메뉴 건너뛰기




Volumn 10, Issue 30, 2004, Pages 3725-3739

Targeting the assembly of the human immunodeficiency virus type I

Author keywords

Anti viral approaches; Drugs; HIV 1; Retrovirus 3 ; Virion assembly

Indexed keywords

1,1' [1,4 PHENYLENEBIS(METHYLENE)]BIS(1,4,8,11 TETRAAZACYCLOTETRADECANE); 3 NITROSOBENZAMIDE; ANTIRETROVIRUS AGENT; ANTIVIRUS AGENT; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BETULIC ACID; BREFELDIN A; COLCHICINE; CYTOCHALASIN D; EFAVIRENZ; EPOXOMICIN; GAG PROTEIN; LACTACYSTIN; LATRUNCULIN B; LEPTOMYCIN B; MESSENGER RNA; MONENSIN; N [4 CHLORO 3 (3 METHYL 2 BUTENYLOXY)PHENYL] 2 METHYL 3 FURANCARBOTHIOAMIDE; NEVIRAPINE; NOCODAZOLE; PEPTIDE DERIVATIVE; POL PROTEIN; PROTEASOME INHIBITOR; RNA DIRECTED DNA POLYMERASE INHIBITOR; TALVIRALINE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VIRUS DNA; VIRUS ENZYME; VIRUS PROTEIN; WORTMANNIN;

EID: 6944223885     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/1381612043382701     Document Type: Review
Times cited : (27)

References (240)
  • 1
    • 0042924181 scopus 로고    scopus 로고
    • Virus entry as a target for anti-HIV intervention
    • Este JA. Virus entry as a target for anti-HIV intervention. Curr Med Chem 2003; 10(17): 1617-32.
    • (2003) Curr. Med. Chem. , vol.10 , Issue.17 , pp. 1617-1632
    • Este, J.A.1
  • 2
    • 0041488800 scopus 로고    scopus 로고
    • Small-molecule HIV-1 integrase inhibitors: The 2001-2002 update
    • Dayam R, Neamati N. Small-molecule HIV-1 integrase inhibitors: the 2001-2002 update. Curr Pharm Des 2003; 9(22): 1789-802.
    • (2003) Curr. Pharm. Des. , vol.9 , Issue.22 , pp. 1789-1802
    • Dayam, R.1    Neamati, N.2
  • 3
    • 0036696712 scopus 로고    scopus 로고
    • Targeting HIV: Antiretroviral therapy and development of drug resistance
    • Menendez-Arias L. Targeting HIV: antiretroviral therapy and development of drug resistance. Trends Pharmacol Sci 2002; 23(8): 381-8.
    • (2002) Trends Pharmacol. Sci. , vol.23 , Issue.8 , pp. 381-388
    • Menendez-Arias, L.1
  • 5
    • 0024429254 scopus 로고
    • Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirusinfected insect cells
    • Gheysen D, Jacobs E, de Foresta F, Thiriart C, Francotte M, Thines D, et al. Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirusinfected insect cells. Cell 1989; 59(1): 103-12.
    • (1989) Cell , vol.59 , Issue.1 , pp. 103-112
    • Gheysen, D.1    Jacobs, E.2    de Foresta, F.3    Thiriart, C.4    Francotte, M.5    Thines, D.6
  • 6
    • 0029103178 scopus 로고
    • Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1
    • Campbell S, Vogt VM. Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1. J Virol 1995; 69(10): 6487-97.
    • (1995) J. Virol. , vol.69 , Issue.10 , pp. 6487-6497
    • Campbell, S.1    Vogt, V.M.2
  • 7
    • 0036635446 scopus 로고    scopus 로고
    • Assembling the human immumodeficiency virus type 1
    • Cimarelli A, Darlix JL. Assembling the human immumodeficiency virus type 1. Cell Mol Life Sci 2002; 59(7): 1166-84.
    • (2002) Cell Mol. Life Sci. , vol.59 , Issue.7 , pp. 1166-1184
    • Cimarelli, A.1    Darlix, J.L.2
  • 8
    • 0036062256 scopus 로고    scopus 로고
    • Charting HIV's remarkable voyage through the cell: Basic science as a passport to future therapy
    • Greene WC, Peterlin BM. Charting HIV's remarkable voyage through the cell: Basic science as a passport to future therapy. Nat Med 2002; 8(7): 673-80.
    • (2002) Nat. Med. , vol.8 , Issue.7 , pp. 673-680
    • Greene, W.C.1    Peterlin, B.M.2
  • 10
    • 0026707722 scopus 로고
    • Interferon gamma induces the expression of human immunodeficiency virus in persistently infected promonocytic cells (U1) and redirects the production of virions to intracytoplasmic vacuoles in phorbol myristate acetate-differentiated U1 cells
    • Biswas P, Poli G, Kinter AL, Justement JS, Stanley SK, Maury WJ, et al. Interferon gamma induces the expression of human immunodeficiency virus in persistently infected promonocytic cells (U1) and redirects the production of virions to intracytoplasmic vacuoles in phorbol myristate acetate-differentiated U1 cells. J Exp Med 1992; 176(3): 739-50.
    • (1992) J. Exp. Med. , vol.176 , Issue.3 , pp. 739-750
    • Biswas, P.1    Poli, G.2    Kinter, A.L.3    Justement, J.S.4    Stanley, S.K.5    Maury, W.J.6
  • 11
    • 0025243844 scopus 로고
    • Human immunodeficiency virus type 1 infection of U937 cells promotes cell differentiation and a new pathway of viral assembly
    • Pautrat G, Suzan M, Salaun D, Corbeau P, Allasia C, Morel G, et al. Human immunodeficiency virus type 1 infection of U937 cells promotes cell differentiation and a new pathway of viral assembly. Virology 1990; 179(2): 749-58.
    • (1990) Virology , vol.179 , Issue.2 , pp. 749-758
    • Pautrat, G.1    Suzan, M.2    Salaun, D.3    Corbeau, P.4    Allasia, C.5    Morel, G.6
  • 12
    • 0026464669 scopus 로고
    • Loss of infectivity by progeny virus from alpha interferon-treated human immunodeficiency virus type 1-infected T cells is associated with defective assembly of envelope gp 120
    • Hansen BD, Nara PL, Maheshwari RK, Sidhu GS, Bernbaum JG, Hoekzema D, et al. Loss of infectivity by progeny virus from alpha interferon-treated human immunodeficiency virus type 1-infected T cells is associated with defective assembly of envelope gp 120. J Virol 1992; 66(12): 7543-8.
    • (1992) J. Virol. , vol.66 , Issue.12 , pp. 7543-7548
    • Hansen, B.D.1    Nara, P.L.2    Maheshwari, R.K.3    Sidhu, G.S.4    Bernbaum, J.G.5    Hoekzema, D.6
  • 13
    • 0027427111 scopus 로고
    • An ultrastructural study of HIV-infected human dendritic cells and monocytes/macrophages
    • Blom J, Nielsen C, Rhodes JM. An ultrastructural study of HIV-infected human dendritic cells and monocytes/macrophages. APMIS 1993; 101(9): 672-80.
    • (1993) APMIS , vol.101 , Issue.9 , pp. 672-680
    • Blom, J.1    Nielsen, C.2    Rhodes, J.M.3
  • 14
    • 0029096937 scopus 로고
    • Suppression of HIV replication in human monocyte-derived macrophages induced by granulocyte/macrophage colony-stimulating factor
    • Matsuda S, Akagawa K, Honda M, Yokota Y, Takebe Y, Takemori T. Suppression of HIV replication in human monocyte-derived macrophages induced by granulocyte/macrophage colony-stimulating factor. AIDS Res Hum Retroviruses 1995; 11(9): 1031-8.
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , Issue.9 , pp. 1031-1038
    • Matsuda, S.1    Akagawa, K.2    Honda, M.3    Yokota, Y.4    Takebe, Y.5    Takemori, T.6
  • 15
    • 0026083790 scopus 로고
    • Transmission of human immunodeficiency virus from monocytes to epithelia
    • Bourinbaiar AS, Phillips DM. Transmission of human immunodeficiency virus from monocytes to epithelia. J Acquir Immune Defic Syndr 1991; 4(1): 56-63.
    • (1991) J. Acquir. Immune Defic. Syndr. , vol.4 , Issue.1 , pp. 56-63
    • Bourinbaiar, A.S.1    Phillips, D.M.2
  • 16
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophages
    • Pelchen-Matthews A, Kramer B, Marsh M. Infectious HIV-1 assembles in late endosomes in primary macrophages. J Cell Biol 2003; 162(3): 443-55.
    • (2003) J. Cell Biol. , vol.162 , Issue.3 , pp. 443-455
    • Pelchen-Matthews, A.1    Kramer, B.2    Marsh, M.3
  • 17
    • 0025728301 scopus 로고
    • Form, function and use of retroviral Gag proteins
    • Wills JW, Craven RC. Form, function and use of retroviral Gag proteins. AIDS 1991; 5: 639-654.
    • (1991) AIDS , vol.5 , pp. 639-654
    • Wills, J.W.1    Craven, R.C.2
  • 18
    • 0342394457 scopus 로고
    • Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1
    • Gottlinger HG, Sodroski JG, Haseltine WA. Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. Proc Natl Acad Sci USA 1989; 86(15): 5781-5.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , Issue.15 , pp. 5781-5785
    • Gottlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 19
    • 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 RL, Krausslich HG. 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 1993; 67(8): 4972-80.
    • (1993) J. Virol. , vol.67 , Issue.8 , pp. 4972-4980
    • Facke, M.1    Janetzko, A.2    Shoeman, R.L.3    Krausslich, H.G.4
  • 20
    • 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. 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 1994; 68(4): 2556-69.
    • (1994) J. Virol. , vol.68 , Issue.4 , pp. 2556-2569
    • Zhou, W.1    Parent, L.J.2    Wills, J.W.3    Resh, M.D.4
  • 21
    • 0028908747 scopus 로고
    • Human immunodeficiency virus type 1 MA deletion mutants expressed in baculovirus-infected cells: Cis and trans effects on the Gag precursor assembly pathway
    • Chazal N, Gay B, Carriere C, Tournier J, Boulanger P. Human immunodeficiency virus type 1 MA deletion mutants expressed in baculovirus-infected cells: cis and trans effects on the Gag precursor assembly pathway. J Virol 1995; 69(1): 365-75.
    • (1995) J. Virol. , vol.69 , Issue.1 , pp. 365-375
    • Chazal, N.1    Gay, B.2    Carriere, C.3    Tournier, J.4    Boulanger, P.5
  • 22
    • 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. Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal. J Virol 1994; 68(10): 6644-54.
    • (1994) J. Virol. , vol.68 , Issue.10 , pp. 6644-6654
    • Lee, P.P.1    Linial, M.L.2
  • 23
    • 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. Identification of human immunodeficiency virus type 1 Gag protein domains essential to membrane binding and particle assembly. J Virol 1994; 68(5): 3232-42.
    • (1994) J. Virol. , vol.68 , Issue.5 , pp. 3232-3242
    • Spearman, P.1    Wang, J.J.2    Vander Heyden, N.3    Ratner, L.4
  • 24
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh MD. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim Biophys Acta 1999; 1451(1): 1-16.
    • (1999) Biochim. Biophys. Acta , vol.1451 , Issue.1 , pp. 1-16
    • Resh, M.D.1
  • 25
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes: Simple physics, complicated biology
    • Murray D, Ben-Tal N, Honig B, McLaughlin S. Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology. Structure 1997; 5(8): 985-9.
    • (1997) Structure , vol.5 , Issue.8 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 26
    • 0024357985 scopus 로고
    • Replication of human immunodeficiency virus 1 and Moloney murine leukemia virus is inhibited by different heteroatom-containing analogs of myristic acid
    • Bryant ML, Heuckeroth RO, Kimata JT, Ratner L, Gordon JI. Replication of human immunodeficiency virus 1 and Moloney murine leukemia virus is inhibited by different heteroatom-containing analogs of myristic acid. Proc Natl Acad Sci USA 1989; 86(22): 8655-9.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , Issue.22 , pp. 8655-8659
    • Bryant, M.L.1    Heuckeroth, R.O.2    Kimata, J.T.3    Ratner, L.4    Gordon, J.I.5
  • 27
    • 0025176624 scopus 로고
    • Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
    • Bryant M, Ratner L. Myristoylation-dependent replication and assembly of human immunodeficiency virus 1. Proc Natl Acad Sci USA 1990; 87(2): 523-7.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , Issue.2 , pp. 523-527
    • Bryant, M.1    Ratner, L.2
  • 28
    • 0026015894 scopus 로고
    • Incorporation of 12-methoxydodecanoate into the human immunodeficiency virus 1 gag polyprotein precursor inhibits its proteolytic processing and virus production in a chronically infected human lymphoid cell line
    • Bryant ML, Ratner L, Duronio RJ, Kishore NS, Devadas B, Adams SP, et al. Incorporation of 12-methoxydodecanoate into the human immunodeficiency virus 1 gag polyprotein precursor inhibits its proteolytic processing and virus production in a chronically infected human lymphoid cell line. Proc Natl Acad Sci USA 1991; 88(6): 2055-9.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , Issue.6 , pp. 2055-2059
    • Bryant, M.L.1    Ratner, L.2    Duronio, R.J.3    Kishore, N.S.4    Devadas, B.5    Adams, S.P.6
  • 30
    • 0028901720 scopus 로고
    • Myosin-actin interaction plays an important role in human immunodeficiency virus type 1 release from host cells
    • Sasaki H, Nakamura M, Ohno T, Matsuda Y, Yuda Y, Nonomura Y. Myosin-actin interaction plays an important role in human immunodeficiency virus type 1 release from host cells. Proc Natl Acad Sci USA 1995; 92(6) 2026-30
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , Issue.6 , pp. 2026-2030
    • Sasaki, H.1    Nakamura, M.2    Ohno, T.3    Matsuda, Y.4    Yuda, Y.5    Nonomura, Y.6
  • 31
    • 0038314400 scopus 로고    scopus 로고
    • Virus entry, assembly, budding, and membrane rafts
    • table of contents
    • Chazal N, Gerlier D. Virus entry, assembly, budding, and membrane rafts. Microbiol Mol Biol Rev 2003; 67(2): 220-37, table of contents.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , Issue.2 , pp. 220-237
    • Chazal, N.1    Gerlier, D.2
  • 32
    • 0037384054 scopus 로고    scopus 로고
    • Do lipid rafts mediate virus assembly and pseudotyping?
    • Briggs JA, Wilk T, Fuller SD. Do lipid rafts mediate virus assembly and pseudotyping? J Gen Virol 2003; 84(Pt 4): 757-68.
    • (2003) J. Gen. Virol. , vol.84 , Issue.PART 4 , pp. 757-768
    • Briggs, J.A.1    Wilk, T.2    Fuller, S.D.3
  • 33
    • 0033858756 scopus 로고    scopus 로고
    • Influenza virus assembly: Effect of influenza virus glycoproteins on the membrane association of M1 protein
    • Ali A, Avalos RT, Ponimaskin E, Nayak DP. Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 protein. J Virol 2000; 74(18): 8709-19.
    • (2000) J. Virol. , vol.74 , Issue.18 , pp. 8709-8719
    • Ali, A.1    Avalos, R.T.2    Ponimaskin, E.3    Nayak, D.P.4
  • 34
    • 0033987081 scopus 로고    scopus 로고
    • Measles virus structural components are enriched into lipid raft microdomains: A potential cellular location for virus assembly
    • Manie SN, Debreyne S, Vincent S, Gerlier D. Measles virus structural components are enriched into lipid raft microdomains: a potential cellular location for virus assembly. J Virol 2000; 74(1): 305-11.
    • (2000) J. Virol. , vol.74 , Issue.1 , pp. 305-311
    • Manie, S.N.1    Debreyne, S.2    Vincent, S.3    Gerlier, D.4
  • 35
    • 0034715352 scopus 로고    scopus 로고
    • Assembly of Sendai virus: M protein interacts with F and HN proteins and with the cytoplasmic tail and transmembrane domain of F protein
    • Ali A, Nayak DP. Assembly of Sendai virus: M protein interacts with F and HN proteins and with the cytoplasmic tail and transmembrane domain of F protein. Virology 2000; 276(2): 289-303.
    • (2000) Virology , vol.276 , Issue.2 , pp. 289-303
    • Ali, A.1    Nayak, D.P.2
  • 36
    • 0033779038 scopus 로고    scopus 로고
    • Measles virus assembly within membrane rafts
    • Vincent S, Gerlier D, Manic SN. Measles virus assembly within membrane rafts. J Virol 2000; 74(21): 9911-5.
    • (2000) J. Virol. , vol.74 , Issue.21 , pp. 9911-9915
    • Vincent, S.1    Gerlier, D.2    Manic, S.N.3
  • 37
    • 0034939645 scopus 로고    scopus 로고
    • Transport of viral proteins to the apical membranes and interaction of matrix protein with glycoproteins in the assembly of influenza viruses
    • Barman S, Ali A, Hui EK, Adhikary L, Nayak DP. Transport of viral proteins to the apical membranes and interaction of matrix protein with glycoproteins in the assembly of influenza viruses. Virus Res 2001; 77(1): 61-9.
    • (2001) Virus Res. , vol.77 , Issue.1 , pp. 61-69
    • Barman, S.1    Ali, A.2    Hui, E.K.3    Adhikary, L.4    Nayak, D.P.5
  • 39
    • 0034602776 scopus 로고    scopus 로고
    • The Nef protein of HIV-1 associates with rafts and primes T cells for activation
    • Wang JK, Kiyokawa E, Verdin E, Trono D. The Nef protein of HIV-1 associates with rafts and primes T cells for activation. Proc Natl Acad Sci USA 2000; 97(1): 394-9.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.1 , pp. 394-399
    • Wang, J.K.1    Kiyokawa, E.2    Verdin, E.3    Trono, D.4
  • 41
    • 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 JE, 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 1980; 255(19): 9044-50.
    • (1980) J. Biol. Chem. , vol.255 , Issue.19 , pp. 9044-9050
    • Pessin, J.E.1    Glaser, M.2
  • 42
    • 0015134207 scopus 로고
    • Phospholipid composition of Rous sarcoma virus, host cell membranes and other enveloped RNA viruses
    • Quigley JP, Rifkin DB, Reich E. Phospholipid composition of Rous sarcoma virus, host cell membranes and other enveloped RNA viruses. Virology 1971; 46(1): 106-16.
    • (1971) Virology , vol.46 , Issue.1 , pp. 106-116
    • Quigley, J.P.1    Rifkin, D.B.2    Reich, E.3
  • 44
    • 0034111529 scopus 로고    scopus 로고
    • Efficient incorporation of HLA class II onto human immunodeficiency virus type 1 requires envelope glycoprotein packaging
    • Poon DT, Coren LV, Ott DE. Efficient incorporation of HLA class II onto human immunodeficiency virus type 1 requires envelope glycoprotein packaging. J Virol 2000; 74(8): 3918-23.
    • (2000) J. Virol. , vol.74 , Issue.8 , pp. 3918-3923
    • Poon, D.T.1    Coren, L.V.2    Ott, D.E.3
  • 45
    • 0029821868 scopus 로고    scopus 로고
    • Characterization of human immunodeficiency virus type 1 Vif particle incorporation
    • Camaur D, Trono D. Characterization of human immunodeficiency virus type 1 Vif particle incorporation. J Virol 1996; 70(9): 6106-11.
    • (1996) J. Virol. , vol.70 , Issue.9 , pp. 6106-6111
    • Camaur, D.1    Trono, D.2
  • 46
    • 0030930244 scopus 로고    scopus 로고
    • Cellular proteins in HIV virions
    • Ott DE. Cellular proteins in HIV virions. Rev Med Virol 1997; 7(3): 167-180.
    • (1997) Rev. Med. Virol. , vol.7 , Issue.3 , pp. 167-180
    • Ott, D.E.1
  • 47
    • 0034955304 scopus 로고    scopus 로고
    • Floating the raft hypothesis: Lipid rafts play a role in immune cell activation
    • Cherukuri A, Dykstra M, Pierce SK. Floating the raft hypothesis: lipid rafts play a role in immune cell activation. Immunity 2001; 14(6): 657-60.
    • (2001) Immunity , vol.14 , Issue.6 , pp. 657-660
    • Cherukuri, A.1    Dykstra, M.2    Pierce, S.K.3
  • 48
  • 49
    • 0035367946 scopus 로고    scopus 로고
    • New views of BCR structure and organization
    • Matsuuchi L, Gold MR. New views of BCR structure and organization. Curr Opin Immunol 2001; 13(3): 270-7.
    • (2001) Curr. Opin. Immunol. , vol.13 , Issue.3 , pp. 270-277
    • Matsuuchi, L.1    Gold, M.R.2
  • 50
    • 0034924486 scopus 로고    scopus 로고
    • The amplification of TCR signaling by dynamic membrane microdomains
    • Viola A. The amplification of TCR signaling by dynamic membrane microdomains. Trends Immunol 2001; 22(6): 322-7.
    • (2001) Trends Immunol. , vol.22 , Issue.6 , pp. 322-327
    • Viola, A.1
  • 51
    • 0035037684 scopus 로고    scopus 로고
    • Membrane lipid microdomains and the role of PKCtheta in T cell activation
    • Bi K, Altman A. Membrane lipid microdomains and the role of PKCtheta in T cell activation. Semin Immunol 2001; 13(2): 139-46.
    • (2001) Semin. Immunol. , vol.13 , Issue.2 , pp. 139-146
    • Bi, K.1    Altman, A.2
  • 52
    • 0035039037 scopus 로고    scopus 로고
    • Co-stimulation and counter-stimulation: Lipid raft clustering controls TCR signaling and functional outcomes
    • Miceli MC, Moran M, Chung CD, Patel VP, Low T, Zinnanti W. Co-stimulation and counter-stimulation: lipid raft clustering controls TCR signaling and functional outcomes. Semin Immunol 2001; 13(2): 115-28.
    • (2001) Semin. Immunol. , vol.13 , Issue.2 , pp. 115-128
    • Miceli, M.C.1    Moran, M.2    Chung, C.D.3    Patel, V.P.4    Low, T.5    Zinnanti, W.6
  • 53
    • 0035028703 scopus 로고    scopus 로고
    • Floating the raft hypothesis: The roles of lipid rafts in B cell antigen receptor function
    • Cheng PC, Cherukuri A, Dykstra M, Malapati S, Sproul T, Chen MR, et al. Floating the raft hypothesis: the roles of lipid rafts in B cell antigen receptor function. Semin Immunol 2001; 13(2): 107-14.
    • (2001) Semin. Immunol. , vol.13 , Issue.2 , pp. 107-114
    • Cheng, P.C.1    Cherukuri, A.2    Dykstra, M.3    Malapati, S.4    Sproul, T.5    Chen, M.R.6
  • 54
    • 0036789937 scopus 로고    scopus 로고
    • Myristoylation as a target for inhibiting HIV assembly: Unsaturated fatty acids block viral budding
    • Lindwasser OW, Resh MD. Myristoylation as a target for inhibiting HIV assembly: unsaturated fatty acids block viral budding. Proc Natl Acad Sci USA 2002; 99(20): 13037-42.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.20 , pp. 13037-13042
    • Lindwasser, O.W.1    Resh, M.D.2
  • 56
    • 0036133095 scopus 로고    scopus 로고
    • Chimeric Human Immunodeficiency Virus Type 1 Containing Murine Leukemia Virus Matrix Assembles in Murine Cells
    • Reed M, Mariani R, Sheppard L, Pekrun K, Landau NR, Soong NW. Chimeric Human Immunodeficiency Virus Type 1 Containing Murine Leukemia Virus Matrix Assembles in Murine Cells. J Virol 2002; 76(1): 436-443.
    • (2002) J. Virol. , vol.76 , Issue.1 , pp. 436-443
    • Reed, M.1    Mariani, R.2    Sheppard, L.3    Pekrun, K.4    Landau, N.R.5    Soong, N.W.6
  • 57
    • 0035910077 scopus 로고    scopus 로고
    • Efficient assembly of an HIV-1/MLV Gag-chimeric virus in murine cells
    • Chen BK, Rousso I, Shim S, Kim PS. Efficient assembly of an HIV-1/MLV Gag-chimeric virus in murine cells. Proc Natl Acad Sci USA 2001; 98(26): 15239-44.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.26 , pp. 15239-15244
    • Chen, B.K.1    Rousso, I.2    Shim, S.3    Kim, P.S.4
  • 58
    • 0033027711 scopus 로고    scopus 로고
    • In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain
    • Campbell S, Rein A. In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain. J Virol 1999; 73(3): 2270-9.
    • (1999) J. Virol. , vol.73 , Issue.3 , pp. 2270-2279
    • Campbell, S.1    Rein, A.2
  • 59
    • 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. 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 1999; 73(10): 8527-40.
    • (1999) J. Virol. , vol.73 , Issue.10 , pp. 8527-8540
    • Burniston, M.T.1    Cimarelli, A.2    Colgan, J.3    Curtis, S.P.4    Luban, J.5
  • 60
    • 0031870255 scopus 로고    scopus 로고
    • Detection of a trimeric human immunodeficiency virus type 1 Gag intermediate is dependent on sequences in the matrix protein, p17
    • Morikawa Y, Zhang WH, Hockley DJ, Nermut MV, Jones IM. Detection of a trimeric human immunodeficiency virus type 1 Gag intermediate is dependent on sequences in the matrix protein, p17. J Virol 1998; 72(9): 7659-63
    • (1998) J. Virol. , vol.72 , Issue.9 , pp. 7659-7663
    • Morikawa, Y.1    Zhang, W.H.2    Hockley, D.J.3    Nermut, M.V.4    Jones, I.M.5
  • 61
    • 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. Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly. Proc Natl Acad Sci USA 1996; 93(7): 3099-104.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , Issue.7 , pp. 3099-3104
    • Hill, C.P.1    Worthylake, D.2    Bancroft, D.P.3    Christensen, A.M.4    Sundquist, W.I.5
  • 62
    • 0034685614 scopus 로고    scopus 로고
    • Molecular modelling study of HIV p17gag (MA) protein shell utilising data from electron microscopy and X-ray crystallography
    • Forster MJ, Mulloy B, Nermut MV. Molecular modelling study of HIV p17gag (MA) protein shell utilising data from electron microscopy and X-ray crystallography. J Mol Biol 2000; 298(5): 841-57.
    • (2000) J. Mol. Biol. , vol.298 , Issue.5 , pp. 841-857
    • Forster, M.J.1    Mulloy, B.2    Nermut, M.V.3
  • 63
    • 0032970528 scopus 로고    scopus 로고
    • Formation and release of viruslike particles by HIV-1 matrix protein
    • Wang JJ, Horton R, Varthakavi V, Spearman P, Ratner L. Formation and release of viruslike particles by HIV-1 matrix protein. AIDS 1999; 13(2): 281-3.
    • (1999) AIDS , vol.13 , Issue.2 , pp. 281-283
    • Wang, J.J.1    Horton, R.2    Varthakavi, V.3    Spearman, P.4    Ratner, L.5
  • 64
    • 0032079344 scopus 로고    scopus 로고
    • Efficient HIV-1 replication can occur in the absence of the viral matrix protein
    • Reil H, Bukovsky AA, Gelderblom HR, Gottlinger HG. Efficient HIV-1 replication can occur in the absence of the viral matrix protein. EMBO J 1998; 17(9): 2699-708.
    • (1998) EMBO J. , vol.17 , Issue.9 , pp. 2699-2708
    • Reil, H.1    Bukovsky, A.A.2    Gelderblom, H.R.3    Gottlinger, H.G.4
  • 65
    • 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. 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 2000; 74(12): 5395-402.
    • (2000) J. Virol. , vol.74 , Issue.12 , pp. 5395-5402
    • Accola, M.A.1    Strack, B.2    Gottlinger, H.G.3
  • 66
    • 0031680643 scopus 로고    scopus 로고
    • The C-terminal half of the human immunodeficiency virus type 1 Gag precursor is sufficient for efficient particle assembly
    • Borsetti A, Ohagen A, Gottlinger HG. The C-terminal half of the human immunodeficiency virus type 1 Gag precursor is sufficient for efficient particle assembly. J Virol 1998; 72(11): 9313-7.
    • (1998) J. Virol. , vol.72 , Issue.11 , pp. 9313-9317
    • Borsetti, A.1    Ohagen, A.2    Gottlinger, H.G.3
  • 67
    • 0032930797 scopus 로고    scopus 로고
    • Assembly and analysis of conical models for the HIV-1 core
    • Ganser BK, Li S, Klishko VY, Finch JT, Sundquist WI. Assembly and analysis of conical models for the HIV-1 core. Science 1999; 283(5398): 80-3.
    • (1999) Science , vol.283 , Issue.5398 , pp. 80-83
    • Ganser, B.K.1    Li, S.2    Klishko, V.Y.3    Finch, J.T.4    Sundquist, W.I.5
  • 69
    • 0032536896 scopus 로고    scopus 로고
    • Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly
    • von Schwedler UK, Stemmler TL, Klishko VY, Li S, Albertine KH, Davis DR, et al. Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly. EMBO J 1998; 17(6): 1555-68.
    • (1998) EMBO J. , vol.17 , Issue.6 , pp. 1555-1568
    • von Schwedler, U.K.1    Stemmler, T.L.2    Klishko, V.Y.3    Li, S.4    Albertine, K.H.5    Davis, D.R.6
  • 71
    • 0026762403 scopus 로고
    • Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro
    • Ehrlich LS, Agresta BE, Carter CA. Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro. J Virol 1992; 66(8): 4874-83.
    • (1992) J. Virol. , vol.66 , Issue.8 , pp. 4874-4883
    • Ehrlich, L.S.1    Agresta, B.E.2    Carter, C.A.3
  • 72
    • 0034950321 scopus 로고    scopus 로고
    • HIV-1 capsid protein forms spherical (immature-like) and tubular (mature-like) particles in vitro: Structure switching by pH-induced conformational changes
    • Ehrlich LS, Liu T, Scarlata S, Chu B, Carter CA. HIV-1 capsid protein forms spherical (immature-like) and tubular (mature-like) particles in vitro: structure switching by pH-induced conformational changes. Biophys J 2001; 81(1): 586-94.
    • (2001) Biophys. J. , vol.81 , Issue.1 , pp. 586-594
    • Ehrlich, L.S.1    Liu, T.2    Scarlata, S.3    Chu, B.4    Carter, C.A.5
  • 73
    • 0029794123 scopus 로고    scopus 로고
    • Structure of the aminoterminal core domain of the HIV-1 capsid protein
    • Gitti RK, Lee BM, Walker J, Summers MY, Yoo S, Sundquist WI. Structure of the aminoterminal core domain of the HIV-1 capsid protein. Science 1996; 273(5272): 231-5.
    • (1996) Science , vol.273 , Issue.5272 , pp. 231-235
    • Gitti, R.K.1    Lee, B.M.2    Walker, J.3    Summers, M.Y.4    Yoo, S.5    Sundquist, W.I.6
  • 74
    • 0030693391 scopus 로고    scopus 로고
    • Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
    • Gamble TR, You S, Vajdos FF, von Schwedler UK, Worthylake DK, Wang H, et al. Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein. Science 1997; 278(5339): 849-53.
    • (1997) Science , vol.278 , Issue.5339 , pp. 849-853
    • Gamble, T.R.1    You, S.2    Vajdos, F.F.3    von Schwedler, U.K.4    Worthylake, D.K.5    Wang, H.6
  • 76
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • Li S, Hill CP, Sundquist WI, Finch JT. Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature 2000; 407(6802): 409-13.
    • (2000) Nature , vol.407 , Issue.6802 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 77
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • Li S, Hill CP, Sundquist WI, Finch JT. Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature 2000; 407(6802): 409-13.
    • (2000) Nature , vol.407 , Issue.6802 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 78
    • 0034855639 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells
    • Tang S, Murakami T, Agresta BE, Campbell S, Freed EO, Levin JG. Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells. J Virol 2001; 75(19): 9357-66.
    • (2001) J. Virol. , vol.75 , Issue.19 , pp. 9357-9366
    • Tang, S.1    Murakami, T.2    Agresta, B.E.3    Campbell, S.4    Freed, E.O.5    Levin, J.G.6
  • 79
    • 0037404501 scopus 로고    scopus 로고
    • Functional surfaces of the human immunodeficiency virus type 1 capsid protein
    • von Schwedler UK, Stray KM, Garrus JE, Sundquist WI. Functional surfaces of the human immunodeficiency virus type 1 capsid protein. J Virol 2003; 77(9): 5439-50.
    • (2003) J. Virol. , vol.77 , Issue.9 , pp. 5439-5450
    • von Schwedler, U.K.1    Stray, K.M.2    Garrus, J.E.3    Sundquist, W.I.4
  • 80
    • 0027997831 scopus 로고
    • Functional domains of the capsid protein of human immunodeficiency virus type 1
    • Dorfman T, Bukovsky A, Ohagen A, Hoglund S, Gottlinger HG. Functional domains of the capsid protein of human immunodeficiency virus type 1. J Virol 1994; 68(12): 8180-7.
    • (1994) J. Virol. , vol.68 , Issue.12 , pp. 8180-8187
    • Dorfman, T.1    Bukovsky, A.2    Ohagen, A.3    Hoglund, S.4    Gottlinger, H.G.5
  • 81
    • 0027335896 scopus 로고
    • Identification of a region in the Pr55gag-polyprotein essential for HIV- 1 particle formation
    • von Poblotzki A, Wagner R, Niedrig M, Wanner G, Wolf H, Modrow S. Identification of a region in the Pr55gag-polyprotein essential for HIV- 1 particle formation. Virology 1993; 193(2): 981-5.
    • (1993) Virology , vol.193 , Issue.2 , pp. 981-985
    • von Poblotzki, A.1    Wagner, R.2    Niedrig, M.3    Wanner, G.4    Wolf, H.5    Modrow, S.6
  • 82
    • 0028873674 scopus 로고
    • Linker insertion mutations in the human immunodeficiency virus type 1 gag gene effects on virion particle assembly, release, and infectivity
    • Reicin AS, Paik S, Berkowitz RD, Luban J, Lowy I, Goff SP. Linker insertion mutations in the human immunodeficiency virus type 1 gag gene effects on virion particle assembly, release, and infectivity. J Virol 1995; 69(2): 642-50.
    • (1995) J. Virol. , vol.69 , Issue.2 , pp. 642-650
    • Reicin, A.S.1    Paik, S.2    Berkowitz, R.D.3    Luban, J.4    Lowy, I.5    Goff, S.P.6
  • 83
    • 0029130067 scopus 로고
    • Characterization of deletion mutations in the capsid region of human immunodeficiency virus type 1 that affect particle formation and Gag-Pol precursor incorporation
    • Srinivasakumar N, Hammarskjold ML, Rekosh D. Characterization of deletion mutations in the capsid region of human immunodeficiency virus type 1 that affect particle formation and Gag-Pol precursor incorporation. J Virol 1995; 69(10): 6106-14.
    • (1995) J. Virol. , vol.69 , Issue.10 , pp. 6106-6114
    • Srinivasakumar, N.1    Hammarskjold, M.L.2    Rekosh, D.3
  • 84
    • 0028342554 scopus 로고
    • Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis
    • Mammano F, Ohagen A, Hoglund S, Gottlinger HG. Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis. J Virol 1994; 69(8): 4927-36.
    • (1994) J. Virol. , vol.69 , Issue.8 , pp. 4927-4936
    • Mammano, F.1    Ohagen, A.2    Hoglund, S.3    Gottlinger, H.G.4
  • 85
    • 0031679786 scopus 로고    scopus 로고
    • Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: Significance for viral replication
    • Rein A, Henderson LE, Levin JG. Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: significance for viral replication. Trends Biochem Sci 1998; 23(8): 297-301.
    • (1998) Trends Biochem. Sci. , vol.23 , Issue.8 , pp. 297-301
    • Rein, A.1    Henderson, L.E.2    Levin, J.G.3
  • 86
    • 0034565966 scopus 로고    scopus 로고
    • Nucleocapsid protein of human immunodeficiency virus as a model protein with chaperoning functions and as a target for antiviral drugs
    • Darlix JL, Cristofari G, Rau M, Pechoux C, Berthoux L, Roques B. Nucleocapsid protein of human immunodeficiency virus as a model protein with chaperoning functions and as a target for antiviral drugs. Adv Pharmacol 2000; 48: 345-72.
    • (2000) Adv. Pharmacol. , vol.48 , pp. 345-372
    • Darlix, J.L.1    Cristofari, G.2    Rau, M.3    Pechoux, C.4    Berthoux, L.5    Roques, B.6
  • 88
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 gag proteins: Diverse functions in the virus life cycle
    • Freed EO. HIV-1 gag proteins: diverse functions in the virus life cycle. Virology 1998; 251(1): 1-15.
    • (1998) Virology , vol.251 , Issue.1 , pp. 1-15
    • Freed, E.O.1
  • 89
    • 0034636984 scopus 로고    scopus 로고
    • NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the psi-RNA packaging signal. Implications for genome recognition
    • Amarasinghe GK, De Guzman RN, Turner RB, Chancellor KJ, Wu ZR, Summers MF. NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the psi-RNA packaging signal. Implications for genome recognition. J Mol Biol 2000; 301(2): 491-511.
    • (2000) J. Mol. Biol. , vol.301 , Issue.2 , pp. 491-511
    • Amarasinghe, G.K.1    De Guzman, R.N.2    Turner, R.B.3    Chancellor, K.J.4    Wu, Z.R.5    Summers, M.F.6
  • 90
    • 0033609448 scopus 로고    scopus 로고
    • Structural investigation on the requirement of CCHH zinc finger type in nucleocapsid protein of human immunodeficiency virus 1
    • Ramboarina S, Morellet N, Fournie-Zaluski MC, Roques BP, Morellet N. Structural investigation on the requirement of CCHH zinc finger type in nucleocapsid protein of human immunodeficiency virus 1. Biochemistry 1999; 38(30): 9600-7.
    • (1999) Biochemistry , vol.38 , Issue.30 , pp. 9600-9607
    • Ramboarina, S.1    Morellet, N.2    Fournie-Zaluski, M.C.3    Roques, B.P.4    Morellet, N.5
  • 91
    • 0141846926 scopus 로고    scopus 로고
    • Encapsidation and transduction of cellular genes by retroviruses
    • Muriaux D, Rein A. Encapsidation and transduction of cellular genes by retroviruses. Front Biosci 2003; 8: d135-42.
    • (2003) Front. Biosci. , vol.8
    • Muriaux, D.1    Rein, A.2
  • 92
    • 0034108444 scopus 로고    scopus 로고
    • Relationship between human immunodeficiency virus type 1 Gag multimerization and membrane binding
    • Ono A, Demirov D, Freed EO. Relationship between human immunodeficiency virus type 1 Gag multimerization and membrane binding. J Virol 2000; 74(11): 5142-50.
    • (2000) J. Virol. , vol.74 , Issue.11 , pp. 5142-5150
    • Ono, A.1    Demirov, D.2    Freed, E.O.3
  • 93
    • 0028363103 scopus 로고
    • Specificity and sequence requirements for interactions between various retroviral Gag proteins
    • Franke EK, Yuan HE, Bossolt KL, Goff SP, Luban J. Specificity and sequence requirements for interactions between various retroviral Gag proteins. J Virol 1994; 68(8): 5300-5.
    • (1994) J. Virol. , vol.68 , Issue.8 , pp. 5300-5305
    • Franke, E.K.1    Yuan, H.E.2    Bossolt, K.L.3    Goff, S.P.4    Luban, J.5
  • 94
    • 0033941571 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 virion density is not determined by nucleocapsid basic residues
    • Cimarelli A, Luban J. Human immunodeficiency virus type 1 virion density is not determined by nucleocapsid basic residues. J Virol 2000; 74(15): 6734-40.
    • (2000) J. Virol. , vol.74 , Issue.15 , pp. 6734-6740
    • Cimarelli, A.1    Luban, J.2
  • 95
    • 0027101766 scopus 로고
    • Distinct signals in human immunodeficiency virus type 1 Pr55 necessary for RNA binding and particle formation
    • Jowett JB, Hockley DJ, Nermut MV, Jones IM. Distinct signals in human immunodeficiency virus type 1 Pr55 necessary for RNA binding and particle formation. J Gen Virol 1992; 73(Pt 12): 3079-86.
    • (1992) J. Gen. Virol. , vol.73 , Issue.PART 12 , pp. 3079-3086
    • Jowett, J.B.1    Hockley, D.J.2    Nermut, M.V.3    Jones, I.M.4
  • 96
    • 0032506295 scopus 로고    scopus 로고
    • The role of nucleocapsid of HIV-1 in virus assembly
    • Dawson L, Yu XF. The role of nucleocapsid of HIV-1 in virus assembly. Virology 1998; 251(1): 141-57.
    • (1998) Virology , vol.251 , Issue.1 , pp. 141-157
    • Dawson, L.1    Yu, X.F.2
  • 97
    • 0028916064 scopus 로고
    • Sequence requirements for encapsidation of deletion mutants and chimeras of human immunodeficiency virus type 1 Gag precursor into retrovirus-like particles
    • Carriere C, Gay B, Chazal N, Morin N, Boulanger P. Sequence requirements for encapsidation of deletion mutants and chimeras of human immunodeficiency virus type 1 Gag precursor into retrovirus-like particles. J Virol 1995; 69(4): 2366-77.
    • (1995) J. Virol. , vol.69 , Issue.4 , pp. 2366-2377
    • Carriere, C.1    Gay, B.2    Chazal, N.3    Morin, N.4    Boulanger, P.5
  • 98
    • 0034011267 scopus 로고    scopus 로고
    • Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA
    • Cimarelli A, Sandin S, Hoglund S, Luban J. Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA. J Virol 2000; 74(7): 3046-57.
    • (2000) J. Virol. , vol.74 , Issue.7 , pp. 3046-3057
    • Cimarelli, A.1    Sandin, S.2    Hoglund, S.3    Luban, J.4
  • 99
    • 0030028806 scopus 로고    scopus 로고
    • Mutations of basic amino acids of NCp7 of human immunodeficiency virus type 1 affect RNA binding in vitro
    • Schmalzbauer E, Strack B, Dannull J, Guehmann S, Moelling K. Mutations of basic amino acids of NCp7 of human immunodeficiency virus type 1 affect RNA binding in vitro. J Virol 1996; 70(2): 771-7.
    • (1996) J. Virol. , vol.70 , Issue.2 , pp. 771-777
    • Schmalzbauer, E.1    Strack, B.2    Dannull, J.3    Guehmann, S.4    Moelling, K.5
  • 100
    • 0036889123 scopus 로고    scopus 로고
    • RNA incorporation is critical for retroviral particle integrity after cell membrane assembly of Gag complexes
    • Wang SW, Aldovini A. RNA incorporation is critical for retroviral particle integrity after cell membrane assembly of Gag complexes. J Virol 2002; 76(23): 11853-65.
    • (2002) J. Virol. , vol.76 , Issue.23 , pp. 11853-11865
    • Wang, S.W.1    Aldovini, A.2
  • 101
    • 0030795040 scopus 로고    scopus 로고
    • Effects of nucleocapsid mutations on human immunodeficiency virus assembly and RNA encapsidation
    • Zhang Y, Barklis E. Effects of nucleocapsid mutations on human immunodeficiency virus assembly and RNA encapsidation. J Virol 1997; 71(9): 6765-76.
    • (1997) J. Virol. , vol.71 , Issue.9 , pp. 6765-6776
    • Zhang, Y.1    Barklis, E.2
  • 102
    • 0031910808 scopus 로고    scopus 로고
    • Analysis of the assembly function of the human immunodeficiency virus type 1 gag protein nucleocapsid domain
    • Zhang Y, Qian H, Love Z, Barklis E. Analysis of the assembly function of the human immunodeficiency virus type 1 gag protein nucleocapsid domain. J Virol 1998; 72(3): 1782-9.
    • (1998) J. Virol. , vol.72 , Issue.3 , pp. 1782-1789
    • Zhang, Y.1    Qian, H.2    Love, Z.3    Barklis, E.4
  • 103
    • 0031106649 scopus 로고    scopus 로고
    • Ordered aggregation of ribonucleic acids by the human immunodeficiency virus type 1 nucleocapsid protein
    • Stoylov SP, Vuilleumier C, Stoylova E, De Rocquigny H, Roques BP, Gerard D, et al. Ordered aggregation of ribonucleic acids by the human immunodeficiency virus type 1 nucleocapsid protein. Biopolymers 1997; 41(3): 301-12.
    • (1997) Biopolymers , vol.41 , Issue.3 , pp. 301-312
    • Stoylov, S.P.1    Vuilleumier, C.2    Stoylova, E.3    De Rocquigny, H.4    Roques, B.P.5    Gerard, D.6
  • 104
    • 0029121697 scopus 로고
    • Formation of stable and functional HIV-1 nucleoprotein complexes in vitro
    • Tanchou V, Gabus C, Rogemond V, Darlix JL. Formation of stable and functional HIV-1 nucleoprotein complexes in vitro. J Mol Biol 1995; 252(5): 563-71.
    • (1995) J. Mol. Biol. , vol.252 , Issue.5 , pp. 563-571
    • Tanchou, V.1    Gabus, C.2    Rogemond, V.3    Darlix, J.L.4
  • 106
    • 0027197020 scopus 로고
    • The two zinc fingers in the human immunodeficiency virus type 1 nucleocapsid protein are not functionally equivalent
    • Gorelick RJ, Chabot DJ, Rein A, Henderson LE, Arthur LO. The two zinc fingers in the human immunodeficiency virus type 1 nucleocapsid protein are not functionally equivalent. J Virol 1993; 67(7): 4027-36.
    • (1993) J. Virol. , vol.67 , Issue.7 , pp. 4027-4036
    • Gorelick, R.J.1    Chabot, D.J.2    Rein, A.3    Henderson, L.E.4    Arthur, L.O.5
  • 108
    • 0027220120 scopus 로고
    • Mapping of functionally important residues of a cysteine-histidine box in the human immunodeficiency virus type 1 nucleocapsid protein
    • Dorfman T, Luban J, Goff SP, Haseltine WA, Gottlinger HG. Mapping of functionally important residues of a cysteine-histidine box in the human immunodeficiency virus type 1 nucleocapsid protein. J Virol 1993; 67(10): 6159-69.
    • (1993) J. Virol. , vol.67 , Issue.10 , pp. 6159-6169
    • Dorfman, T.1    Luban, J.2    Goff, S.P.3    Haseltine, W.A.4    Gottlinger, H.G.5
  • 109
    • 0031547959 scopus 로고    scopus 로고
    • Possible roles of HIV-1 nucleocapsid protein in the specificity of proviral DNA synthesis and in its variability
    • Lapadat-Tapolsky M, Gabus C, Rau M, Darlix JL. Possible roles of HIV-1 nucleocapsid protein in the specificity of proviral DNA synthesis and in its variability. J Mol Biol 1997; 268(2): 250-60.
    • (1997) J. Mol. Biol. , vol.268 , Issue.2 , pp. 250-260
    • Lapadat-Tapolsky, M.1    Gabus, C.2    Rau, M.3    Darlix, J.L.4
  • 110
    • 0031956156 scopus 로고    scopus 로고
    • Role of the N-terminal zinc finger of human immunodeficiency virus type 1 nucleocapsid protein in virus structure and replication
    • Tanchou V, Decimo D, Pechoux C, Lener D, Rogemond V, Berthoux L, et al. Role of the N-terminal zinc finger of human immunodeficiency virus type 1 nucleocapsid protein in virus structure and replication. J Virol 1998; 72(5): 4442-7.
    • (1998) J. Virol. , vol.72 , Issue.5 , pp. 4442-4447
    • Tanchou, V.1    Decimo, D.2    Pechoux, C.3    Lener, D.4    Rogemond, V.5    Berthoux, L.6
  • 111
    • 0034003379 scopus 로고    scopus 로고
    • Rescue of multiple viral functions by a second-site suppressor of a human immunodeficiency virus type 1 nucleocapsid mutation
    • Cimarelli A, Sandin S, Hoglund S, Luban J. Rescue of multiple viral functions by a second-site suppressor of a human immunodeficiency virus type 1 nucleocapsid mutation. J Virol 2000; 74(9): 4273-83.
    • (2000) J. Virol. , vol.74 , Issue.9 , pp. 4273-4283
    • Cimarelli, A.1    Sandin, S.2    Hoglund, S.3    Luban, J.4
  • 112
    • 0038630512 scopus 로고    scopus 로고
    • Analysis of NCp7- dependent activation of HIV-1 cDNA integration and its conservation among retroviral nucleocapsid proteins
    • Poljak L, Batson SM, Ficheux D, Roques BP, Darlix JL, Kas E. Analysis of NCp7- dependent activation of HIV-1 cDNA integration and its conservation among retroviral nucleocapsid proteins. J Mol Biol 2003; 329(3): 411-21.
    • (2003) J. Mol. Biol. , vol.329 , Issue.3 , pp. 411-421
    • Poljak, L.1    Batson, S.M.2    Ficheux, D.3    Roques, B.P.4    Darlix, J.L.5    Kas, E.6
  • 113
    • 0037227942 scopus 로고    scopus 로고
    • Cofactors for human immunodeficiency virus type 1 cDNA integration in vitro
    • Gao K, Gorelick RJ, Johnson DG, Bushman F. Cofactors for human immunodeficiency virus type 1 cDNA integration in vitro. J Virol 2003; 77(2): 1598-603.
    • (2003) J. Virol. , vol.77 , Issue.2 , pp. 1598-1603
    • Gao, K.1    Gorelick, R.J.2    Johnson, D.G.3    Bushman, F.4
  • 114
    • 0030740070 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nucleocapsid protein specifically stimulates Mg2+-dependent DNA integration in vitro
    • Carteau S, Batson SC, Poljak L, Mouscadet JF, de Rocquigny H, Darlix JL, et al. Human immunodeficiency virus type 1 nucleocapsid protein specifically stimulates Mg2+-dependent DNA integration in vitro. J Virol 1997; 71(8): 6225-9.
    • (1997) J. Virol. , vol.71 , Issue.8 , pp. 6225-6229
    • Carteau, S.1    Batson, S.C.2    Poljak, L.3    Mouscadet, J.F.4    de Rocquigny, H.5    Darlix, J.L.6
  • 115
    • 0032776165 scopus 로고    scopus 로고
    • Coupled integration of human immunodeficiency virus type 1 cDNA ends by purified integrase in vitro: Stimulation by the viral nucleocapsid protein
    • Carteau S, Gorelick RJ, Bushman FD. Coupled integration of human immunodeficiency virus type 1 cDNA ends by purified integrase in vitro: stimulation by the viral nucleocapsid protein. J Virol 1999; 73(8): 6670-9.
    • (1999) J. Virol. , vol.73 , Issue.8 , pp. 6670-6679
    • Carteau, S.1    Gorelick, R.J.2    Bushman, F.D.3
  • 116
  • 117
    • 0344671562 scopus 로고    scopus 로고
    • Multiple effects of an anti-human immunodeficiency virus nucleocapsid inhibitor on virus morphology and replication
    • Berthoux L, Pechoux C, Darlix JL. Multiple effects of an anti-human immunodeficiency virus nucleocapsid inhibitor on virus morphology and replication. J Virol 1999; 73(12): 10000-9.
    • (1999) J. Virol. , vol.73 , Issue.12 , pp. 10000-10009
    • Berthoux, L.1    Pechoux, C.2    Darlix, J.L.3
  • 118
    • 0029791790 scopus 로고    scopus 로고
    • Inhibitors of human immunodeficiency virus type 1 zinc fingers prevent normal processing of gag precursors and result in the release of noninfectious virus particles
    • Turpin JA, Terpening SJ, Schaeffer CA, Yu G, Glover CJ, Felsted RL, et al. Inhibitors of human immunodeficiency virus type 1 zinc fingers prevent normal processing of gag precursors and result in the release of noninfectious virus particles. J Virol 1996; 70(9): 6180-9.
    • (1996) J. Virol. , vol.70 , Issue.9 , pp. 6180-6189
    • Turpin, J.A.1    Terpening, S.J.2    Schaeffer, C.A.3    Yu, G.4    Glover, C.J.5    Felsted, R.L.6
  • 119
  • 120
    • 0031046754 scopus 로고    scopus 로고
    • SRR-SB3, a disulfide-containing macrolide that inhibits a late stage of the replicative cycle of human immunodeficiency virus
    • Witvrouw M, Balzarini J, Pannecouque C, Jhaumeer-Laulloo S, Este JA, Schols D, et al. SRR-SB3, a disulfide-containing macrolide that inhibits a late stage of the replicative cycle of human immunodeficiency virus. Antimicrob Agents Chemother 1997; 41(2): 262-8.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , Issue.2 , pp. 262-268
    • Witvrouw, M.1    Balzarini, J.2    Pannecouque, C.3    Jhaumeer-Laulloo, S.4    Este, J.A.5    Schols, D.6
  • 121
    • 0031050622 scopus 로고    scopus 로고
    • Inhibition of multiple phases of human immunodeficiency virus type 1 replication by a dithiane compound that attacks the conserved zinc fingers of retroviral nucleocapsid proteins
    • Rice WG, Baker DC, Schaeffer CA, Graham L, Bu M, Terpening S, et al. Inhibition of multiple phases of human immunodeficiency virus type 1 replication by a dithiane compound that attacks the conserved zinc fingers of retroviral nucleocapsid proteins. Antimicrob Agents Chemother 1997; 41(2): 419-26.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , Issue.2 , pp. 419-426
    • Rice, W.G.1    Baker, D.C.2    Schaeffer, C.A.3    Graham, L.4    Bu, M.5    Terpening, S.6
  • 122
    • 0032560189 scopus 로고    scopus 로고
    • Anti-HIV agents that selectively target retroviral nucleocapsid protein zinc fingers without affecting cellular zinc finger proteins
    • Huang M, Maynard A, Turpin JA, Graham L, Janini GM, Covell DG, et al. Anti-HIV agents that selectively target retroviral nucleocapsid protein zinc fingers without affecting cellular zinc finger proteins. J Med Chem 1998; 41(9): 1371-81.
    • (1998) J. Med. Chem. , vol.41 , Issue.9 , pp. 1371-1381
    • Huang, M.1    Maynard, A.2    Turpin, J.A.3    Graham, L.4    Janini, G.M.5    Covell, D.G.6
  • 123
  • 125
    • 0027523471 scopus 로고
    • Inhibition of HIV-1 infectivity by zinc-ejecting aromatic C-nitroso compounds
    • Rice WG, Schaeffer CA, Harten B, Villinger F, South TL, Summers MF, et al. Inhibition of HIV-1 infectivity by zinc-ejecting aromatic C-nitroso compounds. Nature 1993; 361(6411): 473-5.
    • (1993) Nature , vol.361 , Issue.6411 , pp. 473-475
    • Rice, W.G.1    Schaeffer, C.A.2    Harten, B.3    Villinger, F.4    South, T.L.5    Summers, M.F.6
  • 126
    • 0030013723 scopus 로고    scopus 로고
    • Inactivation of murine leukemia virus by compounds that react with the zinc finger in the viral nucleocapsid protein
    • Rein A, Ott DE, Mirro J, Arthur LO, Rice W, Henderson LE. Inactivation of murine leukemia virus by compounds that react with the zinc finger in the viral nucleocapsid protein. J Virol 1996; 70(8): 4966-72.
    • (1996) J. Virol. , vol.70 , Issue.8 , pp. 4966-4972
    • Rein, A.1    Ott, D.E.2    Mirro, J.3    Arthur, L.O.4    Rice, W.5    Henderson, L.E.6
  • 127
    • 0034685755 scopus 로고    scopus 로고
    • Inactivation of HIV-1 nucleocapsid protein P7 by pyridinioalkanoyl thioesters. Characterization of reaction products and proposed mechanism of action
    • Basrur V, Song Y, Mazur SJ, Higashimoto Y, Turpin JA, Rice WG, et al. Inactivation of HIV-1 nucleocapsid protein P7 by pyridinioalkanoyl thioesters. Characterization of reaction products and proposed mechanism of action. J Biol Chem 2000; 275(20): 14890-7.
    • (2000) J. Biol. Chem. , vol.275 , Issue.20 , pp. 14890-14897
    • Basrur, V.1    Song, Y.2    Mazur, S.J.3    Higashimoto, Y.4    Turpin, J.A.5    Rice, W.G.6
  • 128
    • 0030738085 scopus 로고    scopus 로고
    • Determinants of the human immunodeficiency virus type 1 p15NC-RNA interaction that affect enhanced cleavage by the viral protease
    • Sheng N, Pettit SC, Tritch RJ, Ozturk DH, Rayner MM, Swanstrom R, et al. Determinants of the human immunodeficiency virus type 1 p15NC-RNA interaction that affect enhanced cleavage by the viral protease. J Virol 1997; 71(8): 5723-32.
    • (1997) J. Virol. , vol.71 , Issue.8 , pp. 5723-5732
    • Sheng, N.1    Pettit, S.C.2    Tritch, R.J.3    Ozturk, D.H.4    Rayner, M.M.5    Swanstrom, R.6
  • 129
    • 0035808584 scopus 로고    scopus 로고
    • Phase I/II dose escalation and randomized withdrawal study with add-on azodicarbonamide in patients failing on current antiretroviral therapy
    • Goebel FD, Hemmer R, Schmit JC, Bogner JR, de Clercq E, Witvrouw M, et al. Phase I/II dose escalation and randomized withdrawal study with add-on azodicarbonamide in patients failing on current antiretroviral therapy. Aids 2001; 15(1): 33-45.
    • (2001) Aids , vol.15 , Issue.1 , pp. 33-45
    • Goebel, F.D.1    Hemmer, R.2    Schmit, J.C.3    Bogner, J.R.4    de Clercq, E.5    Witvrouw, M.6
  • 130
    • 0034972460 scopus 로고    scopus 로고
    • Azodicarbonamide as a new T cell immunosuppressant: Synergy with cyclosporin A
    • Tassignon J, Vandevelde M, Goldman M. Azodicarbonamide as a new T cell immunosuppressant: synergy with cyclosporin A. Clin Immunol 2001; 100(1): 24-30.
    • (2001) Clin. Immunol. , vol.100 , Issue.1 , pp. 24-30
    • Tassignon, J.1    Vandevelde, M.2    Goldman, M.3
  • 132
  • 135
    • 0032601402 scopus 로고    scopus 로고
    • HIV integrase structure and function
    • Esposito D, Craigie R. HIV integrase structure and function. Adv Virus Res 1999; 52: 319-33.
    • (1999) Adv. Virus Res. , vol.52 , pp. 319-333
    • Esposito, D.1    Craigie, R.2
  • 136
    • 0024412506 scopus 로고
    • Conserved folding in retroviral proteases: Crystal structure of a synthetic HIV-1 protease
    • Wlodawer A, Miller M, Jaskolski M, Sathyanarayana BK, Baldwin E, Weber IT, et al. Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease. Science 1989; 245(4918): 616-21.
    • (1989) Science , vol.245 , Issue.4918 , pp. 616-621
    • Wlodawer, A.1    Miller, M.2    Jaskolski, M.3    Sathyanarayana, B.K.4    Baldwin, E.5    Weber, I.T.6
  • 137
    • 0024555898 scopus 로고
    • Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1
    • Navia MA, Fitzgerald PM, McKeever BM, Leu CT, Heimbach JC, Herber WK, et al. Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1. Nature 1989; 337(6208): 615-20.
    • (1989) Nature , vol.337 , Issue.6208 , pp. 615-620
    • Navia, M.A.1    Fitzgerald, P.M.2    McKeever, B.M.3    Leu, C.T.4    Heimbach, J.C.5    Herber, W.K.6
  • 139
    • 0028079067 scopus 로고
    • 2.2 A resolution structure of the amino-terminal half of HIV-1 reverse transcriptase (fingers and palm subdomains)
    • Unge T, Knight S, Bhikhabhai R, Lovgren S, Dauter Z, Wilson K, et al. 2.2 A resolution structure of the amino-terminal half of HIV-1 reverse transcriptase (fingers and palm subdomains). Structure 1994; 2(10): 953-61.
    • (1994) Structure , vol.2 , Issue.10 , pp. 953-961
    • Unge, T.1    Knight, S.2    Bhikhabhai, R.3    Lovgren, S.4    Dauter, Z.5    Wilson, K.6
  • 140
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt LA, Wang J, Friedman JM, Rice PA, Steitz TA. Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science 1992; 256(5065): 1783-90.
    • (1992) Science , vol.256 , Issue.5065 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steitz, T.A.5
  • 141
    • 0026322839 scopus 로고
    • Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly and viral infectivity
    • Krausslich HG. Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly and viral infectivity. Proc Natl Acad Sci USA 1991; 88(8): 3213-7.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , Issue.8 , pp. 3213-3217
    • Krausslich, H.G.1
  • 142
    • 0035138477 scopus 로고    scopus 로고
    • Maintenance of the Gag/Gag-Pol ratio is important for human immunodeficiency virus type 1 RNA dimerization and viral infectivity
    • Shehu-Xhilaga M, Crewe SM, Mak J. Maintenance of the Gag/Gag-Pol ratio is important for human immunodeficiency virus type 1 RNA dimerization and viral infectivity. J Virol 2001; 75(4): 1834-41.
    • (2001) J. Virol. , vol.75 , Issue.4 , pp. 1834-1841
    • Shehu-Xhilaga, M.1    Crewe, S.M.2    Mak, J.3
  • 143
    • 0028821437 scopus 로고
    • Overexpression of human immunodeficiency virus type 1 protease increases intracellular cleavage of Gag and reduces virus infectivity
    • Luukkonen BG, Fenyo EM, Schwartz S. Overexpression of human immunodeficiency virus type 1 protease increases intracellular cleavage of Gag and reduces virus infectivity. Virology 1995; 206(2): 854-65.
    • (1995) Virology , vol.206 , Issue.2 , pp. 854-865
    • Luukkonen, B.G.1    Fenyo, E.M.2    Schwartz, S.3
  • 144
    • 0027214941 scopus 로고
    • Overexpression of the HIV- 1 gag-pol polyprotein results in intracellular activation of HIV-1 protease and inhibition of assembly and budding of virus-like particles
    • Karacostas V, Wolffe EJ, Nagashima K, Gonda MA, Moss B. Overexpression of the HIV- 1 gag-pol polyprotein results in intracellular activation of HIV-1 protease and inhibition of assembly and budding of virus-like particles. Virology 1993; 193(2): 661-71.
    • (1993) Virology , vol.193 , Issue.2 , pp. 661-671
    • Karacostas, V.1    Wolffe, E.J.2    Nagashima, K.3    Gonda, M.A.4    Moss, B.5
  • 145
    • 0036753937 scopus 로고    scopus 로고
    • Dimerization inhibitors of HIV-1 protease
    • Boggetto N, Reboud-Ravaux M. Dimerization inhibitors of HIV-1 protease. Biol Chem 2002; 383(9): 1321-4.
    • (2002) Biol. Chem. , vol.383 , Issue.9 , pp. 1321-1324
    • Boggetto, N.1    Reboud-Ravaux, M.2
  • 146
    • 0033609895 scopus 로고    scopus 로고
    • A new potent HIV-1 reverse transcriptase inhibitor. A synthetic peptide derived from the interface subunit domains
    • Morris MC, Robert-Hebmann V, Chaloin L, Mery J, Heitz F, Devaux C, et al. A new potent HIV-1 reverse transcriptase inhibitor. A synthetic peptide derived from the interface subunit domains. J Biol Chem 1999; 274(35): 24941-6.
    • (1999) J. Biol. Chem. , vol.274 , Issue.35 , pp. 24941-24946
    • Morris, M.C.1    Robert-Hebmann, V.2    Chaloin, L.3    Mery, J.4    Heitz, F.5    Devaux, C.6
  • 148
    • 0037463767 scopus 로고    scopus 로고
    • Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization
    • Zhao L, O'Reilly MK, Shultz MD, Chmielewski J. Interfacial peptide inhibitors of HIV-1 integrase activity and dimerization. Bioorg Med Chem Lett 2003; 13(6): 1175-7.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , Issue.6 , pp. 1175-1177
    • Zhao, L.1    O'Reilly, M.K.2    Shultz, M.D.3    Chmielewski, J.4
  • 149
    • 0035912717 scopus 로고    scopus 로고
    • Nonnucleoside reverse transcriptase inhibitors are chemical enhancers of dimerization of the HIV type 1 reverse transcriptase
    • Tachedjian G, Orlova M, Sarafianos SG, Arnold E, Goff SP. Nonnucleoside reverse transcriptase inhibitors are chemical enhancers of dimerization of the HIV type 1 reverse transcriptase. Proc Natl Acad Sci USA 2001; 98(13): 7188-93.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.13 , pp. 7188-7193
    • Tachedjian, G.1    Orlova, M.2    Sarafianos, S.G.3    Arnold, E.4    Goff, S.P.5
  • 150
    • 0036239363 scopus 로고    scopus 로고
    • Viral late domains
    • Freed EO. Viral late domains. J Virol 2002; 76(10): 4679-87.
    • (2002) J. Virol. , vol.76 , Issue.10 , pp. 4679-4687
    • Freed, E.O.1
  • 151
    • 0036133283 scopus 로고    scopus 로고
    • The late domain of human immunodeficiency virus type 1 p6 promotes virus release in a cell type-dependent manner
    • Demirov DG, Orenstein JM, Freed EO. The late domain of human immunodeficiency virus type 1 p6 promotes virus release in a cell type-dependent manner. J Virol 2002; 76(1): 105-17.
    • (2002) J. Virol. , vol.76 , Issue.1 , pp. 105-117
    • Demirov, D.G.1    Orenstein, J.M.2    Freed, E.O.3
  • 152
    • 0033854158 scopus 로고    scopus 로고
    • Infectivity of coloney murine leukemia virus defective in late assembly events is restored by late assembly domains of other retroviruses
    • Yuan B, Campbell S, Bacharach E, Rein A, Goff SP. Infectivity of coloney murine leukemia virus defective in late assembly events is restored by late assembly domains of other retroviruses. J Virol 2000; 74(16): 7250-60.
    • (2000) J. Virol. , vol.74 , Issue.16 , pp. 7250-7260
    • Yuan, B.1    Campbell, S.2    Bacharach, E.3    Rein, A.4    Goff, S.P.5
  • 153
    • 0029978648 scopus 로고    scopus 로고
    • Fine mapping and characterization of the Rous sarcoma Virus Pr76gag late assembly domain
    • Xiang Y, Cameron CE, Wills JW, Leis J. Fine mapping and characterization of the Rous sarcoma Virus Pr76gag late assembly domain. J Virol 1996; 70(8): 5695-700.
    • (1996) J. Virol. , vol.70 , Issue.8 , pp. 5695-5700
    • Xiang, Y.1    Cameron, C.E.2    Wills, J.W.3    Leis, J.4
  • 154
    • 0026317877 scopus 로고
    • Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release
    • Gottlinger HG, Dorfman T, Sodroski JG, Haseltine WA. Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release. Proc Natl Acad Sci USA 1991; 88(8): 3195-9.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , Issue.8 , pp. 3195-3199
    • Gottlinger, H.G.1    Dorfman, T.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 155
    • 0028971135 scopus 로고
    • p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease
    • Huang M, Orenstein JM, Martin MA, Freed EO. p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease. J Virol 1995; 69(11): 6810-8.
    • (1995) J. Virol. , vol.69 , Issue.11 , pp. 6810-6818
    • Huang, M.1    Orenstein, J.M.2    Martin, M.A.3    Freed, E.O.4
  • 156
    • 0029092338 scopus 로고
    • Positionally independent and exchangeable late budding functions of the Rous sarcoma virus and human immunodeficiency virus Gag proteins
    • Parent LJ, Bennett RP, Craven RC, Nelle TD, Krishna NK, Bowzard JB, et al. Positionally independent and exchangeable late budding functions of the Rous sarcoma virus and human immunodeficiency virus Gag proteins. J Virol 1995; 69(9): 5455-60.
    • (1995) J. Virol. , vol.69 , Issue.9 , pp. 5455-5460
    • Parent, L.J.1    Bennett, R.P.2    Craven, R.C.3    Nelle, T.D.4    Krishna, N.K.5    Bowzard, J.B.6
  • 158
    • 0036829172 scopus 로고    scopus 로고
    • Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein
    • Pornillos O, Alam SL, Davis DR, Sundquist WI. Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein. Nat Struct Biol 2002; 9(11): 812-7.
    • (2002) Nat. Struct. Biol. , vol.9 , Issue.11 , pp. 812-817
    • Pornillos, O.1    Alam, S.L.2    Davis, D.R.3    Sundquist, W.I.4
  • 159
    • 0034940214 scopus 로고    scopus 로고
    • Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag)
    • VerPlank L, Bouamr F, LaGrassa TJ, Agresta B, Kikonyogo A, Leis J, et al. Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag). Proc Natl Acad Sci USA 2001; 98(14): 7724-9.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.14 , pp. 7724-7729
    • VerPlank, L.1    Bouamr, F.2    LaGrassa, T.J.3    Agresta, B.4    Kikonyogo, A.5    Leis, J.6
  • 161
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack B, Calistri A, Craig S, Popova E, Gottlinger HG. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 2003; 114: 689-699.
    • (2003) Cell , vol.114 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 162
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann DJ, Babst M, Emr SD. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 2001; 106(2): 145-55.
    • (2001) Cell , vol.106 , Issue.2 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 164
    • 0035658023 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • Martin-Serrano J, Zang T, Bieniasz PD. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat Med 2001; 7(12): 1313-9.
    • (2001) Nat. Med. , vol.7 , Issue.12 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 165
    • 0037383128 scopus 로고    scopus 로고
    • Role of ESCRT-I in retroviral budding
    • Martin-Serrano J, Zang T, Bieniasz PD. Role of ESCRT-I in retroviral budding. J Virol 2003: 77(8): 4794-804.
    • (2003) J. Virol. , vol.77 , Issue.8 , pp. 4794-4804
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 166
    • 0037596749 scopus 로고    scopus 로고
    • TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation
    • Lu Q, Hope LW, Brasch M, Reinhard C, Cohen SN. TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation. Proc Natl Acad Sci USA 2003; 100(13): 7626-31.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.13 , pp. 7626-7631
    • Lu, Q.1    Hope, L.W.2    Brasch, M.3    Reinhard, C.4    Cohen, S.N.5
  • 167
    • 0042232395 scopus 로고    scopus 로고
    • After Hrs with HIV
    • Amara A, Littman DR. After Hrs with HIV. J Cell Biol 2003; 162(3): 371-5.
    • (2003) J. Cell Biol. , vol.162 , Issue.3 , pp. 371-375
    • Amara, A.1    Littman, D.R.2
  • 168
    • 0037688240 scopus 로고    scopus 로고
    • Defects in human immunodeficiency virus budding and endosomal sorting induced by TSG101 overexpression
    • Goila-Gaur R, Demirov DG, Orenstein JM, Ono A, Freed EO. Defects in human immunodeficiency virus budding and endosomal sorting induced by TSG101 overexpression. J Virol 2003; 77(11): 6507-19.
    • (2003) J. Virol. , vol.77 , Issue.11 , pp. 6507-6519
    • Goila-Gaur, R.1    Demirov, D.G.2    Orenstein, J.M.3    Ono, A.4    Freed, E.O.5
  • 169
    • 0032509175 scopus 로고    scopus 로고
    • Exploiting the Oasis of proline recognition by SH3 and WW domains: Design of N-substituted inhibitors
    • Nguyen JT, Turck CW, Cohen FE, Zuckermann RN, Lim WA. Exploiting the Oasis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors. Science 1998; 282(5396): 2088-92.
    • (1998) Science , vol.282 , Issue.5396 , pp. 2088-2092
    • Nguyen, J.T.1    Turck, C.W.2    Cohen, F.E.3    Zuckermann, R.N.4    Lim, W.A.5
  • 170
    • 0031900144 scopus 로고    scopus 로고
    • Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus
    • Ott DE, Coren LV, Copeland TD, Kane BP, Johnson DG, Sowder RC 2nd, et al. Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus. J Virol 1998; 72(4): 2962-8.
    • (1998) J. Virol. , vol.72 , Issue.4 , pp. 2962-2968
    • Ott, D.E.1    Coren, L.V.2    Copeland, T.D.3    Kane, B.P.4    Johnson, D.G.5    Sowder II, R.C.6
  • 171
    • 0034700119 scopus 로고    scopus 로고
    • Ubiquitin in retrovirus assembly: Actor or bystander?
    • Vogt VM. Ubiquitin in retrovirus assembly: actor or bystander? Proc Natl Acad Sci USA 2000; 97(24): 12945-7.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.24 , pp. 12945-12947
    • Vogt, V.M.1
  • 173
    • 0034700088 scopus 로고    scopus 로고
    • Proteasome inhibition interferes with gag polyprotein processing, release, and maturation of HIV- 1 and HIV-2
    • Schubert U, Ott DE, Chertova EN, Welker R, Tessmer U, Princiotta MF, et al. Proteasome inhibition interferes with gag polyprotein processing, release, and maturation of HIV- 1 and HIV-2. Proc Natl Acad Sci USA 2000; 97(24): 13057-62.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.24 , pp. 13057-13062
    • Schubert, U.1    Ott, D.E.2    Chertova, E.N.3    Welker, R.4    Tessmer, U.5    Princiotta, M.F.6
  • 174
    • 0034700146 scopus 로고    scopus 로고
    • Ubiquitin is part of the retrovirus budding machinery
    • Patnaik A, Chau V, Wills JW. Ubiquitin is part of the retrovirus budding machinery. Proc Natl Acad Sci USA 2000; 97(24):
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.24 , pp. 13069-13074
    • Patnaik, A.1    Chau, V.2    Wills, J.W.3
  • 175
    • 0025351117 scopus 로고
    • Ubiquitin in avian leukosis virus particles
    • Putterman D, Pepinsky RB, Vogt VM. Ubiquitin in avian leukosis virus particles. Virology 1990; 176(2): 633-7.
    • (1990) Virology , vol.176 , Issue.2 , pp. 633-637
    • Putterman, D.1    Pepinsky, R.B.2    Vogt, V.M.3
  • 176
    • 0035823032 scopus 로고    scopus 로고
    • A new ticket for entry into budding vesicles-ubiquitin
    • Hicke L. A new ticket for entry into budding vesicles-ubiquitin. Cell 2001; 106(5): 527-30.
    • (2001) Cell , vol.106 , Issue.5 , pp. 527-530
    • Hicke, L.1
  • 177
    • 0034677207 scopus 로고    scopus 로고
    • Monoubiquitin carries a novel internalization signal that is appended to activated receptors
    • Shih SC, Sloper-Mould KE, Hicke L. Monoubiquitin carries a novel internalization signal that is appended to activated receptors. EMBO J 2000; 19(2): 187-98.
    • (2000) EMBO J. , vol.19 , Issue.2 , pp. 187-198
    • Shih, S.C.1    Sloper-Mould, K.E.2    Hicke, L.3
  • 178
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee DIL Goldberg AL. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol 1998; 8(10): 397-403.
    • (1998) Trends Cell Biol. , vol.8 , Issue.10 , pp. 397-403
    • Lee, D.I.L.1    Goldberg, A.L.2
  • 179
    • 0345686713 scopus 로고    scopus 로고
    • PA-457: A potent HIV inhibitor that disrupts core condensation by targeting a late step in Gag processing
    • Li F, Goila-Gaur R, Salzwedel K, Kilgore NR, Reddick M, Matallana C, et al. PA-457: a potent HIV inhibitor that disrupts core condensation by targeting a late step in Gag processing. Proc Natl Acad Sci USA 2003; 100(23): 13555-60.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.23 , pp. 13555-13560
    • Li, F.1    Goila-Gaur, R.2    Salzwedel, K.3    Kilgore, N.R.4    Reddick, M.5    Matallana, C.6
  • 181
    • 0032587326 scopus 로고    scopus 로고
    • Interaction of the human immunodeficiency virus type 1 nucleocapsid with actin
    • Liu B, Dai R, Tian CJ, Dawson L, Gorelick R, Yu XF. Interaction of the human immunodeficiency virus type 1 nucleocapsid with actin. J Virol 1999; 73(4): 2901-8.
    • (1999) J. Virol. , vol.73 , Issue.4 , pp. 2901-2908
    • Liu, B.1    Dai, R.2    Tian, C.J.3    Dawson, L.4    Gorelick, R.5    Yu, X.F.6
  • 182
    • 0032982141 scopus 로고    scopus 로고
    • Actin associates with the nucleocapsid domain of the human immunodeficiency virus Gag polyprotein
    • Wilk T, Gowen B, Fuller SD. Actin associates with the nucleocapsid domain of the human immunodeficiency virus Gag polyprotein. J Virol 1999; 73(3): 1931-40.
    • (1999) J. Virol. , vol.73 , Issue.3 , pp. 1931-1940
    • Wilk, T.1    Gowen, B.2    Fuller, S.D.3
  • 183
    • 0029941433 scopus 로고    scopus 로고
    • HIV-1 Gag protein associates with F-actin present in microfilaments
    • Rey O, Canon J, Krogstad P. HIV-1 Gag protein associates with F-actin present in microfilaments. Virology 1996; 220(2): 530-4.
    • (1996) Virology , vol.220 , Issue.2 , pp. 530-534
    • Rey, O.1    Canon, J.2    Krogstad, P.3
  • 184
    • 0029817030 scopus 로고    scopus 로고
    • Directional budding of human immunodeficiency virus from monocytes
    • Perotti ME, Tan X, Phillips DM. Directional budding of human immunodeficiency virus from monocytes. J Virol 1996; 70(9): 5916-21.
    • (1996) J. Virol. , vol.70 , Issue.9 , pp. 5916-5921
    • Perotti, M.E.1    Tan, X.2    Phillips, D.M.3
  • 185
    • 0030446526 scopus 로고    scopus 로고
    • Targeting of Moloney murine leukemia virus gag precursor to the site of virus budding
    • Suomalainen M, Hultenby K, Garoff H. Targeting of Moloney murine leukemia virus gag precursor to the site of virus budding. J Cell Biol 1996; 135(6 Pt 2): 1841-52.
    • (1996) J. Cell Biol. , vol.135 , Issue.6 PART 2 , pp. 1841-1852
    • Suomalainen, M.1    Hultenby, K.2    Garoff, H.3
  • 186
    • 0038009933 scopus 로고    scopus 로고
    • Retroviral genomic RNAs are transported to the plasma membrane by endosomal vesicles
    • Basyuk E, Galli T, Mougel M, Blanchard JM, Sitbon M, Bertrand E. Retroviral genomic RNAs are transported to the plasma membrane by endosomal vesicles. Dev Cell 2003; 5(1): 161-74.
    • (2003) Dev. Cell , vol.5 , Issue.1 , pp. 161-174
    • Basyuk, E.1    Galli, T.2    Mougel, M.3    Blanchard, J.M.4    Sitbon, M.5    Bertrand, E.6
  • 187
    • 0025183715 scopus 로고
    • Transport and assembly of gag proteins into Moloney murine leukemia virus
    • Hansen M, Jelinek L, Whiting S, Barklis E. Transport and assembly of gag proteins into Moloney murine leukemia virus. J Virol 1990; 64(11): 5306-16.
    • (1990) J. Virol. , vol.64 , Issue.11 , pp. 5306-5316
    • Hansen, M.1    Jelinek, L.2    Whiting, S.3    Barklis, E.4
  • 188
    • 0025767125 scopus 로고
    • Effects of brefeldin A on the processing of viral envelope glycoproteins in murine erythroleukemia cells
    • Ulmer JB, Palade GE. Effects of brefeldin A on the processing of viral envelope glycoproteins in murine erythroleukemia cells. J Biol Chem 1991; 266(14): 9173-9.
    • (1991) J. Biol. Chem. , vol.266 , Issue.14 , pp. 9173-9179
    • Ulmer, J.B.1    Palade, G.E.2
  • 190
    • 0035033183 scopus 로고    scopus 로고
    • Pharmacology of phosphoinositides, regulators of multiple cellular functions
    • Balla T. Pharmacology of phosphoinositides, regulators of multiple cellular functions. Curr Pharm Des 2001; 7(6): 475-507.
    • (2001) Curr. Pharm. Des. , vol.7 , Issue.6 , pp. 475-507
    • Balla, T.1
  • 191
  • 192
    • 0034982825 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase inhibition in cancer treatment
    • Berrie CP. Phosphoinositide 3-kinase inhibition in cancer treatment. Expert Opin Investig Drugs 2001; 10(6): 1085-98.
    • (2001) Expert Opin. Investig. Drugs , vol.10 , Issue.6 , pp. 1085-1098
    • Berrie, C.P.1
  • 193
    • 0028302790 scopus 로고
    • Inhibition of infectious human immunodeficiency virus type 1 particle formation by Gag protein-derived peptides
    • Niedrig M, Gelderblom HR, Pauli G, Marz J, Bickhard H, Wolf H, et al. Inhibition of infectious human immunodeficiency virus type 1 particle formation by Gag protein-derived peptides. J Gen Virol 1994; 75 ( Pt 6): 1469-74.
    • (1994) J. Gen. Virol. , vol.75 , Issue.PART 6 , pp. 1469-1474
    • Niedrig, M.1    Gelderblom, H.R.2    Pauli, G.3    Marz, J.4    Bickhard, H.5    Wolf, H.6
  • 194
    • 0030901738 scopus 로고    scopus 로고
    • Structurefunction studies of the human immunodeficiency virus type 1 matrix protein, p17
    • Cannon PM, Matthews S, Clark N, Byles ED, Iourin O, Hockley DJ, et al. Structurefunction studies of the human immunodeficiency virus type 1 matrix protein, p17. J Virol 1997; 71(5): 3474-83.
    • (1997) J. Virol. , vol.71 , Issue.5 , pp. 3474-3483
    • Cannon, P.M.1    Matthews, S.2    Clark, N.3    Byles, E.D.4    Iourin, O.5    Hockley, D.J.6
  • 196
    • 0035153490 scopus 로고    scopus 로고
    • The nontoxic tripeptide glycyl-prolyl-glycine amide inhibits the replication of human immunodeficiency virus type 1
    • Su J, Andersson E, Horal P, Naghavi MH, Palm A, Wu YP, et al. The nontoxic tripeptide glycyl-prolyl-glycine amide inhibits the replication of human immunodeficiency virus type 1. J Hum Virol 2001; 4(1): 1-7.
    • (2001) J. Hum. Virol. , vol.4 , Issue.1 , pp. 1-7
    • Su, J.1    Andersson, E.2    Horal, P.3    Naghavi, M.H.4    Palm, A.5    Wu, Y.P.6
  • 197
    • 0041922335 scopus 로고    scopus 로고
    • HIV-1 protease inhibitors: A comparative QSAR analysis
    • Kurup A, Mekapati SB, Garg R, Hansch C, HIV-1 protease inhibitors: a comparative QSAR analysis. Curr Med Chem 2003; 10(17): 1679-88.
    • (2003) Curr. Med. Chem. , vol.10 , Issue.17 , pp. 1679-1688
    • Kurup, A.1    Mekapati, S.B.2    Garg, R.3    Hansch, C.4
  • 198
    • 0035160478 scopus 로고    scopus 로고
    • New developments in anti-HIV chemotherapy
    • De Clercq E. New developments in anti-HIV chemotherapy. Curr Med Chem 2001; 8(13): 1543-72.
    • (2001) Curr. Med. Chem. , vol.8 , Issue.13 , pp. 1543-1572
    • De Clercq, E.1
  • 199
    • 0027158754 scopus 로고
    • Partial inhibition of the human immunodeficiency virus type 1 protease results in aberrant virus assembly and the formation of noninfectious particles
    • Kaplan AH, Zack JA, Knigge M, Paul DA, Kempf DJ, Norbeck DW, et al. Partial inhibition of the human immunodeficiency virus type 1 protease results in aberrant virus assembly and the formation of noninfectious particles. J Virol 1993; 67(7): 4050-5.
    • (1993) J. Virol. , vol.67 , Issue.7 , pp. 4050-4055
    • Kaplan, A.H.1    Zack, J.A.2    Knigge, M.3    Paul, D.A.4    Kempf, D.J.5    Norbeck, D.W.6
  • 200
    • 0026772902 scopus 로고
    • Human immunodeficiency virus type 1 protease inhibitors irreversibly block infectivity of purified virions from chronically infected cells
    • Lambert DM, Petteway SR Jr, McDanal CE, Hart TK, Leary JJ, Dreyer GB, et al. Human immunodeficiency virus type 1 protease inhibitors irreversibly block infectivity of purified virions from chronically infected cells. Antimicrob Agents Chemother 1992; 36(5): 982-8.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , Issue.5 , pp. 982-988
    • Lambert, D.M.1    Petteway Jr., S.R.2    McDanal, C.E.3    Hart, T.K.4    Leary, J.J.5    Dreyer, G.B.6
  • 201
    • 0028176540 scopus 로고
    • Anti- AIDS agents, 11. Betulinic acid and platanic acid as anti-HIV principles from Syzigium claviflorum, and the anti-HIV activity of structurally related triterpenoids
    • Fujioka T, Kashiwada Y, Kilkuskie RE, Cosentino LM, Ballas LM, Jiang JB, et al. Anti- AIDS agents, 11. Betulinic acid and platanic acid as anti-HIV principles from Syzigium claviflorum, and the anti-HIV activity of structurally related triterpenoids. J Nat Prod 1994; 57(2): 243-7.
    • (1994) J. Nat. Prod. , vol.57 , Issue.2 , pp. 243-247
    • Fujioka, T.1    Kashiwada, Y.2    Kilkuskie, R.E.3    Cosentino, L.M.4    Ballas, L.M.5    Jiang, J.B.6
  • 202
    • 0028223281 scopus 로고
    • Triterpene derivatives that block entry of human immunodeficiency virus type 1 into cells
    • Mayaux JF, Bousseau A, Pauwels R, Huet T, Henin Y, Dereu N, et al. Triterpene derivatives that block entry of human immunodeficiency virus type 1 into cells. Proc Natl And Sci USA 1994; 91(9): 3564-8.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , Issue.9 , pp. 3564-3568
    • Mayaux, J.F.1    Bousseau, A.2    Pauwels, R.3    Huet, T.4    Henin, Y.5    Dereu, N.6
  • 203
    • 0030802750 scopus 로고    scopus 로고
    • Resistance to a drug blocking human immunodeficiency virus type 1 entry (RPR103611) is conferred by mutations in gp41
    • Labrosse B, Pleskoff O, Sol N, Jones C, Henin Y, Alizon M. Resistance to a drug blocking human immunodeficiency virus type 1 entry (RPR103611) is conferred by mutations in gp41. J Virol 1997; 71(11): 8230-6.
    • (1997) J. Virol. , vol.71 , Issue.11 , pp. 8230-8236
    • Labrosse, B.1    Pleskoff, O.2    Sol, N.3    Jones, C.4    Henin, Y.5    Alizon, M.6
  • 204
    • 0033927489 scopus 로고    scopus 로고
    • Novel compounds in preclinical/early clinical development for the treatment of HIV infections
    • De Clercq E. Novel compounds in preclinical/early clinical development for the treatment of HIV infections. Rev Med Virol 2000; 10(4): 255-77.
    • (2000) Rev. Med. Virol. , vol.10 , Issue.4 , pp. 255-277
    • De Clercq, E.1
  • 205
    • 0035087062 scopus 로고    scopus 로고
    • Antihuman immunodeficiency virus activity of YK-FH312 (a betulinic acid derivative), a novel compound blocking viral maturation
    • Kanamoto T, Kashiwada Y, Kanbara K, Gotoh K, Yoshimori M, Goto T, et al. Antihuman immunodeficiency virus activity of YK-FH312 (a betulinic acid derivative), a novel compound blocking viral maturation. Antimicrob Agents Chemother 2001; 45(4): 1225-30.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , Issue.4 , pp. 1225-1230
    • Kanamoto, T.1    Kashiwada, Y.2    Kanbara, K.3    Gotoh, K.4    Yoshimori, M.5    Goto, T.6
  • 206
    • 0024591695 scopus 로고
    • The structure of antiviral agents that inhibit uncoating when complexed with viral capsids
    • Rossmann MG. The structure of antiviral agents that inhibit uncoating when complexed with viral capsids. Antiviral Res 1989; 11(1): 3-13.
    • (1989) Antiviral Res. , vol.11 , Issue.1 , pp. 3-13
    • Rossmann, M.G.1
  • 207
    • 0022489613 scopus 로고
    • The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating
    • Smith TJ, Kremer MJ, Luo M, Vriend G, Arnold E. Kamer G, et al. The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating. Science 1986; 233(4770): 1286-93.
    • (1986) Science , vol.233 , Issue.4770 , pp. 1286-1293
    • Smith, T.J.1    Kremer, M.J.2    Luo, M.3    Vriend, G.4    Arnold, E.5    Kamer, G.6
  • 208
    • 0347928672 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus replication by drug-induced depletion of nucleocapsids
    • Deres K, Schroder CH, Paessens A, Goldmann S, Hacker HJ, Weber O, et al. Inhibition of hepatitis B virus replication by drug-induced depletion of nucleocapsids. Science 2003; 299(5608): 893-6.
    • (2003) Science , vol.299 , Issue.5608 , pp. 893-896
    • Deres, K.1    Schroder, C.H.2    Paessens, A.3    Goldmann, S.4    Hacker, H.J.5    Weber, O.6
  • 209
    • 0032536896 scopus 로고    scopus 로고
    • Proteolytie refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly
    • von Schwedler UK, Stemmler TL, Klishko VY, Li S, Albertine KH, Davis DR, et al. Proteolytie refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly. EMBO J 1998; 17(6): 1555-68.
    • (1998) EMBO J. , vol.17 , Issue.6 , pp. 1555-1568
    • von Schwedler, U.K.1    Stemmler, T.L.2    Klishko, V.Y.3    Li, S.4    Albertine, K.H.5    Davis, D.R.6
  • 210
    • 0031954466 scopus 로고    scopus 로고
    • N-Terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles
    • Gross I, Hohenberg H, Huckhagel C, Krausslich HG. N-Terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles. J Virol 1998; 72(6): 4798-810.
    • (1998) J. Virol. , vol.72 , Issue.6 , pp. 4798-4810
    • Gross, I.1    Hohenberg, H.2    Huckhagel, C.3    Krausslich, H.G.4
  • 211
    • 0029961364 scopus 로고    scopus 로고
    • The role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps ofthe viral life cycle
    • Reicin AS, Ohagen A, Yin L, Hoglund S, Goff SP. The role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps ofthe viral life cycle. J Virol 1996; 70(12): 8645-52.
    • (1996) J. Virol. , vol.70 , Issue.12 , pp. 8645-8652
    • Reicin, A.S.1    Ohagen, A.2    Yin, L.3    Hoglund, S.4    Goff, S.P.5
  • 212
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • Forshey BM, von Schwedler U, Sundquist WI, Aiken C. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J Virol 2002; 76(11): 5667-77.
    • (2002) J. Virol. , vol.76 , Issue.11 , pp. 5667-5677
    • Forshey, B.M.1    von Schwedler, U.2    Sundquist, W.I.3    Aiken, C.4
  • 214
    • 0026786712 scopus 로고
    • Cell-free transmission of Vif mutants of HIV-1
    • Fan L, Peden K. Cell-free transmission of Vif mutants of HIV-1. Virology 1992; 190(1): 19-29.
    • (1992) Virology , vol.190 , Issue.1 , pp. 19-29
    • Fan, L.1    Peden, K.2
  • 215
    • 0028926644 scopus 로고
    • Peripheral blood mononuclear cells produce normal amounts of defective Vif- human immunodeficiency virus type 1 particles which are restricted for the preretrotranscription steps
    • Courcoul M, Patience C, Rey F, Blanc D, Harmache A, Sire J, et al. Peripheral blood mononuclear cells produce normal amounts of defective Vif- human immunodeficiency virus type 1 particles which are restricted for the preretrotranscription steps. J Virol 1995; 69(4): 2068-74.
    • (1995) J. Virol. , vol.69 , Issue.4 , pp. 2068-2074
    • Courcoul, M.1    Patience, C.2    Rey, F.3    Blanc, D.4    Harmache, A.5    Sire, J.6
  • 216
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy AM, Gaddis NC, Choi JD, Malim MH. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 2002; 418(6898): 646-50.
    • (2002) Nature , vol.418 , Issue.6898 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 217
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • Zhang H, Yang B, Pomerantz RJ, Zhang C, Arunachalam SC, Gao L. The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 2003; 424(6944): 94-8.
    • (2003) Nature , vol.424 , Issue.6944 , pp. 94-98
    • Zhang, H.1    Yang, B.2    Pomerantz, R.J.3    Zhang, C.4    Arunachalam, S.C.5    Gao, L.6
  • 218
    • 0038107587 scopus 로고    scopus 로고
    • Speciesspecific exclusion of APOBEC3G from HIV-1 virions by Vif
    • Mariani R, Chen D, Schrofelbauer B, Navarro F, Konig R, Bollman B, et al. Speciesspecific exclusion of APOBEC3G from HIV-1 virions by Vif. Cell 2003; 114(1): 21-31.
    • (2003) Cell , vol.114 , Issue.1 , pp. 21-31
    • Mariani, R.1    Chen, D.2    Schrofelbauer, B.3    Navarro, F.4    Konig, R.5    Bollman, B.6
  • 219
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Mangeat B, Turelli P, Caron G, Friedli M, Perrin L, Trono D. Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 2003; 424(6944): 99-103.
    • (2003) Nature , vol.424 , Issue.6944 , pp. 99-103
    • Mangeat, B.1    Turelli, P.2    Caron, G.3    Friedli, M.4    Perrin, L.5    Trono, D.6
  • 220
    • 0038363470 scopus 로고    scopus 로고
    • Hypermutation of HIV-1 DNA in the absence of the Vif protein
    • Lecossier D, Bouchonnet F, Clavel F, Hance AJ. Hypermutation of HIV-1 DNA in the absence of the Vif protein. Science 2003; 300(5622): 1112.
    • (2003) Science , vol.300 , Issue.5622 , pp. 1112
    • Lecossier, D.1    Bouchonnet, F.2    Clavel, F.3    Hance, A.J.4
  • 223
    • 0036785579 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 (HIV-1) replication by a two-amino-acid insertion in HIV-1 Vif from a nonprogressing mother and child
    • Alexander L, Aquino-DeJesus MJ, Chan M, Andiman WA. Inhibition of human immunodeficiency virus type 1 (HIV-1) replication by a two-amino-acid insertion in HIV-1 Vif from a nonprogressing mother and child. J Virol 2002; 76(20): 10533-9.
    • (2002) J. Virol. , vol.76 , Issue.20 , pp. 10533-10539
    • Alexander, L.1    Aquino-DeJesus, M.J.2    Chan, M.3    Andiman, W.A.4
  • 224
    • 0034633803 scopus 로고    scopus 로고
    • Characterization of human immunodeficiency virus type 1 vif gene in long-term asymptomatic individuals
    • Hassaine G, Agostini I, Candotti D, Bessou G, Caballero M, Agut H, et al. Characterization of human immunodeficiency virus type 1 vif gene in long-term asymptomatic individuals. Virology 2000; 276(1): 169-80.
    • (2000) Virology , vol.276 , Issue.1 , pp. 169-180
    • Hassaine, G.1    Agostini, I.2    Candotti, D.3    Bessou, G.4    Caballero, M.5    Agut, H.6
  • 225
    • 0032506225 scopus 로고    scopus 로고
    • Peptide inhibitors of HIV-1 protease and viral infection of peripheral blood lymphocytes based on HIV-1 Vif
    • Potash MJ, Bentsman G, Muir T, Krachmarov C, Sova P, Volsky DJ. Peptide inhibitors of HIV-1 protease and viral infection of peripheral blood lymphocytes based on HIV-1 Vif. Proc Natl Acad Sci USA 1998; 95(23): 13865-8.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.23 , pp. 13865-13868
    • Potash, M.J.1    Bentsman, G.2    Muir, T.3    Krachmarov, C.4    Sova, P.5    Volsky, D.J.6
  • 226
    • 0032426645 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif-derived peptides inhibit the viral protease and arrest virus production
    • Baraz L, Friedler A, Blumenzweig I, Nussinuv O, Chen N, Steinitz M, et al. Human immunodeficiency virus type 1 Vif-derived peptides inhibit the viral protease and arrest virus production. FFBS Lett 1998; 441(3): 419-26,
    • (1998) FFBS Lett. , vol.441 , Issue.3 , pp. 419-426
    • Baraz, L.1    Friedler, A.2    Blumenzweig, I.3    Nussinuv, O.4    Chen, N.5    Steinitz, M.6
  • 228
    • 0037458718 scopus 로고    scopus 로고
    • Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins
    • Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, et al. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. J Biol Chem 2003; 278(8): 6596-602,
    • (2003) J. Biol. Chem. , vol.278 , Issue.8 , pp. 6596-6602
    • Yang, B.1    Gao, L.2    Li, L.3    Lu, Z.4    Fan, X.5    Patel, C.A.6
  • 229
    • 0030740060 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 (HIV-1) protein Vif inhibits the activity of HIV-1 protease in bacteria and in vitro
    • Kotler M, Simm M, Zhao YS, Sova P, Chao W, Ohnona SF, et al. Human immunodeficiency virus type 1 (HIV-1) protein Vif inhibits the activity of HIV-1 protease in bacteria and in vitro. J Virol 1997; 71(8): 5774-81.
    • (1997) J. Virol. , vol.71 , Issue.8 , pp. 5774-5781
    • Kotler, M.1    Simm, M.2    Zhao, Y.S.3    Sova, P.4    Chao, W.5    Ohnona, S.F.6
  • 230
    • 0028200823 scopus 로고
    • Role of vif during packing of the core of HIV-1
    • Hoglund S, Ohagen A, Lawrence K, Gabuzda D. Role of vif during packing of the core of HIV-1. Virology 1994; 201(2): 349-55.
    • (1994) Virology , vol.201 , Issue.2 , pp. 349-355
    • Hoglund, S.1    Ohagen, A.2    Lawrence, K.3    Gabuzda, D.4
  • 231
    • 0034899286 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNA
    • Khan MA, Aberham C, Kao S, Akari H, Gorelick R, Bour S, et al. Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNA. J Virol 2001; 75(16): 7252-65.
    • (2001) J. Virol. , vol.75 , Issue.16 , pp. 7252-7265
    • Khan, M.A.1    Aberham, C.2    Kao, S.3    Akari, H.4    Gorelick, R.5    Bour, S.6
  • 232
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element
    • De Guzman RN, Wu ZR, Stalling CC, Pappalardo L, Borer PN, Summers MF. Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element. Science 1998; 279(5349): 384-8.
    • (1998) Science , vol.279 , Issue.5349 , pp. 384-388
    • De Guzman, R.N.1    Wu, Z.R.2    Stalling, C.C.3    Pappalardo, L.4    Borer, P.N.5    Summers, M.F.6
  • 233
    • 0026052031 scopus 로고
    • Brefeldin A inhibits the processing and secretion of envelope glycoproteins of human immunodeficiency virus type 1
    • Pal R, Mumbauer S, Hoke GM, Takatsuki A, Sarngadharan MG. Brefeldin A inhibits the processing and secretion of envelope glycoproteins of human immunodeficiency virus type 1. AIDS Res Hum Retroviruses 1991; 7(8): 707-12.
    • (1991) AIDS Res. Hum. Retroviruses , vol.7 , Issue.8 , pp. 707-712
    • Pal, R.1    Mumbauer, S.2    Hoke, G.M.3    Takatsuki, A.4    Sarngadharan, M.G.5
  • 234
    • 0028267575 scopus 로고
    • Viral interactions with the host-cell cytoskeleton: The role of retroviral proteases
    • Luffig RB, Lupo LD. Viral interactions with the host-cell cytoskeleton: the role of retroviral proteases. Trends Microbiol 1994; 2(5): 178-82.
    • (1994) Trends Microbiol. , vol.2 , Issue.5 , pp. 178-182
    • Luffig, R.B.1    Lupo, L.D.2
  • 235
    • 0037133594 scopus 로고    scopus 로고
    • Nuclear entry and CRM1-dependent nuclear export of the Rous sarcoma virus Gag polyprotein
    • Scheifele LZ, Garbitt RA, Rhoads JD, Parent LJ. Nuclear entry and CRM1-dependent nuclear export of the Rous sarcoma virus Gag polyprotein. Proc Natl Acad Sci USA 2002; 99(6): 3944-9.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.6 , pp. 3944-3949
    • Scheifele, L.Z.1    Garbitt, R.A.2    Rhoads, J.D.3    Parent, L.J.4
  • 236
    • 0016741116 scopus 로고
    • Efficient release of murine xenotropic oncornavirus after murine leukemia virus infection of mouse cells
    • Fischinger PJ, Nomura S. Efficient release of murine xenotropic oncornavirus after murine leukemia virus infection of mouse cells. Virology 1975; 65(1): 304-7.
    • (1975) Virology , vol.65 , Issue.1 , pp. 304-307
    • Fischinger, P.J.1    Nomura, S.2
  • 237
    • 0020073464 scopus 로고
    • Microtubule-depolymerizing agents inhibit Moloney murine leukaemia virus production
    • Satake M, Luftig RB. Microtubule-depolymerizing agents inhibit Moloney murine leukaemia virus production. J Gen Virol 1982; 58(Pt 2): 339-49.
    • (1982) J. Gen. Virol. , vol.58 , Issue.PART 2 , pp. 339-349
    • Satake, M.1    Luftig, R.B.2
  • 238
    • 0037699898 scopus 로고    scopus 로고
    • Minidefensins: Antimicrobial peptides with activity against HIV-1
    • Cole AM, Lehrer RI. Minidefensins: antimicrobial peptides with activity against HIV-1. Curr Pharm Design 2003; 9(18): 1463-73.
    • (2003) Curr. Pharm. Design , vol.9 , Issue.18 , pp. 1463-1473
    • Cole, A.M.1    Lehrer, R.I.2
  • 239
  • 240
    • 0041488689 scopus 로고    scopus 로고
    • Proteolytic events of HIV-1 replication as targets for therapeutic intervention
    • Tozser J, Oroszlan S, Proteolytic events of HIV-1 replication as targets for therapeutic intervention. Curr Pharm Design 2003; 9(22): 1803-15.
    • (2003) Curr. Pharm. Design , vol.9 , Issue.22 , pp. 1803-1815
    • Tozser, J.1    Oroszlan, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.