyi, W.4    Fackler, O.T.5
  • 22
    • 80051922428 scopus 로고    scopus 로고
    • Vpu-mediated Tetherin antagonism of ongoing HIV-1 infection in CD4(+) T-cells is not directly related to the extent of Tetherin cell surface downmodulation
    • Kuhl B.D., Sloan R.D., Donahue D.A., Liang C., Wainberg M.A. Vpu-mediated Tetherin antagonism of ongoing HIV-1 infection in CD4(+) T-cells is not directly related to the extent of Tetherin cell surface downmodulation. Virology 2011, 417:353-361.
    • (2011) Virology , vol.417 , pp. 353-361
    • Kuhl, B.D.1    Sloan, R.D.2    Donahue, D.A.3    Liang, C.4    Wainberg, M.A.5
  • 23
    • 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, 4:694-709.
    • (2003) Traffic , vol.4 , pp. 694-709
    • Kupzig, S.1    Korolchuk, V.2    Rollason, R.3    Sugden, A.4    Wilde, A.5    Banting, G.6
  • 24
    • 80054000378 scopus 로고    scopus 로고
    • Role of the endocytic pathway in the counteraction of BST-2 by human lentiviral pathogens
    • Lau D., Kwan W., Guatelli J. Role of the endocytic pathway in the counteraction of BST-2 by human lentiviral pathogens. J. Virol. 2011, 85:9834-9846.
    • (2011) J. Virol. , vol.85 , pp. 9834-9846
    • Lau, D.1    Kwan, W.2    Guatelli, J.3
  • 25
    • 0031755752 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern
    • Li H., Papadopoulos V. Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern. Endocrinology 1998, 139:4991-4997.
    • (1998) Endocrinology , vol.139 , pp. 4991-4997
    • Li, H.1    Papadopoulos, V.2
  • 26
    • 0037388897 scopus 로고    scopus 로고
    • Monocyte lipid rafts contain proteins implicated in vesicular trafficking and phagosome formation
    • Li N., Mak A., Richards D.P., Naber C., Keller B.O., Li L., Shaw A.R. Monocyte lipid rafts contain proteins implicated in vesicular trafficking and phagosome formation. Proteomics 2003, 3:536-548.
    • (2003) Proteomics , vol.3 , pp. 536-548
    • Li, N.1    Mak, A.2    Richards, D.P.3    Naber, C.4    Keller, B.O.5    Li, L.6    Shaw, A.R.7
  • 27
    • 0036789937 scopus 로고    scopus 로고
    • Myristoylation as a target for inhibiting HIV assembly: unsaturated fatty acids block viral budding
    • Lindwasser O.W., Resh M.D. Myristoylation as a target for inhibiting HIV assembly: unsaturated fatty acids block viral budding. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:13037-13042.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 13037-13042
    • Lindwasser, O.W.1    Resh, M.D.2
  • 28
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D., Simons K. Lipid rafts as a membrane-organizing principle. Science 2010, 327:46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 29
    • 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:e1000574.
    • (2009) PLoS Pathog. , vol.5
    • Mangeat, B.1    Gers-Huber, G.2    Lehmann, M.3    Zufferey, M.4    Luban, J.5    Piguet, V.6
  • 30
    • 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, 83:9672-9681.
    • (2009) J. Virol. , vol.83 , 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
  • 32
    • 18044378256 scopus 로고    scopus 로고
    • The Nef protein of human immunodeficiency virus establishes superinfection immunity by a dual strategy to downregulate cell-surface CCR5 and CD4
    • Michel N., Allespach I., Venzke S., Fackler O.T., Keppler O.T. The Nef protein of human immunodeficiency virus establishes superinfection immunity by a dual strategy to downregulate cell-surface CCR5 and CD4. Curr. Biol. 2005, 15:714-723.
    • (2005) Curr. Biol. , vol.15 , pp. 714-723
    • Michel, N.1    Allespach, I.2    Venzke, S.3    Fackler, O.T.4    Keppler, O.T.5
  • 34
    • 62449325310 scopus 로고    scopus 로고
    • Vpu enhances HIV-1 virus release in the absence of Bst-2 cell surface down-modulation and intracellular depletion
    • Miyagi E., Andrew A.J., Kao S., Strebel K. Vpu enhances HIV-1 virus release in the absence of Bst-2 cell surface down-modulation and intracellular depletion. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:2868-2873.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 2868-2873
    • Miyagi, E.1    Andrew, A.J.2    Kao, S.3    Strebel, K.4
  • 35
    • 23844462163 scopus 로고    scopus 로고
    • Flotillins and the PHB domain protein family: rafts, worms and anaesthetics
    • Morrow I.C., Parton R.G. Flotillins and the PHB domain protein family: rafts, worms and anaesthetics. Traffic 2005, 6:725-740.
    • (2005) Traffic , vol.6 , pp. 725-740
    • Morrow, I.C.1    Parton, R.G.2
  • 36
    • 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, 451:425-430.
    • (2008) Nature , vol.451 , pp. 425-430
    • Neil, S.J.1    Zang, T.2    Bieniasz, P.D.3
  • 37
    • 0034015604 scopus 로고    scopus 로고
    • Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts
    • Nguyen D.H., Hildreth J.E. Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts. J. Virol. 2000, 74:3264-3272.
    • (2000) J. Virol. , vol.74 , pp. 3264-3272
    • Nguyen, D.H.1    Hildreth, J.E.2
  • 38
    • 1342343136 scopus 로고    scopus 로고
    • Codon optimization of the HIV-1 vpu and vif genes stabilizes their mRNA and allows for highly efficient Rev-independent expression
    • Nguyen K.L., Llano M., Akari H., Miyagi E., Poeschla E.M., Strebel K., Bour S. Codon optimization of the HIV-1 vpu and vif genes stabilizes their mRNA and allows for highly efficient Rev-independent expression. Virology 2004, 319:163-175.
    • (2004) Virology , vol.319 , pp. 163-175
    • Nguyen, K.L.1    Llano, M.2    Akari, H.3    Miyagi, E.4    Poeschla, E.M.5    Strebel, K.6    Bour, S.7
  • 39
    • 0035923525 scopus 로고    scopus 로고
    • Plasma membrane rafts play a critical role in HIV-1 assembly and release
    • Ono A., Freed E.O. Plasma membrane rafts play a critical role in HIV-1 assembly and release. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:13925-13930.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 13925-13930
    • Ono, A.1    Freed, E.O.2
  • 40
    • 77954043624 scopus 로고    scopus 로고
    • The RING-CH ligase K5 antagonizes restriction of KSHV and HIV-1 particle release by mediating ubiquitin-dependent endosomal degradation of Tetherin
    • Pardieu C., Vigan R., Wilson S.J., Calvi A., Zang T., Bieniasz P., Kellam P., Towers G.J., Neil S.J. The RING-CH ligase K5 antagonizes restriction of KSHV and HIV-1 particle release by mediating ubiquitin-dependent endosomal degradation of Tetherin. PLoS Pathog. 2010, 6:e1000843.
    • (2010) PLoS Pathog. , vol.6
    • Pardieu, C.1    Vigan, R.2    Wilson, S.J.3    Calvi, A.4    Zang, T.5    Bieniasz, P.6    Kellam, P.7    Towers, G.J.8    Neil, S.J.9
  • 42
    • 33745241638 scopus 로고    scopus 로고
    • Effects of signal peptide exchange on HIV-1 glycoprotein expression and viral infectivity in mammalian cells
    • Pfeiffer T., Pisch T., Devitt G., Holtkotte D., Bosch V. Effects of signal peptide exchange on HIV-1 glycoprotein expression and viral infectivity in mammalian cells. FEBS Lett. 2006, 580:3775-3778.
    • (2006) FEBS Lett. , vol.580 , pp. 3775-3778
    • Pfeiffer, T.1    Pisch, T.2    Devitt, G.3    Holtkotte, D.4    Bosch, V.5
  • 44
    • 40149097137 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef recruits the guanine exchange factor Vav1 via an unexpected interface into plasma membrane microdomains for association with p21-activated kinase 2 activity
    • Rauch S., Pulkkinen K., Saksela K., Fackler O.T. Human immunodeficiency virus type 1 Nef recruits the guanine exchange factor Vav1 via an unexpected interface into plasma membrane microdomains for association with p21-activated kinase 2 activity. J. Virol. 2008, 82:2918-2929.
    • (2008) J. Virol. , vol.82 , pp. 2918-2929
    • Rauch, S.1    Pulkkinen, K.2    Saksela, K.3    Fackler, O.T.4
  • 45
    • 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, 120:3850-3858.
    • (2007) J. Cell Sci. , vol.120 , pp. 3850-3858
    • Rollason, R.1    Korolchuk, V.2    Hamilton, C.3    Schu, P.4    Banting, G.5
  • 46
    • 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, 83:7536-7546.
    • (2009) J. Virol. , vol.83 , 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
  • 47
    • 0033578016 scopus 로고    scopus 로고
    • Inhibition of HIV-1 progeny virion release by cell-surface CD4 is relieved by expression of the viral Nef protein
    • Ross T.M., Oran A.E., Cullen B.R. Inhibition of HIV-1 progeny virion release by cell-surface CD4 is relieved by expression of the viral Nef protein. Curr. Biol. 1999, 9:613-621.
    • (1999) Curr. Biol. , vol.9 , pp. 613-621
    • Ross, T.M.1    Oran, A.E.2    Cullen, B.R.3
  • 48
    • 78049268481 scopus 로고    scopus 로고
    • Membrane raft association of the Vpu protein of human immunodeficiency virus type 1 correlates with enhanced virus release
    • Ruiz A., Hill M.S., Schmitt K., Stephens E.B. Membrane raft association of the Vpu protein of human immunodeficiency virus type 1 correlates with enhanced virus release. Virology 2010, 408:89-102.
    • (2010) Virology , vol.408 , pp. 89-102
    • Ruiz, A.1    Hill, M.S.2    Schmitt, K.3    Stephens, E.B.4
  • 49
    • 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, 83:2382-2385.
    • (2009) J. Virol. , vol.83 , pp. 2382-2385
    • Sakuma, T.1    Noda, T.2    Urata, S.3    Kawaoka, Y.4    Yasuda, J.5
  • 50
    • 84855187526 scopus 로고    scopus 로고
    • HIV-1 Vpu blocks recycling and biosynthetic transport of the intrinsic immunity factor CD317/Tetherin to overcome the virion release restriction
    • Schmidt S., Fritz J.V., Bitzegeio J., Fackler O.T., Keppler O.T. HIV-1 Vpu blocks recycling and biosynthetic transport of the intrinsic immunity factor CD317/Tetherin to overcome the virion release restriction. mBio 2011, 2:e00036-11.
    • (2011) mBio , vol.2
    • Schmidt, S.1    Fritz, J.V.2    Bitzegeio, J.3    Fackler, O.T.4    Keppler, O.T.5
  • 51
    • 78751505454 scopus 로고    scopus 로고
    • Compensatory changes in the cytoplasmic tail of gp41 confer resistance to Tetherin/BST-2 in a pathogenic nef-deleted SIV
    • Serra-Moreno R., Jia B., Breed M., Alvarez X., Evans D.T. Compensatory changes in the cytoplasmic tail of gp41 confer resistance to Tetherin/BST-2 in a pathogenic nef-deleted SIV. Cell Host Microbe 2011, 9:46-57.
    • (2011) Cell Host Microbe , vol.9 , pp. 46-57
    • Serra-Moreno, R.1    Jia, B.2    Breed, M.3    Alvarez, X.4    Evans, D.T.5
  • 52
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., Ikonen E. Functional rafts in cell membranes. Nature 1997, 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 53
    • 79751526122 scopus 로고    scopus 로고
    • Beta-TrCP is dispensable for Vpu's ability to overcome the CD317/Tetherin-imposed restriction to HIV-1 release
    • Tervo H.M., Homann S., Ambiel I., Fritz J.V., Fackler O.T., Keppler O.T. beta-TrCP is dispensable for Vpu's ability to overcome the CD317/Tetherin-imposed restriction to HIV-1 release. Retrovirology 2011, 8:9.
    • (2011) Retrovirology , vol.8 , pp. 9
    • Tervo, H.M.1    Homann, S.2    Ambiel, I.3    Fritz, J.V.4    Fackler, O.T.5    Keppler, O.T.6
  • 55
    • 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, 84:12958-12970.
    • (2010) J. Virol. , vol.84 , pp. 12958-12970
    • Vigan, R.1    Neil, S.J.2
  • 56
    • 37849019272 scopus 로고    scopus 로고
    • Hydrophobic substitutions in the first residue of the CRAC segment of the gp41 protein of HIV
    • Vishwanathan S.A., Thomas A., Brasseur R., Epand R.F., Hunter E., Epand R.M. Hydrophobic substitutions in the first residue of the CRAC segment of the gp41 protein of HIV. Biochemistry 2008, 47:124-130.
    • (2008) Biochemistry , vol.47 , pp. 124-130
    • Vishwanathan, S.A.1    Thomas, A.2    Brasseur, R.3    Epand, R.F.4    Hunter, E.5    Epand, R.M.6
  • 57
    • 78649404289 scopus 로고    scopus 로고
    • Interferon-induced cell membrane proteins, IFITM3 and Tetherin, inhibit vesicular stomatitis virus infection via distinct mechanisms
    • Weidner J.M., Jiang D., Pan X.B., Chang J., Block T.M., Guo J.T. Interferon-induced cell membrane proteins, IFITM3 and Tetherin, inhibit vesicular stomatitis virus infection via distinct mechanisms. J. Virol. 2010, 84:12646-12657.
    • (2010) J. Virol. , vol.84 , pp. 12646-12657
    • Weidner, J.M.1    Jiang, D.2    Pan, X.B.3    Chang, J.4    Block, T.M.5    Guo, J.T.6
  • 60
    • 60649093057 scopus 로고    scopus 로고
    • Biochemical and proteomic approaches for the study of membrane microdomains
    • Zheng Y.Z., Foster L.J. Biochemical and proteomic approaches for the study of membrane microdomains. J. Proteomics 2009, 72:12-22.
    • (2009) J. Proteomics , vol.72 , pp. 12-22
    • Zheng, Y.Z.1    Foster, L.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.