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Volumn 9, Issue , 2012, Pages

Human Immunodeficiency Virus gag and protease: Partners in resistance

Author keywords

Cross resistance; Gag mutations; HIV; Maturation inhibitors; Particle maturation; Protease inhibitors; Resistance

Indexed keywords

AMPRENAVIR; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; ATAZANAVIR; BEVIRIMAT; CA ASSEMBLY INHIBITOR; CA P2 INHIBITOR; DARUNAVIR; FOSAMPRENAVIR; GAG PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE INHIBITOR; INDINAVIR; LOPINAVIR; MATURATION INHIBITOR; MPC 426; MPC 9055; MPI 461359; NELFINAVIR; NONNUCLEOSIDE REVERSE TRANSCRIPTASE INHIBITOR; PA 1050040; PF 46396; POLYPROTEIN; PROTEIN PRECURSOR; RITONAVIR; RNA DIRECTED DNA POLYMERASE INHIBITOR; SAQUINAVIR; TIPRANAVIR; UNCLASSIFIED DRUG; VIVECON; POL PROTEIN;

EID: 84864505786     PISSN: None     EISSN: 17424690     Source Type: Journal    
DOI: 10.1186/1742-4690-9-63     Document Type: Review
Times cited : (120)

References (127)
  • 1
    • 0023870815 scopus 로고
    • Characterization of ribosomal frameshifting in HIV-1 gag-pol expression
    • 10.1038/331280a0, 2447506
    • Jacks T, Power MD, Masiarz FR, Luciw PA, Barr PJ, Varmus HE. Characterization of ribosomal frameshifting in HIV-1 gag-pol expression. Nature 1988, 331:280-283. 10.1038/331280a0, 2447506.
    • (1988) Nature , vol.331 , pp. 280-283
    • Jacks, T.1    Power, M.D.2    Masiarz, F.R.3    Luciw, P.A.4    Barr, P.J.5    Varmus, H.E.6
  • 2
    • 0036121219 scopus 로고    scopus 로고
    • Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes
    • 10.1016/S0969-2126(02)00720-7, 12005435
    • Prabu-Jeyabalan M, Nalivaika E, Schiffer CA. Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes. Structure 2002, 10:369-381. 10.1016/S0969-2126(02)00720-7, 12005435.
    • (2002) Structure , vol.10 , pp. 369-381
    • Prabu-Jeyabalan, M.1    Nalivaika, E.2    Schiffer, C.A.3
  • 3
    • 1542502945 scopus 로고
    • Activity of purified biosynthetic proteinase of human immunodeficiency virus on natural substrates and synthetic peptides
    • 10.1073/pnas.86.3.807, 286566, 2644644
    • Krausslich HG, Ingraham RH, Skoog MT, Wimmer E, Pallai PV, Carter CA. Activity of purified biosynthetic proteinase of human immunodeficiency virus on natural substrates and synthetic peptides. Proc Natl Acad Sci U S A 1989, 86:807-811. 10.1073/pnas.86.3.807, 286566, 2644644.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , 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
  • 4
    • 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
    • 237265, 7966591
    • Pettit SC, Moody MD, Wehbie RS, Kaplan AH, Nantermet PV, Klein CA, Swanstrom R. The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions. J Virol 1994, 68:8017-8027. 237265, 7966591.
    • (1994) J Virol , vol.68 , 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    Swanstrom, R.7
  • 5
    • 0031925586 scopus 로고    scopus 로고
    • Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites
    • 109729, 9525604
    • Wiegers K, Rutter G, Kottler H, Tessmer U, Hohenberg H, Krausslich HG. Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites. J Virol 1998, 72:2846-2854. 109729, 9525604.
    • (1998) J Virol , vol.72 , pp. 2846-2854
    • Wiegers, K.1    Rutter, G.2    Kottler, H.3    Tessmer, U.4    Hohenberg, H.5    Krausslich, H.G.6
  • 6
    • 27744572130 scopus 로고    scopus 로고
    • Processing sites in the human immunodeficiency virus type 1 (HIV-1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates
    • 10.1186/1742-4690-2-66, 1291402, 16262906
    • Pettit SC, Lindquist JN, Kaplan AH, Swanstrom R. Processing sites in the human immunodeficiency virus type 1 (HIV-1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates. Retrovirology 2005, 2:66. 10.1186/1742-4690-2-66, 1291402, 16262906.
    • (2005) Retrovirology , vol.2 , pp. 66
    • Pettit, S.C.1    Lindquist, J.N.2    Kaplan, A.H.3    Swanstrom, R.4
  • 7
    • 80051739212 scopus 로고    scopus 로고
    • Dynamics of preferential substrate recognition in HIV-1 protease: redefining the substrate envelope
    • 10.1016/j.jmb.2011.03.053, 3139114, 21762811
    • Ozen A, Haliloglu T, Schiffer CA. Dynamics of preferential substrate recognition in HIV-1 protease: redefining the substrate envelope. J Mol Biol 2011, 410:726-744. 10.1016/j.jmb.2011.03.053, 3139114, 21762811.
    • (2011) J Mol Biol , vol.410 , pp. 726-744
    • Ozen, A.1    Haliloglu, T.2    Schiffer, C.A.3
  • 8
    • 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
    • 10.1128/JVI.76.20.10226-10233.2002, 136535, 12239298
    • Pettit SC, Henderson GJ, Schiffer CA, Swanstrom R. 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 2002, 76:10226-10233. 10.1128/JVI.76.20.10226-10233.2002, 136535, 12239298.
    • (2002) J Virol , vol.76 , pp. 10226-10233
    • Pettit, S.C.1    Henderson, G.J.2    Schiffer, C.A.3    Swanstrom, R.4
  • 9
    • 0036310578 scopus 로고    scopus 로고
    • Changes in human immunodeficiency virus type 1 Gag at positions L449 and P453 are linked to I50V protease mutants in vivo and cause reduction of sensitivity to amprenavir and improved viral fitness in vitro
    • 10.1128/JVI.76.15.7398-7406.2002, 136352, 12097552
    • Maguire MF, Guinea R, Griffin P, Macmanus S, Elston RC, Wolfram J, Richards N, Hanlon MH, Porter DJ, Wrin T, Parkin N, Tisdale M, Furfine E, Petropoulos C, Snowden BW, Kleim JP. Changes in human immunodeficiency virus type 1 Gag at positions L449 and P453 are linked to I50V protease mutants in vivo and cause reduction of sensitivity to amprenavir and improved viral fitness in vitro. J Virol 2002, 76:7398-7406. 10.1128/JVI.76.15.7398-7406.2002, 136352, 12097552.
    • (2002) J Virol , vol.76 , pp. 7398-7406
    • Maguire, M.F.1    Guinea, R.2    Griffin, P.3    Macmanus, S.4    Elston, R.C.5    Wolfram, J.6    Richards, N.7    Hanlon, M.H.8    Porter, D.J.9    Wrin, T.10    Parkin, N.11    Tisdale, M.12    Furfine, E.13    Petropoulos, C.14    Snowden, B.W.15    Kleim, J.P.16
  • 11
    • 79953675052 scopus 로고    scopus 로고
    • Within-host co-evolution of Gag P453L and protease D30N/N88D demonstrates virological advantage in a highly protease inhibitor-exposed HIV-1 case
    • 10.1016/j.antiviral.2011.02.004, 21338625
    • Shibata J, Sugiura W, Ode H, Iwatani Y, Sato H, Tsang H, Matsuda M, Hasegawa N, Ren F, Tanaka H. Within-host co-evolution of Gag P453L and protease D30N/N88D demonstrates virological advantage in a highly protease inhibitor-exposed HIV-1 case. Antiviral Res 2011, 90:33-41. 10.1016/j.antiviral.2011.02.004, 21338625.
    • (2011) Antiviral Res , vol.90 , pp. 33-41
    • Shibata, J.1    Sugiura, W.2    Ode, H.3    Iwatani, Y.4    Sato, H.5    Tsang, H.6    Matsuda, M.7    Hasegawa, N.8    Ren, F.9    Tanaka, H.10
  • 12
    • 63449110982 scopus 로고    scopus 로고
    • Gag mutations strongly contribute to HIV-1 resistance to protease inhibitors in highly drug-experienced patients besides compensating for fitness loss
    • 10.1371/journal.ppat.1000345, 2652074, 19300491
    • Dam E, Quercia R, Glass B, Descamps D, Launay O, Duval X, Krausslich HG, Hance AJ, Clavel F. Gag mutations strongly contribute to HIV-1 resistance to protease inhibitors in highly drug-experienced patients besides compensating for fitness loss. PLoS Pathog 2009, 5:e1000345. 10.1371/journal.ppat.1000345, 2652074, 19300491.
    • (2009) PLoS Pathog , vol.5
    • Dam, E.1    Quercia, R.2    Glass, B.3    Descamps, D.4    Launay, O.5    Duval, X.6    Krausslich, H.G.7    Hance, A.J.8    Clavel, F.9
  • 13
    • 84859043686 scopus 로고    scopus 로고
    • Modulation of HIV-1 Gag NC/p1 cleavage efficiency affects protease inhibitor resistance and viral replicative capacity
    • 10.1186/1742-4690-9-29, 3349524, 22462820
    • van Maarseveen NM, Andersson D, Lepsik M, Fun A, Schipper PJ, de Jong D, Boucher CA, Nijhuis M. Modulation of HIV-1 Gag NC/p1 cleavage efficiency affects protease inhibitor resistance and viral replicative capacity. Retrovirology 2012, 9:29. 10.1186/1742-4690-9-29, 3349524, 22462820.
    • (2012) Retrovirology , vol.9 , pp. 29
    • van Maarseveen, N.M.1    Andersson, D.2    Lepsik, M.3    Fun, A.4    Schipper, P.J.5    de Jong, D.6    Boucher, C.A.7    Nijhuis, M.8
  • 16
    • 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
    • 10.1128/JVI.78.16.8477-8485.2004, 479095, 15280456
    • Pettit SC, Everitt LE, Choudhury S, Dunn BM, Kaplan AH. Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism. J Virol 2004, 78:8477-8485. 10.1128/JVI.78.16.8477-8485.2004, 479095, 15280456.
    • (2004) J Virol , vol.78 , pp. 8477-8485
    • Pettit, S.C.1    Everitt, L.E.2    Choudhury, S.3    Dunn, B.M.4    Kaplan, A.H.5
  • 17
    • 53349152834 scopus 로고    scopus 로고
    • Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease
    • 10.1038/nature07342, 2798589, 18833280
    • Tang C, Louis JM, Aniana A, Suh JY, Clore GM. Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease. Nature 2008, 455:693-696. 10.1038/nature07342, 2798589, 18833280.
    • (2008) Nature , vol.455 , pp. 693-696
    • Tang, C.1    Louis, J.M.2    Aniana, A.3    Suh, J.Y.4    Clore, G.M.5
  • 18
    • 0025790338 scopus 로고
    • Antiviral properties of Ro 31-8959, an inhibitor of human immunodeficiency virus (HIV) proteinase
    • 10.1016/0166-3542(91)90045-S, 1810306
    • Craig JC, Duncan IB, Hockley D, Grief C, Roberts NA, Mills JS. Antiviral properties of Ro 31-8959, an inhibitor of human immunodeficiency virus (HIV) proteinase. Antiviral Res 1991, 16:295-305. 10.1016/0166-3542(91)90045-S, 1810306.
    • (1991) Antiviral Res , vol.16 , pp. 295-305
    • Craig, J.C.1    Duncan, I.B.2    Hockley, D.3    Grief, C.4    Roberts, N.A.5    Mills, J.S.6
  • 20
    • 0029092503 scopus 로고
    • In vitro selection and characterization of human immunodeficiency virus type 1 (HIV-1) isolates with reduced sensitivity to hydroxyethylamino sulfonamide inhibitors of HIV-1 aspartyl protease
    • 189353, 7636964
    • Partaledis JA, Yamaguchi K, Tisdale M, Blair EE, Falcione C, Maschera B, Myers RE, Pazhanisamy S, Futer O, Cullinan AB, et al. In vitro selection and characterization of human immunodeficiency virus type 1 (HIV-1) isolates with reduced sensitivity to hydroxyethylamino sulfonamide inhibitors of HIV-1 aspartyl protease. J Virol 1995, 69:5228-5235. 189353, 7636964.
    • (1995) J Virol , vol.69 , pp. 5228-5235
    • Partaledis, J.A.1    Yamaguchi, K.2    Tisdale, M.3    Blair, E.E.4    Falcione, C.5    Maschera, B.6    Myers, R.E.7    Pazhanisamy, S.8    Futer, O.9    Cullinan, A.B.10
  • 24
    • 0033931167 scopus 로고    scopus 로고
    • BMS-232632, a highly potent human immunodeficiency virus protease inhibitor that can be used in combination with other available antiretroviral agents
    • 10.1128/AAC.44.8.2093-2099.2000, 90019, 10898681
    • Robinson BS, Riccardi KA, Gong YF, Guo Q, Stock DA, Blair WS, Terry BJ, Deminie CA, Djang F, Colonno RJ, Lin PF. BMS-232632, a highly potent human immunodeficiency virus protease inhibitor that can be used in combination with other available antiretroviral agents. Antimicrob Agents Chemother 2000, 44:2093-2099. 10.1128/AAC.44.8.2093-2099.2000, 90019, 10898681.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 2093-2099
    • Robinson, B.S.1    Riccardi, K.A.2    Gong, Y.F.3    Guo, Q.4    Stock, D.A.5    Blair, W.S.6    Terry, B.J.7    Deminie, C.A.8    Djang, F.9    Colonno, R.J.10    Lin, P.F.11
  • 28
    • 79959371401 scopus 로고    scopus 로고
    • Inhibition of autoprocessing of natural variants and multidrug resistant mutant precursors of HIV-1 protease by clinical inhibitors
    • 10.1073/pnas.1102278108, 3107318, 21576495
    • Louis JM, Aniana A, Weber IT, Sayer JM. Inhibition of autoprocessing of natural variants and multidrug resistant mutant precursors of HIV-1 protease by clinical inhibitors. Proc Natl Acad Sci U S A 2011, 108:9072-9077. 10.1073/pnas.1102278108, 3107318, 21576495.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 9072-9077
    • Louis, J.M.1    Aniana, A.2    Weber, I.T.3    Sayer, J.M.4
  • 29
    • 84862551062 scopus 로고    scopus 로고
    • Activity of Human Immunodeficiency Virus Type 1 Protease Inhibitors against the Initial Autocleavage in Gag-Pol Polyprotein Processing
    • Davis DA, Soule EE, Davidoff KS, Daniels SI, Naiman NE, Yarchoan R. Activity of Human Immunodeficiency Virus Type 1 Protease Inhibitors against the Initial Autocleavage in Gag-Pol Polyprotein Processing. Antimicrob Agents Chemother 2012, 56:3620-3628.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 3620-3628
    • Davis, D.A.1    Soule, E.E.2    Davidoff, K.S.3    Daniels, S.I.4    Naiman, N.E.5    Yarchoan, R.6
  • 30
    • 2642709177 scopus 로고    scopus 로고
    • Declining morbidity and mortality among patients with advanced human immunodeficiency virus infection. HIV Outpatient Study Investigators
    • 10.1056/NEJM199803263381301, 9516219
    • Palella FJ, Delaney KM, Moorman AC, Loveless MO, Fuhrer J, Satten GA, Aschman DJ, Holmberg SD. Declining morbidity and mortality among patients with advanced human immunodeficiency virus infection. HIV Outpatient Study Investigators. N Engl J Med 1998, 338:853-860. 10.1056/NEJM199803263381301, 9516219.
    • (1998) N Engl J Med , vol.338 , pp. 853-860
    • Palella, F.J.1    Delaney, K.M.2    Moorman, A.C.3    Loveless, M.O.4    Fuhrer, J.5    Satten, G.A.6    Aschman, D.J.7    Holmberg, S.D.8
  • 32
    • 0035717630 scopus 로고    scopus 로고
    • Combination of protease inhibitors for the treatment of HIV-1-infected patients: a review of pharmacokinetics and clinical experience
    • van Heeswijk RP, Veldkamp A, Mulder JW, Meenhorst PL, Lange JM, Beijnen JH, Hoetelmans RM. Combination of protease inhibitors for the treatment of HIV-1-infected patients: a review of pharmacokinetics and clinical experience. Antivir Ther 2001, 6:201-229.
    • (2001) Antivir Ther , vol.6 , pp. 201-229
    • van Heeswijk, R.P.1    Veldkamp, A.2    Mulder, J.W.3    Meenhorst, P.L.4    Lange, J.M.5    Beijnen, J.H.6    Hoetelmans, R.M.7
  • 33
    • 0034623020 scopus 로고    scopus 로고
    • Tipranavir inhibits broadly protease inhibitor-resistant HIV-1 clinical samples
    • 10.1097/00002030-200009080-00009, 10997398
    • Larder BA, Hertogs K, Bloor S, van den Eynde CH, DeCian W, Wang Y, Freimuth WW, Tarpley G. Tipranavir inhibits broadly protease inhibitor-resistant HIV-1 clinical samples. AIDS 2000, 14:1943-1948. 10.1097/00002030-200009080-00009, 10997398.
    • (2000) AIDS , vol.14 , pp. 1943-1948
    • Larder, B.A.1    Hertogs, K.2    Bloor, S.3    van den Eynde, C.H.4    DeCian, W.5    Wang, Y.6    Freimuth, W.W.7    Tarpley, G.8
  • 36
    • 19544386471 scopus 로고    scopus 로고
    • TMC114, a novel human immunodeficiency virus type 1 protease inhibitor active against protease inhibitor-resistant viruses, including a broad range of clinical isolates
    • 10.1128/AAC.49.6.2314-2321.2005, 1140553, 15917527
    • De Meyer S, Azijn H, Surleraux D, Jochmans D, Tahri A, Pauwels R, Wigerinck P, de Bethune MP. TMC114, a novel human immunodeficiency virus type 1 protease inhibitor active against protease inhibitor-resistant viruses, including a broad range of clinical isolates. Antimicrob Agents Chemother 2005, 49:2314-2321. 10.1128/AAC.49.6.2314-2321.2005, 1140553, 15917527.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 2314-2321
    • De Meyer, S.1    Azijn, H.2    Surleraux, D.3    Jochmans, D.4    Tahri, A.5    Pauwels, R.6    Wigerinck, P.7    de Bethune, M.P.8
  • 37
    • 33646043172 scopus 로고    scopus 로고
    • Co-evolution of nelfinavir-resistant HIV-1 protease and the p1-p6 substrate
    • 10.1016/j.virol.2005.11.049, 16430939
    • Kolli M, Lastere S, Schiffer CA. Co-evolution of nelfinavir-resistant HIV-1 protease and the p1-p6 substrate. Virology 2006, 347:405-409. 10.1016/j.virol.2005.11.049, 16430939.
    • (2006) Virology , vol.347 , pp. 405-409
    • Kolli, M.1    Lastere, S.2    Schiffer, C.A.3
  • 38
    • 33645227102 scopus 로고    scopus 로고
    • Mechanism of substrate recognition by drug-resistant human immunodeficiency virus type 1 protease variants revealed by a novel structural intermediate
    • 10.1128/JVI.80.7.3607-3616.2006, 1440387, 16537628
    • Prabu-Jeyabalan M, Nalivaika EA, Romano K, Schiffer CA. Mechanism of substrate recognition by drug-resistant human immunodeficiency virus type 1 protease variants revealed by a novel structural intermediate. J Virol 2006, 80:3607-3616. 10.1128/JVI.80.7.3607-3616.2006, 1440387, 16537628.
    • (2006) J Virol , vol.80 , pp. 3607-3616
    • Prabu-Jeyabalan, M.1    Nalivaika, E.A.2    Romano, K.3    Schiffer, C.A.4
  • 39
    • 77951484077 scopus 로고    scopus 로고
    • Evaluating the substrate-envelope hypothesis: structural analysis of novel HIV-1 protease inhibitors designed to be robust against drug resistance
    • 10.1128/JVI.02531-09, 2863851, 20237088
    • Nalam MN, Ali A, Altman MD, Reddy GS, Chellappan S, Kairys V, Ozen A, Cao H, Gilson MK, Tidor B, Rana TM, Schiffer CA. Evaluating the substrate-envelope hypothesis: structural analysis of novel HIV-1 protease inhibitors designed to be robust against drug resistance. J Virol 2010, 84:5368-5378. 10.1128/JVI.02531-09, 2863851, 20237088.
    • (2010) J Virol , vol.84 , pp. 5368-5378
    • Nalam, M.N.1    Ali, A.2    Altman, M.D.3    Reddy, G.S.4    Chellappan, S.5    Kairys, V.6    Ozen, A.7    Cao, H.8    Gilson, M.K.9    Tidor, B.10    Rana, T.M.11    Schiffer, C.A.12
  • 40
    • 0029151345 scopus 로고
    • Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure
    • 10.1021/bi00029a002, 7626598
    • Gulnik SV, Suvorov LI, Liu B, Yu B, Anderson B, Mitsuya H, Erickson JW. Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure. Biochemistry 1995, 34:9282-9287. 10.1021/bi00029a002, 7626598.
    • (1995) Biochemistry , vol.34 , pp. 9282-9287
    • Gulnik, S.V.1    Suvorov, L.I.2    Liu, B.3    Yu, B.4    Anderson, B.5    Mitsuya, H.6    Erickson, J.W.7
  • 41
    • 0031015475 scopus 로고    scopus 로고
    • Impaired fitness of human immunodeficiency virus type 1 variants with high-level resistance to protease inhibitors
    • 191160, 8995629
    • Croteau G, Doyon L, Thibeault D, McKercher G, Pilote L, Lamarre D. Impaired fitness of human immunodeficiency virus type 1 variants with high-level resistance to protease inhibitors. J Virol 1997, 71:1089-1096. 191160, 8995629.
    • (1997) J Virol , vol.71 , pp. 1089-1096
    • Croteau, G.1    Doyon, L.2    Thibeault, D.3    McKercher, G.4    Pilote, L.5    Lamarre, D.6
  • 43
    • 0030065565 scopus 로고    scopus 로고
    • Resistance of human immunodeficiency virus type 1 to protease inhibitors: selection of resistance mutations in the presence and absence of the drug
    • Borman AM, Paulous S, Clavel F. Resistance of human immunodeficiency virus type 1 to protease inhibitors: selection of resistance mutations in the presence and absence of the drug. J Gen Virol 1996, 77(Pt 3):419-426.
    • (1996) J Gen Virol , vol.77 , Issue.PART 3 , pp. 419-426
    • Borman, A.M.1    Paulous, S.2    Clavel, F.3
  • 44
    • 0029899093 scopus 로고    scopus 로고
    • Second locus involved in human immunodeficiency virus type 1 resistance to protease inhibitors
    • 190252, 8648711
    • Doyon L, Croteau G, Thibeault D, Poulin F, Pilote L, Lamarre D. Second locus involved in human immunodeficiency virus type 1 resistance to protease inhibitors. J Virol 1996, 70:3763-3769. 190252, 8648711.
    • (1996) J Virol , vol.70 , pp. 3763-3769
    • Doyon, L.1    Croteau, G.2    Thibeault, D.3    Poulin, F.4    Pilote, L.5    Lamarre, D.6
  • 45
    • 0030769354 scopus 로고    scopus 로고
    • Drug resistance during indinavir therapy is caused by mutations in the protease gene and in its Gag substrate cleavage sites
    • 191944, 9261388
    • Zhang YM, Imamichi H, Imamichi T, Lane HC, Falloon J, Vasudevachari MB, Salzman NP. Drug resistance during indinavir therapy is caused by mutations in the protease gene and in its Gag substrate cleavage sites. J Virol 1997, 71:6662-6670. 191944, 9261388.
    • (1997) J Virol , vol.71 , pp. 6662-6670
    • Zhang, Y.M.1    Imamichi, H.2    Imamichi, T.3    Lane, H.C.4    Falloon, J.5    Vasudevachari, M.B.6    Salzman, N.P.7
  • 46
    • 0031846317 scopus 로고    scopus 로고
    • Resistance-associated loss of viral fitness in human immunodeficiency virus type 1: phenotypic analysis of protease and gag coevolution in protease inhibitor-treated patients
    • 110025, 9696866
    • Mammano F, Petit C, Clavel F. Resistance-associated loss of viral fitness in human immunodeficiency virus type 1: phenotypic analysis of protease and gag coevolution in protease inhibitor-treated patients. J Virol 1998, 72:7632-7637. 110025, 9696866.
    • (1998) J Virol , vol.72 , pp. 7632-7637
    • Mammano, F.1    Petit, C.2    Clavel, F.3
  • 47
    • 0032804864 scopus 로고    scopus 로고
    • Increased fitness of drug resistant HIV-1 protease as a result of acquisition of compensatory mutations during suboptimal therapy
    • 10.1097/00002030-199912030-00006, 10597776
    • Nijhuis M, Schuurman R, de Jong D, Erickson J, Gustchina E, Albert J, Schipper P, Gulnik S, Boucher CA. Increased fitness of drug resistant HIV-1 protease as a result of acquisition of compensatory mutations during suboptimal therapy. AIDS 1999, 13:2349-2359. 10.1097/00002030-199912030-00006, 10597776.
    • (1999) AIDS , vol.13 , pp. 2349-2359
    • Nijhuis, M.1    Schuurman, R.2    de Jong, D.3    Erickson, J.4    Gustchina, E.5    Albert, J.6    Schipper, P.7    Gulnik, S.8    Boucher, C.A.9
  • 48
    • 0033863985 scopus 로고    scopus 로고
    • Retracing the evolutionary pathways of human immunodeficiency virus type 1 resistance to protease inhibitors: virus fitness in the absence and in the presence of drug
    • 10.1128/JVI.74.18.8524-8531.2000, 116364, 10954553
    • Mammano F, Trouplin V, Zennou V, Clavel F. Retracing the evolutionary pathways of human immunodeficiency virus type 1 resistance to protease inhibitors: virus fitness in the absence and in the presence of drug. J Virol 2000, 74:8524-8531. 10.1128/JVI.74.18.8524-8531.2000, 116364, 10954553.
    • (2000) J Virol , vol.74 , pp. 8524-8531
    • Mammano, F.1    Trouplin, V.2    Zennou, V.3    Clavel, F.4
  • 49
    • 0037012979 scopus 로고    scopus 로고
    • Amprenavir-resistant HIV-1 exhibits lopinavir cross-resistance and reduced replication capacity
    • 10.1097/00002030-200205030-00007, 11953467
    • Prado JG, Wrin T, Beauchaine J, Ruiz L, Petropoulos CJ, Frost SD, Clotet B, D'Aquila RT, Martinez-Picado J. Amprenavir-resistant HIV-1 exhibits lopinavir cross-resistance and reduced replication capacity. AIDS 2002, 16:1009-1017. 10.1097/00002030-200205030-00007, 11953467.
    • (2002) AIDS , vol.16 , pp. 1009-1017
    • Prado, J.G.1    Wrin, T.2    Beauchaine, J.3    Ruiz, L.4    Petropoulos, C.J.5    Frost, S.D.6    Clotet, B.7    D'Aquila, R.T.8    Martinez-Picado, J.9
  • 50
    • 77954324656 scopus 로고    scopus 로고
    • Full-length HIV-1 Gag determines protease inhibitor susceptibility within in vitro assays
    • 10.1097/QAD.0b013e3283398216, 2923069, 20597164
    • Gupta RK, Kohli A, McCormick AL, Towers GJ, Pillay D, Parry CM. Full-length HIV-1 Gag determines protease inhibitor susceptibility within in vitro assays. AIDS 2010, 24:1651-1655. 10.1097/QAD.0b013e3283398216, 2923069, 20597164.
    • (2010) AIDS , vol.24 , pp. 1651-1655
    • Gupta, R.K.1    Kohli, A.2    McCormick, A.L.3    Towers, G.J.4    Pillay, D.5    Parry, C.M.6
  • 51
    • 0035163687 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 protease cleavage site mutations associated with protease inhibitor cross-resistance selected by indinavir, ritonavir, and/or saquinavir
    • 10.1128/JVI.75.2.589-594.2001, 113954, 11134271
    • Cote HC, Brumme ZL, Harrigan PR. Human immunodeficiency virus type 1 protease cleavage site mutations associated with protease inhibitor cross-resistance selected by indinavir, ritonavir, and/or saquinavir. J Virol 2001, 75:589-594. 10.1128/JVI.75.2.589-594.2001, 113954, 11134271.
    • (2001) J Virol , vol.75 , pp. 589-594
    • Cote, H.C.1    Brumme, Z.L.2    Harrigan, P.R.3
  • 52
    • 0041888278 scopus 로고    scopus 로고
    • Variability at human immunodeficiency virus type 1 subtype C protease cleavage sites: an indication of viral fitness?
    • 10.1128/JVI.77.17.9422-9430.2003, 187406, 12915557
    • de Oliveira T, Engelbrecht S, Janse van Rensburg E, Gordon M, Bishop K, zur Megede J, Barnett SW, Cassol S. Variability at human immunodeficiency virus type 1 subtype C protease cleavage sites: an indication of viral fitness?. J Virol 2003, 77:9422-9430. 10.1128/JVI.77.17.9422-9430.2003, 187406, 12915557.
    • (2003) J Virol , vol.77 , pp. 9422-9430
    • de Oliveira, T.1    Engelbrecht, S.2    Janse van Rensburg, E.3    Gordon, M.4    Bishop, K.5    zur Megede, J.6    Barnett, S.W.7    Cassol, S.8
  • 55
    • 70350317566 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 protease-correlated cleavage site mutations enhance inhibitor resistance
    • 10.1128/JVI.00628-09, 2772784, 19706699
    • Kolli M, Stawiski E, Chappey C, Schiffer CA. Human immunodeficiency virus type 1 protease-correlated cleavage site mutations enhance inhibitor resistance. J Virol 2009, 83:11027-11042. 10.1128/JVI.00628-09, 2772784, 19706699.
    • (2009) J Virol , vol.83 , pp. 11027-11042
    • Kolli, M.1    Stawiski, E.2    Chappey, C.3    Schiffer, C.A.4
  • 57
    • 0034284897 scopus 로고    scopus 로고
    • Polymorphism of HIV type 1 gag p7/p1 and p1/p6 cleavage sites: clinical significance and implications for resistance to protease inhibitors
    • 10.1089/08892220050116970, 10957718
    • Bally F, Martinez R, Peters S, Sudre P, Telenti A. Polymorphism of HIV type 1 gag p7/p1 and p1/p6 cleavage sites: clinical significance and implications for resistance to protease inhibitors. AIDS Res Hum Retroviruses 2000, 16:1209-1213. 10.1089/08892220050116970, 10957718.
    • (2000) AIDS Res Hum Retroviruses , vol.16 , pp. 1209-1213
    • Bally, F.1    Martinez, R.2    Peters, S.3    Sudre, P.4    Telenti, A.5
  • 59
    • 0037155193 scopus 로고    scopus 로고
    • Amino acid substitutions in Gag protein at non-cleavage sites are indispensable for the development of a high multitude of HIV-1 resistance against protease inhibitors
    • 10.1074/jbc.M108005200, 11741936
    • Gatanaga H, Suzuki Y, Tsang H, Yoshimura K, Kavlick MF, Nagashima K, Gorelick RJ, Mardy S, Tang C, Summers MF, Mitsuya H. Amino acid substitutions in Gag protein at non-cleavage sites are indispensable for the development of a high multitude of HIV-1 resistance against protease inhibitors. J Biol Chem 2002, 277:5952-5961. 10.1074/jbc.M108005200, 11741936.
    • (2002) J Biol Chem , vol.277 , pp. 5952-5961
    • Gatanaga, H.1    Suzuki, Y.2    Tsang, H.3    Yoshimura, K.4    Kavlick, M.F.5    Nagashima, K.6    Gorelick, R.J.7    Mardy, S.8    Tang, C.9    Summers, M.F.10    Mitsuya, H.11
  • 60
    • 63149156274 scopus 로고    scopus 로고
    • Non-cleavage site gag mutations in amprenavir-resistant human immunodeficiency virus type 1 (HIV-1) predispose HIV-1 to rapid acquisition of amprenavir resistance but delay development of resistance to other protease inhibitors
    • 10.1128/JVI.02539-08, 2655547, 19176623
    • Aoki M, Venzon DJ, Koh Y, Aoki-Ogata H, Miyakawa T, Yoshimura K, Maeda K, Mitsuya H. Non-cleavage site gag mutations in amprenavir-resistant human immunodeficiency virus type 1 (HIV-1) predispose HIV-1 to rapid acquisition of amprenavir resistance but delay development of resistance to other protease inhibitors. J Virol 2009, 83:3059-3068. 10.1128/JVI.02539-08, 2655547, 19176623.
    • (2009) J Virol , vol.83 , pp. 3059-3068
    • Aoki, M.1    Venzon, D.J.2    Koh, Y.3    Aoki-Ogata, H.4    Miyakawa, T.5    Yoshimura, K.6    Maeda, K.7    Mitsuya, H.8
  • 61
    • 62949083325 scopus 로고    scopus 로고
    • GRL-02031, a novel nonpeptidic protease inhibitor (PI) containing a stereochemically defined fused cyclopentanyltetrahydrofuran potent against multi-PI-resistant human immunodeficiency virus type 1 in vitro
    • 10.1128/AAC.00689-08, 2650524, 18955518
    • Koh Y, Das D, Leschenko S, Nakata H, Ogata-Aoki H, Amano M, Nakayama M, Ghosh AK, Mitsuya H. GRL-02031, a novel nonpeptidic protease inhibitor (PI) containing a stereochemically defined fused cyclopentanyltetrahydrofuran potent against multi-PI-resistant human immunodeficiency virus type 1 in vitro. Antimicrob Agents Chemother 2009, 53:997-1006. 10.1128/AAC.00689-08, 2650524, 18955518.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 997-1006
    • Koh, Y.1    Das, D.2    Leschenko, S.3    Nakata, H.4    Ogata-Aoki, H.5    Amano, M.6    Nakayama, M.7    Ghosh, A.K.8    Mitsuya, H.9
  • 62
    • 79952327508 scopus 로고    scopus 로고
    • Three residues in HIV-1 matrix contribute to protease inhibitor susceptibility and replication capacity
    • 10.1128/AAC.01228-10, 3067102, 21149628
    • Parry CM, Kolli M, Myers RE, Cane PA, Schiffer C, Pillay D. Three residues in HIV-1 matrix contribute to protease inhibitor susceptibility and replication capacity. Antimicrob Agents Chemother 2011, 55:1106-1113. 10.1128/AAC.01228-10, 3067102, 21149628.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 1106-1113
    • Parry, C.M.1    Kolli, M.2    Myers, R.E.3    Cane, P.A.4    Schiffer, C.5    Pillay, D.6
  • 63
    • 69449097224 scopus 로고    scopus 로고
    • Gag determinants of fitness and drug susceptibility in protease inhibitor-resistant human immunodeficiency virus type 1
    • 10.1128/JVI.02356-08, 2738216, 19587031
    • Parry CM, Kohli A, Boinett CJ, Towers GJ, McCormick AL, Pillay D. Gag determinants of fitness and drug susceptibility in protease inhibitor-resistant human immunodeficiency virus type 1. J Virol 2009, 83:9094-9101. 10.1128/JVI.02356-08, 2738216, 19587031.
    • (2009) J Virol , vol.83 , pp. 9094-9101
    • Parry, C.M.1    Kohli, A.2    Boinett, C.J.3    Towers, G.J.4    McCormick, A.L.5    Pillay, D.6
  • 64
    • 42449118624 scopus 로고    scopus 로고
    • In vitro HIV-1 resistance selection to GS8374, a novel phosphonate protease inhibitor: comparison with lopinavir, atazanavir and darunavir
    • Callebaut C, Stray K, Tsai L, Xu L, Lee W, Cihlar T. In vitro HIV-1 resistance selection to GS8374, a novel phosphonate protease inhibitor: comparison with lopinavir, atazanavir and darunavir. Antivir Ther 2007, 12:S18.
    • (2007) Antivir Ther , vol.12
    • Callebaut, C.1    Stray, K.2    Tsai, L.3    Xu, L.4    Lee, W.5    Cihlar, T.6
  • 66
    • 42149119569 scopus 로고    scopus 로고
    • Impact of Gag cleavage site mutations on the virological response to darunavir/ritonavir in treatment-experienced patients in POWER 1, 2 and 3
    • Dierynck I, De Meyer S, C-V K, Van Marck H, Lathouwers E, Thys K, Maes B, de Bethune MP. Impact of Gag cleavage site mutations on the virological response to darunavir/ritonavir in treatment-experienced patients in POWER 1, 2 and 3. Antivir Ther 2007, 12:S23.
    • (2007) Antivir Ther , vol.12
    • Dierynck, I.1    De Meyer, S.2    C-V, K.3    Van Marck, H.4    Lathouwers, E.5    Thys, K.6    Maes, B.7    de Bethune, M.P.8
  • 67
    • 33646028218 scopus 로고    scopus 로고
    • Role of HIV-1 minority populations on resistance mutational pattern evolution and susceptibility to protease inhibitors
    • 10.1097/01.aids.0000202650.03279.69, 16511425
    • Roquebert B, Malet I, Wirden M, Tubiana R, Valantin MA, Simon A, Katlama C, Peytavin G, Calvez V, Marcelin AG. Role of HIV-1 minority populations on resistance mutational pattern evolution and susceptibility to protease inhibitors. AIDS 2006, 20:287-289. 10.1097/01.aids.0000202650.03279.69, 16511425.
    • (2006) AIDS , vol.20 , pp. 287-289
    • Roquebert, B.1    Malet, I.2    Wirden, M.3    Tubiana, R.4    Valantin, M.A.5    Simon, A.6    Katlama, C.7    Peytavin, G.8    Calvez, V.9    Marcelin, A.G.10
  • 68
    • 25144487293 scopus 로고    scopus 로고
    • Selection and characterization of HIV-1 showing reduced susceptibility to the non-peptidic protease inhibitor tipranavir
    • 10.1016/j.antiviral.2005.07.003, 16122817
    • Doyon L, Tremblay S, Bourgon L, Wardrop E, Cordingley MG. Selection and characterization of HIV-1 showing reduced susceptibility to the non-peptidic protease inhibitor tipranavir. Antiviral Res 2005, 68:27-35. 10.1016/j.antiviral.2005.07.003, 16122817.
    • (2005) Antiviral Res , vol.68 , pp. 27-35
    • Doyon, L.1    Tremblay, S.2    Bourgon, L.3    Wardrop, E.4    Cordingley, M.G.5
  • 69
    • 80052028225 scopus 로고    scopus 로고
    • HIV-1 protease inhibitor mutations affect the development of HIV-1 resistance to the maturation inhibitor bevirimat
    • 10.1186/1742-4690-8-70, 3184055, 21864346
    • Fun A, van Maarseveen NM, Pokorna J, Maas RE, Schipper PJ, Konvalinka J, Nijhuis M. HIV-1 protease inhibitor mutations affect the development of HIV-1 resistance to the maturation inhibitor bevirimat. Retrovirology 2011, 8:70. 10.1186/1742-4690-8-70, 3184055, 21864346.
    • (2011) Retrovirology , vol.8 , pp. 70
    • Fun, A.1    van Maarseveen, N.M.2    Pokorna, J.3    Maas, R.E.4    Schipper, P.J.5    Konvalinka, J.6    Nijhuis, M.7
  • 70
    • 77952635262 scopus 로고    scopus 로고
    • Phenotypic Susceptibility to Bevirimat in Isolates from HIV-1-Infected Patients without Prior Exposure to Bevirimat
    • 10.1128/AAC.01784-09, 2876391, 20308382
    • Margot NA, Gibbs CS, Miller MD. Phenotypic Susceptibility to Bevirimat in Isolates from HIV-1-Infected Patients without Prior Exposure to Bevirimat. Antimicrob Agents Chemother 2010, 54:2345-2353. 10.1128/AAC.01784-09, 2876391, 20308382.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 2345-2353
    • Margot, N.A.1    Gibbs, C.S.2    Miller, M.D.3
  • 72
    • 66149150956 scopus 로고    scopus 로고
    • Susceptibility of human immunodeficiency virus type 1 to the maturation inhibitor bevirimat is modulated by baseline polymorphisms in Gag spacer peptide 1
    • 10.1128/AAC.01650-08, 2681549, 19223634
    • Van Baelen K, Salzwedel K, Rondelez E, Van Eygen V, De Vos S, Verheyen A, Steegen K, Verlinden Y, Allaway GP, Stuyver LJ. Susceptibility of human immunodeficiency virus type 1 to the maturation inhibitor bevirimat is modulated by baseline polymorphisms in Gag spacer peptide 1. Antimicrob Agents Chemother 2009, 53:2185-2188. 10.1128/AAC.01650-08, 2681549, 19223634.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 2185-2188
    • Van Baelen, K.1    Salzwedel, K.2    Rondelez, E.3    Van Eygen, V.4    De Vos, S.5    Verheyen, A.6    Steegen, K.7    Verlinden, Y.8    Allaway, G.P.9    Stuyver, L.J.10
  • 73
    • 33845451578 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 resistance to the small molecule maturation inhibitor 3-O-(3',3'-dimethylsuccinyl)-betulinic acid is conferred by a variety of single amino acid substitutions at the CA-SP1 cleavage site in Gag
    • 10.1128/JVI.01626-06, 1676313, 17035324
    • Zhou J, Chen CH, Aiken C. Human immunodeficiency virus type 1 resistance to the small molecule maturation inhibitor 3-O-(3',3'-dimethylsuccinyl)-betulinic acid is conferred by a variety of single amino acid substitutions at the CA-SP1 cleavage site in Gag. J Virol 2006, 80:12095-12101. 10.1128/JVI.01626-06, 1676313, 17035324.
    • (2006) J Virol , vol.80 , pp. 12095-12101
    • Zhou, J.1    Chen, C.H.2    Aiken, C.3
  • 76
    • 77950929797 scopus 로고    scopus 로고
    • Polymorphisms in Gag spacer peptide 1 confer varying levels of resistance to the HIV- 1 maturation inhibitor bevirimat
    • 10.1186/1742-4690-7-36, 2873507, 20406463
    • Adamson CS, Sakalian M, Salzwedel K, Freed EO. Polymorphisms in Gag spacer peptide 1 confer varying levels of resistance to the HIV- 1 maturation inhibitor bevirimat. Retrovirology 2010, 7:36. 10.1186/1742-4690-7-36, 2873507, 20406463.
    • (2010) Retrovirology , vol.7 , pp. 36
    • Adamson, C.S.1    Sakalian, M.2    Salzwedel, K.3    Freed, E.O.4
  • 77
    • 0942290560 scopus 로고    scopus 로고
    • Gag non-cleavage site mutations contribute to full recovery of viral fitness in protease inhibitor-resistant human immunodeficiency virus type 1
    • 10.1128/AAC.48.2.444-452.2004, 321554, 14742193
    • Myint L, Matsuda M, Matsuda Z, Yokomaku Y, Chiba T, Okano A, Yamada K, Sugiura W. Gag non-cleavage site mutations contribute to full recovery of viral fitness in protease inhibitor-resistant human immunodeficiency virus type 1. Antimicrob Agents Chemother 2004, 48:444-452. 10.1128/AAC.48.2.444-452.2004, 321554, 14742193.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 444-452
    • Myint, L.1    Matsuda, M.2    Matsuda, Z.3    Yokomaku, Y.4    Chiba, T.5    Okano, A.6    Yamada, K.7    Sugiura, W.8
  • 79
    • 33846572284 scopus 로고    scopus 로고
    • Identification and structural characterization of I84C and I84A mutations that are associated with high-level resistance to human immunodeficiency virus protease inhibitors and impair viral replication
    • 10.1128/AAC.00690-06, 1797770, 17101675
    • Mo H, Parkin N, Stewart KD, Lu L, Dekhtyar T, Kempf DJ, Molla A. Identification and structural characterization of I84C and I84A mutations that are associated with high-level resistance to human immunodeficiency virus protease inhibitors and impair viral replication. Antimicrob Agents Chemother 2007, 51:732-735. 10.1128/AAC.00690-06, 1797770, 17101675.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 732-735
    • Mo, H.1    Parkin, N.2    Stewart, K.D.3    Lu, L.4    Dekhtyar, T.5    Kempf, D.J.6    Molla, A.7
  • 80
    • 23244440228 scopus 로고    scopus 로고
    • Evolution of human immunodeficiency virus type 1 protease genotypes and phenotypes in vivo under selective pressure of the protease inhibitor ritonavir
    • 10.1128/JVI.79.16.10638-10649.2005, 1182672, 16051856
    • Resch W, Parkin N, Watkins T, Harris J, Swanstrom R. Evolution of human immunodeficiency virus type 1 protease genotypes and phenotypes in vivo under selective pressure of the protease inhibitor ritonavir. J Virol 2005, 79:10638-10649. 10.1128/JVI.79.16.10638-10649.2005, 1182672, 16051856.
    • (2005) J Virol , vol.79 , pp. 10638-10649
    • Resch, W.1    Parkin, N.2    Watkins, T.3    Harris, J.4    Swanstrom, R.5
  • 81
    • 70349337052 scopus 로고    scopus 로고
    • Failure of treatment with first-line lopinavir boosted with ritonavir can be explained by novel resistance pathways with protease mutation 76 V
    • 10.1086/605329, 19627247
    • Nijhuis M, Wensing AM, Bierman WF, de Jong D, Kagan R, Fun A, Jaspers CA, Schurink KA, van Agtmael MA, Boucher CA. Failure of treatment with first-line lopinavir boosted with ritonavir can be explained by novel resistance pathways with protease mutation 76 V. J Infect Dis 2009, 200:698-709. 10.1086/605329, 19627247.
    • (2009) J Infect Dis , vol.200 , pp. 698-709
    • Nijhuis, M.1    Wensing, A.M.2    Bierman, W.F.3    de Jong, D.4    Kagan, R.5    Fun, A.6    Jaspers, C.A.7    Schurink, K.A.8    van Agtmael, M.A.9    Boucher, C.A.10
  • 83
    • 77949356168 scopus 로고    scopus 로고
    • The evolution of protease mutation 76 V is associated with protease mutation 46I and gag mutation 431 V
    • 10.1097/QAD.0b013e328336784d, 20139751
    • Knops E, Kemper I, Schulter E, Pfister H, Kaiser R, Verheyen J. The evolution of protease mutation 76 V is associated with protease mutation 46I and gag mutation 431 V. AIDS 2010, 24:779-781. 10.1097/QAD.0b013e328336784d, 20139751.
    • (2010) AIDS , vol.24 , pp. 779-781
    • Knops, E.1    Kemper, I.2    Schulter, E.3    Pfister, H.4    Kaiser, R.5    Verheyen, J.6
  • 84
    • 0037310296 scopus 로고    scopus 로고
    • Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors
    • 10.1128/AAC.47.2.759-769.2003, 151730, 12543689
    • Watkins T, Resch W, Irlbeck D, Swanstrom R. Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors. Antimicrob Agents Chemother 2003, 47:759-769. 10.1128/AAC.47.2.759-769.2003, 151730, 12543689.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 759-769
    • Watkins, T.1    Resch, W.2    Irlbeck, D.3    Swanstrom, R.4
  • 85
    • 0031849665 scopus 로고    scopus 로고
    • In vitro selection and characterization of human immunodeficiency virus type 1 variants with increased resistance to ABT-378, a novel protease inhibitor
    • 109995, 9696850
    • Carrillo A, Stewart KD, Sham HL, Norbeck DW, Kohlbrenner WE, Leonard JM, Kempf DJ, Molla A. In vitro selection and characterization of human immunodeficiency virus type 1 variants with increased resistance to ABT-378, a novel protease inhibitor. J Virol 1998, 72:7532-7541. 109995, 9696850.
    • (1998) J Virol , vol.72 , pp. 7532-7541
    • Carrillo, A.1    Stewart, K.D.2    Sham, H.L.3    Norbeck, D.W.4    Kohlbrenner, W.E.5    Leonard, J.M.6    Kempf, D.J.7    Molla, A.8
  • 87
    • 33644645939 scopus 로고    scopus 로고
    • In vitro development of resistance to human immunodeficiency virus protease inhibitor GW640385
    • 10.1128/AAC.50.3.1092-1095.2006, 1426426, 16495277
    • Yates PJ, Hazen R, St Clair M, Boone L, Tisdale M, Elston RC. In vitro development of resistance to human immunodeficiency virus protease inhibitor GW640385. Antimicrob Agents Chemother 2006, 50:1092-1095. 10.1128/AAC.50.3.1092-1095.2006, 1426426, 16495277.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 1092-1095
    • Yates, P.J.1    Hazen, R.2    St Clair, M.3    Boone, L.4    Tisdale, M.5    Elston, R.C.6
  • 88
    • 80052959305 scopus 로고    scopus 로고
    • Polymorphism in Gag Gene Cleavage Sites of HIV-1 Non-B Subtype and Virological Outcome of a First-Line Lopinavir/Ritonavir Single Drug Regimen
    • 10.1371/journal.pone.0024798, 3176769, 21949754
    • Ghosn J, Delaugerre C, Flandre P, Galimand J, Cohen-Codar I, Raffi F, Delfraissy JF, Rouzioux C, Chaix ML. Polymorphism in Gag Gene Cleavage Sites of HIV-1 Non-B Subtype and Virological Outcome of a First-Line Lopinavir/Ritonavir Single Drug Regimen. PLoS One 2011, 6:e24798. 10.1371/journal.pone.0024798, 3176769, 21949754.
    • (2011) PLoS One , vol.6
    • Ghosn, J.1    Delaugerre, C.2    Flandre, P.3    Galimand, J.4    Cohen-Codar, I.5    Raffi, F.6    Delfraissy, J.F.7    Rouzioux, C.8    Chaix, M.L.9
  • 90
    • 7644230388 scopus 로고    scopus 로고
    • Structural basis for coevolution of a human immunodeficiency virus type 1 nucleocapsid-p1 cleavage site with a V82A drug-resistant mutation in viral protease
    • 10.1128/JVI.78.22.12446-12454.2004, 525094, 15507631
    • Prabu-Jeyabalan M, Nalivaika EA, King NM, Schiffer CA. Structural basis for coevolution of a human immunodeficiency virus type 1 nucleocapsid-p1 cleavage site with a V82A drug-resistant mutation in viral protease. J Virol 2004, 78:12446-12454. 10.1128/JVI.78.22.12446-12454.2004, 525094, 15507631.
    • (2004) J Virol , vol.78 , pp. 12446-12454
    • Prabu-Jeyabalan, M.1    Nalivaika, E.A.2    King, N.M.3    Schiffer, C.A.4
  • 96
    • 79957593407 scopus 로고    scopus 로고
    • Accumulation of P(T/S)AP late domain duplications in HIV type 1 subtypes B, C, and F derived from individuals failing ARV therapy and ARV drug-naive patients
    • 10.1089/aid.2010.0282, 21083435
    • Martins AN, Arruda MB, Pires AF, Tanuri A, Brindeiro RM. Accumulation of P(T/S)AP late domain duplications in HIV type 1 subtypes B, C, and F derived from individuals failing ARV therapy and ARV drug-naive patients. AIDS Res Hum Retroviruses 2011, 27:687-692. 10.1089/aid.2010.0282, 21083435.
    • (2011) AIDS Res Hum Retroviruses , vol.27 , pp. 687-692
    • Martins, A.N.1    Arruda, M.B.2    Pires, A.F.3    Tanuri, A.4    Brindeiro, R.M.5
  • 97
  • 98
    • 0037338574 scopus 로고    scopus 로고
    • Changes in the human immunodeficiency virus p7-p1-p6 gag gene in drug-naive and pretreated patients
    • 10.1128/JCM.41.3.1245-1247.2003, 150303, 12624058
    • Gallego O, de Mendoza C, Corral A, Soriano V. Changes in the human immunodeficiency virus p7-p1-p6 gag gene in drug-naive and pretreated patients. J Clin Microbiol 2003, 41:1245-1247. 10.1128/JCM.41.3.1245-1247.2003, 150303, 12624058.
    • (2003) J Clin Microbiol , vol.41 , pp. 1245-1247
    • Gallego, O.1    de Mendoza, C.2    Corral, A.3    Soriano, V.4
  • 99
    • 33645410524 scopus 로고    scopus 로고
    • Variability in the P6gag domains of HIV-1 involved in viral budding
    • 10.1097/01.aids.0000210619.75707.21, 16470130
    • Holguin A, Alvarez A, Soriano V. Variability in the P6gag domains of HIV-1 involved in viral budding. AIDS 2006, 20:624-627. 10.1097/01.aids.0000210619.75707.21, 16470130.
    • (2006) AIDS , vol.20 , pp. 624-627
    • Holguin, A.1    Alvarez, A.2    Soriano, V.3
  • 100
    • 0034915565 scopus 로고    scopus 로고
    • Impact of HIV type 1 protease, reverse transcriptase, cleavage site, and p6 mutations on the virological response to quadruple therapy with saquinavir, ritonavir, and two nucleoside analogs
    • 10.1089/08892220151126526, 11350662
    • Kaufmann GR, Suzuki K, Cunningham P, Mukaide M, Kondo M, Imai M, Zaunders J, Cooper DA. Impact of HIV type 1 protease, reverse transcriptase, cleavage site, and p6 mutations on the virological response to quadruple therapy with saquinavir, ritonavir, and two nucleoside analogs. AIDS Res Hum Retroviruses 2001, 17:487-497. 10.1089/08892220151126526, 11350662.
    • (2001) AIDS Res Hum Retroviruses , vol.17 , pp. 487-497
    • Kaufmann, G.R.1    Suzuki, K.2    Cunningham, P.3    Mukaide, M.4    Kondo, M.5    Imai, M.6    Zaunders, J.7    Cooper, D.A.8
  • 104
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • 10.1038/35030177, 11014200
    • Li S, Hill CP, Sundquist WI, Finch JT. Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature 2000, 407:409-413. 10.1038/35030177, 11014200.
    • (2000) Nature , vol.407 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 107
    • 34548844198 scopus 로고    scopus 로고
    • Structure of the antiviral assembly inhibitor CAP-1 complex with the HIV-1 CA protein
    • 10.1016/j.jmb.2007.07.070, 2066180, 17826792
    • Kelly BN, Kyere S, Kinde I, Tang C, Howard BR, Robinson H, Sundquist WI, Summers MF, Hill CP. Structure of the antiviral assembly inhibitor CAP-1 complex with the HIV-1 CA protein. J Mol Biol 2007, 373:355-366. 10.1016/j.jmb.2007.07.070, 2066180, 17826792.
    • (2007) J Mol Biol , vol.373 , pp. 355-366
    • Kelly, B.N.1    Kyere, S.2    Kinde, I.3    Tang, C.4    Howard, B.R.5    Robinson, H.6    Sundquist, W.I.7    Summers, M.F.8    Hill, C.P.9
  • 112
    • 78650064115 scopus 로고    scopus 로고
    • Small-molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization
    • 10.1128/JVI.01406-10, 3014163, 20962083
    • Shi J, Zhou J, Shah VB, Aiken C, Whitby K. Small-molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization. J Virol 2011, 85:542-549. 10.1128/JVI.01406-10, 3014163, 20962083.
    • (2011) J Virol , vol.85 , pp. 542-549
    • Shi, J.1    Zhou, J.2    Shah, V.B.3    Aiken, C.4    Whitby, K.5
  • 115
    • 82755190460 scopus 로고    scopus 로고
    • The prototype HIV-1 maturation inhibitor, bevirimat, binds to the CA-SP1 cleavage site in immature Gag particles
    • 10.1186/1742-4690-8-101, 3267693, 22151792
    • Nguyen AT, Feasley CL, Jackson KW, Nitz TJ, Salzwedel K, Air GM, Sakalian M. The prototype HIV-1 maturation inhibitor, bevirimat, binds to the CA-SP1 cleavage site in immature Gag particles. Retrovirology 2011, 8:101. 10.1186/1742-4690-8-101, 3267693, 22151792.
    • (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    Sakalian, M.7
  • 116
    • 78951488338 scopus 로고    scopus 로고
    • HIV-1 maturation inhibitor bevirimat stabilizes the immature Gag lattice
    • 10.1128/JVI.01926-10, 3028903, 21106735
    • Keller PW, Adamson CS, Heymann JB, Freed EO, Steven AC. HIV-1 maturation inhibitor bevirimat stabilizes the immature Gag lattice. J Virol 2011, 85:1420-1428. 10.1128/JVI.01926-10, 3028903, 21106735.
    • (2011) J Virol , vol.85 , pp. 1420-1428
    • Keller, P.W.1    Adamson, C.S.2    Heymann, J.B.3    Freed, E.O.4    Steven, A.C.5
  • 123
    • 78650883987 scopus 로고    scopus 로고
    • In Vitro Selection of Clinically Relevant Bevirimat Resistance Mutations Revealed by " Deep" Sequencing of Serially Passaged, Quasispecies-Containing Recombinant HIV-1
    • 10.1128/JCM.01868-10, 3020451, 21084518
    • Knapp DJ, Harrigan PR, Poon AF, Brumme ZL, Brockman M, Cheung PK. In Vitro Selection of Clinically Relevant Bevirimat Resistance Mutations Revealed by " Deep" Sequencing of Serially Passaged, Quasispecies-Containing Recombinant HIV-1. J Clin Microbiol 2011, 49:201-208. 10.1128/JCM.01868-10, 3020451, 21084518.
    • (2011) J Clin Microbiol , vol.49 , pp. 201-208
    • Knapp, D.J.1    Harrigan, P.R.2    Poon, A.F.3    Brumme, Z.L.4    Brockman, M.5    Cheung, P.K.6
  • 124
    • 75649142120 scopus 로고    scopus 로고
    • High prevalence of natural polymorphisms in Gag (CA-SP1) associated with reduced response to Bevirimat, an HIV-1 maturation inhibitor
    • 10.1097/QAD.0b013e328335ce07, 19996935
    • Seclen E, Gonzalez Mdel M, Corral A, de Mendoza C, Soriano V, Poveda E. High prevalence of natural polymorphisms in Gag (CA-SP1) associated with reduced response to Bevirimat, an HIV-1 maturation inhibitor. AIDS 2010, 24:467-469. 10.1097/QAD.0b013e328335ce07, 19996935.
    • (2010) AIDS , vol.24 , pp. 467-469
    • Seclen, E.1    Gonzalez Mdel, M.2    Corral, A.3    de Mendoza, C.4    Soriano, V.5    Poveda, E.6
  • 125
    • 79959241949 scopus 로고    scopus 로고
    • A single polymorphism in HIV-1 subtype C SP1 is sufficient to confer natural resistance to the maturation inhibitor bevirimat
    • 10.1128/AAC.01435-10, 3122462, 21502630
    • Lu W, Salzwedel K, Wang D, Chakravarty S, Freed EO, Wild CT, Li F. A single polymorphism in HIV-1 subtype C SP1 is sufficient to confer natural resistance to the maturation inhibitor bevirimat. Antimicrob Agents Chemother 2011, 55:3324-3329. 10.1128/AAC.01435-10, 3122462, 21502630.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 3324-3329
    • Lu, W.1    Salzwedel, K.2    Wang, D.3    Chakravarty, S.4    Freed, E.O.5    Wild, C.T.6    Li, F.7
  • 126
    • 34147127041 scopus 로고    scopus 로고
    • Primary genotypic resistance of HIV-1 to the maturation inhibitor PA-457 in protease inhibitor-experienced patients
    • 10.1097/QAD.0b013e3280b079d9, 17415044
    • Malet I, Wirden M, Derache A, Simon A, Katlama C, Calvez V, Marcelin AG. Primary genotypic resistance of HIV-1 to the maturation inhibitor PA-457 in protease inhibitor-experienced patients. AIDS 2007, 21:871-873. 10.1097/QAD.0b013e3280b079d9, 17415044.
    • (2007) AIDS , vol.21 , pp. 871-873
    • Malet, I.1    Wirden, M.2    Derache, A.3    Simon, A.4    Katlama, C.5    Calvez, V.6    Marcelin, A.G.7
  • 127
    • 65349162716 scopus 로고    scopus 로고
    • Impact of human immunodeficiency virus type 1 resistance to protease inhibitors on evolution of resistance to the maturation inhibitor bevirimat (PA-457)
    • 10.1128/JVI.02659-08, 2682084, 19279107
    • Adamson CS, Waki K, Ablan SD, Salzwedel K, Freed EO. Impact of human immunodeficiency virus type 1 resistance to protease inhibitors on evolution of resistance to the maturation inhibitor bevirimat (PA-457). J Virol 2009, 83:4884-4894. 10.1128/JVI.02659-08, 2682084, 19279107.
    • (2009) J Virol , vol.83 , pp. 4884-4894
    • Adamson, C.S.1    Waki, K.2    Ablan, S.D.3    Salzwedel, K.4    Freed, E.O.5


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