메뉴 건너뛰기




Volumn 87, Issue 12, 2013, Pages 7113-7126

Basic residues in the matrix domain and multimerization target murine leukemia virus gag to the virological synapse

Author keywords

[No Author keywords available]

Indexed keywords

GAG PROTEIN; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PHOSPHATIDYLSERINE; PROTEIN KINASE FYN; PROTEIN TYROSINE KINASE; VIRUS ENVELOPE PROTEIN;

EID: 84878576356     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03263-12     Document Type: Article
Times cited : (13)

References (71)
  • 2
    • 68049136145 scopus 로고    scopus 로고
    • Assembly of the murine leukemia virus is directed towards sites of cell-cell contact
    • doi:10.1371/journal.pbio.1000163
    • Jin J, Sherer NM, Heidecker G, Derse D, Mothes W. 2009. Assembly of the murine leukemia virus is directed towards sites of cell-cell contact. PLoS Biol. 7:e1000163. doi:10.1371/journal.pbio.1000163.
    • (2009) PLoS Biol. , vol.7
    • Jin, J.1    Sherer, N.M.2    Heidecker, G.3    Derse, D.4    Mothes, W.5
  • 5
    • 26444444082 scopus 로고    scopus 로고
    • Retroviral matrix domains share electrostatic homology: models for membrane binding function throughout the viral life cycle
    • Murray PS, Li Z, Wang J, Tang CL, Honig B, Murray D. 2005. Retroviral matrix domains share electrostatic homology: models for membrane binding function throughout the viral life cycle. Structure 13: 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
  • 6
    • 0028355603 scopus 로고
    • Identification of human immunodeficiency virus type 1 Gag protein domains essential to membrane binding and particle assembly
    • Spearman P, Wang JJ, Vander Heyden N, Ratner L. 1994. Identification of human immunodeficiency virus type 1 Gag protein domains essential to membrane binding and particle assembly. J. Virol. 68:3232-3242.
    • (1994) J. Virol. , vol.68 , pp. 3232-3242
    • Spearman, P.1    Wang, J.J.2    Vander Heyden, N.3    Ratner, L.4
  • 7
    • 0028218274 scopus 로고
    • Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids
    • Zhou W, Parent LJ, Wills JW, Resh MD. 1994. Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids. J. Virol. 68:2556-2569.
    • (1994) J. Virol. , vol.68 , pp. 2556-2569
    • Zhou, W.1    Parent, L.J.2    Wills, J.W.3    Resh, M.D.4
  • 8
    • 0029861657 scopus 로고    scopus 로고
    • Differential membrane binding of the human immunodeficiency virus type 1 matrix protein
    • Zhou W, Resh MD. 1996. Differential membrane binding of the human immunodeficiency virus type 1 matrix protein. J. Virol. 70:8540-8548.
    • (1996) J. Virol. , vol.70 , pp. 8540-8548
    • Zhou, W.1    Resh, M.D.2
  • 9
    • 0028234481 scopus 로고
    • Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production
    • Freed EO, Orenstein JM, Bucklerwhite AJ, Martin MA. 1994. Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production. J. Virol. 68:5311-5320.
    • (1994) J. Virol. , vol.68 , pp. 5311-5320
    • Freed, E.O.1    Orenstein, J.M.2    Bucklerwhite, A.J.3    Martin, M.A.4
  • 10
    • 0027947366 scopus 로고
    • Substitution mutations affecting a small region of the Moloney murine leukemia virus MA Gag protein block assembly and release of virion particles
    • Granowitz C, Goff SP. 1994. Substitution mutations affecting a small region of the Moloney murine leukemia virus MA Gag protein block assembly and release of virion particles. Virology 205:336-344.
    • (1994) Virology , vol.205 , pp. 336-344
    • Granowitz, C.1    Goff, S.P.2
  • 12
    • 0033856584 scopus 로고    scopus 로고
    • Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging
    • Hermida-Matsumoto L, Resh MD. 2000. Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging. J. Virol. 74:8670-8679.
    • (2000) J. Virol. , vol.74 , pp. 8670-8679
    • Hermida-Matsumoto, L.1    Resh, M.D.2
  • 13
    • 84891855299 scopus 로고    scopus 로고
    • Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 gag targeting to the plasma membrane
    • Ono A, Ablan SD, Lockett SJ, Nagashima K, Freed EO. 2004. Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 gag targeting to the plasma membrane. Mol. Biol. Cell 15:122a-123a.
    • (2004) Mol. Biol. Cell , vol.15
    • Ono, A.1    Ablan, S.D.2    Lockett, S.J.3    Nagashima, K.4    Freed, E.O.5
  • 14
    • 0032951899 scopus 로고    scopus 로고
    • Binding of human immunodeficiency virus type 1 Gag to membrane: role of the matrix amino terminus
    • Ono A, Freed EO. 1999. Binding of human immunodeficiency virus type 1 Gag to membrane: role of the matrix amino terminus. J. Virol. 73:4136-4144.
    • (1999) J. Virol. , vol.73
    • Ono, A.1    Freed, E.O.2
  • 15
    • 0030922098 scopus 로고    scopus 로고
    • Mutagenesis analysis of the murine leukemia virus matrix protein: Identification of regions important for membrane localization and intracellular transport
    • Soneoka Y, Kingsman SM, Kingsman AJ. 1997. Mutagenesis analysis of the murine leukemia virus matrix protein: Identification of regions important for membrane localization and intracellular transport. J. Virol. 71:5549-5559.
    • (1997) J. Virol. , vol.71 , pp. 5549-5559
    • Soneoka, Y.1    Kingsman, S.M.2    Kingsman, A.J.3
  • 16
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh MD. 1999. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451:1-16.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 17
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch-a modulator of reversible protein-membrane interactions
    • McLaughlin S, Aderem A. 1995. The myristoyl-electrostatic switch-a modulator of reversible protein-membrane interactions. Trends Biochem. Sci. 20:272-276.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 19
    • 0034581528 scopus 로고    scopus 로고
    • Analysis of function and regulation of proteins that mediate signal transduction by use of lipid-modified plasma membrane-targeting sequences
    • Reuther GW, Buss JE, Quilliam LA, Clark GJ, Der CJ. 2000. Analysis of function and regulation of proteins that mediate signal transduction by use of lipid-modified plasma membrane-targeting sequences. Methods Enzymol. 327:331-350.
    • (2000) Methods Enzymol. , vol.327 , pp. 331-350
    • Reuther, G.W.1    Buss, J.E.2    Quilliam, L.A.3    Clark, G.J.4    Der, C.J.5
  • 20
    • 0028053759 scopus 로고
    • Aminoterminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids
    • Sigal CT, Zhou WJ, Buser CA, Mclaughlin S, Resh MD. 1994. Aminoterminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids. Proc. Natl. Acad. Sci. U. S. A. 91:12253-12257.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 12253-12257
    • Sigal, C.T.1    Zhou, W.J.2    Buser, C.A.3    Mclaughlin, S.4    Resh, M.D.5
  • 21
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo G, De Camilli P. 2006. Phosphoinositides in cell regulation and membrane dynamics. Nature 443:651-657.
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 22
    • 77952944942 scopus 로고    scopus 로고
    • The distribution and function of phosphatidylserine in cellular membranes
    • Leventis PA, Grinstein S. 2010. The distribution and function of phosphatidylserine in cellular membranes. Annu. Rev. Biophys. 39:407-427.
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 407-427
    • Leventis, P.A.1    Grinstein, S.2
  • 23
    • 33845313646 scopus 로고    scopus 로고
    • PI(3,4,5)P-3 and PI(4,5)P-2 lipids target proteins with polybasic clusters to the plasma membrane
    • Heo WD, Inoue T, Park WS, Kim ML, Park BO, Wandless TJ, Meyer T. 2006. PI(3,4,5)P-3 and PI(4,5)P-2 lipids target proteins with polybasic clusters to the plasma membrane. Science 314:1458-1461.
    • (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
  • 24
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • McLaughlin S, Murray D. 2005. Plasma membrane phosphoinositide organization by protein electrostatics. Nature 438:605-611.
    • (2005) Nature , vol.438 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 25
    • 38149094836 scopus 로고    scopus 로고
    • Membrane phosphatidylserine regulates surface charge and protein localization
    • Yeung T, Gilbert GE, Shi J, Silvius J, Kapus A, Grinstein S. 2008. Membrane phosphatidylserine regulates surface charge and protein localization. Science 319:210-213.
    • (2008) Science , vol.319 , pp. 210-213
    • Yeung, T.1    Gilbert, G.E.2    Shi, J.3    Silvius, J.4    Kapus, A.5    Grinstein, S.6
  • 26
    • 79952229154 scopus 로고    scopus 로고
    • Retroviral matrix and lipids, the intimate interaction
    • Hamard-Peron E, Muriaux D. 2011. Retroviral matrix and lipids, the intimate interaction. Retrovirology 8:15.
    • (2011) Retrovirology , vol.8 , pp. 15
    • Hamard-Peron, E.1    Muriaux, D.2
  • 27
    • 70350113492 scopus 로고    scopus 로고
    • HIV-1 assembly at the plasma membrane: Gag trafficking and localization
    • Ono A. 2009. HIV-1 assembly at the plasma membrane: Gag trafficking and localization. Future Virol. 4:241-257.
    • (2009) Future Virol. , vol.4 , pp. 241-257
    • Ono, A.1
  • 28
    • 55549118226 scopus 로고    scopus 로고
    • Retroviruses human immunodeficiency virus and murine leukemia virus are enriched in phosphoinositides
    • Chan R, Uchil PD, Jin J, Shui G, Ott DE, Mothes W, Wenk MR. 2008. Retroviruses human immunodeficiency virus and murine leukemia virus are enriched in phosphoinositides. J. Virol. 82:11228-11238.
    • (2008) J. Virol. , vol.82 , pp. 11228-11238
    • Chan, R.1    Uchil, P.D.2    Jin, J.3    Shui, G.4    Ott, D.E.5    Mothes, W.6    Wenk, M.R.7
  • 29
    • 39649098475 scopus 로고    scopus 로고
    • Solution NMR characterizations of oligomerization and dynamics of equine infectious anemia virus matrix protein and its interaction with PIP2
    • Chen K, Bachtair I, Piszczek G, Bouamr F, Carter C, Tjandra N. 2008. Solution NMR characterizations of oligomerization and dynamics of equine infectious anemia virus matrix protein and its interaction with PIP2. Biochemistry 47:1928-1937.
    • (2008) Biochemistry , vol.47 , pp. 1928-1937
    • Chen, K.1    Bachtair, I.2    Piszczek, G.3    Bouamr, F.4    Carter, C.5    Tjandra, N.6
  • 30
  • 31
    • 50049091709 scopus 로고    scopus 로고
    • Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting
    • Saad JS, Ablan SD, Ghanam RH, Kim A, Andrews K, Nagashima K, Soheilian F, Freed EO, Summers MF. 2008. Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting. J. Mol. Biol. 382:434-447.
    • (2008) J. Mol. Biol. , vol.382 , pp. 434-447
    • Saad, J.S.1    Ablan, S.D.2    Ghanam, R.H.3    Kim, A.4    Andrews, K.5    Nagashima, K.6    Soheilian, F.7    Freed, E.O.8    Summers, M.F.9
  • 33
    • 34548182230 scopus 로고    scopus 로고
    • Basic residues in the Mason-Pfizer monkey virus Gag matrix domain regulate intracellular trafficking and capsid-membrane interactions
    • Stansell E, Apkarian R, Haubova S, Diehl WE, Tytler EM, Hunter E. 2007. Basic residues in the Mason-Pfizer monkey virus Gag matrix domain regulate intracellular trafficking and capsid-membrane interactions. J. Virol. 81:8977-8988.
    • (2007) J. Virol. , vol.81 , pp. 8977-8988
    • Stansell, E.1    Apkarian, R.2    Haubova, S.3    Diehl, W.E.4    Tytler, E.M.5    Hunter, E.6
  • 35
    • 0037302342 scopus 로고    scopus 로고
    • Independent segregation of human immunodeficiency virus type 1 Gag protein complexes and lipid rafts
    • Ding LM, Derdowski A, Wang JJ, Spearman P. 2003. Independent segregation of human immunodeficiency virus type 1 Gag protein complexes and lipid rafts. J. Virol. 77:1916-1926.
    • (2003) J. Virol. , vol.77 , pp. 1916-1926
    • Ding, L.M.1    Derdowski, A.2    Wang, J.J.3    Spearman, P.4
  • 36
    • 0037379284 scopus 로고    scopus 로고
    • Rapid localization of Gag/GagPol complexes to detergent-resistant membrane during the assembly of human immunodeficiency virus type 1
    • Halwani R, Khorchid A, Cen S, Kleiman L. 2003. Rapid localization of Gag/GagPol complexes to detergent-resistant membrane during the assembly of human immunodeficiency virus type 1. J. Virol. 77:3973-3984.
    • (2003) J. Virol. , vol.77 , pp. 3973-3984
    • Halwani, R.1    Khorchid, A.2    Cen, S.3    Kleiman, L.4
  • 37
    • 0034864631 scopus 로고    scopus 로고
    • Multimerization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains
    • Lindwasser OW, Resh MD. 2001. Multimerization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains. J. Virol. 75:7913-7924.
    • (2001) J. Virol. , vol.75 , pp. 7913-7924
    • Lindwasser, O.W.1    Resh, M.D.2
  • 38
    • 78449233400 scopus 로고    scopus 로고
    • Nucleocapsid promotes localization of HIV-1 gag to uropods that participate in virological synapses between T cells
    • doi:10.1371/journal .ppat.1001167
    • Llewellyn GN, Hogue IB, Grover JR, Ono A. 2010. Nucleocapsid promotes localization of HIV-1 gag to uropods that participate in virological synapses between T cells. PLoS Pathog. 6:e1001167. doi:10.1371/journal .ppat.1001167.
    • (2010) PLoS Pathog. , vol.6
    • Llewellyn, G.N.1    Hogue, I.B.2    Grover, J.R.3    Ono, A.4
  • 39
    • 0035923525 scopus 로고    scopus 로고
    • Plasma membrane rafts play a critical role in HIV-1 assembly and release
    • Ono A, Freed EO. 2001. Plasma membrane rafts play a critical role in HIV-1 assembly and release. Proc. Natl. Acad. Sci. U. S. A. 98:13925-13930.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98
    • Ono, A.1    Freed, E.O.2
  • 40
    • 0026762403 scopus 로고
    • Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro
    • Ehrlich LS, Agresta BE, Carter CA. 1992. Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro. J. Virol. 66:4874-4883.
    • (1992) J. Virol. , vol.66 , pp. 4874-4883
    • Ehrlich, L.S.1    Agresta, B.E.2    Carter, C.A.3
  • 42
    • 0032874018 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsid-dimer interface and the basic region of matrix protein
    • Burniston MT, Cimarelli A, Colgan J, Curtis SP, Luban J. 1999. Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsid-dimer interface and the basic region of matrix protein. J. Virol. 73:8527-8540.
    • (1999) J. Virol. , vol.73 , pp. 8527-8540
    • Burniston, M.T.1    Cimarelli, A.2    Colgan, J.3    Curtis, S.P.4    Luban, J.5
  • 43
    • 0032506295 scopus 로고    scopus 로고
    • The role of nucleocapsid of HIV-1 in virus assembly
    • Dawson L, Yu XF. 1998. The role of nucleocapsid of HIV-1 in virus assembly. Virology 251:141-157.
    • (1998) Virology , vol.251 , pp. 141-157
    • Dawson, L.1    Yu, X.F.2
  • 45
    • 0029966361 scopus 로고    scopus 로고
    • Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly
    • Hill CP, Worthylake D, Bancroft DP, Christensen AM, Sundquist WI. 1996. Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly. Proc. Natl. Acad. Sci. U. S. A. 93:3099-3104.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 3099-3104
    • Hill, C.P.1    Worthylake, D.2    Bancroft, D.P.3    Christensen, A.M.4    Sundquist, W.I.5
  • 47
    • 64849116750 scopus 로고    scopus 로고
    • HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphate
    • Alfadhli A, Barklis RL, Barklis E. 2009. HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphate. Virology 387:466-472.
    • (2009) Virology , vol.387 , pp. 466-472
    • Alfadhli, A.1    Barklis, R.L.2    Barklis, E.3
  • 48
    • 33846500107 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 matrix protein assembles on membranes as a hexamer
    • Alfadhli A, Huseby D, Kapit E, Colman D, Barklis E. 2007. Human immunodeficiency virus type 1 matrix protein assembles on membranes as a hexamer. J. Virol. 81:1472-1478.
    • (2007) J. Virol. , vol.81 , pp. 1472-1478
    • Alfadhli, A.1    Huseby, D.2    Kapit, E.3    Colman, D.4    Barklis, E.5
  • 49
    • 33847389795 scopus 로고    scopus 로고
    • Bridging efficient viral infection
    • Hope TJ. 2007. Bridging efficient viral infection. Nat. Cell Biol. 9:243-244.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 243-244
    • Hope, T.J.1
  • 52
    • 0036133058 scopus 로고    scopus 로고
    • Directed egress of animal viruses promotes cell-to-cell spread
    • Johnson DC, Huber MT. 2002. Directed egress of animal viruses promotes cell-to-cell spread. J. Virol. 76:1-8.
    • (2002) J. Virol. , vol.76 , pp. 1-8
    • Johnson, D.C.1    Huber, M.T.2
  • 53
    • 4444231440 scopus 로고    scopus 로고
    • Retroviral spread by induction of virological synapses
    • Jolly C, Sattentau QJ. 2004. Retroviral spread by induction of virological synapses. Traffic 5:643-650.
    • (2004) Traffic , vol.5 , pp. 643-650
    • Jolly, C.1    Sattentau, Q.J.2
  • 56
    • 0028233744 scopus 로고
    • The role of cell-to-cell transmission in HIV infection
    • Phillips DM. 1994. The role of cell-to-cell transmission in HIV infection. AIDS 8:719-731.
    • (1994) AIDS , vol.8 , pp. 719-731
    • Phillips, D.M.1
  • 58
    • 54149119141 scopus 로고    scopus 로고
    • Avoiding the void: cell-to-cell spread of human viruses
    • Sattentau Q. 2008. Avoiding the void: cell-to-cell spread of human viruses. Nat. Rev. Microbiol. 6:815-826.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 815-826
    • Sattentau, Q.1
  • 59
    • 79960422189 scopus 로고    scopus 로고
    • Viral determinants of polarized assembly for the murine leukemia virus
    • Jin J, Li F, Mothes W. 2011. Viral determinants of polarized assembly for the murine leukemia virus. J. Virol. 85:7672-7682.
    • (2011) J. Virol. , vol.85 , pp. 7672-7682
    • Jin, J.1    Li, F.2    Mothes, W.3
  • 63
    • 13544249968 scopus 로고    scopus 로고
    • In vivo analysis of 3-phosphoinositide dynamics during Dictyostelium phagocytosis and chemotaxis
    • Dormann D, Weijer G, Dowler S, Weijer CJ. 2004. In vivo analysis of 3-phosphoinositide dynamics during Dictyostelium phagocytosis and chemotaxis. J. Cell Sci. 117:6497-6509.
    • (2004) J. Cell Sci. , vol.117 , pp. 6497-6509
    • Dormann, D.1    Weijer, G.2    Dowler, S.3    Weijer, C.J.4
  • 64
    • 0346365290 scopus 로고    scopus 로고
    • A point mutation in the binding subunit of a retroviral envelope protein arrests virus entry at hemifusion
    • Zavorotinskaya T, Qian Z, Franks J, Albritton LM. 2004. A point mutation in the binding subunit of a retroviral envelope protein arrests virus entry at hemifusion. J. Virol. 78:473-481.
    • (2004) J. Virol. , vol.78 , pp. 473-481
    • Zavorotinskaya, T.1    Qian, Z.2    Franks, J.3    Albritton, L.M.4
  • 66
    • 0034088332 scopus 로고    scopus 로고
    • Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain
    • Accola MA, Strack B, Gottlinger HG. 2000. Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain. J. Virol. 74:5395-5402.
    • (2000) J. Virol. , vol.74 , pp. 5395-5402
    • Accola, M.A.1    Strack, B.2    Gottlinger, H.G.3
  • 67
    • 0028168754 scopus 로고
    • Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal
    • Lee PP, Linial ML. 1994. Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal. J. Virol. 68:6644-6654.
    • (1994) J. Virol. , vol.68 , pp. 6644-6654
    • Lee, P.P.1    Linial, M.L.2
  • 68
    • 0027487961 scopus 로고
    • Conditional infectivity of a human immunodeficiency virus matrix domain deletion mutant
    • Wang CT, Zhang Y, McDermott J, Barklis E. 1993. Conditional infectivity of a human immunodeficiency virus matrix domain deletion mutant. J. Virol. 67:7067-7076.
    • (1993) J. Virol. , vol.67 , pp. 7067-7076
    • Wang, C.T.1    Zhang, Y.2    McDermott, J.3    Barklis, E.4
  • 69
    • 84878166615 scopus 로고    scopus 로고
    • HIV-1 Gag associates with specific uropod-directed microdomains in a manner dependent on its MA highly basic region
    • Llewellyn GN, Grover JR, Olety B, Ono A. 2013. HIV-1 Gag associates with specific uropod-directed microdomains in a manner dependent on its MA highly basic region. J. Virol. 87:6441-6454.
    • (2013) J. Virol. , vol.87 , pp. 6441-6454
    • Llewellyn, G.N.1    Grover, J.R.2    Olety, B.3    Ono, A.4
  • 70
    • 79952850453 scopus 로고    scopus 로고
    • Gag localization and virus-like particle release mediated by the matrix domain of human Tlymphotropic virus type 1 Gag are less dependent on phosphatidylinositol-( 4,5)-bisphosphate than those mediated by the matrix domain of HIV-1 Gag
    • Inlora J, Chukkapalli V, Derse D, Ono A. 2011. Gag localization and virus-like particle release mediated by the matrix domain of human Tlymphotropic virus type 1 Gag are less dependent on phosphatidylinositol-( 4,5)-bisphosphate than those mediated by the matrix domain of HIV-1 Gag. J. Virol. 85:3802-3810.
    • (2011) J. Virol. , vol.85 , pp. 3802-3810
    • Inlora, J.1    Chukkapalli, V.2    Derse, D.3    Ono, A.4
  • 71
    • 84873050158 scopus 로고    scopus 로고
    • Multiple Gag domains contribute to selective recruitment of murine leukemia virus (MLV) Env to MLV virions
    • Gregory DA, Lyddon TD, Johnson MC. 2012. Multiple Gag domains contribute to selective recruitment of murine leukemia virus (MLV) Env to MLV virions. J. Virol. 87:1518-1527.
    • (2012) J. Virol. , vol.87 , pp. 1518-1527
    • Gregory, D.A.1    Lyddon, T.D.2    Johnson, M.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.