메뉴 건너뛰기




Volumn 5, Issue JUN, 2014, Pages

Role of Gag and lipids during HIV-1 assembly in CD4+ T cells and macrophages

Author keywords

Assembly; Gag; HIV 1; Lipids; Macrophages

Indexed keywords

CHOLESTEROL; GAG PROTEIN; LIPID; MEMBRANE LIPID; PHOSPHATIDYLINOSITOL 3, 4 BISPHOSPHATE; TETRASPANIN; UNCLASSIFIED DRUG;

EID: 84904890951     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2014.00312     Document Type: Review
Times cited : (31)

References (91)
  • 1
    • 0027325411 scopus 로고
    • Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes
    • doi:10.1073/pnas.90.11.5181
    • Aloia, R. C., Tian, H., and Jensen, F. C. (1993). Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes. Proc. Natl. Acad. Sci. U.S.A. 90, 5181-5185. doi: 10.1073/pnas.90.11.5181
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 5181-5185
    • Aloia, R.C.1    Tian, H.2    Jensen, F.C.3
  • 2
    • 77954743165 scopus 로고    scopus 로고
    • Circulating NEF induces dyslipidemia in simian immunodeficiency virus-infected Macaques by suppressing cholesterol efflux
    • doi:10.1086/654817
    • Asztalos, B. F., Mujawar, Z., Morrow, M. P., Grant, A., Pushkarsky, T., Wanke, C., et al. (2010). Circulating NEF induces dyslipidemia in simian immunodeficiency virus-infected Macaques by suppressing cholesterol efflux. J. Infect. Dis. 202, 614-623. doi: 10.1086/654817
    • (2010) J. Infect. Dis. , vol.202 , pp. 614-623
    • Asztalos, B.F.1    Mujawar, Z.2    Morrow, M.P.3    Grant, A.4    Pushkarsky, T.5    Wanke, C.6
  • 4
    • 70349686333 scopus 로고    scopus 로고
    • Ion-abrasion scanning electron microscopy reveals surface-connected tubular conduits in HIV-infected macrophages
    • doi:10.1371/journal.ppat.1000591
    • Bennett, A. E., Narayan, K., Shi, D., Hartnell, L. M., Gousset, K., He, H., et al. (2009). Ion-abrasion scanning electron microscopy reveals surface-connected tubular conduits in HIV-infected macrophages. PLoS Pathog. 5:e1000591. doi: 10.1371/journal.ppat.1000591
    • (2009) PLoS Pathog. , vol.5
    • Bennett, A.E.1    Narayan, K.2    Shi, D.3    Hartnell, L.M.4    Gousset, K.5    He, H.6
  • 5
    • 84888112411 scopus 로고    scopus 로고
    • Cd36-specific antibodies block release of HIV-1 from infected primary macrophages and its transmission to t cells
    • doi:10.1084/jem.20130566
    • Berre, S., Gaudin, R., de Alencar, B. C., Desdouits, M., Chabaud, M., Naffakh, N., et al. (2013). Cd36-specific antibodies block release of HIV-1 from infected primary macrophages and its transmission to t cells. J. Exp. Med. 210, 2523-2538. doi: 10.1084/jem.20130566
    • (2013) J. Exp. Med. , vol.210 , pp. 2523-2538
    • Berre, S.1    Gaudin, R.2    de Alencar, B.C.3    Desdouits, M.4    Chabaud, M.5    Naffakh, N.6
  • 6
    • 33644927263 scopus 로고    scopus 로고
    • Exosomes and HIV Gag bud from endosome-like domains of the T cell plasma membrane
    • doi:10.1083/jcb.200508014
    • Booth, A. M., Fang, Y., Fallon, J. K., Yang, J.-M., Hildreth, J. E., and Gould, S. J. (2006). Exosomes and HIV Gag bud from endosome-like domains of the T cell plasma membrane. J. Cell Biol. 172, 923-935. doi: 10.1083/jcb.200508014
    • (2006) J. Cell Biol. , vol.172 , pp. 923-935
    • Booth, A.M.1    Fang, Y.2    Fallon, J.K.3    Yang, J.-M.4    Hildreth, J.E.5    Gould, S.J.6
  • 8
    • 35948969818 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nef protein modulates the lipid composition of virions and host cell membrane microdomains
    • doi:10.1186/1742-4690-4-70
    • Brügger, B., Krautkrämer, E., Tibroni, N., Munte, C. E., Rauch, S., Leibrecht, I., et al. (2007). Human immunodeficiency virus type 1 nef protein modulates the lipid composition of virions and host cell membrane microdomains. Retrovirology 4, 70. doi: 10.1186/1742-4690-4-70
    • (2007) Retrovirology , vol.4 , pp. 70
    • Brügger, B.1    Krautkrämer, E.2    Tibroni, N.3    Munte, C.E.4    Rauch, S.5    Leibrecht, I.6
  • 9
    • 0025176624 scopus 로고
    • Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
    • doi:10.1073/pnas.87.2.523
    • Bryant, M., and Ratner, L. (1990). Myristoylation-dependent replication and assembly of human immunodeficiency virus 1. Proc. Natl. Acad. Sci U.S.A. 87, 523-527. doi: 10.1073/pnas.87.2.523
    • (1990) Proc. Natl. Acad. Sci U.S.A. , vol.87 , pp. 523-527
    • Bryant, M.1    Ratner, L.2
  • 10
    • 80054992503 scopus 로고    scopus 로고
    • Rous sarcoma virus gag has no specific requirement for phosphatidylinositol-(4,5)-bisphosphate for plasma membrane association in vivo or for liposome interaction in vitro
    • doi:10.1128/JVI.00760-11
    • Chan, J., Dick, R. A., and Vogt, V. M. (2011). Rous sarcoma virus gag has no specific requirement for phosphatidylinositol-(4,5)-bisphosphate for plasma membrane association in vivo or for liposome interaction in vitro. J. Virol. 85, 10851-10860. doi: 10.1128/JVI.00760-11
    • (2011) J. Virol. , vol.85 , pp. 10851-10860
    • Chan, J.1    Dick, R.A.2    Vogt, V.M.3
  • 11
    • 55549118226 scopus 로고    scopus 로고
    • Retroviruses human immunodeficiency virus and murine leukemia virus are enriched in phosphoinositides
    • doi:10.1128/JVI.00981-08
    • Chan, R., Uchil, P. D., Jin, J., Shui, G., Ott, D. E., Mothes, W., et al. (2008). Retroviruses human immunodeficiency virus and murine leukemia virus are enriched in phosphoinositides. J. Virol. 82, 11228-11238. doi: 10.1128/JVI.00981-08
    • (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
  • 12
    • 84893467134 scopus 로고    scopus 로고
    • Coarse-grained simulations of the HIV-1 matrix protein anchoring: revisiting its assembly on membrane domains
    • doi:10.1016/j.bpj.2013.12.019
    • Charlier, L., Louet, M., Chaloin, L., Fuchs, P., Martinez, J., Muriaux, D., et al. (2014). Coarse-grained simulations of the HIV-1 matrix protein anchoring: revisiting its assembly on membrane domains. Biophys. J. 106, 577-585. doi: 10.1016/j.bpj.2013.12.019
    • (2014) Biophys. J. , vol.106 , pp. 577-585
    • Charlier, L.1    Louet, M.2    Chaloin, L.3    Fuchs, P.4    Martinez, J.5    Muriaux, D.6
  • 13
    • 80051737642 scopus 로고    scopus 로고
    • HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation
    • doi:10.1016/j.jmb.2011.04.042
    • Checkley, M. A., Luttge, B. G., and Freed, E. O. (2011). HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation. J. Mol. Biol. 410, 582-608. doi: 10.1016/j.jmb.2011.04.042
    • (2011) J. Mol. Biol. , vol.410 , pp. 582-608
    • Checkley, M.A.1    Luttge, B.G.2    Freed, E.O.3
  • 14
    • 39649098475 scopus 로고    scopus 로고
    • Solution nmr characterizations of oligomerization and dynamics of equine infectious anemia virus matrix protein and its interaction with pip2
    • doi:10.1021/bi701984h
    • Chen, K., Bachtiar, I., Piszczek, G., Bouamr, F., Carter, C., and 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. doi: 10.1021/bi701984h
    • (2008) Biochemistry , vol.47 , pp. 1928-1937
    • Chen, K.1    Bachtiar, I.2    Piszczek, G.3    Bouamr, F.4    Carter, C.5    Tjandra, N.6
  • 15
    • 33748479920 scopus 로고    scopus 로고
    • Proteomic and biochemical analysis of purified human immunodeficiency virus type 1 produced from infected monocyte-derived macrophages
    • doi:10.1128/JVI.01013-06
    • Chertova, E., Chertov, O., Coren, L. V., Roser, J. D., Trubey, C. M., Bess, J. W., et al. (2006). Proteomic and biochemical analysis of purified human immunodeficiency virus type 1 produced from infected monocyte-derived macrophages. J. Virol. 80, 9039-9052. doi: 10.1128/JVI.01013-06
    • (2006) J. Virol. , vol.80 , pp. 9039-9052
    • Chertova, E.1    Chertov, O.2    Coren, L.V.3    Roser, J.D.4    Trubey, C.M.5    Bess, J.W.6
  • 16
    • 77954385815 scopus 로고    scopus 로고
    • Calmodulin disrupts the structure of the HIV-1 ma protein
    • doi:10.1016/j.jmb.2010.05.022
    • Chow, J. Y. H., Jeffries, C. M., Kwan, A. H., Guss, J. M., and Trewhella, J. (2010). Calmodulin disrupts the structure of the HIV-1 ma protein. J. Mol. Biol. 400, 702-714. doi: 10.1016/j.jmb.2010.05.022
    • (2010) J. Mol. Biol. , vol.400 , pp. 702-714
    • Chow, J.Y.H.1    Jeffries, C.M.2    Kwan, A.H.3    Guss, J.M.4    Trewhella, J.5
  • 17
    • 39749170507 scopus 로고    scopus 로고
    • Interaction between the human immunodeficiency virus type 1 Gag matrix domain and phosphatidylinositol-(4,5)-bisphosphate is essential for efficient gag membrane binding
    • doi:10.1128/JVI.01614-07
    • Chukkapalli, V., Hogue, I. B., Boyko, V., Hu, W.-S., and Ono, A. (2008). Interaction between the human immunodeficiency virus type 1 Gag matrix domain and phosphatidylinositol-(4,5)-bisphosphate is essential for efficient gag membrane binding. J. Virol. 82, 2405-2417. doi: 10.1128/JVI.01614-07
    • (2008) J. Virol. , vol.82 , pp. 2405-2417
    • Chukkapalli, V.1    Hogue, I.B.2    Boyko, V.3    Hu, W.-S.4    Ono, A.5
  • 18
    • 76549119994 scopus 로고    scopus 로고
    • Opposing mechanisms involving RNA and lipids regulate HIV-1 Gag membrane binding through the highly basic region of the matrix domain
    • doi:10.1073/pnas.0908661107
    • Chukkapalli, V., Oh, S. J., and Ono, A. (2010). Opposing mechanisms involving RNA and lipids regulate HIV-1 Gag membrane binding through the highly basic region of the matrix domain. Proc. Natl. Acad. Sci. U.S.A. 107, 1600-1605. doi: 10.1073/pnas.0908661107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1600-1605
    • Chukkapalli, V.1    Oh, S.J.2    Ono, A.3
  • 19
    • 80051718223 scopus 로고    scopus 로고
    • Molecular determinants that regulate plasma membrane association of HIV-1 gag
    • doi:10.1016/j.jmb.2011.04.015
    • Chukkapalli, V., and Ono, A. (2011). Molecular determinants that regulate plasma membrane association of HIV-1 gag. J. Mol. Biol. 410, 512-524. doi: 10.1016/j.jmb.2011.04.015
    • (2011) J. Mol. Biol. , vol.410 , pp. 512-524
    • Chukkapalli, V.1    Ono, A.2
  • 20
    • 0036635446 scopus 로고    scopus 로고
    • Assembling the human immunodeficiency virus type 1
    • doi:10.1007/s00018-002-8495-6
    • Cimarelli, A., and Darlix, J. L. (2002). Assembling the human immunodeficiency virus type 1. Cell Mol. Life Sci. 59, 1166-1184. doi: 10.1007/s00018-002-8495-6
    • (2002) Cell Mol. Life Sci. , vol.59 , pp. 1166-1184
    • Cimarelli, A.1    Darlix, J.L.2
  • 21
    • 48549087436 scopus 로고    scopus 로고
    • Cd45 immunoaffinity depletion of vesicles from jurkat t cells demonstrates that exosomes contain cd45: no evidence for a distinct exosome/HIV-1 budding pathway
    • doi:10.1186/1742-4690-5-64
    • Coren, L. V., Shatzer, T., and Ott, D. E. (2008). Cd45 immunoaffinity depletion of vesicles from jurkat t cells demonstrates that exosomes contain cd45: no evidence for a distinct exosome/HIV-1 budding pathway. Retrovirology 5, 64. doi: 10.1186/1742-4690-5-64
    • (2008) Retrovirology , vol.5 , pp. 64
    • Coren, L.V.1    Shatzer, T.2    Ott, D.E.3
  • 22
    • 84859389772 scopus 로고    scopus 로고
    • HIV-1 nef mobilizes lipid rafts in macrophages through a pathway that competes with abca1-dependent cholesterol efflux
    • doi:10.1194/jlr.M023119
    • Cui, H. L., Grant, A., Mukhamedova, N., Pushkarsky, T., Jennelle, L., Dubrovsky, L., et al. (2012). HIV-1 nef mobilizes lipid rafts in macrophages through a pathway that competes with abca1-dependent cholesterol efflux. J. Lipid Res. 53, 696-708. doi: 10.1194/jlr.M023119
    • (2012) J. Lipid Res. , vol.53 , pp. 696-708
    • Cui, H.L.1    Grant, A.2    Mukhamedova, N.3    Pushkarsky, T.4    Jennelle, L.5    Dubrovsky, L.6
  • 23
    • 33845651410 scopus 로고    scopus 로고
    • Conformation of the HIV-1 gag protein in solution
    • doi:10.1016/j.jmb.2006.10.073
    • Datta, S. A. K., Curtis, J. E., Ratcliff, W., Clark, P. K., Crist, R. M., Lebowitz, J., et al. (2007). Conformation of the HIV-1 gag protein in solution. J. Mol. Biol. 365, 812-824. doi: 10.1016/j.jmb.2006.10.073
    • (2007) J. Mol. Biol. , vol.365 , pp. 812-824
    • Datta, S.A.K.1    Curtis, J.E.2    Ratcliff, W.3    Clark, P.K.4    Crist, R.M.5    Lebowitz, J.6
  • 24
    • 85027946224 scopus 로고    scopus 로고
    • Translation initiation is driven by different mechanisms on the HIV-1 and HIV-2 genomic rnas
    • doi:10.1016/j.virusres.2012.10.006
    • De Breyne, S., Soto-Rifo, R., López-Lastra, M., and Ohlmann, T. (2013). Translation initiation is driven by different mechanisms on the HIV-1 and HIV-2 genomic rnas. Virus Res. 171, 366-381. doi: 10.1016/j.virusres.2012.10.006
    • (2013) Virus Res. , vol.171 , pp. 366-381
    • De Breyne, S.1    Soto-Rifo, R.2    López-Lastra, M.3    Ohlmann, T.4
  • 25
    • 34247529467 scopus 로고    scopus 로고
    • In macrophages, HIV-1 assembles into an intracellular plasma membrane domain containing the tetraspanins cd81, cd9, and cd53
    • doi:10.1083/jcb.200609050
    • Deneka, M., Pelchen-Matthews, A., Byland, R., Ruiz-Mateos, E., and Marsh, M. (2007). In macrophages, HIV-1 assembles into an intracellular plasma membrane domain containing the tetraspanins cd81, cd9, and cd53. J. Cell. Biol. 177, 329-341. doi: 10.1083/jcb.200609050
    • (2007) J. Cell. Biol. , vol.177 , pp. 329-341
    • Deneka, M.1    Pelchen-Matthews, A.2    Byland, R.3    Ruiz-Mateos, E.4    Marsh, M.5
  • 26
    • 84869217910 scopus 로고    scopus 로고
    • HIV-1 gag protein can sense the cholesterol and acyl chain environment in model membranes
    • doi:10.1073/pnas.1209408109
    • Dick, R. A., Goh, S. L., Feigenson, G. W., and Vogt, V. M. (2012). HIV-1 gag protein can sense the cholesterol and acyl chain environment in model membranes. Proc. Natl. Acad. Sci. U.S.A. 109, 18761-18766. doi: 10.1073/pnas.1209408109
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 18761-18766
    • Dick, R.A.1    Goh, S.L.2    Feigenson, G.W.3    Vogt, V.M.4
  • 27
    • 84886748172 scopus 로고    scopus 로고
    • HIV assembly and budding: Ca(2+) signaling and non-escrt proteins set the stage
    • doi:10.1155/2012/851670
    • Ehrlich, L. S., and Carter, C. A. (2012). HIV assembly and budding: Ca(2+) signaling and non-escrt proteins set the stage. Mol. Biol. Int. 2012, 851670. doi: 10.1155/2012/851670
    • (2012) Mol. Biol. Int. , vol.2012 , pp. 851670
    • Ehrlich, L.S.1    Carter, C.A.2
  • 28
    • 80051744355 scopus 로고    scopus 로고
    • Sprouty2 regulates pi(4,5)p2/ca2+ signaling and HIV-1 gag release
    • doi:10.1016/j.jmb.2011.04.069
    • Ehrlich, L. S., Medina, G. N., and Carter, C. A. (2011). Sprouty2 regulates pi(4,5)p2/ca2+ signaling and HIV-1 gag release. J. Mol. Biol. 410, 716-725. doi: 10.1016/j.jmb.2011.04.069
    • (2011) J. Mol. Biol. , vol.410 , pp. 716-725
    • Ehrlich, L.S.1    Medina, G.N.2    Carter, C.A.3
  • 29
    • 77953316920 scopus 로고    scopus 로고
    • Activation of the inositol (1,4,5)-triphosphate calcium gate receptor is required for HIV-1 gag release
    • doi:10.1128/JVI.01588-09
    • Ehrlich, L. S., Medina, G. N., Khan, M. B., Powell, M. D., Mikoshiba, K., and Carter, C. A. (2010). Activation of the inositol (1,4,5)-triphosphate calcium gate receptor is required for HIV-1 gag release. J. Virol. 84, 6438-6451. doi: 10.1128/JVI.01588-09
    • (2010) J. Virol. , vol.84 , pp. 6438-6451
    • Ehrlich, L.S.1    Medina, G.N.2    Khan, M.B.3    Powell, M.D.4    Mikoshiba, K.5    Carter, C.A.6
  • 30
    • 79952613075 scopus 로고    scopus 로고
    • Phosphoinositides direct equine infectious anemia virus gag trafficking and release
    • doi:10.1111/j.1600-0854.2010.01153.x
    • Fernandes, F., Chen, K., Ehrlich, L. S., Jin, J., Chen, M. H., Medina, G. N., et al. (2011). Phosphoinositides direct equine infectious anemia virus gag trafficking and release. Traffic 12, 438-451. doi: 10.1111/j.1600-0854.2010.01153.x
    • (2011) Traffic , vol.12 , pp. 438-451
    • Fernandes, F.1    Chen, K.2    Ehrlich, L.S.3    Jin, J.4    Chen, M.H.5    Medina, G.N.6
  • 31
    • 0000829669 scopus 로고    scopus 로고
    • HIVs and their replication
    • 4th Edn., eds D. M. Knipe and P. M. Howley (Philadelphia, PA: Wolters Kluwer Health/Lippincott Williams & Wilkins)
    • Freed, E. O., and Martin, M. A. (2001). "HIVs and their replication," in Fields Virology, 4th Edn., eds D. M. Knipe and P. M. Howley (Philadelphia, PA: Wolters Kluwer Health/Lippincott Williams & Wilkins), 1971-2041.
    • (2001) in Fields Virology , pp. 1971-2041
    • Freed, E.O.1    Martin, M.A.2
  • 32
    • 84944282429 scopus 로고
    • Virus isolation from and identification of HTLV-III/LAV-producing cells in brain tissue from a patient with aids
    • doi:10.1001/jama.1986.03380170081023
    • Gartner, S., Markovits, P., Markovitz, D. M., Betts, R. F., and Popovic, M. (1986). Virus isolation from and identification of HTLV-III/LAV-producing cells in brain tissue from a patient with aids. JAMA 256, 2365-2371. doi: 10.1001/jama.1986.03380170081023
    • (1986) JAMA , vol.256 , pp. 2365-2371
    • Gartner, S.1    Markovits, P.2    Markovitz, D.M.3    Betts, R.F.4    Popovic, M.5
  • 33
    • 84880769116 scopus 로고    scopus 로고
    • Dynamics of HIV-containing compartments in macrophages reveal sequestration of virions and transient surface connections
    • doi:10.1371/journal.pone.0069450
    • Gaudin, R., Berre, S., de Alencar, B. C., Decalf, J., Schindler, M., Gobert, F.-X., et al. (2013). Dynamics of HIV-containing compartments in macrophages reveal sequestration of virions and transient surface connections. PLoS ONE 8:e69450. doi: 10.1371/journal.pone.0069450
    • (2013) PLoS ONE , vol.8
    • Gaudin, R.1    Berre, S.2    de Alencar, B.C.3    Decalf, J.4    Schindler, M.5    Gobert, F.-X.6
  • 34
    • 78650636013 scopus 로고    scopus 로고
    • Binding of calmodulin to the HIV-1 matrix protein triggers myristate exposure
    • doi:10.1074/jbc.M110.179093
    • Ghanam, R. H., Fernandez, T. F., Fledderman, E. L., and Saad, J. S. (2010). Binding of calmodulin to the HIV-1 matrix protein triggers myristate exposure. J. Biol. Chem. 285, 41911-41920. doi: 10.1074/jbc.M110.179093
    • (2010) J. Biol. Chem. , vol.285 , pp. 41911-41920
    • Ghanam, R.H.1    Fernandez, T.F.2    Fledderman, E.L.3    Saad, J.S.4
  • 35
    • 42949175719 scopus 로고    scopus 로고
    • Real-time visualization of HIV-1 GAG trafficking in infected macrophages
    • doi:10.1371/journal.ppat.1000015
    • Gousset, K., Ablan, S. D., Coren, L. V., Ono, A., Soheilian, F., Nagashima, K., et al. (2008). Real-time visualization of HIV-1 GAG trafficking in infected macrophages. PLoS Pathog. 4:e1000015. doi: 10.1371/journal.ppat.1000015
    • (2008) PLoS Pathog. , vol.4
    • Gousset, K.1    Ablan, S.D.2    Coren, L.V.3    Ono, A.4    Soheilian, F.5    Nagashima, K.6
  • 36
    • 33744938142 scopus 로고    scopus 로고
    • Assembly of infectious HIV-1 in human epithelial and T-lymphoblastic cell lines
    • doi:10.1016/j.jmb.2006.04.017
    • Grigorov, B., Arcanger, F., Roingeard, P., Darlix, J.-L., and Muriaux, D. (2006). Assembly of infectious HIV-1 in human epithelial and T-lymphoblastic cell lines. J. Mol. Biol. 359, 848-862. doi: 10.1016/j.jmb.2006.04.017
    • (2006) J. Mol. Biol. , vol.359 , pp. 848-862
    • Grigorov, B.1    Arcanger, F.2    Roingeard, P.3    Darlix, J.-L.4    Muriaux, D.5
  • 37
    • 63049133705 scopus 로고    scopus 로고
    • A role for CD81 on the late steps of HIV-1 replication in a chronically infected T cell line
    • doi:10.1186/1742-4690-6-28
    • Grigorov, B., Attuil-Audenis, V., Perugi, F., Nedelec, M., Watson, S., Pique, C., et al. (2009). A role for CD81 on the late steps of HIV-1 replication in a chronically infected T cell line. Retrovirology 6, 28. doi: 10.1186/1742-4690-6-28
    • (2009) Retrovirology , vol.6 , pp. 28
    • Grigorov, B.1    Attuil-Audenis, V.2    Perugi, F.3    Nedelec, M.4    Watson, S.5    Pique, C.6
  • 38
    • 72849142782 scopus 로고    scopus 로고
    • Targeting of murine leukemia virus gag to the plasma membrane is mediated by PI(4,5)P2/PS and a polybasic region in the matrix
    • doi:10.1128/JVI.01134-09
    • Hamard-Peron, E., Juillard, F., Saad, J. S., Roy, C., Roingeard, P., Summers, M. F., et al. (2010). Targeting of murine leukemia virus gag to the plasma membrane is mediated by PI(4,5)P2/PS and a polybasic region in the matrix. J. Virol. 84, 503-515. doi: 10.1128/JVI.01134-09
    • (2010) J. Virol. , vol.84 , pp. 503-515
    • Hamard-Peron, E.1    Juillard, F.2    Saad, J.S.3    Roy, C.4    Roingeard, P.5    Summers, M.F.6
  • 39
    • 84886931584 scopus 로고    scopus 로고
    • Gag-dependent enrichment of HIV-1 rna near the uropod membrane of polarized t cells
    • doi:10.1128/JVI.01680-13
    • Hatch, S. C., Sardo, L., Chen, J., Burdick, R., Gorelick, R., Fivash, M. J., et al. (2013). Gag-dependent enrichment of HIV-1 rna near the uropod membrane of polarized t cells. J. Virol. 87, 11912-11915. doi: 10.1128/JVI.01680-13
    • (2013) J. Virol. , vol.87 , pp. 11912-11915
    • Hatch, S.C.1    Sardo, L.2    Chen, J.3    Burdick, R.4    Gorelick, R.5    Fivash, M.J.6
  • 40
    • 80053962808 scopus 로고    scopus 로고
    • Gag induces the coalescence of clustered lipid rafts and tetraspanin-enriched microdomains at HIV-1 assembly sites on the plasma membrane
    • doi:10.1128/JVI.00743-11
    • Hogue, I. B., Grover, J. R., Soheilian, F., Nagashima, K., and Ono, A. (2011). Gag induces the coalescence of clustered lipid rafts and tetraspanin-enriched microdomains at HIV-1 assembly sites on the plasma membrane. J. Virol. 85, 9749-9766. doi: 10.1128/JVI.00743-11
    • (2011) J. Virol. , vol.85 , pp. 9749-9766
    • Hogue, I.B.1    Grover, J.R.2    Soheilian, F.3    Nagashima, K.4    Ono, A.5
  • 41
    • 79952850453 scopus 로고    scopus 로고
    • Gag localization and virus-like particle release mediated by the matrix domain of human t-lymphotropic virus type 1 gag are less dependent on phosphatidylinositol-(4,5)-bisphosphate than those mediated by the matrix domain of HIV-1 gag
    • doi:10.1128/JVI.02383-10
    • Inlora, J., Chukkapalli, V., Derse, D., and Ono, A. (2011). Gag localization and virus-like particle release mediated by the matrix domain of human t-lymphotropic 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. doi: 10.1128/JVI.02383-10
    • (2011) J. Virol. , vol.85 , pp. 3802-3810
    • Inlora, J.1    Chukkapalli, V.2    Derse, D.3    Ono, A.4
  • 42
    • 84880510399 scopus 로고    scopus 로고
    • Nature, nurture and HIV: the effect of producer cell on viral physiology
    • doi:10.1016/j.virol.2013.05.023
    • Iordanskiy, S., Santos, S., and Bukrinsky, M. (2013). Nature, nurture and HIV: the effect of producer cell on viral physiology. Virology 443, 208-213. doi: 10.1016/j.virol.2013.05.023
    • (2013) Virology , vol.443 , pp. 208-213
    • Iordanskiy, S.1    Santos, S.2    Bukrinsky, M.3
  • 43
    • 84904869329 scopus 로고    scopus 로고
    • Small alveolar macrophages are infected preferentially by HIV and exhibit impaired phagocytic function
    • doi: 10.1038/mi.2013.127. [Epub ahead of print].
    • Jambo, K. C., Banda, D. H., Kankwatira, A. M., Sukumar, N., Allain, T. J., Heyderman, R. S., et al. (2014). Small alveolar macrophages are infected preferentially by HIV and exhibit impaired phagocytic function. Mucosal Immunol. doi: 10.1038/mi.2013.127. [Epub ahead of print].
    • (2014) Mucosal Immunol
    • Jambo, K.C.1    Banda, D.H.2    Kankwatira, A.M.3    Sukumar, N.4    Allain, T.J.5    Heyderman, R.S.6
  • 44
    • 34547105037 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 assembly, budding, and cell-cell spread in T cells take place in tetraspanin-enriched plasma membrane domains
    • doi:10.1128/JVI.01469-06
    • Jolly, C., and Sattentau, Q. J. (2007). Human immunodeficiency virus type 1 assembly, budding, and cell-cell spread in T cells take place in tetraspanin-enriched plasma membrane domains. J. Virol. 81, 7873-7884. doi: 10.1128/JVI.01469-06
    • (2007) J. Virol. , vol.81 , pp. 7873-7884
    • Jolly, C.1    Sattentau, Q.J.2
  • 45
    • 34547687819 scopus 로고    scopus 로고
    • HIV-1 buds and accumulates in "nonacidic" endosomes of macrophages
    • doi:10.1016/j.chom.2007.06.011
    • Jouve, M., Sol-Foulon, N., Watson, S., Schwartz, O., and Benaroch, P. (2007). HIV-1 buds and accumulates in "nonacidic" endosomes of macrophages. Cell Host Microbe 2, 85-95. doi: 10.1016/j.chom.2007.06.011
    • (2007) Cell Host Microbe , vol.2 , pp. 85-95
    • Jouve, M.1    Sol-Foulon, N.2    Watson, S.3    Schwartz, O.4    Benaroch, P.5
  • 46
    • 85028119064 scopus 로고    scopus 로고
    • Virus assembly and plasma membrane domains: which came first?
    • doi: 10.1016/j.virusres.2012.08.014
    • Kerviel, A., Thomas, A., Chaloin, L., Favard, C., and Muriaux, D. (2013). Virus assembly and plasma membrane domains: which came first? Virus Res. 171, 332-340. doi: 10.1016/j.virusres.2012.08.014
    • (2013) Virus Res. , vol.171 , pp. 332-340
    • Kerviel, A.1    Thomas, A.2    Chaloin, L.3    Favard, C.4    Muriaux, D.5
  • 47
    • 84866885992 scopus 로고    scopus 로고
    • Macrophages and their relevance in human immunodeficiency virus type I infection
    • doi:10.1186/1742-4690-9-82
    • Koppensteiner, H., Brack-Werner, R., and Schindler, M. (2012). Macrophages and their relevance in human immunodeficiency virus type I infection. Retrovirology 9, 82. doi: 10.1186/1742-4690-9-82
    • (2012) Retrovirology , vol.9 , pp. 82
    • Koppensteiner, H.1    Brack-Werner, R.2    Schindler, M.3
  • 48
    • 78649471247 scopus 로고    scopus 로고
    • HIV-1 assembly differentially alters dynamics and partitioning of tetraspanins and raft components
    • doi:10.1111/j.1600-0854.2010.01111.x
    • Krementsov, D. N., Rassam, P., Margeat, E., Roy, N. H., Schneider-Schaulies, J., Milhiet, P.-E., et al. (2010). HIV-1 assembly differentially alters dynamics and partitioning of tetraspanins and raft components. Traffic 11, 1401-1414. doi: 10.1111/j.1600-0854.2010.01111.x
    • (2010) Traffic , vol.11 , pp. 1401-1414
    • Krementsov, D.N.1    Rassam, P.2    Margeat, E.3    Roy, N.H.4    Schneider-Schaulies, J.5    Milhiet, P.-E.6
  • 49
    • 40549111715 scopus 로고    scopus 로고
    • HIV-1 pathogenesis and clinical manifestations
    • 5th Edn., eds D. M. Knipe and P. M. Howley (Philadelphia, PA: Lippincott Williams & Wilkins)
    • Kuritzkes, D. R., W. B. (2007). "HIV-1 pathogenesis and clinical manifestations," in Fields Virology, 5th Edn., eds D. M. Knipe and P. M. Howley (Philadelphia, PA: Lippincott Williams & Wilkins), 2187-2214.
    • (2007) in Fields Virology , pp. 2187-2214
    • Kuritzkes, D.R.W.B.1
  • 50
    • 79251506313 scopus 로고    scopus 로고
    • Analysis of the initiating events in HIV-1 particle assembly and genome packaging
    • doi:10.1371/journal.ppat.1001200
    • Kutluay, S. B., and Bieniasz, P. D. (2010). Analysis of the initiating events in HIV-1 particle assembly and genome packaging. PLoS Pathog 6:e1001200. doi: 10.1371/journal.ppat.1001200
    • (2010) PLoS Pathog , vol.6
    • Kutluay, S.B.1    Bieniasz, P.D.2
  • 51
    • 2442662800 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 gag contains a dileucine-like motif that regulates association with multivesicular bodies
    • doi:10.1128/JVI.78.11.6013-6023.2004
    • Lindwasser, O. W., and Resh, M. D. (2004). Human immunodeficiency virus type 1 gag contains a dileucine-like motif that regulates association with multivesicular bodies. J. Virol. 78, 6013-6023. doi: 10.1128/JVI.78.11.6013-6023.2004
    • (2004) J. Virol. , vol.78 , pp. 6013-6023
    • Lindwasser, O.W.1    Resh, M.D.2
  • 52
    • 84878166615 scopus 로고    scopus 로고
    • Hiv-1 gag associates with specific uropod-directed microdomains in a manner dependent on its ma highly basic region
    • doi:10.1128/JVI.00040-13
    • Llewellyn, G. N., Grover, J. R., Olety, B., and 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. doi: 10.1128/JVI.00040-13
    • (2013) J. Virol. , vol.87 , pp. 6441-6454
    • Llewellyn, G.N.1    Grover, J.R.2    Olety, B.3    Ono, A.4
  • 53
    • 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, G. N., Hogue, I. B., Grover, J. R., and 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
  • 54
    • 84872610774 scopus 로고    scopus 로고
    • Comparative lipidomics analysis of HIV-1 particles and their producer cell membrane in different cell lines
    • doi:10.1111/cmi.12101
    • Lorizate, M., Sachsenheimer, T., Glass, B., Habermann, A., Gerl, M. J., Kräusslich, H.-G., et al. (2013). Comparative lipidomics analysis of HIV-1 particles and their producer cell membrane in different cell lines. Cell. Microbiol. 15, 292-304. doi: 10.1111/cmi.12101
    • (2013) Cell. Microbiol. , vol.15 , pp. 292-304
    • Lorizate, M.1    Sachsenheimer, T.2    Glass, B.3    Habermann, A.4    Gerl, M.J.5    Kräusslich, H.-G.6
  • 55
    • 80051766524 scopus 로고    scopus 로고
    • Structural determinants and mechanism of HIV-1 genome packaging
    • doi:10.1016/j.jmb.2011.04.029
    • Lu, K., Heng, X., and Summers, M. F. (2011). Structural determinants and mechanism of HIV-1 genome packaging. J. Mol. Biol. 410, 609-633. doi: 10.1016/j.jmb.2011.04.029
    • (2011) J. Mol. Biol. , vol.410 , pp. 609-633
    • Lu, K.1    Heng, X.2    Summers, M.F.3
  • 56
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • doi:10.1038/nature04398
    • McLaughlin, S., and Murray, D. (2005). Plasma membrane phosphoinositide organization by protein electrostatics. Nature 438, 605-611. doi: 10.1038/nature04398
    • (2005) Nature , vol.438 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 57
    • 84881145334 scopus 로고    scopus 로고
    • Organization and regulation of intracellular plasma membrane-connected HIV-1 assembly compartments in macrophages
    • doi:10.1186/1741-7007-11-89
    • Mlcochova, P., Pelchen-Matthews, A., and Marsh, M. (2013). Organization and regulation of intracellular plasma membrane-connected HIV-1 assembly compartments in macrophages. BMC Biol. 11:89. doi: 10.1186/1741-7007-11-89
    • (2013) BMC Biol. , vol.11 , pp. 89
    • Mlcochova, P.1    Pelchen-Matthews, A.2    Marsh, M.3
  • 58
    • 79952601192 scopus 로고    scopus 로고
    • Assembly and replication of HIV-1 in t cells with low levels of phosphatidylinositol-(4,5)-bisphosphate
    • doi:10.1128/JVI.02266-10
    • Monde, K., Chukkapalli, V., and Ono, A. (2011). Assembly and replication of HIV-1 in t cells with low levels of phosphatidylinositol-(4,5)-bisphosphate. J. Virol. 85, 3584-3595. doi: 10.1128/JVI.02266-10
    • (2011) J. Virol. , vol.85 , pp. 3584-3595
    • Monde, K.1    Chukkapalli, V.2    Ono, A.3
  • 59
    • 77954944601 scopus 로고    scopus 로고
    • Stimulation of the liver x receptor pathway inhibits HIV-1 replication via induction of atp-binding cassette transporter a1
    • doi:10.1124/mol.110.065029
    • Morrow, M. P., Grant, A., Mujawar, Z., Dubrovsky, L., Pushkarsky, T., Kiselyeva, Y., et al. (2010). Stimulation of the liver x receptor pathway inhibits HIV-1 replication via induction of atp-binding cassette transporter a1. Mol. Pharmacol. 78, 215-225. doi: 10.1124/mol.110.065029
    • (2010) Mol. Pharmacol. , vol.78 , pp. 215-225
    • Morrow, M.P.1    Grant, A.2    Mujawar, Z.3    Dubrovsky, L.4    Pushkarsky, T.5    Kiselyeva, Y.6
  • 60
    • 33751062798 scopus 로고    scopus 로고
    • Human immunodeficiency virus impairs reverse cholesterol transport from macrophages
    • doi:10.1371/journal.pbio.0040365
    • Mujawar, Z., Rose, H., Morrow, M. P., Pushkarsky, T., Dubrovsky, L., Mukhamedova, N., et al. (2006). Human immunodeficiency virus impairs reverse cholesterol transport from macrophages. PLoS Biol. 4:e365. doi: 10.1371/journal.pbio.0040365
    • (2006) PLoS Biol. , vol.4
    • Mujawar, Z.1    Rose, H.2    Morrow, M.P.3    Pushkarsky, T.4    Dubrovsky, L.5    Mukhamedova, N.6
  • 61
    • 84896696477 scopus 로고    scopus 로고
    • A conformational transition observed in single HIV-1 gag molecules during in vitro assembly of virus-like particles
    • doi:10.1128/JVI.03353-13
    • Munro, J. B., Nath, A., Färber, M., Datta, S. A. K., Rein, A., Rhoades, E., et al. (2014). A conformational transition observed in single HIV-1 gag molecules during in vitro assembly of virus-like particles. J. Virol. 88, 3577-3585. doi: 10.1128/JVI.03353-13
    • (2014) J. Virol. , vol.88 , pp. 3577-3585
    • Munro, J.B.1    Nath, A.2    Färber, M.3    Datta, S.A.K.4    Rein, A.5    Rhoades, E.6
  • 62
    • 78751670345 scopus 로고    scopus 로고
    • Properties and functions of the nucleocapsid protein in virus assembly
    • doi:10.4161/rna.7.6.14065
    • Muriaux, D., and Darlix, J.-L. (2010). Properties and functions of the nucleocapsid protein in virus assembly. RNA Biol. 7, 744-753. doi: 10.4161/rna.7.6.14065
    • (2010) RNA Biol. , vol.7 , pp. 744-753
    • Muriaux, D.1    Darlix, J.-L.2
  • 63
    • 26444444082 scopus 로고    scopus 로고
    • Retroviral matrix domains share electrostatic homology: models for membrane binding function throughout the viral life cycle
    • doi:10.1016/j.str.2005.07.010
    • Murray, P. S., Li, Z., Wang, J., Tang, C. L., Honig, B., and Murray, D. (2005). Retroviral matrix domains share electrostatic homology: models for membrane binding function throughout the viral life cycle. Structure 13, 1521-1531. doi: 10.1016/j.str.2005.07.010
    • (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
  • 64
    • 84874678574 scopus 로고    scopus 로고
    • Alterations in the ma and nc domains modulate phosphoinositide-dependent plasma membrane localization of the rous sarcoma virus gag protein
    • doi:10.1128/JVI.03059-12
    • Nadaraia-Hoke, S., Bann, D. V., Lochmann, T. L., Gudleski-O'Regan, N., and Parent, L. J. (2013). Alterations in the ma and nc domains modulate phosphoinositide-dependent plasma membrane localization of the rous sarcoma virus gag protein. J. Virol. 87, 3609-3615. doi: 10.1128/JVI.03059-12
    • (2013) J. Virol. , vol.87 , pp. 3609-3615
    • Nadaraia-Hoke, S.1    Bann, D.V.2    Lochmann, T.L.3    Gudleski-O'Regan, N.4    Parent, L.J.5
  • 65
    • 33747394451 scopus 로고    scopus 로고
    • Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1
    • doi:10.1083/jcb.200508165
    • Nydegger, S., Khurana, S., Krementsov, D. N., Foti, M., and Thali, M. (2006). Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1. J. Cell Biol. 173, 795-807. doi: 10.1083/jcb.200508165
    • (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
  • 66
    • 85027932076 scopus 로고    scopus 로고
    • Elements in HIV-1 gag contributing to virus particle assembly
    • doi:10.1016/j.virusres.2012.10.016
    • O'Carroll, I. P., Soheilian, F., Kamata, A., Nagashima, K., and Rein, A. (2013). Elements in HIV-1 gag contributing to virus particle assembly. Virus Res. 171, 341-345. doi: 10.1016/j.virusres.2012.10.016
    • (2013) Virus Res. , vol.171 , pp. 341-345
    • O'Carroll, I.P.1    Soheilian, F.2    Kamata, A.3    Nagashima, K.4    Rein, A.5
  • 67
    • 70350113492 scopus 로고    scopus 로고
    • HIV-1 assembly at the plasma membrane: gag trafficking and localization
    • doi:10.2217/fvl.09.4
    • Ono, A. (2009). HIV-1 assembly at the plasma membrane: gag trafficking and localization. Future Virol. 4, 241-257. doi: 10.2217/fvl.09.4
    • (2009) Future Virol. , vol.4 , pp. 241-257
    • Ono, A.1
  • 68
    • 6944255361 scopus 로고    scopus 로고
    • Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane
    • doi:10.1073/pnas.0405596101
    • Ono, A., Ablan, S. D., Lockett, S. J., Nagashima, K., and Freed, E. O. (2004a). Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane. Proc. Natl. Acad. Sci. U.S.A. 101, 14889-14894. doi: 10.1073/pnas.0405596101
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 14889-14894
    • Ono, A.1    Ablan, S.D.2    Lockett, S.J.3    Nagashima, K.4    Freed, E.O.5
  • 69
    • 6944255361 scopus 로고    scopus 로고
    • Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 gag targeting to the plasma membrane
    • doi:10.1073/pnas.0405596101
    • Ono, A., Ablan, S. D., Lockett, S. J., Nagashima, K., and Freed, E. O. (2004b). Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 gag targeting to the plasma membrane. Proc. Natl. Acad. Sci. U.S.A. 101, 14889-14894. doi: 10.1073/pnas.0405596101
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 14889-14894
    • Ono, A.1    Ablan, S.D.2    Lockett, S.J.3    Nagashima, K.4    Freed, E.O.5
  • 70
    • 0035923525 scopus 로고    scopus 로고
    • Plasma membrane rafts play a critical role in HIV-1 assembly and release
    • doi:10.1073/pnas.241320298
    • Ono, A., and Freed, E. O. (2001). Plasma membrane rafts play a critical role in HIV-1 assembly and release. Proc. Natl. Acad. Sci. U.S.A. 98, 13925-13930. doi: 10.1073/pnas.241320298
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 13925-13930
    • Ono, A.1    Freed, E.O.2
  • 71
    • 0031732835 scopus 로고    scopus 로고
    • The warthin-finkeldey-type giant cell in HIV infection, what is it? Ultrastruct
    • doi:10.3109/01913129809103350
    • Orenstein, J. M. (1998). The warthin-finkeldey-type giant cell in HIV infection, what is it? Ultrastruct. Pathol. 22, 293-303. doi: 10.3109/01913129809103350
    • (1998) Pathol. , vol.22 , pp. 293-303
    • Orenstein, J.M.1
  • 72
    • 0023678515 scopus 로고
    • Cytoplasmic assembly and accumulation of human immunodeficiency virus types 1 and 2 in recombinant human colony-stimulating factor-1-treated human Monocytes: an ultrastructural study
    • Orenstein, J. M., Meltzer, M. S., Phipps, T., and Gendelman, H. (1988). Cytoplasmic assembly and accumulation of human immunodeficiency virus types 1 and 2 in recombinant human colony-stimulating factor-1-treated human Monocytes: an ultrastructural study. J. Virol. 68, 2579-2586.
    • (1988) J. Virol. , vol.68 , pp. 2579-2586
    • Orenstein, J.M.1    Meltzer, M.S.2    Phipps, T.3    Gendelman, H.4
  • 73
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophages
    • doi:10.1083/jcb.200304008
    • Pelchen-Matthews, A. (2003). Infectious HIV-1 assembles in late endosomes in primary macrophages. J. Cell Biol. 162, 443-455. doi: 10.1083/jcb.200304008
    • (2003) J. Cell Biol. , vol.162 , pp. 443-455
    • Pelchen-Matthews, A.1
  • 74
    • 33646410462 scopus 로고    scopus 로고
    • Identification of an intracellular trafficking and assembly pathway for HIV-1 gag
    • doi:10.1111/j.1398-9219.2006.00428.x
    • Perlman, M., and Resh, M. D. (2006). Identification of an intracellular trafficking and assembly pathway for HIV-1 gag. Traffic 7, 731-745. doi: 10.1111/j.1398-9219.2006.00428.x
    • (2006) Traffic , vol.7 , pp. 731-745
    • Perlman, M.1    Resh, M.D.2
  • 75
    • 84867071581 scopus 로고    scopus 로고
    • The structure of myristoylated mason-pfizer monkey virus matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in its membrane binding
    • doi:10.1016/j.jmb.2012.07.021
    • Prchal, J., Srb, P., Hunter, E., Ruml, T., and Hrabal, R. (2012). The structure of myristoylated mason-pfizer monkey virus matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in its membrane binding. J. Mol. Biol. 423, 427-438. doi: 10.1016/j.jmb.2012.07.021
    • (2012) J. Mol. Biol. , vol.423 , pp. 427-438
    • Prchal, J.1    Srb, P.2    Hunter, E.3    Ruml, T.4    Hrabal, R.5
  • 76
    • 0036788110 scopus 로고    scopus 로고
    • Human macrophages accumulate HIV-1 particles in MHC II compartments
    • doi:10.1034/j.1600-0854.2002.31004.x
    • Raposo, G., Moore, M., Innes, D., Leijendekker, R., Leigh-Brown, A., Benaroch, P., et al. (2002). Human macrophages accumulate HIV-1 particles in MHC II compartments. Traffic 3, 718-729. doi: 10.1034/j.1600-0854.2002.31004.x
    • (2002) Traffic , vol.3 , pp. 718-729
    • Raposo, G.1    Moore, M.2    Innes, D.3    Leijendekker, R.4    Leigh-Brown, A.5    Benaroch, P.6
  • 77
    • 23144434990 scopus 로고    scopus 로고
    • Intracellular trafficking of HIV-1 gag: how gag interacts with cell membranes and makes viral particles
    • Resh, M. D. (2005). Intracellular trafficking of HIV-1 gag: how gag interacts with cell membranes and makes viral particles. AIDS Rev. 7, 84-91.
    • (2005) AIDS Rev. , vol.7 , pp. 84-91
    • Resh, M.D.1
  • 78
    • 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
    • doi:10.1016/j.jmb.2008.07.027
    • Saad, J. S., Ablan, S. D., Ghanam, R. H., Kim, A., Andrews, K., Nagashima, K., et al. (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. doi: 10.1016/j.jmb.2008.07.027
    • (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
  • 79
    • 33746625935 scopus 로고    scopus 로고
    • Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
    • doi:10.1073/pnas.0602818103
    • Saad, J. S., Miller, J., Tai, J., Kim, A., Ghanam, R. H., and Summers, M. F. (2006). Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly. Proc. Natl. Acad. Sci. U.S.A. 103, 11364-11369. doi: 10.1073/pnas.0602818103
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 80
    • 80053001284 scopus 로고    scopus 로고
    • NMR, biophysical, and biochemical studies reveal the minimal calmodulin binding domain of the HIV-1 matrix protein
    • doi:10.1074/jbc.M111.273623
    • Samal, A. B., Ghanam, R. H., Fernandez, T. F., Monroe, E. B., and Saad, J. S. (2011). NMR, biophysical, and biochemical studies reveal the minimal calmodulin binding domain of the HIV-1 matrix protein. J. Biol. Chem. 286, 33533-33543. doi: 10.1074/jbc.M111.273623
    • (2011) J. Biol. Chem. , vol.286 , pp. 33533-33543
    • Samal, A.B.1    Ghanam, R.H.2    Fernandez, T.F.3    Monroe, E.B.4    Saad, J.S.5
  • 81
    • 77952311080 scopus 로고    scopus 로고
    • Cholesterol-binding viral proteins in virus entry and morphogenesis
    • doi:10.1007/978-90-481-8622-8_3
    • Schroeder, C. (2010). Cholesterol-binding viral proteins in virus entry and morphogenesis. Subcell Biochem. 51, 77-108. doi: 10.1007/978-90-481-8622-8_3
    • (2010) Subcell Biochem. , vol.51 , pp. 77-108
    • Schroeder, C.1
  • 82
    • 22744433225 scopus 로고    scopus 로고
    • Macrophages archive hiv-1 virions for dissemination in trans
    • doi:10.1038/sj.emboj.7600707
    • Sharova, N., Swingler, C., Sharkey, M., and Stevenson, M. (2005). Macrophages archive hiv-1 virions for dissemination in trans. EMBO J. 24, 2481-2489. doi: 10.1038/sj.emboj.7600707
    • (2005) EMBO J. , vol.24 , pp. 2481-2489
    • Sharova, N.1    Swingler, C.2    Sharkey, M.3    Stevenson, M.4
  • 83
    • 63149107945 scopus 로고    scopus 로고
    • Macrophages in vaginal but not intestinal mucosa are monocyte-like and permissive to human immunodeficiency virus type 1 infection
    • doi:10.1128/JVI.01796-08
    • Shen, R., Richter, H. E., Clements, R. H., Novak, L., Huff, K., Bimczok, D., et al. (2009). Macrophages in vaginal but not intestinal mucosa are monocyte-like and permissive to human immunodeficiency virus type 1 infection. J. Virol. 83, 3258-3267. doi: 10.1128/JVI.01796-08
    • (2009) J. Virol. , vol.83 , pp. 3258-3267
    • Shen, R.1    Richter, H.E.2    Clements, R.H.3    Novak, L.4    Huff, K.5    Bimczok, D.6
  • 84
    • 20444428008 scopus 로고    scopus 로고
    • Regulation of ion channels by phosphatidylinositol 4,5-bisphosphate
    • doi:10.1016/j.conb.2005.05.005
    • Suh, B.-C., and Hille, B. (2005). Regulation of ion channels by phosphatidylinositol 4,5-bisphosphate. Curr. Opin. Neurobiol. 15, 370-378. doi: 10.1016/j.conb.2005.05.005
    • (2005) Curr. Opin. Neurobiol. , vol.15 , pp. 370-378
    • Suh, B.-C.1    Hille, B.2
  • 85
    • 84881023780 scopus 로고    scopus 로고
    • The HIV-1-containing macrophage compartment: a perfect cellular niche?
    • doi: 10.1016/j.tim.2013.05.001
    • Tan, J., and Sattentau, Q. J. (2013). The HIV-1-containing macrophage compartment: a perfect cellular niche? Trends Microbiol. 21, 1-8. doi: 10.1016/j.tim.2013.05.001
    • (2013) Trends Microbiol. , vol.21 , pp. 1-8
    • Tan, J.1    Sattentau, Q.J.2
  • 86
    • 84864678856 scopus 로고    scopus 로고
    • Calmodulin binds a highly extended HIV-1 ma protein that refolds upon its release
    • doi:10.1016/j.bpj.2012.06.042
    • Taylor, J. E., Chow, J. Y. H., Jeffries, C. M., Kwan, A. H., Duff, A. P., Hamilton, W. A., et al. (2012). Calmodulin binds a highly extended HIV-1 ma protein that refolds upon its release. Biophys. J. 103, 541-549. doi: 10.1016/j.bpj.2012.06.042
    • (2012) Biophys. J. , vol.103 , pp. 541-549
    • Taylor, J.E.1    Chow, J.Y.H.2    Jeffries, C.M.3    Kwan, A.H.4    Duff, A.P.5    Hamilton, W.A.6
  • 87
    • 77950501337 scopus 로고    scopus 로고
    • The roles of tetraspanins in HIV-1 replication
    • doi:10.1007/978-3-642-02175-6_5
    • Thali, M. (2009). The roles of tetraspanins in HIV-1 replication. Curr. Top. Microbiol. Immunol. 339, 85-102. doi: 10.1007/978-3-642-02175-6_5
    • (2009) Curr. Top. Microbiol. Immunol. , vol.339 , pp. 85-102
    • Thali, M.1
  • 88
    • 81855221892 scopus 로고    scopus 로고
    • Membrane protein sequestering by ionic protein-lipid interactions
    • doi:10.1038/nature10545
    • Van Den Bogaart, G., Meyenberg, K., Risselada, H. J., Amin, H., Willig, K. I., Hubrich, B. E., et al. (2011). Membrane protein sequestering by ionic protein-lipid interactions. Nature 479, 552-555. doi: 10.1038/nature10545
    • (2011) Nature , vol.479 , pp. 552-555
    • Van Den Bogaart, G.1    Meyenberg, K.2    Risselada, H.J.3    Amin, H.4    Willig, K.I.5    Hubrich, B.E.6
  • 89
    • 84896957928 scopus 로고    scopus 로고
    • Solution structure of calmodulin bound to the binding domain of the HIV-1 matrix protein
    • doi:10.1074/jbc.M113.543694
    • Vlach, J., Samal, A. B., and Saad, J. S. (2014). Solution structure of calmodulin bound to the binding domain of the HIV-1 matrix protein. J. Biol. Chem. 289, 8697-705. doi: 10.1074/jbc.M113.543694
    • (2014) J. Biol. Chem. , vol.289 , pp. 8697-8705
    • Vlach, J.1    Samal, A.B.2    Saad, J.S.3
  • 91
    • 69549088095 scopus 로고    scopus 로고
    • Tetraspanin-enriched microdomains: a functional unit in cell plasma membranes
    • doi:10.1016/j.tcb.2009.06.004
    • Yanez-Mo, M., Barreiro, O., Gordon-Alonso, M., Sala-Valdes, M., and Sanchez-Madrid, F. (2009). Tetraspanin-enriched microdomains: a functional unit in cell plasma membranes. Trends Cell. Biol. 19, 434-446. doi: 10.1016/j.tcb.2009.06.004
    • (2009) Trends Cell. Biol. , vol.19 , pp. 434-446
    • Yanez-Mo, M.1    Barreiro, O.2    Gordon-Alonso, M.3    Sala-Valdes, M.4    Sanchez-Madrid, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.