메뉴 건너뛰기




Volumn 581, Issue 11, 2007, Pages 2089-2097

More than one door - Budding of enveloped viruses through cellular membranes

Author keywords

Budding; ESCRT; Virus envelopment

Indexed keywords

LIPID; MATRIX PROTEIN;

EID: 34248229690     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.03.060     Document Type: Short Survey
Times cited : (155)

References (97)
  • 1
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophages
    • Pelchen-Matthews A., Kramer B., and Marsh M. Infectious HIV-1 assembles in late endosomes in primary macrophages. J. Cell. Biol. 162 (2003) 443-455
    • (2003) J. Cell. Biol. , vol.162 , pp. 443-455
    • Pelchen-Matthews, A.1    Kramer, B.2    Marsh, M.3
  • 3
    • 22744433225 scopus 로고    scopus 로고
    • Macrophages archive HIV-1 virions for dissemination in trans
    • Sharova N., Swingler C., Sharkey M., and Stevenson M. Macrophages archive HIV-1 virions for dissemination in trans. Embo. J. 24 (2005) 2481-2489
    • (2005) Embo. J. , vol.24 , pp. 2481-2489
    • Sharova, N.1    Swingler, C.2    Sharkey, M.3    Stevenson, M.4
  • 6
    • 0036145462 scopus 로고    scopus 로고
    • Assembly of vaccinia virus revisited: de novo membrane synthesis or acquisition from the host?
    • Sodeik B., and Krijnse-Locker J. Assembly of vaccinia virus revisited: de novo membrane synthesis or acquisition from the host?. Trends. Microbiol. 10 (2002) 15-24
    • (2002) Trends. Microbiol. , vol.10 , pp. 15-24
    • Sodeik, B.1    Krijnse-Locker, J.2
  • 7
    • 0034755323 scopus 로고    scopus 로고
    • Structure and assembly of intracellular mature vaccinia virus: isolated-particle analysis
    • Griffiths G., Wepf R., Wendt T., Locker J.K., Cyrklaff M., and Roos N. Structure and assembly of intracellular mature vaccinia virus: isolated-particle analysis. J. Virol. 75 (2001) 11034-11055
    • (2001) J. Virol. , vol.75 , pp. 11034-11055
    • Griffiths, G.1    Wepf, R.2    Wendt, T.3    Locker, J.K.4    Cyrklaff, M.5    Roos, N.6
  • 8
    • 0032935036 scopus 로고    scopus 로고
    • Vaccinia virus intracellular mature virions contain only one lipid membrane
    • Hollinshead M., Vanderplasschen A., Smith G.L., and Vaux D.J. Vaccinia virus intracellular mature virions contain only one lipid membrane. J. Virol. 73 (1999) 1503-1517
    • (1999) J. Virol. , vol.73 , pp. 1503-1517
    • Hollinshead, M.1    Vanderplasschen, A.2    Smith, G.L.3    Vaux, D.J.4
  • 9
    • 0028097957 scopus 로고
    • Assembly of vaccinia virus: the second wrapping cisterna is derived from the trans Golgi network
    • Schmelz M., Sodeik B., Ericsson M., Wolffe E.J., Shida H., Hiller G., and Griffiths G. Assembly of vaccinia virus: the second wrapping cisterna is derived from the trans Golgi network. J. Virol. 68 (1994) 130-147
    • (1994) J. Virol. , vol.68 , pp. 130-147
    • Schmelz, M.1    Sodeik, B.2    Ericsson, M.3    Wolffe, E.J.4    Shida, H.5    Hiller, G.6    Griffiths, G.7
  • 11
    • 2542497232 scopus 로고
    • Location of the spike glycoproteins in the Semliki Forest virus membrane
    • Garoff H., and Simons K. Location of the spike glycoproteins in the Semliki Forest virus membrane. Proc. Natl. Acad. Sci. USA 71 (1974) 3988-3992
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 3988-3992
    • Garoff, H.1    Simons, K.2
  • 12
    • 0029933250 scopus 로고    scopus 로고
    • Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes
    • Vennema H., Godeke G.J., Rossen J.W., Voorhout W.F., Horzinek M.C., Opstelten D.J., and Rottier P.J. Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes. Embo J. 15 (1996) 2020-2028
    • (1996) Embo J. , vol.15 , pp. 2020-2028
    • Vennema, H.1    Godeke, G.J.2    Rossen, J.W.3    Voorhout, W.F.4    Horzinek, M.C.5    Opstelten, D.J.6    Rottier, P.J.7
  • 13
    • 0029162425 scopus 로고
    • Synthesis and secretion of recombinant tick-borne encephalitis virus protein E in soluble and particulate form
    • Allison S.L., Stadler K., Mandl C.W., Kunz C., and Heinz F.X. Synthesis and secretion of recombinant tick-borne encephalitis virus protein E in soluble and particulate form. J. Virol. 69 (1995) 5816-5820
    • (1995) J. Virol. , vol.69 , pp. 5816-5820
    • Allison, S.L.1    Stadler, K.2    Mandl, C.W.3    Kunz, C.4    Heinz, F.X.5
  • 14
    • 9644260511 scopus 로고    scopus 로고
    • Envelopment of the hepatitis B virus nucleocapsid
    • Bruss V. Envelopment of the hepatitis B virus nucleocapsid. Virus. Res. 106 (2004) 199-209
    • (2004) Virus. Res. , vol.106 , pp. 199-209
    • Bruss, V.1
  • 16
    • 0027986768 scopus 로고
    • Novel infectious particles generated by expression of the vesicular stomatitis virus glycoprotein from a self-replicating RNA
    • Rolls M.M., Webster P., Balba N.H., and Rose J.K. Novel infectious particles generated by expression of the vesicular stomatitis virus glycoprotein from a self-replicating RNA. Cell 79 (1994) 497-506
    • (1994) Cell , vol.79 , pp. 497-506
    • Rolls, M.M.1    Webster, P.2    Balba, N.H.3    Rose, J.K.4
  • 17
    • 0029912922 scopus 로고    scopus 로고
    • Budding of rabies virus particles in the absence of the spike glycoprotein
    • Mebatsion T., Konig M., and Conzelmann K.K. Budding of rabies virus particles in the absence of the spike glycoprotein. Cell 84 (1996) 941-951
    • (1996) Cell , vol.84 , pp. 941-951
    • Mebatsion, T.1    Konig, M.2    Conzelmann, K.K.3
  • 19
    • 0141856160 scopus 로고    scopus 로고
    • Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles [corrected]
    • Strecker T., Eichler R., Meulen J., Weissenhorn W., Dieter Klenk H., Garten W., and Lenz O. Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles [corrected]. J. Virol. 77 (2003) 10700-10705
    • (2003) J. Virol. , vol.77 , pp. 10700-10705
    • Strecker, T.1    Eichler, R.2    Meulen, J.3    Weissenhorn, W.4    Dieter Klenk, H.5    Garten, W.6    Lenz, O.7
  • 20
    • 9644281042 scopus 로고    scopus 로고
    • Molecular mechanism of paramyxovirus budding
    • Takimoto T., and Portner A. Molecular mechanism of paramyxovirus budding. Virus. Res. 106 (2004) 133-145
    • (2004) Virus. Res. , vol.106 , pp. 133-145
    • Takimoto, T.1    Portner, A.2
  • 22
    • 7644233177 scopus 로고    scopus 로고
    • Generation of synthetic severe acute respiratory syndrome coronavirus pseudoparticles: implications for assembly and vaccine production
    • Huang Y., Yang Z.Y., Kong W.P., and Nabel G.J. Generation of synthetic severe acute respiratory syndrome coronavirus pseudoparticles: implications for assembly and vaccine production. J. Virol. 78 (2004) 12557-12565
    • (2004) J. Virol. , vol.78 , pp. 12557-12565
    • Huang, Y.1    Yang, Z.Y.2    Kong, W.P.3    Nabel, G.J.4
  • 23
    • 0037572249 scopus 로고    scopus 로고
    • The replication strategy of foamy viruses
    • Rethwilm A. The replication strategy of foamy viruses. Curr. Top. Microbiol. Immunol. 277 (2003) 1-26
    • (2003) Curr. Top. Microbiol. Immunol. , vol.277 , pp. 1-26
    • Rethwilm, A.1
  • 25
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms R.W., Lamb R.A., Rose J.K., and Helenius A. Folding and assembly of viral membrane proteins. Virology 193 (1993) 545-562
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 27
    • 33846821654 scopus 로고    scopus 로고
    • A conserved dileucine motif mediates clathrin and AP-2-dependent endocytosis of the HIV-1 envelope protein
    • Byland R., Vance P.J., Hoxie J.A., and Marsh M. A conserved dileucine motif mediates clathrin and AP-2-dependent endocytosis of the HIV-1 envelope protein. Mol. Biol. Cell. 18 (2007) 414-425
    • (2007) Mol. Biol. Cell. , vol.18 , pp. 414-425
    • Byland, R.1    Vance, P.J.2    Hoxie, J.A.3    Marsh, M.4
  • 29
    • 0141605864 scopus 로고    scopus 로고
    • M-PMV capsid transport is mediated by Env/Gag interactions at the pericentriolar recycling endosome
    • Sfakianos J.N., and Hunter E. M-PMV capsid transport is mediated by Env/Gag interactions at the pericentriolar recycling endosome. Traffic 4 (2003) 671-680
    • (2003) Traffic , vol.4 , pp. 671-680
    • Sfakianos, J.N.1    Hunter, E.2
  • 30
    • 33745753571 scopus 로고    scopus 로고
    • Foamy virus capsid assembly occurs at a pericentriolar region through a cytoplasmic targeting/retention signal in Gag
    • Yu S.F., Eastman S.W., and Linial M.L. Foamy virus capsid assembly occurs at a pericentriolar region through a cytoplasmic targeting/retention signal in Gag. Traffic 7 (2006) 966-977
    • (2006) Traffic , vol.7 , pp. 966-977
    • Yu, S.F.1    Eastman, S.W.2    Linial, M.L.3
  • 31
    • 22944458202 scopus 로고    scopus 로고
    • Altering the tropism of lentiviral vectors through pseudotyping
    • Cronin J., Zhang X.Y., and Reiser J. Altering the tropism of lentiviral vectors through pseudotyping. Curr. Gene. Ther. 5 (2005) 387-398
    • (2005) Curr. Gene. Ther. , vol.5 , pp. 387-398
    • Cronin, J.1    Zhang, X.Y.2    Reiser, J.3
  • 32
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions
    • McLaughlin S., and Aderem A. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. Trends. Biochem. Sci. 20 (1995) 272-276
    • (1995) Trends. Biochem. Sci. , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 33
    • 0344766117 scopus 로고    scopus 로고
    • Opposing effects of human immunodeficiency virus type 1 matrix mutations support a myristyl switch model of gag membrane targeting
    • Paillart J.C., and Gottlinger H.G. Opposing effects of human immunodeficiency virus type 1 matrix mutations support a myristyl switch model of gag membrane targeting. J. Virol. 73 (1999) 2604-2612
    • (1999) J. Virol. , vol.73 , pp. 2604-2612
    • Paillart, J.C.1    Gottlinger, H.G.2
  • 34
    • 0030763024 scopus 로고    scopus 로고
    • Membrane binding of human immunodeficiency virus type 1 matrix protein in vivo supports a conformational myristyl switch mechanism
    • Spearman P., Horton R., Ratner L., and Kuli-Zade I. Membrane binding of human immunodeficiency virus type 1 matrix protein in vivo supports a conformational myristyl switch mechanism. J. Virol. 71 (1997) 6582-6592
    • (1997) J. Virol. , vol.71 , pp. 6582-6592
    • Spearman, P.1    Horton, R.2    Ratner, L.3    Kuli-Zade, I.4
  • 36
    • 0029861657 scopus 로고    scopus 로고
    • Differential membrane binding of the human immunodeficiency virus type 1 matrix protein
    • Zhou W., and Resh M.D. Differential membrane binding of the human immunodeficiency virus type 1 matrix protein. J. Virol. 70 (1996) 8540-8548
    • (1996) J. Virol. , vol.70 , pp. 8540-8548
    • Zhou, W.1    Resh, M.D.2
  • 37
    • 0027432307 scopus 로고
    • Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins
    • Peitzsch R.M., and McLaughlin S. Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins. Biochemistry 32 (1993) 10436-10443
    • (1993) Biochemistry , vol.32 , pp. 10436-10443
    • Peitzsch, R.M.1    McLaughlin, S.2
  • 38
    • 1842859044 scopus 로고    scopus 로고
    • Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins
    • Riffel N., Harlos K., Iourin O., Rao Z., Kingsman A., Stuart D., and Fry E. Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins. Structure 10 (2002) 1627-1636
    • (2002) Structure , vol.10 , pp. 1627-1636
    • Riffel, N.1    Harlos, K.2    Iourin, O.3    Rao, Z.4    Kingsman, A.5    Stuart, D.6    Fry, E.7
  • 39
    • 0032486598 scopus 로고    scopus 로고
    • Retroviral matrix proteins: a structural perspective
    • Conte M.R., and Matthews S. Retroviral matrix proteins: a structural perspective. Virology 246 (1998) 191-198
    • (1998) Virology , vol.246 , pp. 191-198
    • Conte, M.R.1    Matthews, S.2
  • 40
    • 26444444082 scopus 로고    scopus 로고
    • Retroviral matrix domains share electrostatic homology: models for membrane binding function throughout the viral life cycle
    • Murray P.S., Li Z., Wang J., Tang C.L., Honig B., and Murray D. Retroviral matrix domains share electrostatic homology: models for membrane binding function throughout the viral life cycle. Structure 13 (2005) 1521-1531
    • (2005) Structure , vol.13 , pp. 1521-1531
    • Murray, P.S.1    Li, Z.2    Wang, J.3    Tang, C.L.4    Honig, B.5    Murray, D.6
  • 41
    • 0027177935 scopus 로고
    • A large deletion in the matrix domain of the human immunodeficiency virus gag gene redirects virus particle assembly from the plasma membrane to the endoplasmic reticulum
    • Facke M., Janetzko A., Shoeman R.L., and Krausslich H.G. A large deletion in the matrix domain of the human immunodeficiency virus gag gene redirects virus particle assembly from the plasma membrane to the endoplasmic reticulum. J. Virol. 67 (1993) 4972-4980
    • (1993) J. Virol. , vol.67 , pp. 4972-4980
    • Facke, M.1    Janetzko, A.2    Shoeman, R.L.3    Krausslich, H.G.4
  • 42
    • 0033999270 scopus 로고    scopus 로고
    • Role of the Gag matrix domain in targeting human immunodeficiency virus type 1 assembly
    • Ono A., Orenstein J.M., and Freed E.O. Role of the Gag matrix domain in targeting human immunodeficiency virus type 1 assembly. J. Virol. 74 (2000) 2855-2866
    • (2000) J. Virol. , vol.74 , pp. 2855-2866
    • Ono, A.1    Orenstein, J.M.2    Freed, E.O.3
  • 43
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology
    • Murray D., Ben-Tal N., Honig B., and McLaughlin S. Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology. Structure 5 (1997) 985-989
    • (1997) Structure , vol.5 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 44
    • 6944255361 scopus 로고    scopus 로고
    • Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane
    • Ono A., Ablan S.D., Lockett S.J., Nagashima K., and Freed E.O. Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane. Proc. Natl. Acad. Sci. USA 101 (2004) 14889-14894
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14889-14894
    • Ono, A.1    Ablan, S.D.2    Lockett, S.J.3    Nagashima, K.4    Freed, E.O.5
  • 45
    • 33845313646 scopus 로고    scopus 로고
    • PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane
    • Heo W.D., Inoue T., Park W.S., Kim M.L., Park B.O., Wandless T.J., and Meyer T. PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane. Science 314 (2006) 1458-1461
    • (2006) Science , vol.314 , pp. 1458-1461
    • Heo, W.D.1    Inoue, T.2    Park, W.S.3    Kim, M.L.4    Park, B.O.5    Wandless, T.J.6    Meyer, T.7
  • 46
    • 33746625935 scopus 로고    scopus 로고
    • Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
    • Saad J.S., Miller J., Tai J., Kim A., Ghanam R.H., and Summers M.F. Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly. Proc. Natl. Acad. Sci. USA 103 (2006) 11364-11369
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11364-11369
    • Saad, J.S.1    Miller, J.2    Tai, J.3    Kim, A.4    Ghanam, R.H.5    Summers, M.F.6
  • 47
    • 0026934552 scopus 로고
    • Cell biology of viruses that assemble along the biosynthetic pathway
    • Griffiths G., and Rottier P. Cell biology of viruses that assemble along the biosynthetic pathway. Semin. Cell. Biol. 3 (1992) 367-381
    • (1992) Semin. Cell. Biol. , vol.3 , pp. 367-381
    • Griffiths, G.1    Rottier, P.2
  • 48
    • 0029150472 scopus 로고
    • The phospholipid composition of enveloped viruses depends on the intracellular membrane through which they bud
    • van Genderen I.L., Godeke G.J., Rottier P.J., and van Meer G. The phospholipid composition of enveloped viruses depends on the intracellular membrane through which they bud. Biochem. Soc. Trans. 23 (1995) 523-526
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 523-526
    • van Genderen, I.L.1    Godeke, G.J.2    Rottier, P.J.3    van Meer, G.4
  • 49
    • 0027325411 scopus 로고
    • Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes
    • Aloia R.C., Tian H., and Jensen F.C. Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes. Proc. Natl. Acad. Sci. USA 90 (1993) 5181-5185
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5181-5185
    • Aloia, R.C.1    Tian, H.2    Jensen, F.C.3
  • 50
    • 0018832901 scopus 로고
    • Effect of membrane phospholipid composition changes on adenylate cyclase activity in normal and rous-sarcoma-transformed chicken embryo fibroblasts
    • Gidwitz S., Pessin J.E., Weber M.J., Glaser M., and Storm D.R. Effect of membrane phospholipid composition changes on adenylate cyclase activity in normal and rous-sarcoma-transformed chicken embryo fibroblasts. Biochim. Biophys. Acta 628 (1980) 263-276
    • (1980) Biochim. Biophys. Acta , vol.628 , pp. 263-276
    • Gidwitz, S.1    Pessin, J.E.2    Weber, M.J.3    Glaser, M.4    Storm, D.R.5
  • 51
    • 0014981789 scopus 로고
    • Lipid composition of purified vesicular stomatitis viruses
    • McSharry J.J., and Wagner R.R. Lipid composition of purified vesicular stomatitis viruses. J. Virol. 7 (1971) 59-70
    • (1971) J. Virol. , vol.7 , pp. 59-70
    • McSharry, J.J.1    Wagner, R.R.2
  • 52
    • 0019321627 scopus 로고
    • Budding of Rous sarcoma virus and vesicular stomatitis virus from localized lipid regions in the plasma membrane of chicken embryo fibroblasts
    • Pessin J.E., and Glaser M. Budding of Rous sarcoma virus and vesicular stomatitis virus from localized lipid regions in the plasma membrane of chicken embryo fibroblasts. J. Biol. Chem. 255 (1980) 9044-9050
    • (1980) J. Biol. Chem. , vol.255 , pp. 9044-9050
    • Pessin, J.E.1    Glaser, M.2
  • 53
    • 0015134207 scopus 로고
    • Phospholipid composition of Rous sarcoma virus, host cell membranes and other enveloped RNA viruses
    • Quigley J.P., Rifkin D.B., and Reich E. Phospholipid composition of Rous sarcoma virus, host cell membranes and other enveloped RNA viruses. Virology 46 (1971) 106-116
    • (1971) Virology , vol.46 , pp. 106-116
    • Quigley, J.P.1    Rifkin, D.B.2    Reich, E.3
  • 54
    • 0015147957 scopus 로고
    • The lipid class composition of Semliki forest virus and plasma membranes of the host cells
    • Renkonen O., Kaarainen L., Simons K., and Gahmberg C.G. The lipid class composition of Semliki forest virus and plasma membranes of the host cells. Virology 46 (1971) 318-326
    • (1971) Virology , vol.46 , pp. 318-326
    • Renkonen, O.1    Kaarainen, L.2    Simons, K.3    Gahmberg, C.G.4
  • 56
    • 0037384054 scopus 로고    scopus 로고
    • Do lipid rafts mediate virus assembly and pseudotyping?
    • Briggs J.A., Wilk T., and Fuller S.D. Do lipid rafts mediate virus assembly and pseudotyping?. J. Gen. Virol. 84 (2003) 757-768
    • (2003) J. Gen. Virol. , vol.84 , pp. 757-768
    • Briggs, J.A.1    Wilk, T.2    Fuller, S.D.3
  • 57
    • 26944452885 scopus 로고    scopus 로고
    • Role of lipid rafts in virus replication
    • Ono A., and Freed E.O. Role of lipid rafts in virus replication. Adv. Virus. Res. 64 (2005) 311-358
    • (2005) Adv. Virus. Res. , vol.64 , pp. 311-358
    • Ono, A.1    Freed, E.O.2
  • 58
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder T., Scheiffele P., Verkade P., and Simons K. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell. Biol. 141 (1998) 929-942
    • (1998) J. Cell. Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 59
    • 33847254050 scopus 로고    scopus 로고
    • Depletion of cellular cholesterol inhibits membrane binding and higher-order multimerization of human immunodeficiency virus type 1 Gag
    • Ono A., Waheed A.A., and Freed E.O. Depletion of cellular cholesterol inhibits membrane binding and higher-order multimerization of human immunodeficiency virus type 1 Gag. Virology 360 (2006) 27-35
    • (2006) Virology , vol.360 , pp. 27-35
    • Ono, A.1    Waheed, A.A.2    Freed, E.O.3
  • 60
    • 0032930413 scopus 로고    scopus 로고
    • The cholesterol requirement for sindbis virus entry and exit and characterization of a spike protein region involved in cholesterol dependence
    • Lu Y.E., Cassese T., and Kielian M. The cholesterol requirement for sindbis virus entry and exit and characterization of a spike protein region involved in cholesterol dependence. J. Virol. 73 (1999) 4272-4278
    • (1999) J. Virol. , vol.73 , pp. 4272-4278
    • Lu, Y.E.1    Cassese, T.2    Kielian, M.3
  • 61
    • 0033871174 scopus 로고    scopus 로고
    • Semliki forest virus budding: assay, mechanisms, and cholesterol requirement
    • Lu Y.E., and Kielian M. Semliki forest virus budding: assay, mechanisms, and cholesterol requirement. J. Virol. 74 (2000) 7708-7719
    • (2000) J. Virol. , vol.74 , pp. 7708-7719
    • Lu, Y.E.1    Kielian, M.2
  • 63
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh M.D. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451 (1999) 1-16
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 64
    • 0347087223 scopus 로고    scopus 로고
    • A myristoyl switch regulates membrane binding of HIV-1 Gag
    • Resh M.D. A myristoyl switch regulates membrane binding of HIV-1 Gag. Proc. Natl. Acad. Sci. USA 101 (2004) 417-418
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 417-418
    • Resh, M.D.1
  • 65
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler M.E. Tetraspanin functions and associated microdomains. Nat. Rev. Mol. Cell. Biol. 6 (2005) 801-811
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 801-811
    • Hemler, M.E.1
  • 66
    • 0027332763 scopus 로고
    • Association of host cell surface adhesion receptors and other membrane proteins with HIV and SIV
    • Orentas R.J., and Hildreth J.E. Association of host cell surface adhesion receptors and other membrane proteins with HIV and SIV. AIDS. Res. Hum. Retroviruses 9 (1993) 1157-1165
    • (1993) AIDS. Res. Hum. Retroviruses , vol.9 , pp. 1157-1165
    • Orentas, R.J.1    Hildreth, J.E.2
  • 67
    • 33747394451 scopus 로고    scopus 로고
    • Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1
    • Nydegger S., Khurana S., Krementsov D.N., Foti M., and Thali M. Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1. J. Cell. Biol. 173 (2006) 795-807
    • (2006) J. Cell. Biol. , vol.173 , pp. 795-807
    • Nydegger, S.1    Khurana, S.2    Krementsov, D.N.3    Foti, M.4    Thali, M.5
  • 68
    • 0026317877 scopus 로고
    • Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release
    • Gottlinger H.G., Dorfman T., Sodroski J.G., and Haseltine W.A. Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release. Proc. Natl. Acad. Sci. USA 88 (1991) 3195-3199
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3195-3199
    • Gottlinger, H.G.1    Dorfman, T.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 69
    • 0028070639 scopus 로고
    • An assembly domain of the Rous sarcoma virus Gag protein required late in budding
    • Wills J.W., Cameron C.E., Wilson C.B., Xiang Y., Bennett R.P., and Leis J. An assembly domain of the Rous sarcoma virus Gag protein required late in budding. J. Virol. 68 (1994) 6605-6618
    • (1994) J. Virol. , vol.68 , pp. 6605-6618
    • Wills, J.W.1    Cameron, C.E.2    Wilson, C.B.3    Xiang, Y.4    Bennett, R.P.5    Leis, J.6
  • 70
    • 29144474443 scopus 로고    scopus 로고
    • Late budding domains and host proteins in enveloped virus release
    • Bieniasz P.D. Late budding domains and host proteins in enveloped virus release. Virology 344 (2006) 55-63
    • (2006) Virology , vol.344 , pp. 55-63
    • Bieniasz, P.D.1
  • 72
    • 13944252828 scopus 로고    scopus 로고
    • Evidence for a new viral late-domain core sequence, FPIV, necessary for budding of a paramyxovirus
    • Schmitt A.P., Leser G.P., Morita E., Sundquist W.I., and Lamb R.A. Evidence for a new viral late-domain core sequence, FPIV, necessary for budding of a paramyxovirus. J. Virol. 79 (2005) 2988-2997
    • (2005) J. Virol. , vol.79 , pp. 2988-2997
    • Schmitt, A.P.1    Leser, G.P.2    Morita, E.3    Sundquist, W.I.4    Lamb, R.A.5
  • 74
    • 23844481792 scopus 로고    scopus 로고
    • Depletion of TSG101 forms a mammalian "Class E" compartment: a multicisternal early endosome with multiple sorting defects
    • Doyotte A., Russell M.R., Hopkins C.R., and Woodman P.G. Depletion of TSG101 forms a mammalian "Class E" compartment: a multicisternal early endosome with multiple sorting defects. J. Cell. Sci. 118 (2005) 3003-3017
    • (2005) J. Cell. Sci. , vol.118 , pp. 3003-3017
    • Doyotte, A.1    Russell, M.R.2    Hopkins, C.R.3    Woodman, P.G.4
  • 75
    • 2342423251 scopus 로고    scopus 로고
    • ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles
    • Sachse M., Strous G.J., and Klumperman J. ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles. J. Cell. Sci. 117 (2004) 1699-1708
    • (2004) J. Cell. Sci. , vol.117 , pp. 1699-1708
    • Sachse, M.1    Strous, G.J.2    Klumperman, J.3
  • 76
    • 12444347534 scopus 로고    scopus 로고
    • A protein's final ESCRT
    • Babst M. A protein's final ESCRT. Traffic 6 (2005) 2-9
    • (2005) Traffic , vol.6 , pp. 2-9
    • Babst, M.1
  • 77
    • 33646010475 scopus 로고    scopus 로고
    • The ESCRT complexes: structure and mechanism of a membrane-trafficking network
    • Hurley J.H., and Emr S.D. The ESCRT complexes: structure and mechanism of a membrane-trafficking network. Annu. Rev. Biophys. Biomol. Struct. 35 (2006) 277-298
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 277-298
    • Hurley, J.H.1    Emr, S.D.2
  • 83
    • 29144487064 scopus 로고    scopus 로고
    • Filovirus assembly and budding
    • Hartlieb B., and Weissenhorn W. Filovirus assembly and budding. Virology 344 (2006) 64-70
    • (2006) Virology , vol.344 , pp. 64-70
    • Hartlieb, B.1    Weissenhorn, W.2
  • 84
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • Babst M., Wendland B., Estepa E.J., and Emr S.D. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. Embo. J. 17 (1998) 2982-2993
    • (1998) Embo. J. , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 85
    • 0033959713 scopus 로고    scopus 로고
    • ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking
    • Bishop N., and Woodman P. ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking. Mol. Biol. Cell. 11 (2000) 227-239
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 227-239
    • Bishop, N.1    Woodman, P.2
  • 87
    • 21644454519 scopus 로고    scopus 로고
    • Analysis of human immunodeficiency virus type 1 Gag ubiquitination
    • Gottwein E., and Krausslich H.G. Analysis of human immunodeficiency virus type 1 Gag ubiquitination. J. Virol. 79 (2005) 9134-9144
    • (2005) J. Virol. , vol.79 , pp. 9134-9144
    • Gottwein, E.1    Krausslich, H.G.2
  • 88
    • 2642552933 scopus 로고    scopus 로고
    • Late assembly motifs of human T-cell leukemia virus type 1 and their relative roles in particle release
    • Heidecker G., Lloyd P.A., Fox K., Nagashima K., and Derse D. Late assembly motifs of human T-cell leukemia virus type 1 and their relative roles in particle release. J. Virol. 78 (2004) 6636-6648
    • (2004) J. Virol. , vol.78 , pp. 6636-6648
    • Heidecker, G.1    Lloyd, P.A.2    Fox, K.3    Nagashima, K.4    Derse, D.5
  • 89
    • 0042389562 scopus 로고    scopus 로고
    • The Mason-Pfizer monkey virus PPPY and PSAP motifs both contribute to virus release
    • Gottwein E., Bodem J., Muller B., Schmechel A., Zentgraf H., and Krausslich H.G. The Mason-Pfizer monkey virus PPPY and PSAP motifs both contribute to virus release. J. Virol. 77 (2003) 9474-9485
    • (2003) J. Virol. , vol.77 , pp. 9474-9485
    • Gottwein, E.1    Bodem, J.2    Muller, B.3    Schmechel, A.4    Zentgraf, H.5    Krausslich, H.G.6
  • 90
    • 22844435415 scopus 로고    scopus 로고
    • Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding
    • Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R., Bertrand E., and Basyuk E. Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding. J. Biol. Chem. 280 (2005) 27004-27012
    • (2005) J. Biol. Chem. , vol.280 , pp. 27004-27012
    • Segura-Morales, C.1    Pescia, C.2    Chatellard-Causse, C.3    Sadoul, R.4    Bertrand, E.5    Basyuk, E.6
  • 92
    • 18144371606 scopus 로고    scopus 로고
    • Identification of domains in gag important for prototypic foamy virus egress
    • Patton G.S., Morris S.A., Chung W., Bieniasz P.D., and McClure M.O. Identification of domains in gag important for prototypic foamy virus egress. J. Virol. 79 (2005) 6392-6399
    • (2005) J. Virol. , vol.79 , pp. 6392-6399
    • Patton, G.S.1    Morris, S.A.2    Chung, W.3    Bieniasz, P.D.4    McClure, M.O.5
  • 93
    • 33749394947 scopus 로고    scopus 로고
    • Gamma-adaptin, a novel ubiquitin-interacting adaptor, and Nedd4 ubiquitin ligase control hepatitis B virus maturation
    • Rost M., Mann S., Lambert C., Doring T., Thome N., and Prange R. Gamma-adaptin, a novel ubiquitin-interacting adaptor, and Nedd4 ubiquitin ligase control hepatitis B virus maturation. J. Biol. Chem. 281 (2006) 29297-29308
    • (2006) J. Biol. Chem. , vol.281 , pp. 29297-29308
    • Rost, M.1    Mann, S.2    Lambert, C.3    Doring, T.4    Thome, N.5    Prange, R.6
  • 95
  • 97
    • 0036776607 scopus 로고    scopus 로고
    • The PPPY motif of human T-cell leukemia virus type 1 Gag protein is required early in the budding process
    • Le Blanc I., Prevost M.C., Dokhelar M.C., and Rosenberg A.R. The PPPY motif of human T-cell leukemia virus type 1 Gag protein is required early in the budding process. J. Virol. 76 (2002) 10024-10029
    • (2002) J. Virol. , vol.76 , pp. 10024-10029
    • Le Blanc, I.1    Prevost, M.C.2    Dokhelar, M.C.3    Rosenberg, A.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.