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Volumn 3, Issue 6, 2008, Pages 627-632

Novel mechanisms of HIV protease inhibitor resistance

Author keywords

Gag cleavage sites; Protease inhibitor therapy; Resistance

Indexed keywords

DARUNAVIR; GAG PROTEIN; LOPINAVIR; LOPINAVIR PLUS RITONAVIR; PROTEINASE; PROTEINASE INHIBITOR; RITONAVIR; VIRUS ENZYME;

EID: 67649576660     PISSN: 1746630X     EISSN: 17466318     Source Type: Journal    
DOI: 10.1097/COH.0b013e3283136cd9     Document Type: Review
Times cited : (10)

References (51)
  • 1
    • 0005241362 scopus 로고
    • Active human immunodeficiency virus protease is required for viral infectivity
    • Kohl NE, Emini EA, Schleif WA, et al. Active human immunodeficiency virus protease is required for viral infectivity. Proc Natl Acad Sci U S A 1988; 85:4686-4690.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 4686-4690
    • Kohl, N.E.1    Emini, E.A.2    Schleif, W.A.3
  • 2
    • 0023870815 scopus 로고
    • Characterization of ribosomal frame-shifting in HIV-1 gag-pol expression
    • Jacks T, Power MD, Masiarz FR, et al. Characterization of ribosomal frame-shifting in HIV-1 gag-pol expression. Nature 1988; 331:280-283.
    • (1988) Nature , vol.331 , pp. 280-283
    • Jacks, T.1    Power, M.D.2    Masiarz, F.R.3
  • 3
    • 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, Crowe 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; 75:1834-1841.
    • (2001) J Virol , vol.75 , pp. 1834-1841
    • Shehu-Xhilaga, M.1    Crowe, S.M.2    Mak, J.3
  • 4
    • 30844443739 scopus 로고    scopus 로고
    • Decreasing the frameshift efficiency translates into an equivalent reduction of the replication of the human immunodeficiency virus type 1
    • Dulude D, Berchiche YA, Gendron K, et al. Decreasing the frameshift efficiency translates into an equivalent reduction of the replication of the human immunodeficiency virus type 1. Virology 2006; 345:127-136.
    • (2006) Virology , vol.345 , pp. 127-136
    • Dulude, D.1    Berchiche, Y.A.2    Gendron, K.3
  • 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, et al. 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.
    • (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
  • 6
    • 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, et al. Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites. J Virol 1998; 72:2846-2854.
    • (1998) J Virol , vol.72 , pp. 2846-2854
    • Wiegers, K.1    Rutter, G.2    Kottler, H.3
  • 7
    • 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, et al. 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.
    • (1994) J Virol , vol.68 , pp. 8017-8027
    • Pettit, S.C.1    Moody, M.D.2    Wehbie, R.S.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
    • Pettit SC, Henderson GJ, Schiffer CA, et al. 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.
    • (2002) J Virol , vol.76 , pp. 10226-10233
    • Pettit, S.C.1    Henderson, G.J.2    Schiffer, C.A.3
  • 9
    • 33846702679 scopus 로고    scopus 로고
    • A novel substrate-based HIV-1 protease inhibitor drug resistance mechanism
    • This study describes the in-vitro selection of protease inhibitor-resistant viruses with mutations in the Gag NC/p1 cleavage site in the absence of resistance mutations in protease
    • Nijhuis M, van Maarseveen NM, Lastere S, et al. A novel substrate-based HIV-1 protease inhibitor drug resistance mechanism. PLoS Med 2007; 4:e36. This study describes the in-vitro selection of protease inhibitor-resistant viruses with mutations in the Gag NC/p1 cleavage site in the absence of resistance mutations in protease.
    • (2007) PLoS Med , vol.4
    • Nijhuis, M.1    van Maarseveen, N.M.2    Lastere, S.3
  • 10
    • 0024412506 scopus 로고
    • Conserved folding in retroviral proteases: Crystal structure of a synthetic HIV-1 protease
    • Wlodawer A, Miller M, Jaskólski M, et al. Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease. Science 1989; 245:616-621.
    • (1989) Science , vol.245 , pp. 616-621
    • Wlodawer, A.1    Miller, M.2    Jaskólski, M.3
  • 11
    • 0024555898 scopus 로고
    • Three dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1
    • Navia MA, Fitzgerald PMD, McKeever BM, et al. Three dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1. Nature 1989;337:615-620.
    • (1989) Nature , vol.337 , pp. 615-620
    • Navia, M.A.1    Fitzgerald, P.M.D.2    McKeever, B.M.3
  • 12
    • 0031015475 scopus 로고    scopus 로고
    • Impaired fitness of human immunodeficiency virus type 1 variants with high-level resistance to protease inhibitors
    • Croteau G, Doyon L, Thibeault D, et al. Impaired fitness of human immunodeficiency virus type 1 variants with high-level resistance to protease inhibitors. J Virol 1997; 71:1089-1096.
    • (1997) J Virol , vol.71 , pp. 1089-1096
    • Croteau, G.1    Doyon, L.2    Thibeault, D.3
  • 13
    • 0032804864 scopus 로고    scopus 로고
    • Increased fitness of drug resistant HIV-1 protease as a result of acquisition of compensatory mutations during suboptimal therapy
    • Nijhuis M, Schuurman R, de Jong D, et al. Increased fitness of drug resistant HIV-1 protease as a result of acquisition of compensatory mutations during suboptimal therapy. AIDS 1999; 13:2349-2359.
    • (1999) AIDS , vol.13 , pp. 2349-2359
    • Nijhuis, M.1    Schuurman, R.2    de Jong, D.3
  • 14
    • 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
    • Mammano F, Trouplin V, Zennou V, et al. 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.
    • (2000) J Virol , vol.74 , pp. 8524-8531
    • Mammano, F.1    Trouplin, V.2    Zennou, V.3
  • 15
    • 0001769435 scopus 로고    scopus 로고
    • HIV-1 Fitness: Implications for drug resistance, disease progression an global epidemic evolution
    • Kuiken C, Foley B, Hahn B, et al, editors, Theoretical Biology and Biophysics Group, Los Alamos National Laboratory;
    • Quinones-Mateu ME, Arts EJ. HIV-1 Fitness: implications for drug resistance, disease progression an global epidemic evolution. In: Kuiken C, Foley B, Hahn B, et al., editors. HIV sequence compendium 2001. Theoretical Biology and Biophysics Group, Los Alamos National Laboratory; 2001.
    • (2001) HIV sequence compendium 2001
    • Quinones-Mateu, M.E.1    Arts, E.J.2
  • 16
    • 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
    • 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.
    • (1998) J Virol , vol.72 , pp. 7632-7637
    • Mammano, F.1    Petit, C.2    Clavel, F.3
  • 17
    • 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
    • Zhang Y-M, Imamichi H, Imamichi T, et al. 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.
    • (1997) J Virol , vol.71 , pp. 6662-6670
    • Zhang, Y.-M.1    Imamichi, H.2    Imamichi, T.3
  • 18
    • 0029899093 scopus 로고    scopus 로고
    • Second locus involved in human immunodeficiency virus type 1 resistance to protease inhibitors
    • Doyon L, Croteau G, Thibeault D, et al. Second locus involved in human immunodeficiency virus type 1 resistance to protease inhibitors. J Virol 1996;70:3763-3769.
    • (1996) J Virol , vol.70 , pp. 3763-3769
    • Doyon, L.1    Croteau, G.2    Thibeault, D.3
  • 19
    • 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
    • Maguire MF, Guinea R, Griffin P, et al. 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.
    • (2002) J Virol , vol.76 , pp. 7398-7406
    • Maguire, M.F.1    Guinea, R.2    Griffin, P.3
  • 20
    • 0034812843 scopus 로고    scopus 로고
    • Resistance to nucleoside analog reverse transcriptase inhibitors mediated by human immunodeficiency virus type 1 p6 protein
    • Peters S, Munoz M, Yerly S, et al. Resistance to nucleoside analog reverse transcriptase inhibitors mediated by human immunodeficiency virus type 1 p6 protein. J Virol 2001; 75:9644-9653.
    • (2001) J Virol , vol.75 , pp. 9644-9653
    • Peters, S.1    Munoz, M.2    Yerly, S.3
  • 21
    • 0037338574 scopus 로고    scopus 로고
    • Changes in the human immunodeficiency virus p7-p1-p6 gag gene in drug-naive and pretreated patients
    • Gallego O, de Mendoza C, Corral A, et al. Changes in the human immunodeficiency virus p7-p1-p6 gag gene in drug-naive and pretreated patients. J Clin Microbiol 2003; 41:1245-1247.
    • (2003) J Clin Microbiol , vol.41 , pp. 1245-1247
    • Gallego, O.1    de Mendoza, C.2    Corral, A.3
  • 22
    • 0141481971 scopus 로고    scopus 로고
    • Polymorphisms in p1-p6/p6* of HIV type 1 can delay protease autoprocessing and increase drug susceptibility
    • Whitehurst N, Chappey C, Petropoulos C, et al. Polymorphisms in p1-p6/p6* of HIV type 1 can delay protease autoprocessing and increase drug susceptibility. AIDS Res Hum Retroviruses 2003; 19:779-784.
    • (2003) AIDS Res Hum Retroviruses , vol.19 , pp. 779-784
    • Whitehurst, N.1    Chappey, C.2    Petropoulos, C.3
  • 23
    • 0033618280 scopus 로고    scopus 로고
    • Competitive inhibition of human immunodeficiency virus type-1 protease by the Gag-Pol transframe protein
    • Paulus C, Hellebrand S, Tessmer U, et al. Competitive inhibition of human immunodeficiency virus type-1 protease by the Gag-Pol transframe protein. J Biol Chem 1999; 274:21539-21543.
    • (1999) J Biol Chem , vol.274 , pp. 21539-21543
    • Paulus, C.1    Hellebrand, S.2    Tessmer, U.3
  • 24
    • 2642680072 scopus 로고    scopus 로고
    • Cleavage of human immunodeficiency virus type 1 proteinase from the N-terminally adjacent p6* protein is essential for efficient Gag polyprotein processing and viral infectivity
    • Tessmer U, Krausslich HG. Cleavage of human immunodeficiency virus type 1 proteinase from the N-terminally adjacent p6* protein is essential for efficient Gag polyprotein processing and viral infectivity. J Virol 1998; 72:3459-3463.
    • (1998) J Virol , vol.72 , pp. 3459-3463
    • Tessmer, U.1    Krausslich, H.G.2
  • 25
    • 7444244966 scopus 로고    scopus 로고
    • Contribution of the Gag-Pol transframe domain p6* and its coding sequence to morphogenesis and replication of human immunodeficiency virus type 1
    • Paulus C, Ludwig C, Wagner R. Contribution of the Gag-Pol transframe domain p6* and its coding sequence to morphogenesis and replication of human immunodeficiency virus type 1. Virology 2004; 330:271-283.
    • (2004) Virology , vol.330 , pp. 271-283
    • Paulus, C.1    Ludwig, C.2    Wagner, R.3
  • 26
    • 42449098891 scopus 로고    scopus 로고
    • Importance of protease cleavage sites within and flanking human immunodeficiency virus type 1 transframe protein p6* for spatiotemporal regulation of protease activation
    • Ludwig C, Leiherer A, Wagner R. Importance of protease cleavage sites within and flanking human immunodeficiency virus type 1 transframe protein p6* for spatiotemporal regulation of protease activation. J Virol 2008; 82:4573-4584.
    • (2008) J Virol , vol.82 , pp. 4573-4584
    • Ludwig, C.1    Leiherer, A.2    Wagner, R.3
  • 27
    • 0031748806 scopus 로고    scopus 로고
    • Novel Gag-Pol frameshift site in human immunodeficiency virus type 1 variants resistant to protease inhibitors
    • Doyon L, Payant C, Brakier Gingras L, et al. Novel Gag-Pol frameshift site in human immunodeficiency virus type 1 variants resistant to protease inhibitors. J Virol 1998; 72:6146-6150.
    • (1998) J Virol , vol.72 , pp. 6146-6150
    • Doyon, L.1    Payant, C.2    Brakier Gingras, L.3
  • 28
    • 33846143163 scopus 로고    scopus 로고
    • Structure-function analysis of the ribosomal frameshifting signal of two human immunodeficiency virus type 1 isolates with increased resistance to viral protease inhibitors
    • Girnary R, King L, Robinson L, et al. Structure-function analysis of the ribosomal frameshifting signal of two human immunodeficiency virus type 1 isolates with increased resistance to viral protease inhibitors. J Gen Virol 2007; 88:226-235.
    • (2007) J Gen Virol , vol.88 , pp. 226-235
    • Girnary, R.1    King, L.2    Robinson, L.3
  • 29
    • 0037012979 scopus 로고    scopus 로고
    • Amprenavir-resistant HIV-1 exhibits lopinavir cross-resistance and reduced replication capacity
    • Prado JG, Wrin T, Beauchaine J, et al. Amprenavir-resistant HIV-1 exhibits lopinavir cross-resistance and reduced replication capacity. AIDS 2002; 16:1009-1017.
    • (2002) AIDS , vol.16 , pp. 1009-1017
    • Prado, J.G.1    Wrin, T.2    Beauchaine, J.3
  • 30
    • 33845971010 scopus 로고    scopus 로고
    • The pathway leading to TMC114 resistance is different for TMC114 compared with other protease inhibitors
    • De Meyer S, Azijn H, Fransen E, et al. The pathway leading to TMC114 resistance is different for TMC114 compared with other protease inhibitors. Antivir Ther 2006; 11:S24.
    • (2006) Antivir Ther , vol.11
    • De Meyer, S.1    Azijn, H.2    Fransen, E.3
  • 31
    • 10744226241 scopus 로고    scopus 로고
    • Novel bis- tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI) UIC-94017 (TMC114) with potent activity against multi-PI-resistant human immunodeficiency virus in vitro
    • Koh Y, Nakata H, Maeda K, et al. Novel bis- tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI) UIC-94017 (TMC114) with potent activity against multi-PI-resistant human immunodeficiency virus in vitro. Antimicrob Agents Chemother 2003; 47:3123-3129.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 3123-3129
    • Koh, Y.1    Nakata, H.2    Maeda, K.3
  • 32
    • 33846706048 scopus 로고    scopus 로고
    • In vitro cross resistance profile of RO033-4649 against a panel of multiply-substituted protease inhibitor resistant viruses: Role of common protease resistance mutations
    • Heilek-Snyder G, Kohli A, Cammack N, et al. In vitro cross resistance profile of RO033-4649 against a panel of multiply-substituted protease inhibitor resistant viruses: role of common protease resistance mutations. Antivir Ther 2003; 8:S21.
    • (2003) Antivir Ther , vol.8
    • Heilek-Snyder, G.1    Kohli, A.2    Cammack, N.3
  • 33
    • 37549060149 scopus 로고    scopus 로고
    • A novel genetic pathway involving L76V and M46I leading to lopinavir/r resistance
    • Nijhuis M, Wensing AM, Bierman W, et al. A novel genetic pathway involving L76V and M46I leading to lopinavir/r resistance. Antivir Ther 2007; 12:S140.
    • (2007) Antivir Ther , vol.12
    • Nijhuis, M.1    Wensing, A.M.2    Bierman, W.3
  • 34
    • 42449118624 scopus 로고    scopus 로고
    • In vitro HIV-1 resistance selection to GS-8374, a novel phosphonate protease inhibitor: Comparison with lopinavir, atazanavir and darunavir
    • Callebaut C, Stray K, Tsai L, et al. In vitro HIV-1 resistance selection to GS-8374, 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
  • 35
    • 0037155193 scopus 로고    scopus 로고
    • Amino acid substitutions in Gag protein at noncleavage sites are indispensable for the development of a high multitude of HIV-1 resistance against protease inhibitors
    • Gatanaga H, Suzuki Y, Tsang H, et al. Amino acid substitutions in Gag protein at noncleavage sites are indispensable for the development of a high multitude of HIV-1 resistance against protease inhibitors. J Biol Chem 2002; 277:5952-5961.
    • (2002) J Biol Chem , vol.277 , pp. 5952-5961
    • Gatanaga, H.1    Suzuki, Y.2    Tsang, H.3
  • 36
    • 67649613101 scopus 로고    scopus 로고
    • Substitutions within Gag but outside the cleavage sites can cause protease inhibitor resistance
    • Nijhuis M, van Maarseveen NM, de Jong D, et al. Substitutions within Gag but outside the cleavage sites can cause protease inhibitor resistance. Antivir Ther 2006; 11:S149.
    • (2006) Antivir Ther , vol.11
    • Nijhuis, M.1    van Maarseveen, N.M.2    de Jong, D.3
  • 37
    • 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
    • Bally F, Martinez R, Peters S, et al. 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.
    • (2000) AIDS Res Hum Retroviruses , vol.16 , pp. 1209-1213
    • Bally, F.1    Martinez, R.2    Peters, S.3
  • 38
    • 67649616585 scopus 로고    scopus 로고
    • HIV p7/p1 cleavage-site mutations are selected by the immune system and/or by antiretroviral therapy
    • Verheyen J, Schweitzer F, Harrer E, et al. HIV p7/p1 cleavage-site mutations are selected by the immune system and/or by antiretroviral therapy. Antivir Ther 2006; 13:A71.
    • (2006) Antivir Ther , vol.13
    • Verheyen, J.1    Schweitzer, F.2    Harrer, E.3
  • 39
    • 33750937532 scopus 로고    scopus 로고
    • Compensatory mutations at the HIV cleavage sites p7/p1 and p1/p6-gag in therapy-naive and therapy-experienced patients
    • This study shows accumulation of mutations in the HIV Gag NC/p1 and p1/p6 cleavage sites during protease inhibitor therapy
    • Verheyen J, Litau E, Sing T, et al. Compensatory mutations at the HIV cleavage sites p7/p1 and p1/p6-gag in therapy-naive and therapy-experienced patients. Antivir Ther 2006; 11:879-887. This study shows accumulation of mutations in the HIV Gag NC/p1 and p1/p6 cleavage sites during protease inhibitor therapy
    • (2006) Antivir Ther , vol.11 , pp. 879-887
    • Verheyen, J.1    Litau, E.2    Sing, T.3
  • 40
    • 67649607505 scopus 로고    scopus 로고
    • Relevance of HIV gag cleavage site mutations in failures of protease inhibitor therapies
    • Verheyen J, Altmann A, Knops E, et al. Relevance of HIV gag cleavage site mutations in failures of protease inhibitor therapies. Antivir Ther 2008; 13:A53.
    • (2008) Antivir Ther , vol.13
    • Verheyen, J.1    Altmann, A.2    Knops, E.3
  • 41
    • 67649580547 scopus 로고    scopus 로고
    • Cleavage site mutations in transmitted primary resistant HIV of therapy-naive patients
    • March, Cascais, Portugal;
    • Verheyen J, Kücherer C, Litau E, et al. Cleavage site mutations in transmitted primary resistant HIV of therapy-naive patients. 5th European HIV Drug Resistance Workshop; 28-30 March 2007; Cascais, Portugal; 2007.
    • (2007) 5th European HIV Drug Resistance Workshop; 28-30
    • Verheyen, J.1    Kücherer, C.2    Litau, E.3
  • 42
    • 42149119569 scopus 로고    scopus 로고
    • Impact of Gag cleavage site mutations on virological response to darunavir/ritonavir in treatment-experienced patients in POWER 1, 2 and 3
    • This study demonstrates that Gag cleavage site mutations may affect the virological response to a boosted protease inhibitor regimen
    • Dierynck I, De Meyer S, Cao-Van K, et al. Impact of Gag cleavage site mutations on virological response to darunavir/ritonavir in treatment-experienced patients in POWER 1, 2 and 3. Antivir Ther 2007; 12:S23. This study demonstrates that Gag cleavage site mutations may affect the virological response to a boosted protease inhibitor regimen.
    • (2007) Antivir Ther , vol.12
    • Dierynck, I.1    De Meyer, S.2    Cao-Van, K.3
  • 43
    • 67649631555 scopus 로고    scopus 로고
    • Treatment-emergent gag cleavage site mutations during virological failure of ritonavir-boosted protease inhibitors
    • Garcia-Diaz A, Fox Z, Dragsted UB, et al. Treatment-emergent gag cleavage site mutations during virological failure of ritonavir-boosted protease inhibitors. Antivir Ther 2008; 13:A80.
    • (2008) Antivir Ther , vol.13
    • Garcia-Diaz, A.1    Fox, Z.2    Dragsted, U.B.3
  • 44
    • 33747795928 scopus 로고    scopus 로고
    • Analysis of interference and co-evolution between protease inhibitor resistant mutations and gag mutations
    • Ueda T, Myint L, Shiino T, et al. Analysis of interference and co-evolution between protease inhibitor resistant mutations and gag mutations. Antivir Ther 2005; 10:S116.
    • (2005) Antivir Ther , vol.10
    • Ueda, T.1    Myint, L.2    Shiino, T.3
  • 45
    • 67649625562 scopus 로고    scopus 로고
    • Compensation of resistance-associated loss of replicative capacity by Gag is restricted to the NC-p1-p6 domains
    • Dam E, Faudon JL, Launay O, et al. Compensation of resistance-associated loss of replicative capacity by Gag is restricted to the NC-p1-p6 domains. Antivir Ther 2007; 12:S117.
    • (2007) Antivir Ther , vol.12
    • Dam, E.1    Faudon, J.L.2    Launay, O.3
  • 46
    • 33947173159 scopus 로고    scopus 로고
    • Association of Gag cleavage sites to protease mutations and to virological response in HIV-1 treated patients
    • Malet I, Roquebert B, Dalban C, et al. Association of Gag cleavage sites to protease mutations and to virological response in HIV-1 treated patients. J Infect 2007; 54:367-374.
    • (2007) J Infect , vol.54 , pp. 367-374
    • Malet, I.1    Roquebert, B.2    Dalban, C.3
  • 47
    • 77953308964 scopus 로고    scopus 로고
    • Changes in HIV Gag and protease cannot explain persistent viraemia in the majority of patients failing first-line lopinavir/ritonavir therapy
    • Nijhuis M, Schipper PJ, King M, et al. Changes in HIV Gag and protease cannot explain persistent viraemia in the majority of patients failing first-line lopinavir/ritonavir therapy. Antivir Ther 2007; 12:S146.
    • (2007) Antivir Ther , vol.12
    • Nijhuis, M.1    Schipper, P.J.2    King, M.3
  • 48
    • 67649616586 scopus 로고    scopus 로고
    • Discordant effects of Gag cleavage site mutations on the IC50 of protease inhibitors and on HIV replicative capacity
    • 3-6 February, Boston, MA;
    • Quercia R, Dam E, Descamps D, et al. Discordant effects of Gag cleavage site mutations on the IC50 of protease inhibitors and on HIV replicative capacity. 15th Conference on Retroviruses and Opportunistic Infections; 3-6 February 2008; Boston, MA; 2008.
    • (2008) 15th Conference on Retroviruses and Opportunistic Infections
    • Quercia, R.1    Dam, E.2    Descamps, D.3
  • 49
    • 67649625564 scopus 로고    scopus 로고
    • Gag-protease inter-relationships in drug-resistance and viral fitness
    • Parry CM, Kohli A, Pillay D. Gag-protease inter-relationships in drug-resistance and viral fitness. Antivir Ther 2008; 13:A81.
    • (2008) Antivir Ther , vol.13
    • Parry, C.M.1    Kohli, A.2    Pillay, D.3
  • 50
    • 67649574255 scopus 로고    scopus 로고
    • Increase of cleavage site mutations in the German HIV-1 seroconverter study over time
    • Verheyen J, Hamouda O, Somogy O, et al. Increase of cleavage site mutations in the German HIV-1 seroconverter study over time. Antivir Ther 2007; 12:S145.
    • (2007) Antivir Ther , vol.12
    • Verheyen, J.1    Hamouda, O.2    Somogy, O.3
  • 51
    • 67649583571 scopus 로고    scopus 로고
    • Absence of protease mutations upon virological failure of first-line fosamprenavir/ritonavir is not explained by the alternative selection of p7/p1 or p1/p6 Gag cleavage site mutations
    • Ait-Khaled M, Xu F, Tisdale M, et al. Absence of protease mutations upon virological failure of first-line fosamprenavir/ritonavir is not explained by the alternative selection of p7/p1 or p1/p6 Gag cleavage site mutations. Antivir Ther 2006; 11:S148.
    • (2006) Antivir Ther , vol.11
    • Ait-Khaled, M.1    Xu, F.2    Tisdale, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.