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Volumn , Issue , 2013, Pages 153-166

HIV-1 maturation

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EID: 84929524636     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4614-7729-7_6     Document Type: Chapter
Times cited : (3)

References (73)
  • 1
    • 80051767703 scopus 로고    scopus 로고
    • The role of cellular factors in promoting HIV budding
    • Weiss ER, Gottlinger H (2011) The role of cellular factors in promoting HIV budding. J Mol Biol 410(4):525-533
    • (2011) J Mol Biol , vol.410 , Issue.4 , pp. 525-533
    • Weiss, E.R.1    Gottlinger, H.2
  • 2
    • 3543142335 scopus 로고    scopus 로고
    • Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism
    • Pettit SC, Everitt LE, Choudhury S, Dunn BM, Kaplan AH (2004) Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism. J Virol 78(16):8477-8485
    • (2004) J Virol , vol.78 , Issue.16 , pp. 8477-8485
    • Pettit, S.C.1    Everitt, L.E.2    Choudhury, S.3    Dunn, B.M.4    Kaplan, A.H.5
  • 3
    • 84859762033 scopus 로고    scopus 로고
    • Context surrounding processing sites is crucial in determining cleavage rate of a subset of processing sites in HIV-1 Gag and Gag-Pro-Pol polyprotein precursors by viral protease
    • Lee SK, Potempa M, Kolli M, Ozen A, Schiffer CA, Swanstrom R (2012) Context surrounding processing sites is crucial in determining cleavage rate of a subset of processing sites in HIV-1 Gag and Gag-Pro-Pol polyprotein precursors by viral protease. J Biol Chem 287(16): 13279-13290
    • (2012) J Biol Chem , vol.287 , Issue.16 , pp. 13279-13290
    • Lee, S.K.1    Potempa, M.2    Kolli, M.3    Ozen, A.4    Schiffer, C.A.5    Swanstrom, R.6
  • 4
    • 0026086220 scopus 로고
    • Mutagenesis of protease cleavage sites in the human immunodeficiency virus type 1 gag polyprotein
    • Tritch RJ, Cheng Y-SE, Yin FH, Erickson-Viitanen S (1991) Mutagenesis of protease cleavage sites in the human immunodeficiency virus type 1 gag polyprotein. J Virol 65(2):922-930
    • (1991) J Virol , vol.65 , Issue.2 , pp. 922-930
    • Tritch, R.J.1    Y-Se, C.2    Yin, F.H.3    Erickson-Viitanen, S.4
  • 5
    • 1542502945 scopus 로고
    • Activity of purified biosynthetic proteinase of human immunodeficiency virus on natural substrates and synthetic peptides
    • Krausslich HG, Ingraham RH, Skoog MT, Wimmer E, Pallai PV, Carter CA (1989) Activity of purified biosynthetic proteinase of human immunodeficiency virus on natural substrates and synthetic peptides. Proc Natl Acad Sci USA 86(3):807-811
    • (1989) Proc Natl Acad Sci USA , vol.86 , Issue.3 , pp. 807-811
    • Krausslich, H.G.1    Ingraham, R.H.2    Skoog, M.T.3    Wimmer, E.4    Pallai, P.V.5    Carter, C.A.6
  • 6
    • 0027971621 scopus 로고
    • The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions
    • Pettit SC, Moody MD, Wehbie RS, Kaplan AH, Nantermet PV, Klein CA et al (1994) The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions. J Virol 68(12):8017-8027
    • (1994) J Virol , vol.68 , Issue.12 , pp. 8017-8027
    • Pettit, S.C.1    Moody, M.D.2    Wehbie, R.S.3    Kaplan, A.H.4    Nantermet, P.V.5    Klein, C.A.6
  • 7
    • 69249216636 scopus 로고    scopus 로고
    • A strongly transdominant mutation in the human immunodeficiency virus type 1 gag gene defines an Achilles heel in the virus life cycle
    • Lee SK, Harris J, Swanstrom R (2009) A strongly transdominant mutation in the human immunodeficiency virus type 1 gag gene defines an Achilles heel in the virus life cycle. J Virol 83(17):8536-8543
    • (2009) J Virol , vol.83 , Issue.17 , pp. 8536-8543
    • Lee, S.K.1    Harris, J.2    Swanstrom, R.3
  • 8
    • 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 (2002) Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J Virol 76(11): 5667-5677
    • (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
  • 9
    • 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 (2003) Functional surfaces of the human immunodeficiency virus type 1 capsid protein. J Virol 77(9):5439-5450
    • (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
  • 10
    • 70350771279 scopus 로고    scopus 로고
    • Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function
    • Byeon IJ, Meng X, Jung J, Zhao G, Yang R, Ahn J et al (2009) Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. Cell 139(4):780-790
    • (2009) Cell , vol.139 , Issue.4 , pp. 780-790
    • Byeon, I.J.1    Meng, X.2    Jung, J.3    Zhao, G.4    Yang, R.5    Ahn, J.6
  • 11
    • 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 (2001) 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 75(19):9357-9366
    • (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
  • 12
    • 80355146829 scopus 로고    scopus 로고
    • The interdomain linker region of HIV-1 capsid protein is a critical determinant of proper core assembly and stability
    • Jiang J, Ablan SD, Derebail S, Hercik K, Soheilian F, Thomas JA et al (2011) The interdomain linker region of HIV-1 capsid protein is a critical determinant of proper core assembly and stability. Virology 421(2):253-265
    • (2011) Virology , vol.421 , Issue.2 , pp. 253-265
    • Jiang, J.1    Ablan, S.D.2    Derebail, S.3    Hercik, K.4    Soheilian, F.5    Thomas, J.A.6
  • 13
    • 33846847729 scopus 로고    scopus 로고
    • A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein
    • Tang S, Ablan S, Dueck M, Ayala-Lopez W, Soto B, Caplan M et al (2007) A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein. Virology 359(1):105-115
    • (2007) Virology , vol.359 , Issue.1 , pp. 105-115
    • Tang, S.1    Ablan, S.2    Dueck, M.3    Ayala-Lopez, W.4    Soto, B.5    Caplan, M.6
  • 14
    • 34247135950 scopus 로고    scopus 로고
    • A mutation in alpha helix 3 of CA renders human immunodeficiency virus type 1 cyclosporin A resistant and dependent: Rescue by a second-site substitution in a distal region of CA
    • Yang R, Aiken C (2007) A mutation in alpha helix 3 of CA renders human immunodeficiency virus type 1 cyclosporin A resistant and dependent: rescue by a second-site substitution in a distal region of CA. J Virol 81(8):3749-3756
    • (2007) J Virol , vol.81 , Issue.8 , pp. 3749-3756
    • Yang, R.1    Aiken, C.2
  • 15
    • 84859844937 scopus 로고    scopus 로고
    • Identification of secondsite suppressors of human immunodeficiency virus type 1 CA mutants: Restoration of intracellular activities without correction of intrinsic capsid stability defects
    • Yang R, Shi J, Byeon I-JL, Ahn J, Sheehan JH, Meiler J et al (2012) Identification of secondsite suppressors of human immunodeficiency virus type 1 CA mutants: restoration of intracellular activities without correction of intrinsic capsid stability defects. Retrovirology 9:30
    • (2012) Retrovirology , vol.9 , pp. 30
    • Yang, R.1    Shi, J.2    I-Jl, B.3    Ahn, J.4    Sheehan, J.H.5    Meiler, J.6
  • 16
    • 0024519430 scopus 로고
    • Human immunodeficiency virus 1 reverse transcriptase. Template binding, processivity, strand displacement synthesis, and template switching
    • Huber HE, McCoy JM, Seehra JS, Richardson CC (1989) Human immunodeficiency virus 1 reverse transcriptase. Template binding, processivity, strand displacement synthesis, and template switching. J Biol Chem 264(8):4669-4678
    • (1989) J Biol Chem , vol.264 , Issue.8 , pp. 4669-4678
    • Huber, H.E.1    McCoy, J.M.2    Seehra, J.S.3    Richardson, C.C.4
  • 17
    • 0024438889 scopus 로고
    • Specificity and mechanism of error-prone replication by human immunodeficiency virus-1 reverse transcriptase
    • Bebenek K, Abbotts J, Roberts JD, Wilson SH, Kunkel TA (1989) Specificity and mechanism of error-prone replication by human immunodeficiency virus-1 reverse transcriptase. J Biol Chem 264(28):16948-16956
    • (1989) J Biol Chem , vol.264 , Issue.28 , pp. 16948-16956
    • Bebenek, K.1    Abbotts, J.2    Roberts, J.D.3    Wilson, S.H.4    Kunkel, T.A.5
  • 18
    • 78650042418 scopus 로고    scopus 로고
    • HIV capsid is a tractable target for small molecule therapeutic intervention
    • Blair WS, Pickford C, Irving SL, Brown DG, Anderson M, Bazin R et al (2010) HIV capsid is a tractable target for small molecule therapeutic intervention. PLoS Pathog 6(12):e1001220
    • (2010) PLoS Pathog , vol.6 , Issue.12 , pp. e1001220
    • Blair, W.S.1    Pickford, C.2    Irving, S.L.3    Brown, D.G.4    Anderson, M.5    Bazin, R.6
  • 19
    • 84865063652 scopus 로고    scopus 로고
    • Inhibiting early-stage events in HIV-1 replication by small-molecule targeting of the HIV-1 capsid
    • Kortagere S, Madani N, Mankowski MK, Schon A, Zentner I, Swaminathan G et al (2012) Inhibiting early-stage events in HIV-1 replication by small-molecule targeting of the HIV-1 capsid. J Virol 86(16):8472-8481
    • (2012) J Virol , vol.86 , Issue.16 , pp. 8472-8481
    • Kortagere, S.1    Madani, N.2    Mankowski, M.K.3    Schon, A.4    Zentner, I.5    Swaminathan, G.6
  • 20
    • 78650064115 scopus 로고    scopus 로고
    • Small-molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization
    • Shi J, Zhou J, Shah VB, Aiken C, Whitby K (2011) Small-molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization. J Virol 85(1): 542-549
    • (2011) J Virol , vol.85 , Issue.1 , pp. 542-549
    • Shi, J.1    Zhou, J.2    Shah, V.B.3    Aiken, C.4    Whitby, K.5
  • 21
    • 33644806492 scopus 로고    scopus 로고
    • The mechanism of HIV-1 core assembly: Insights from three-dimensional reconstructions of authentic virions
    • Briggs JA, Grunewald K, Glass B, Forster F, Krausslich HG, Fuller SD (2006) The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions. Structure 14(1):15-20
    • (2006) Structure , vol.14 , Issue.1 , pp. 15-20
    • Briggs, J.A.1    Grunewald, K.2    Glass, B.3    Forster, F.4    Krausslich, H.G.5    Fuller, S.D.6
  • 23
    • 34247185183 scopus 로고    scopus 로고
    • Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells
    • Wright ER, Schooler JB, Ding HJ, Kieffer C, Fillmore C, Sundquist WI et al (2007) Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells. EMBO J 26(8):2218-2226
    • (2007) EMBO J , vol.26 , Issue.8 , pp. 2218-2226
    • Wright, E.R.1    Schooler, J.B.2    Ding, H.J.3    Kieffer, C.4    Fillmore, C.5    Sundquist, W.I.6
  • 25
    • 80051756121 scopus 로고    scopus 로고
    • Design of in vitro symmetric complexes and analysis by hybrid methods reveal mechanisms of HIV capsid assembly
    • Yeager M (2011) Design of in vitro symmetric complexes and analysis by hybrid methods reveal mechanisms of HIV capsid assembly. J Mol Biol 410(4):534-552
    • (2011) J Mol Biol , vol.410 , Issue.4 , pp. 534-552
    • Yeager, M.1
  • 27
    • 78751670547 scopus 로고    scopus 로고
    • Atomic-level modelling of the HIV capsid
    • Pornillos O, Ganser-Pornillos BK, Yeager M (2011) Atomic-level modelling of the HIV capsid. Nature 469(7330):424-427
    • (2011) Nature , vol.469 , Issue.7330 , pp. 424-427
    • Pornillos, O.1    Ganser-Pornillos, B.K.2    Yeager, M.3
  • 28
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • Li S, Hill CP, Sundquist WI, Finch JT (2000) Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature 407:409-413
    • (2000) Nature , vol.407 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 29
    • 84866149401 scopus 로고    scopus 로고
    • Protease cleavage leads to formation of mature trimer interface in HIV-1 capsid
    • Meng X, Zhao G, Yufenyuy E, Ke D, Ning J, Delucia M et al (2012) Protease cleavage leads to formation of mature trimer interface in HIV-1 capsid. PLoS Pathog 8(8):e1002886
    • (2012) PLoS Pathog , vol.8 , Issue.8 , pp. e1002886
    • Meng, X.1    Zhao, G.2    Yufenyuy, E.3    Ke, D.4    Ning, J.5    Delucia, M.6
  • 31
    • 78951488338 scopus 로고    scopus 로고
    • HIV-1 maturation inhibitor bevirimat stabilizes the immature Gag lattice
    • Keller PW, Adamson CS, Heymann JB, Freed EO, Steven AC (2011) HIV-1 maturation inhibitor bevirimat stabilizes the immature Gag lattice. J Virol 85(4):1420-1428
    • (2011) J Virol , vol.85 , Issue.4 , pp. 1420-1428
    • Keller, P.W.1    Adamson, C.S.2    Heymann, J.B.3    Freed, E.O.4    Steven, A.C.5
  • 32
    • 0346688636 scopus 로고    scopus 로고
    • Small-molecule inhibition of human immunodeficiency virus type 1 replication by specific targeting of thefinal step of virion maturation
    • Zhou J, Yuan X, Dismuke D, Forshey BM, Lundquist C, Lee KH et al (2004) Small-molecule inhibition of human immunodeficiency virus type 1 replication by specific targeting of thefinal step of virion maturation. J Virol 78(2):922-929
    • (2004) J Virol , vol.78 , Issue.2 , pp. 922-929
    • Zhou, J.1    Yuan, X.2    Dismuke, D.3    Forshey, B.M.4    Lundquist, C.5    Lee, K.H.6
  • 33
    • 0031925586 scopus 로고    scopus 로고
    • Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites
    • Wiegers K, Rutter G, Kottler H, Tessmer U, Hohenberg H, Krausslich H-G (1998) Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites. J Virol 72(4):2846-2854
    • (1998) J Virol , vol.72 , Issue.4 , pp. 2846-2854
    • Wiegers, K.1    Rutter, G.2    Kottler, H.3    Tessmer, U.4    Hohenberg, H.5    Krausslich, H.-G.6
  • 34
    • 0032536896 scopus 로고    scopus 로고
    • Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly
    • von Schwedler UK, Stemmler TL, Sundquist WI (1998) Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly. EMBO J 17:1555
    • (1998) EMBO J , vol.17 , pp. 1555
    • Von Schwedler, U.K.1    Stemmler, T.L.2    Sundquist, W.I.3
  • 35
    • 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 H-G (1998) N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles. J Virol 72:4798-4810
    • (1998) J Virol , vol.72 , pp. 4798-4810
    • Gross, I.1    Hohenberg, H.2    Huckhagel, C.3    Krausslich, H.-G.4
  • 36
    • 52049096820 scopus 로고    scopus 로고
    • The effect of point mutations within the N-terminal domain of Mason-Pfizer monkey virus capsid protein on virus core assembly and infectivity
    • Wildova M, Hadravova R, Stokrova J, Krizova I, Ruml T, Hunter E et al (2008) The effect of point mutations within the N-terminal domain of Mason-Pfizer monkey virus capsid protein on virus core assembly and infectivity. Virology 380(1):157-163
    • (2008) Virology , vol.380 , Issue.1 , pp. 157-163
    • Wildova, M.1    Hadravova, R.2    Stokrova, J.3    Krizova, I.4    Ruml, T.5    Hunter, E.6
  • 37
    • 80051768952 scopus 로고    scopus 로고
    • A retroviral chimeric capsid protein reveals the role of the N-terminal beta-hairpin in mature core assembly
    • Cortines JR, Monroe EB, Kang S, Prevelige PE Jr (2011) A retroviral chimeric capsid protein reveals the role of the N-terminal beta-hairpin in mature core assembly. J Mol Biol 410(4): 641-652
    • (2011) J Mol Biol , vol.410 , Issue.4 , pp. 641-652
    • Cortines, J.R.1    Monroe, E.B.2    Kang, S.3    Prevelige, P.E.4
  • 38
    • 0036294666 scopus 로고    scopus 로고
    • Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
    • Tang C, Ndassa Y, Summers MF (2002) Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. Nat Struct Biol 9(7):537-543
    • (2002) Nat Struct Biol , vol.9 , Issue.7 , pp. 537-543
    • Tang, C.1    Ndassa, Y.2    Summers, M.F.3
  • 40
    • 4644301808 scopus 로고    scopus 로고
    • High-resolution structure of a retroviral capsid hexameric amino-terminal domain
    • Mortuza GB, Haire LF, Stevens A, Smerdon SJ, Stoye JP, Taylor IA (2004) High-resolution structure of a retroviral capsid hexameric amino-terminal domain. Nature 431(7007): 481-485
    • (2004) Nature , vol.431 , Issue.7007 , pp. 481-485
    • Mortuza, G.B.1    Haire, L.F.2    Stevens, A.3    Smerdon, S.J.4    Stoye, J.P.5    Taylor, I.A.6
  • 42
    • 84863982480 scopus 로고    scopus 로고
    • Structure of the immature retroviral capsid at 8 A resolution by cryo-electron microscopy
    • Bharat TA, Davey NE, Ulbrich P, Riches JD, de Marco A, Rumlova M et al (2012) Structure of the immature retroviral capsid at 8 A resolution by cryo-electron microscopy. Nature 487(7407):385-389
    • (2012) Nature , vol.487 , Issue.7407 , pp. 385-389
    • Bharat, T.A.1    Davey, N.E.2    Ulbrich, P.3    Riches, J.D.4    De Marco, A.5    Rumlova, M.6
  • 43
    • 2642607039 scopus 로고    scopus 로고
    • A putative a-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 Gag precursor is crucial for viral particle assembly
    • Accola MA, Hoglund S, Gottlinger HG (1998) A putative a-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 Gag precursor is crucial for viral particle assembly. J Virol 72(3):2072-2078
    • (1998) J Virol , vol.72 , Issue.3 , pp. 2072-2078
    • Accola, M.A.1    Hoglund, S.2    Gottlinger, H.G.3
  • 44
    • 0036828096 scopus 로고    scopus 로고
    • Characterization of a putative alpha-helix across the capsid-SP1 boundary that is critical for the multimerization of human immunodeficiency virus type 1 gag
    • Liang C, Hu J, Russell RS, Roldan A, Kleiman L, Wainberg MA (2002) Characterization of a putative alpha-helix across the capsid-SP1 boundary that is critical for the multimerization of human immunodeficiency virus type 1 gag. J Virol 76(22):11729-11737
    • (2002) J Virol , vol.76 , Issue.22 , pp. 11729-11737
    • Liang, C.1    Hu, J.2    Russell, R.S.3    Roldan, A.4    Kleiman, L.5    Wainberg, M.A.6
  • 45
    • 13244256815 scopus 로고    scopus 로고
    • Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: Implications for particle assembly and RNA packaging
    • Morellet N, Druillennec S, Lenoir C, Bouaziz S, Roques BP (2005) Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packaging. Protein Sci 14(2):375-386
    • (2005) Protein Sci , vol.14 , Issue.2 , pp. 375-386
    • Morellet, N.1    Druillennec, S.2    Lenoir, C.3    Bouaziz, S.4    Roques, B.P.5
  • 46
    • 79955399123 scopus 로고    scopus 로고
    • On the role of the SP1 domain in HIV-1 particle assembly: A molecular switch?
    • Datta SA, Temeselew LG, Crist RM, Soheilian F, Kamata A, Mirro J et al (2011) On the role of the SP1 domain in HIV-1 particle assembly: A molecular switch? J Virol 85(9):4111-4121
    • (2011) J Virol , vol.85 , Issue.9 , pp. 4111-4121
    • Datta, S.A.1    Temeselew, L.G.2    Crist, R.M.3    Soheilian, F.4    Kamata, A.5    Mirro, J.6
  • 47
    • 0036784575 scopus 로고    scopus 로고
    • Replacement of the P1 amino acid of human immunodeficiency virus type 1 Gag processing sites can inhibit or enhance the rate of cleavage by the viral protease
    • Pettit SC, Henderson GJ, Schiffer CA, Swanstrom R (2002) Replacement of the P1 amino acid of human immunodeficiency virus type 1 Gag processing sites can inhibit or enhance the rate of cleavage by the viral protease. J Virol 76(20):10226-10233
    • (2002) J Virol , vol.76 , Issue.20 , pp. 10226-10233
    • Pettit, S.C.1    Henderson, G.J.2    Schiffer, C.A.3    Swanstrom, R.4
  • 48
    • 0034625320 scopus 로고    scopus 로고
    • Large conformational changes in the maturation of a simple RNA virus, nudaurelia capensis omega virus (NomegaV)
    • Canady MA, Tihova M, Hanzlik TN, Johnson JE, Yeager M (2000) Large conformational changes in the maturation of a simple RNA virus, nudaurelia capensis omega virus (NomegaV). J Mol Biol 299(3):573-584
    • (2000) J Mol Biol , vol.299 , Issue.3 , pp. 573-584
    • Canady, M.A.1    Tihova, M.2    Hanzlik, T.N.3    Johnson, J.E.4    Yeager, M.5
  • 49
    • 41349112304 scopus 로고    scopus 로고
    • Structure of the immature dengue virus at low pH primes proteolytic maturation
    • Yu IM, Zhang W, Holdaway HA, Li L, Kostyuchenko VA, Chipman PR et al (2008) Structure of the immature dengue virus at low pH primes proteolytic maturation. Science 319(5871): 1834-1837
    • (2008) Science , vol.319 , Issue.5871 , pp. 1834-1837
    • Yu, I.M.1    Zhang, W.2    Holdaway, H.A.3    Li, L.4    Kostyuchenko, V.A.5    Chipman, P.R.6
  • 50
    • 0035957688 scopus 로고    scopus 로고
    • Virus maturation involving large subunit rotations and local refolding
    • Conway JF, Wikoff WR, Cheng N, Duda RL, Hendrix RW, Johnson JE et al (2001) Virus maturation involving large subunit rotations and local refolding. Science 292(5517):744-748
    • (2001) Science , vol.292 , Issue.5517 , pp. 744-748
    • Conway, J.F.1    Wikoff, W.R.2    Cheng, N.3    Duda, R.L.4    Hendrix, R.W.5    Johnson, J.E.6
  • 53
    • 0036091735 scopus 로고    scopus 로고
    • Rous sarcoma virus Gag protein-oligonucleotide interaction suggests a critical role for protein dimer formation in assembly
    • Ma YM, Vogt VM (2002) Rous sarcoma virus Gag protein-oligonucleotide interaction suggests a critical role for protein dimer formation in assembly. J Virol 76(11):5452-5462
    • (2002) J Virol , vol.76 , Issue.11 , pp. 5452-5462
    • Ma, Y.M.1    Vogt, V.M.2
  • 54
    • 0028338652 scopus 로고
    • Characterization of human immunodeficiency virus type 1 dimeric RNA from wild-type and protease-defective virions
    • Fu W, Gorelick RJ, Rein A (1994) Characterization of human immunodeficiency virus type 1 dimeric RNA from wild-type and protease-defective virions. J Virol 68(8):5013-5018
    • (1994) J Virol , vol.68 , Issue.8 , pp. 5013-5018
    • Fu, W.1    Gorelick, R.J.2    Rein, A.3
  • 55
    • 0034856077 scopus 로고    scopus 로고
    • Proteolytic processing of the p2/nucleocapsid cleavage site is critical for human immunodefi-ciency virus type 1 RNA dimer maturation
    • Shehu-Xhilaga M, Kraeusslich HG, Pettit S, Swanstrom R, Lee JY, Marshall JA et al (2001) Proteolytic processing of the p2/nucleocapsid cleavage site is critical for human immunodefi-ciency virus type 1 RNA dimer maturation. J Virol 75(19):9156-9164
    • (2001) J Virol , vol.75 , Issue.19 , pp. 9156-9164
    • Shehu-Xhilaga, M.1    Kraeusslich, H.G.2    Pettit, S.3    Swanstrom, R.4    Lee, J.Y.5    Marshall, J.A.6
  • 56
    • 78751652821 scopus 로고    scopus 로고
    • Nucleic acid chaperone activity of retroviral Gag proteins
    • Rein A (2010) Nucleic acid chaperone activity of retroviral Gag proteins. RNA Biol 7(6):700-705
    • (2010) RNA Biol , vol.7 , Issue.6 , pp. 700-705
    • Rein, A.1
  • 57
    • 0033761894 scopus 로고    scopus 로고
    • Roles of Pr55(gag) and NCp7 in tRNA(3)(Lys) genomic placement and the initiation step of reverse transcription in human immunodeficiency virus type 1
    • Cen S, Khorchid A, Gabor J, Rong L, Wainberg MA, Kleiman L (2000) Roles of Pr55(gag) and NCp7 in tRNA(3)(Lys) genomic placement and the initiation step of reverse transcription in human immunodeficiency virus type 1. J Virol 74(22):10796-10800
    • (2000) J Virol , vol.74 , Issue.22 , pp. 10796-10800
    • Cen, S.1    Khorchid, A.2    Gabor, J.3    Rong, L.4    Wainberg, M.A.5    Kleiman, L.6
  • 59
    • 0029857253 scopus 로고    scopus 로고
    • Direct interaction between the envelope and matrix proteins of HIV-1
    • Cosson P (1996) Direct interaction between the envelope and matrix proteins of HIV-1. EMBO J 15(21):5783-5788
    • (1996) EMBO J , vol.15 , Issue.21 , pp. 5783-5788
    • Cosson, P.1
  • 60
    • 0034026083 scopus 로고    scopus 로고
    • Genetic evidence for an interaction between human immunodeficiency virus type 1 matrix and alpha-helix 2 of the gp41 cytoplasmic tail
    • Murakami T, Freed EO (2000) Genetic evidence for an interaction between human immunodeficiency virus type 1 matrix and alpha-helix 2 of the gp41 cytoplasmic tail. J Virol 74(8): 3548-3554
    • (2000) J Virol , vol.74 , Issue.8 , pp. 3548-3554
    • Murakami, T.1    Freed, E.O.2
  • 61
    • 0029655514 scopus 로고    scopus 로고
    • Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation
    • Freed EO, Martin MA (1996) Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation. J Virol 70:341-351
    • (1996) J Virol , vol.70 , pp. 341-351
    • Freed, E.O.1    Martin, M.A.2
  • 62
    • 0034602736 scopus 로고    scopus 로고
    • The long cytoplasmic tail of gp41 is required in a cell typedependent manner for HIV-1 envelope glycoprotein incorporation into virions
    • Murakami T, Freed EO (2000) The long cytoplasmic tail of gp41 is required in a cell typedependent manner for HIV-1 envelope glycoprotein incorporation into virions. Proc Natl Acad Sci USA 97(1):343-348
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.1 , pp. 343-348
    • Murakami, T.1    Freed, E.O.2
  • 63
    • 0033809342 scopus 로고    scopus 로고
    • Evidence for a stable interaction of gp41 with Pr55(Gag) in immature human immunodeficiency virus type 1 particles
    • Wyma DJ, Kotov A, Aiken C (2000) Evidence for a stable interaction of gp41 with Pr55(Gag) in immature human immunodeficiency virus type 1 particles. J Virol 74(20):9381-9387
    • (2000) J Virol , vol.74 , Issue.20 , pp. 9381-9387
    • Wyma, D.J.1    Kotov, A.2    Aiken, C.3
  • 64
    • 0347319099 scopus 로고    scopus 로고
    • Regulation of human immunodeficiency virus type 1 Env-mediated membrane fusion by viral protease activity
    • Murakami T, Ablan S, Freed EO, Tanaka Y (2004) Regulation of human immunodeficiency virus type 1 Env-mediated membrane fusion by viral protease activity. J Virol 78(2): 1026-1031
    • (2004) J Virol , vol.78 , Issue.2 , pp. 1026-1031
    • Murakami, T.1    Ablan, S.2    Freed, E.O.3    Tanaka, Y.4
  • 65
    • 1842457792 scopus 로고    scopus 로고
    • Coupling of human immunodeficiency virus type 1 fusion to virion maturation: A novel role of the gp41 cytoplasmic tail
    • Wyma DJ, Jiang J, Shi J, Zhou J, Lineberger JE, Miller MD et al (2004) Coupling of human immunodeficiency virus type 1 fusion to virion maturation: A novel role of the gp41 cytoplasmic tail. J Virol 78(7):3429-3435
    • (2004) J Virol , vol.78 , Issue.7 , pp. 3429-3435
    • Wyma, D.J.1    Jiang, J.2    Shi, J.3    Zhou, J.4    Lineberger, J.E.5    Miller, M.D.6
  • 67
    • 80053440098 scopus 로고    scopus 로고
    • Maturation-induced cloaking of neutralization epitopes on HIV-1 particles
    • Joyner AS, Willis JR, Crowe JE Jr, Aiken C (2011) Maturation-induced cloaking of neutralization epitopes on HIV-1 particles. PLoS Pathog 7(9):e1002234
    • (2011) PLoS Pathog , vol.7 , Issue.9 , pp. e1002234
    • Joyner, A.S.1    Willis, J.R.2    Crowe, J.E.3    Aiken, C.4
  • 68
    • 84867827687 scopus 로고    scopus 로고
    • Maturationdependent HIV-1 surface protein redistribution revealed byfluorescence nanoscopy
    • Chojnacki J, Staudt T, Glass B, Bingen P, Engelhardt J, Anders M et al (2012) Maturationdependent HIV-1 surface protein redistribution revealed byfluorescence nanoscopy. Science 338(6106):524-528
    • (2012) Science , vol.338 , Issue.6106 , pp. 524-528
    • Chojnacki, J.1    Staudt, T.2    Glass, B.3    Bingen, P.4    Engelhardt, J.5    Anders, M.6
  • 69
    • 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 (2003) PA-457: A potent HIV inhibitor that disrupts core condensation by targeting a late step in Gag processing. Proc Natl Acad Sci USA 100(23):13555-13560
    • (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
  • 70
    • 77950929797 scopus 로고    scopus 로고
    • Polymorphisms in Gag spacer peptide 1 confer varying levels of resistance to the HIV-1 maturation inhibitor bevirimat
    • Adamson CS, Sakalian M, Salzwedel K, Freed EO (2010) Polymorphisms in Gag spacer peptide 1 confer varying levels of resistance to the HIV-1 maturation inhibitor bevirimat. Retrovirology 7:36
    • (2010) Retrovirology , vol.7 , pp. 36
    • Adamson, C.S.1    Sakalian, M.2    Salzwedel, K.3    Freed, E.O.4
  • 71
    • 33750695698 scopus 로고    scopus 로고
    • In vitro resistance to the human immunodeficiency virus type 1 maturation inhibitor PA-457 (Bevirimat)
    • Adamson CS, Ablan SD, Boeras I, Goila-Gaur R, Soheilian F, Nagashima K et al (2006) In vitro resistance to the human immunodeficiency virus type 1 maturation inhibitor PA-457 (Bevirimat). J Virol 80(22):10957-10971
    • (2006) J Virol , vol.80 , Issue.22 , pp. 10957-10971
    • Adamson, C.S.1    Ablan, S.D.2    Boeras, I.3    Goila-Gaur, R.4    Soheilian, F.5    Nagashima, K.6
  • 72
    • 82755190460 scopus 로고    scopus 로고
    • The prototype HIV-1 maturation inhibitor, bevirimat, binds to the CA-SP1 cleavage site in immature Gag particles
    • Nguyen AT, Feasley CL, Jackson KW, Nitz TJ, Salzwedel K, Air GM et al (2011) The prototype HIV-1 maturation inhibitor, bevirimat, binds to the CA-SP1 cleavage site in immature Gag particles. Retrovirology 8:101
    • (2011) Retrovirology , vol.8 , pp. 101
    • Nguyen, A.T.1    Feasley, C.L.2    Jackson, K.W.3    Nitz, T.J.4    Salzwedel, K.5    Air, G.M.6
  • 73
    • 71249123121 scopus 로고    scopus 로고
    • New smallmolecule inhibitor class targeting human immunodeficiency virus type 1 virion maturation
    • Blair WS, Cao J, Fok-Seang J, Griffin P, Isaacson J, Jackson RL et al (2009) New smallmolecule inhibitor class targeting human immunodeficiency virus type 1 virion maturation. Antimicrob Agents Chemother 53(12):5080-5087
    • (2009) Antimicrob Agents Chemother , vol.53 , Issue.12 , pp. 5080-5087
    • Blair, W.S.1    Cao, J.2    Fok-Seang, J.3    Griffin, P.4    Isaacson, J.5    Jackson, R.L.6


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