메뉴 건너뛰기




Volumn 287, Issue 49, 2012, Pages 40867-40874

The choreography of HIV-1 proteolytic processing and virion assembly

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL LEVEL; CELLULAR TARGETS; ENZYMATIC ACTIVITIES; HOST PROTEINS; INTEGRASE; INTENSIVE RESEARCH; NUCLEOCAPSIDS; PROTEIN-BINDING; PROTEIN-CODING; PROTEIN-PROTEIN INTERACTIONS; PROTEOLYTIC PROCESSING; REVERSE TRANSCRIPTASES; RNASE H; STRUCTURAL PROTEINS; VIRAL GENOME; VIRAL LIFE CYCLE; VIRAL PROTEASE; VIRAL PROTEINS; VIRAL REPLICATION;

EID: 84870340629     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R112.399444     Document Type: Short Survey
Times cited : (99)

References (101)
  • 1
    • 67649407509 scopus 로고    scopus 로고
    • The cell biology of HIV-1 virion genesis
    • Bieniasz, P. D. (2009) The cell biology of HIV-1 virion genesis. Cell Host Microbe 5, 550-558
    • (2009) Cell Host Microbe , vol.5 , pp. 550-558
    • Bieniasz, P.D.1
  • 2
    • 80051767703 scopus 로고    scopus 로고
    • The role of cellular factors in promoting HIV budding
    • Weiss, E. R., and Göttlinger, H. (2011) The role of cellular factors in promoting HIV budding. J. Mol. Biol. 410, 525-533
    • (2011) J. Mol. Biol. , vol.410 , pp. 525-533
    • Weiss, E.R.1    Göttlinger, H.2
  • 4
    • 84881193881 scopus 로고    scopus 로고
    • Three-Dimensional Analysis of Budding Sites and Released Virus Suggests a Revised Model for HIV-1 Morphogenesis
    • DOI 10.1016/j.chom.2008.10.013, PII S1931312808003673
    • Carlson, L. A., Briggs, J. A., Glass, B., Riches, J. D., Simon, M. N., Johnson, M. C., Müller, B., Grünewald, K., and Kräusslich, H. G. (2008) Three-dimensional analysis of budding sites and released virus suggests a revised model for HIV-1 morphogenesis. Cell Host Microbe 4, 592-599 (Pubitemid 352762957)
    • (2008) Cell Host and Microbe , vol.4 , Issue.6 , pp. 592-599
    • Carlson, L.-A.1    Briggs, J.A.G.2    Glass, B.3    Riches, J.D.4    Simon, M.N.5    Johnson, M.C.6    Muller, B.7    Grunewald, K.8    Krausslich, H.-G.9
  • 5
    • 0025297912 scopus 로고
    • Translational suppression in gene expression in retroviruses and retrotransposons
    • Jacks, T. (1990) Translational suppression in gene expression in retroviruses and retrotransposons. Curr. Top. Microbiol. Immunol. 157, 93-124
    • (1990) Curr. Top. Microbiol. Immunol. , vol.157 , pp. 93-124
    • Jacks, T.1
  • 6
    • 0004131381 scopus 로고    scopus 로고
    • Coffin, J. M., Hughes, S. H., and Varmus, H. E., ed Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Swanstrom, R., and Wills, J. W. (1997) in Retroviruses (Coffin, J. M., Hughes, S. H., and Varmus, H. E., ed) pp. 263-334, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.W.2
  • 8
    • 33144463548 scopus 로고    scopus 로고
    • The level of reverse transcriptase (RT) in human immunodeficiency virus type 1 particles affects susceptibility to nonnucleoside RT inhibitors but not to lamivudine
    • DOI 10.1128/JVI.80.5.2578-2581.2006
    • Ambrose, Z., Julias, J. G., Boyer, P. L., Kewalramani, V. N., and Hughes, S. H. (2006) The level of reverse transcriptase (RT) in human immunodeficiency virus type 1 particles affects susceptibility to nonnucleoside RT inhibitors but not to lamivudine. J. Virol. 80, 2578-2581 (Pubitemid 43271563)
    • (2006) Journal of Virology , vol.80 , Issue.5 , pp. 2578-2581
    • Ambrose, Z.1    Julias, J.G.2    Boyer, P.L.3    KewalRamani, V.N.4    Hughes, S.H.5
  • 10
    • 79956291343 scopus 로고    scopus 로고
    • Doseresponse curve slope is a missing dimension in the analysis of HIV-1 drug resistance
    • Sampah, M. E., Shen, L., Jilek, B. L., and Siliciano, R. F. (2011) Doseresponse curve slope is a missing dimension in the analysis of HIV-1 drug resistance. Proc. Natl. Acad. Sci. U.S.A. 108, 7613-7618
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 7613-7618
    • Sampah, M.E.1    Shen, L.2    Jilek, B.L.3    Siliciano, R.F.4
  • 11
    • 79960373686 scopus 로고    scopus 로고
    • A critical subset model provides a conceptual basis for the high antiviral activity of major HIV drugs
    • Shen, L., Rabi, S. A., Sedaghat, A. R., Shan, L., Lai, J., Xing, S., and Siliciano, R. F. (2011) A critical subset model provides a conceptual basis for the high antiviral activity of major HIV drugs. Sci. Transl. Med. 3, 91ra63
    • (2011) Sci. Transl. Med. , vol.3
    • Shen, L.1    Rabi, S.A.2    Sedaghat, A.R.3    Shan, L.4    Lai, J.5    Xing, S.6    Siliciano, R.F.7
  • 12
    • 0344334073 scopus 로고    scopus 로고
    • Effects of human immunodeficiency virus type 1 resistance to protease inhibitors on reverse transcriptase processing, activity, and drug sensitivity
    • de la Carrière, L. C., Paulous, S., Clavel, F., and Mammano, F. (1999) Effects of human immunodeficiency virus type 1 resistance to protease inhibitors on reverse transcriptase processing, activity, and drug sensitivity. J. Virol. 73, 3455-3459
    • (1999) J. Virol. , vol.73 , pp. 3455-3459
    • De La Carrière, L.C.1    Paulous, S.2    Clavel, F.3    Mammano, F.4
  • 13
    • 84862915396 scopus 로고    scopus 로고
    • Interplay between single resistance-associated mutations in the HIV-1 protease and viral infectivity, protease activity, and inhibitor sensitivity
    • Henderson, G. J., Lee, S. K., Irlbeck, D. M., Harris, J., Kline, M., Pollom, E., Parkin, N., and Swanstrom, R. (2012) Interplay between single resistance-associated mutations in the HIV-1 protease and viral infectivity, protease activity, and inhibitor sensitivity. Antimicrob. Agents Chemother. 56, 623-633
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 623-633
    • Henderson, G.J.1    Lee, S.K.2    Irlbeck, D.M.3    Harris, J.4    Kline, M.5    Pollom, E.6    Parkin, N.7    Swanstrom, R.8
  • 14
    • 0035031936 scopus 로고    scopus 로고
    • Selective excision of AZTMP by drug-resistant human immunodeficiency virus reverse transcriptase
    • DOI 10.1128/JVI.75.10.4832-4842.2001
    • Boyer, P. L., Sarafianos, S. G., Arnold, E., and Hughes, S. H. (2001) Selective excision of AZTMP by drug-resistant human immunodeficiency virus reverse transcriptase. J. Virol. 75, 4832-4842 (Pubitemid 32381526)
    • (2001) Journal of Virology , vol.75 , Issue.10 , pp. 4832-4842
    • Boyer, P.L.1    Sarafianos, S.G.2    Arnold, E.3    Hughes, S.H.4
  • 15
    • 0030987309 scopus 로고    scopus 로고
    • Nucleotide-induced stable complex formation by HIV-1 reverse transcriptase
    • DOI 10.1021/bi962410z
    • Tong, W., Lu, C. D., Sharma, S. K., Matsuura, S., So, A. G., and Scott, W. A. (1997) Nucleotide-induced stable complex formation by HIV-1 reverse transcriptase. Biochemistry 36, 5749-5757 (Pubitemid 27214926)
    • (1997) Biochemistry , vol.36 , Issue.19 , pp. 5749-5757
    • Tong, W.1    Lu, C.-D.2    Sharma, S.K.3    Matsuura, S.4    So, A.G.5    Scott, W.A.6
  • 16
    • 0033165851 scopus 로고    scopus 로고
    • A mechanism of AZT resistance: An increase in nucleotide-dependent primer unblocking by mutant HIV-1 reverse transcriptase
    • DOI 10.1016/S1097-2765(00)80185-9
    • Meyer, P. R., Matsuura, S. E., Mian, A. M., So, A. G., and Scott, W. A. (1999) A mechanism of AZT resistance: an increase in nucleotide-dependent primer unblocking by mutant HIV-1 reverse transcriptase. Mol. Cell 4, 35-43 (Pubitemid 29386129)
    • (1999) Molecular Cell , vol.4 , Issue.1 , pp. 35-43
    • Meyer, P.R.1    Matsuura, S.E.2    Mohsin, M.A.3    So, A.G.4    Scott, W.A.5
  • 17
    • 73149122533 scopus 로고    scopus 로고
    • Imaging the interaction of HIV-1 genomes and Gag during assembly of individual viral particles
    • Jouvenet, N., Simon, S. M., and Bieniasz, P. D. (2009) Imaging the interaction of HIV-1 genomes and Gag during assembly of individual viral particles. Proc. Natl. Acad. Sci. U.S.A. 106, 19114-19119
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 19114-19119
    • Jouvenet, N.1    Simon, S.M.2    Bieniasz, P.D.3
  • 19
    • 79251506313 scopus 로고    scopus 로고
    • Analysis of the initiating events in HIV-1 particle assembly and genome packaging
    • Kutluay, S. B., and Bieniasz, P. D. (2010) Analysis of the initiating events in HIV-1 particle assembly and genome packaging. PLoS Pathog. 6, e1001200
    • (2010) PLoS Pathog. , vol.6
    • Kutluay, S.B.1    Bieniasz, P.D.2
  • 21
    • 55049134097 scopus 로고    scopus 로고
    • Resilience to resistance of HIV-1 protease inhibitors: Profile of darunavir
    • Lefebvre, E., and Schiffer, C. A. (2008) Resilience to resistance of HIV-1 protease inhibitors: profile of darunavir. AIDS Rev. 10, 131-142
    • (2008) AIDS Rev. , vol.10 , pp. 131-142
    • Lefebvre, E.1    Schiffer, C.A.2
  • 22
    • 84856710288 scopus 로고    scopus 로고
    • Terminal interface conformations modulate dimer stability prior to amino-terminal autoprocessing of HIV-1 protease
    • Agniswamy, J., Sayer, J. M., Weber, I. T., and Louis, J. M. (2012) Terminal interface conformations modulate dimer stability prior to amino-terminal autoprocessing of HIV-1 protease. Biochemistry 51, 1041-1050
    • (2012) Biochemistry , vol.51 , pp. 1041-1050
    • Agniswamy, J.1    Sayer, J.M.2    Weber, I.T.3    Louis, J.M.4
  • 23
    • 17444392445 scopus 로고    scopus 로고
    • Autoprocessing of HIV-1 protease is tightly coupled to protein folding
    • DOI 10.1038/12327
    • Louis, J. M., Clore, G. M., and Gronenborn, A. M. (1999) Autoprocessing of HIV-1 protease is tightly coupled to protein folding. Nat. Struct. Biol. 6, 868-875 (Pubitemid 29415180)
    • (1999) Nature Structural Biology , vol.6 , Issue.9 , pp. 868-875
    • Louis, J.M.1    Marius, C.G.2    Gronenborn, A.M.3
  • 24
    • 80053605302 scopus 로고    scopus 로고
    • Flexible catalytic site conformations implicated in modulation of HIV-1 protease autoprocessing reactions
    • Huang, L., Li, Y., and Chen, C. (2011) Flexible catalytic site conformations implicated in modulation of HIV-1 protease autoprocessing reactions. Retrovirology 8, 79
    • (2011) Retrovirology , vol.8 , pp. 79
    • Huang, L.1    Li, Y.2    Chen, C.3
  • 25
    • 53349152834 scopus 로고    scopus 로고
    • Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease
    • Tang, C., Louis, J. M., Aniana, A., Suh, J. Y., and Clore, G. M. (2008) Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease. Nature 455, 693-696
    • (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
  • 26
    • 0037213627 scopus 로고    scopus 로고
    • The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage
    • DOI 10.1128/JVI.77.1.366-374.2003
    • Pettit, S. C., Gulnik, S., Everitt, L., and Kaplan, A. H. (2003) The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of Gag-Pol cleavage. J. Virol. 77, 366-374 (Pubitemid 36004976)
    • (2003) Journal of Virology , vol.77 , Issue.1 , pp. 366-374
    • Pettit, S.C.1    Gulnik, S.2    Everitt, L.3    Kaplan, A.H.4
  • 27
    • 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
    • DOI 10.1128/JVI.02353-07
    • Ludwig, C., Leiherer, A., and Wagner, R. (2008) Importance of protease cleavage sites within and flanking human immunodeficiency virus type 1 transframe protein p6*for spatiotemporal regulation of protease activation. J. Virol. 82, 4573-4584 (Pubitemid 351563694)
    • (2008) Journal of Virology , vol.82 , Issue.9 , pp. 4573-4584
    • Ludwig, C.1    Leiherer, A.2    Wagner, R.3
  • 28
    • 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
    • DOI 10.1128/JVI.78.16.8477-8485.2004
    • Pettit, S. C., Everitt, L. E., Choudhury, S., Dunn, B. M., and Kaplan, A. H. (2004) Initial cleavage of the human immunodeficiency virus type 1 Gag-Pol precursor by its activated protease occurs by an intramolecular mechanism. J. Virol. 78, 8477-8485 (Pubitemid 39025113)
    • (2004) Journal of Virology , 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
  • 30
    • 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
    • Pettit, S. C., Lindquist, J. N., Kaplan, A. H., and Swanstrom, R. (2005) 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 2, 66
    • (2005) Retrovirology , vol.2 , pp. 66
    • Pettit, S.C.1    Lindquist, J.N.2    Kaplan, A.H.3    Swanstrom, R.4
  • 31
    • 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, S. C., Moody, M. D., Wehbie, R. S., Kaplan, A. H., Nantermet, P. V., Klein, C. A., and Swanstrom, R. (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, 8017-8027 (Pubitemid 24362690)
    • (1994) Journal of Virology , 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    Swanstrom, R.7
  • 32
    • 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., and Kräusslich, H. G. (1998) Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites. J. Virol. 72, 2846-2854 (Pubitemid 28175521)
    • (1998) Journal of Virology , 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
  • 33
    • 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, S. K., Harris, J., and 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, 8536-8543
    • (2009) J. Virol. , vol.83 , pp. 8536-8543
    • Lee, S.K.1    Harris, J.2    Swanstrom, R.3
  • 35
    • 0026086220 scopus 로고
    • Mutagenesis of protease cleavage sites in the human immunodeficiency virus type 1 Gag polyprotein
    • Tritch, R. J., Cheng, Y. E., Yin, F. H., and Erickson-Viitanen, S. (1991) Mutagenesis of protease cleavage sites in the human immunodeficiency virus type 1 Gag polyprotein. J. Virol. 65, 922-930
    • (1991) J. Virol. , vol.65 , pp. 922-930
    • Tritch, R.J.1    Cheng, Y.E.2    Yin, F.H.3    Erickson-Viitanen, S.4
  • 36
    • 0026316549 scopus 로고
    • Analysis of retroviral protease cleavage sites reveals two types of cleavage sites and the structural requirements of the P1 amino acid
    • Pettit, S. C., Simsic, J., Loeb, D. D., Everitt, L., Hutchison, C. A., 3rd, and Swanstrom, R. (1991) Analysis of retroviral protease cleavage sites reveals two types of cleavage sites and the structural requirements of the P1 amino acid. J. Biol. Chem. 266, 14539-14547 (Pubitemid 21907537)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.22 , pp. 14539-14547
    • Pettit, S.C.1    Simsic, J.2    Loeb, D.D.3    Everitt, L.4    Hutchison III, C.A.5    Swanstrom, R.6
  • 37
    • 0036121219 scopus 로고    scopus 로고
    • Substrate shape determines specificity of recognition for HIV-1 protease: Analysis of crystal structures of six substrate complexes
    • DOI 10.1016/S0969-2126(02)00720-7, PII S0969212602007207
    • Prabu-Jeyabalan, M., Nalivaika, E., and Schiffer, C. A. (2002) Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes. Structure 10, 369-381 (Pubitemid 34230624)
    • (2002) Structure , vol.10 , Issue.3 , pp. 369-381
    • Prabu-Jeyabalan, M.1    Nalivaika, E.2    Schiffer, C.A.3
  • 38
    • 80051739212 scopus 로고    scopus 로고
    • Dynamics of preferential substrate recognition in HIV-1 protease: Redefining the substrate envelope
    • Ozen, A., Haliloǧlu, T., and Schiffer, C. A. (2011) Dynamics of preferential substrate recognition in HIV-1 protease: redefining the substrate envelope. J. Mol. Biol. 410, 726-744
    • (2011) J. Mol. Biol. , vol.410 , pp. 726-744
    • Ozen, A.1    Haliloǧlu, T.2    Schiffer, C.A.3
  • 39
    • 47049130164 scopus 로고    scopus 로고
    • Imaging the biogenesis of individual HIV-1 virions in live cells
    • DOI 10.1038/nature06998, PII NATURE06998
    • Jouvenet, N., Bieniasz, P. D., and Simon, S. M. (2008) Imaging the biogenesis of individual HIV-1 virions in live cells. Nature 454, 236-240 (Pubitemid 351969887)
    • (2008) Nature , vol.454 , Issue.7201 , pp. 236-240
    • Jouvenet, N.1    Bieniasz, P.D.2    Simon, S.M.3
  • 40
    • 0026322839 scopus 로고
    • Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly and viral infectivity
    • Kräusslich, H. G. (1991) Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly and viral infectivity. Proc. Natl. Acad. Sci. U.S.A. 88, 3213-3217
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 3213-3217
    • Kräusslich, H.G.1
  • 41
    • 67650925011 scopus 로고    scopus 로고
    • The nucleocapsid region of human immunodeficiency virus type 1 Gag assists in the coordination of assembly and Gag processing: Role for RNA-Gag binding in the early stages of assembly
    • Ott, D. E., Coren, L. V., and Shatzer, T. (2009) The nucleocapsid region of human immunodeficiency virus type 1 Gag assists in the coordination of assembly and Gag processing: role for RNA-Gag binding in the early stages of assembly. J. Virol. 83, 7718-7727
    • (2009) J. Virol. , vol.83 , pp. 7718-7727
    • Ott, D.E.1    Coren, L.V.2    Shatzer, T.3
  • 42
    • 0027932364 scopus 로고
    • The activity of the protease of human immunodeficiency virus type 1 is initiated at the membrane of infected cells before the release of viral proteins and is required for release to occur with maximum efficiency
    • Kaplan, A. H., Manchester, M., and Swanstrom, R. (1994) The activity of the protease of human immunodeficiency virus type 1 is initiated at the membrane of infected cells before the release of viral proteins and is required for release to occur with maximum efficiency. J. Virol. 68, 6782-6786
    • (1994) J. Virol. , vol.68 , pp. 6782-6786
    • Kaplan, A.H.1    Manchester, M.2    Swanstrom, R.3
  • 44
    • 0141571239 scopus 로고    scopus 로고
    • Covariation of amino acid positions in HIV-1 protease
    • DOI 10.1016/S0042-6822(03)00484-7
    • Hoffman, N. G., Schiffer, C. A., and Swanstrom, R. (2003) Covariation of amino acid positions in HIV-1 protease. Virology 314, 536-548 (Pubitemid 37206360)
    • (2003) Virology , vol.314 , Issue.2 , pp. 536-548
    • Hoffman, N.G.1    Schiffer, C.A.2    Swanstrom, R.3
  • 46
    • 0037310296 scopus 로고    scopus 로고
    • Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors
    • DOI 10.1128/AAC.47.2.759-769.2003
    • Watkins, T., Resch, W., Irlbeck, D., and Swanstrom, R. (2003) Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors. Antimicrob. Agents Chemother. 47, 759-769 (Pubitemid 36158112)
    • (2003) Antimicrobial Agents and Chemotherapy , vol.47 , Issue.2 , pp. 759-769
    • Watkins, T.1    Resch, W.2    Irlbeck, D.3    Swanstrom, R.4
  • 50
    • 0029151345 scopus 로고
    • Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure
    • Gulnik, S. V., Suvorov, L. I., Liu, B., Yu, B., Anderson, B., Mitsuya, H., and Erickson, J. W. (1995) Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure. Biochemistry 34, 9282-9287
    • (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
  • 51
    • 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., Erickson, J., Gustchina, E., Albert, J., Schipper, P., Gulnik, S., and Boucher, C. A. (1999) Increased fitness of drug-resistant HIV-1 protease as a result of acquisition of compensatory mutations during suboptimal therapy. AIDS 13, 2349-2359
    • (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
  • 52
    • 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
    • Partaledis, J. A., Yamaguchi, K., Tisdale, M., Blair, E. E., Falcione, C., Maschera, B., Myers, R. E., Pazhanisamy, S., Futer, O., and Cullinan, A. B. (1995) 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. 69, 5228-5235
    • (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
  • 53
  • 54
    • 0029731556 scopus 로고    scopus 로고
    • Mutational anatomy of an HIV-1 protease variant conferring cross- resistance to protease inhibitors in clinical trials. Compensatory modulations of binding and activity
    • DOI 10.1074/jbc.271.50.31957
    • Schock, H. B., Garsky, V. M., and Kuo, L. C. (1996) Mutational anatomy of an HIV-1 protease variant conferring cross-resistance to protease inhibitors in clinical trials. Compensatory modulations of binding and activity. J. Biol. Chem. 271, 31957-31963 (Pubitemid 26422220)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.50 , pp. 31957-31963
    • Schock, H.B.1    Garsky, V.M.2    Kuo, L.C.3
  • 55
    • 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
    • DOI 10.1128/JVI.78.22.12446-12454.2004
    • Prabu-Jeyabalan, M., Nalivaika, E. A., King, N. M., and Schiffer, C. A. (2004) 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. 78, 12446-12454 (Pubitemid 39458763)
    • (2004) Journal of Virology , vol.78 , Issue.22 , pp. 12446-12454
    • Prabu-Jeyabalan, M.1    Nalivaika, E.A.2    King, N.M.3    Schiffer, C.A.4
  • 56
    • 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., McKercher, G., Pilote, L., and Lamarre, D. (1997) Impaired fitness of human immunodeficiency virus type 1 variants with high-level resistance to protease inhibitors. J. Virol. 71, 1089-1096 (Pubitemid 27030280)
    • (1997) Journal of Virology , vol.71 , Issue.2 , pp. 1089-1096
    • Croteau, G.1    Doyon, L.2    Thibeault, D.3    Mckercher, G.4    Pilote, L.5    Lamarre, D.6
  • 57
    • 0036337934 scopus 로고    scopus 로고
    • Nelfinavir-resistant, amprenavir-hypersusceptible strains of human immunodeficiency virus type 1 carrying an N88S mutation in protease have reduced infectivity, reduced replication capacity, and reduced fitness and process the Gag polyprotein precursor aberrantly
    • DOI 10.1128/JVI.76.17.8659-8666.2002
    • Resch, W., Ziermann, R., Parkin, N., Gamarnik, A., and Swanstrom, R. (2002) Nelfinavir-resistant, amprenavir-hypersusceptible strains of human immunodeficiency virus type 1 carrying an N88S mutation in protease have reduced infectivity, reduced replication capacity, and reduced fitness and process the Gag polyprotein precursor aberrantly. J. Virol. 76, 8659-8666 (Pubitemid 34864060)
    • (2002) Journal of Virology , vol.76 , Issue.17 , pp. 8659-8666
    • Resch, W.1    Ziermann, R.2    Parkin, N.3    Gamarnik, A.4    Swanstrom, R.5
  • 58
    • 0031946007 scopus 로고    scopus 로고
    • Loss of viral fitness associated with multiple Gag and Gag-Pol processing defects in human immunodeficiency virus type 1 variants selected for resistance to protease inhibitors in vivo
    • Zennou, V., Mammano, F., Paulous, S., Mathez, D., and Clavel, F. (1998) Loss of viral fitness associated with multiple Gag and Gag-Pol processing defects in human immunodeficiency virus type 1 variants selected for resistance to protease inhibitors in vivo. J. Virol. 72, 3300-3306 (Pubitemid 28175575)
    • (1998) Journal of Virology , vol.72 , Issue.4 , pp. 3300-3306
    • Zennou, V.1    Mammano, F.2    Paulous, S.3    Mathez, D.4    Clavel, F.5
  • 59
    • 0029131607 scopus 로고
    • Three-dimensional structure of a mutant HIV-1 protease displaying cross-resistance to all protease inhibitors in clinical trials
    • Chen, Z., Li, Y., Schock, H. B., Hall, D., Chen, E., and Kuo, L. C. (1995) Three-dimensional structure of a mutant HIV-1 protease displaying cross-resistance to all protease inhibitors in clinical trials. J. Biol. Chem. 270, 21433-21436
    • (1995) J. Biol. Chem. , vol.270 , pp. 21433-21436
    • Chen, Z.1    Li, Y.2    Schock, H.B.3    Hall, D.4    Chen, E.5    Kuo, L.C.6
  • 62
    • 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
    • DOI 10.1128/JVI.74.18.8524-8531.2000
    • Mammano, F., Trouplin, V., Zennou, V., and Clavel, F. (2000) 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. 74, 8524-8531 (Pubitemid 30666703)
    • (2000) Journal of Virology , vol.74 , Issue.18 , pp. 8524-8531
    • Mammano, F.1    Trouplin, V.2    Zennou, V.3    Clavel, F.4
  • 63
    • 0028854676 scopus 로고
    • Selection and analysis of human immunodeficiency virus type 1 variants with increased resistance to ABT-538, a novel protease inhibitor
    • Markowitz, M., Mo, H., Kempf, D. J., Norbeck, D. W., Bhat, T. N., Erickson, J. W., and Ho, D. D. (1995) Selection and analysis of human immunodeficiency virus type 1 variants with increased resistance to ABT-538, a novel protease inhibitor. J. Virol. 69, 701-706
    • (1995) J. Virol. , vol.69 , pp. 701-706
    • Markowitz, M.1    Mo, H.2    Kempf, D.J.3    Norbeck, D.W.4    Bhat, T.N.5    Erickson, J.W.6    Ho, D.D.7
  • 64
    • 0032928065 scopus 로고    scopus 로고
    • Replicative fitness of protease inhibitor-resistant mutants of human immunodeficiency virus type 1
    • Martinez-Picado, J., Savara, A. V., Sutton, L., and D'Aquila, R. T. (1999) Replicative fitness of protease inhibitor-resistant mutants of human immunodeficiency virus type 1. J. Virol. 73, 3744-3752 (Pubitemid 29189817)
    • (1999) Journal of Virology , vol.73 , Issue.5 , pp. 3744-3752
    • Martinez-Picado, J.1    Savara, A.V.2    Sutton, L.3    D'Aquila, R.T.4
  • 65
    • 80051749007 scopus 로고    scopus 로고
    • Accessory mutations maintain stability in drug-resistant HIV-1 protease
    • Chang, M. W., and Torbett, B. E. (2011) Accessory mutations maintain stability in drug-resistant HIV-1 protease. J. Mol. Biol. 410, 756-760
    • (2011) J. Mol. Biol. , vol.410 , pp. 756-760
    • Chang, M.W.1    Torbett, B.E.2
  • 66
    • 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., Sudre, P., and Telenti, A. (2000) 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 16, 1209-1213
    • (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
  • 67
    • 0029899093 scopus 로고    scopus 로고
    • Second locus involved in human immunodeficiency virus type 1 resistance to protease inhibitors
    • Doyon, L., Croteau, G., Thibeault, D., Poulin, F., Pilote, L., and Lamarre, D. (1996) Second locus involved in human immunodeficiency virus type 1 resistance to protease inhibitors. J. Virol. 70, 3763-3769 (Pubitemid 26161824)
    • (1996) Journal of Virology , vol.70 , Issue.6 , pp. 3763-3769
    • Doyon, L.1    Croteau, G.2    Thibeault, D.3    Poulin, F.4    Pilote, L.5    Lamarre, D.6
  • 68
    • 0035831126 scopus 로고    scopus 로고
    • Mutations in HIV-1 gag cleavage sites and their association with protease mutations
    • DOI 10.1097/00002030-200103090-00013
    • Koch, N., Yahi, N., Fantini, J., and Tamalet, C. (2001) Mutations in HIV-1 Gag cleavage sites and their association with protease mutations. AIDS 15, 526-528 (Pubitemid 32207574)
    • (2001) AIDS , vol.15 , Issue.4 , pp. 526-528
    • Koch, N.1    Yahi, N.2    Fantini, J.3    Tamalet, C.4
  • 69
    • 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., and Clavel, F. (1998) 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. 72, 7632-7637 (Pubitemid 28377901)
    • (1998) Journal of Virology , vol.72 , Issue.9 , pp. 7632-7637
    • Mammano, F.1    Petit, C.2    Clavel, F.3
  • 70
    • 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., Lane, H. C., Falloon, J., Vasudevachari, M. B., and Salzman, N. P. (1997) Drug resistance during indinavir therapy is caused by mutations in the protease gene and in its Gag substrate cleavage sites. J. Virol. 71, 6662-6670 (Pubitemid 27355324)
    • (1997) Journal of Virology , vol.71 , Issue.9 , 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
  • 71
    • 69449097224 scopus 로고    scopus 로고
    • Gag determinants of fitness and drug susceptibility in protease inhibitor-resistant human immunodeficiency virus type 1
    • Parry, C. M., Kohli, A., Boinett, C. J., Towers, G. J., McCormick, A. L., and Pillay, D. (2009) Gag determinants of fitness and drug susceptibility in protease inhibitor-resistant human immunodeficiency virus type 1. J. Virol. 83, 9094-9101
    • (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
  • 73
    • 4644301808 scopus 로고    scopus 로고
    • High-resolution structure of a retrovial capsid hexameric amino-terminal domain
    • DOI 10.1038/nature02915
    • Mortuza, G. B., Haire, L. F., Stevens, A., Smerdon, S. J., Stoye, J. P., and Taylor, I. A. (2004) High-resolution structure of a retroviral capsid hexameric amino-terminal domain. Nature 431, 481-485 (Pubitemid 39329590)
    • (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
  • 74
    • 0032536896 scopus 로고    scopus 로고
    • Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly
    • DOI 10.1093/emboj/17.6.1555
    • von Schwedler, U. K., Stemmler, T. L., Klishko, V. Y., Li, S., Albertine, K. H., Davis, D. R., and Sundquist, W. I. (1998) Proteolytic refolding of the HIV-1 capsid protein amino terminus facilitates viral core assembly. EMBO J. 17, 1555-1568 (Pubitemid 28119109)
    • (1998) EMBO Journal , vol.17 , Issue.6 , pp. 1555-1568
    • Von Schwedler, U.K.1    Stemmler, T.L.2    Klishko, V.Y.3    Li, S.4    Albertine, K.H.5    Davis, D.R.6    Sundquist, W.I.7
  • 75
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • Li, S., Hill, C. P., Sundquist, W. I., and Finch, J. T. (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
  • 77
    • 26944455601 scopus 로고    scopus 로고
    • The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor
    • DOI 10.1038/nsmb967, PII NSMB967
    • Ternois, F., Sticht, J., Duquerroy, S., Kräusslich, H. G., and Rey, F. A. (2005) The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor. Nat. Struct. Mol. Biol. 12, 678-682 (Pubitemid 43086273)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.8 , pp. 678-682
    • Ternois, F.1    Sticht, J.2    Duquerroy, S.3    Krausslich, H.-G.4    Rey, F.A.5
  • 81
    • 78650064115 scopus 로고    scopus 로고
    • Smallmolecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization
    • Shi, J., Zhou, J., Shah, V. B., Aiken, C., and Whitby, K. (2011) Smallmolecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization. J. Virol. 85, 542-549
    • (2011) J. Virol. , vol.85 , pp. 542-549
    • Shi, J.1    Zhou, J.2    Shah, V.B.3    Aiken, C.4    Whitby, K.5
  • 83
    • 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, S. C., Henderson, G. J., Schiffer, C. A., and 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, 10226-10233
    • (2002) J. Virol. , vol.76 , pp. 10226-10233
    • Pettit, S.C.1    Henderson, G.J.2    Schiffer, C.A.3    Swanstrom, R.4
  • 84
    • 35348911923 scopus 로고    scopus 로고
    • Mutational analysis of the C-terminal Gag cleavage sites in human immunodeficiency virus type 1
    • DOI 10.1128/JVI.02496-06
    • Coren, L. V., Thomas, J. A., Chertova, E., Sowder, R. C., 2nd, Gagliardi, T. D., Gorelick, R. J., and Ott, D. E. (2007) Mutational analysis of the C-terminal Gag cleavage sites in human immunodeficiency virus type 1. J. Virol. 81, 10047-10054 (Pubitemid 350067708)
    • (2007) Journal of Virology , vol.81 , Issue.18 , pp. 10047-10054
    • Coren, L.V.1    Thomas, J.A.2    Chertova, E.3    Sowder II, R.C.4    Gagliardi, T.D.5    Gorelick, R.J.6    Ott, D.E.7
  • 86
    • 0346688636 scopus 로고    scopus 로고
    • Small-Molecule Inhibition of Human Immunodeficiency Virus Type 1 Replication by Specific Targeting of the Final Step of Virion Maturation
    • DOI 10.1128/JVI.78.2.922-929.2004
    • Zhou, J., Yuan, X., Dismuke, D., Forshey, B. M., Lundquist, C., Lee, K. H., Aiken, C., and Chen, C. H. (2004) Small-molecule inhibition of human immunodeficiency virus type 1 replication by specific targeting of the final step of virion maturation. J. Virol. 78, 922-929 (Pubitemid 38067613)
    • (2004) Journal of Virology , 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    Aiken, C.7    Chen, C.H.8
  • 87
    • 78951488338 scopus 로고    scopus 로고
    • HIV-1 maturation inhibitor bevirimat stabilizes the immature Gag lattice
    • Keller, P. W., Adamson, C. S., Heymann, J. B., Freed, E. O., and Steven, A. C. (2011) HIV-1 maturation inhibitor bevirimat stabilizes the immature Gag lattice. J. Virol. 85, 1420-1428
    • (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
  • 88
    • 28344449442 scopus 로고    scopus 로고
    • Inhibition of HIV-1 maturation via drug association with the viral Gag protein in immature HIV-1 particles
    • DOI 10.1074/jbc.M508951200
    • Zhou, J., Huang, L., Hachey, D. L., Chen, C. H., and Aiken, C. (2005) Inhibition of HIV-1 maturation via drug association with the viral Gag protein in immature HIV-1 particles. J. Biol. Chem. 280, 42149-42155 (Pubitemid 43023184)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.51 , pp. 42149-42155
    • Zhou, J.1    Huang, L.2    Hachey, D.L.3    Chen, C.H.4    Aiken, C.5
  • 89
    • 82755190460 scopus 로고    scopus 로고
    • The prototype HIV-1 maturation inhibitor, bevirimat, binds to the CA-SP1 cleavage site in immature Gag particles
    • Nguyen, A. T., Feasley, C. L., Jackson, K. W., Nitz, T. J., Salzwedel, K., Air, G. M., and Sakalian, M. (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    Sakalian, M.7
  • 90
    • 77649179193 scopus 로고    scopus 로고
    • The capsid-spacer peptide 1 Gag processing intermediate is a dominant-negative inhibitor of HIV-1 maturation
    • Checkley, M. A., Luttge, B. G., Soheilian, F., Nagashima, K., and Freed, E. O. (2010) The capsid-spacer peptide 1 Gag processing intermediate is a dominant-negative inhibitor of HIV-1 maturation. Virology 400, 137-144
    • (2010) Virology , vol.400 , pp. 137-144
    • Checkley, M.A.1    Luttge, B.G.2    Soheilian, F.3    Nagashima, K.4    Freed, E.O.5
  • 91
    • 33646021013 scopus 로고    scopus 로고
    • Mutant murine leukemia virus Gag proteins lacking proline at the N terminus of the capsid domain block infectivity in virions containing wild-type Gag
    • Rulli, S. J., Jr., Muriaux, D., Nagashima, K., Mirro, J., Oshima, M., Baumann, J. G., and Rein, A. (2006) Mutant murine leukemia virus Gag proteins lacking proline at the N terminus of the capsid domain block infectivity in virions containing wild-type Gag. Virology 347, 364-371
    • (2006) Virology , vol.347 , pp. 364-371
    • Rulli Jr., S.J.1    Muriaux, D.2    Nagashima, K.3    Mirro, J.4    Oshima, M.5    Baumann, J.G.6    Rein, A.7
  • 92
    • 0028338652 scopus 로고
    • Characterization of human immunodeficiency virus type 1 dimeric RNA from wild-type and protease-defective virions
    • Fu, W., Gorelick, R. J., and Rein, A. (1994) Characterization of human immunodeficiency virus type 1 dimeric RNA from wild-type and protease-defective virions. J. Virol. 68, 5013-5018 (Pubitemid 24226568)
    • (1994) Journal of Virology , vol.68 , Issue.8 , pp. 5013-5018
    • Fu, W.1    Gorelick, R.J.2    Rein, A.3
  • 93
    • 0034856077 scopus 로고    scopus 로고
    • Proteolytic processing of the p2/nucleocapsid cleavage site is critical for human immunodeficiency virus type 1 RNA dimer maturation
    • DOI 10.1128/JVI.75.19.9156-9164.2001
    • Shehu-Xhilaga, M., Kraeusslich, H. G., Pettit, S., Swanstrom, R., Lee, J. Y., Marshall, J. A., Crowe, S. M., and Mak, J. (2001) Proteolytic processing of the p2/nucleocapsid cleavage site is critical for human immunodeficiency virus type 1 RNA dimer maturation. J. Virol. 75, 9156-9164 (Pubitemid 32851920)
    • (2001) Journal of Virology , 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    Crowe, S.M.7    Mak, J.8
  • 94
    • 43049089699 scopus 로고    scopus 로고
    • Nucleocapsid protein function in early infection processes
    • Thomas, J. A., and Gorelick, R. J. (2008) Nucleocapsid protein function in early infection processes. Virus Res. 134, 39-63
    • (2008) Virus Res. , vol.134 , pp. 39-63
    • Thomas, J.A.1    Gorelick, R.J.2
  • 95
    • 0028133360 scopus 로고
    • Cleavage of p15 protein in vitro by human immunodeficiency virus type 1 protease is RNA dependent
    • Sheng, N., and Erickson-Viitanen, S. (1994) Cleavage of p15 protein in vitro by human immunodeficiency virus type 1 protease is RNA-dependent. J. Virol. 68, 6207-6214 (Pubitemid 24294870)
    • (1994) Journal of Virology , vol.68 , Issue.10 , pp. 6207-6214
    • Sheng, N.1    Erickson-Viitanen, S.2
  • 96
    • 0030738085 scopus 로고    scopus 로고
    • Determinants of the human immunodeficiency virus type 1 p15NC-RNA interaction that affect enhanced cleavage by the viral protease
    • Sheng, N., Pettit, S. C., Tritch, R. J., Ozturk, D. H., Rayner, M. M., Swanstrom, R., and Erickson-Viitanen, S. (1997) Determinants of the human immunodeficiency virus type 1 p15NC-RNA interaction that affect enhanced cleavage by the viral protease. J. Virol. 71, 5723-5732 (Pubitemid 27304905)
    • (1997) Journal of Virology , vol.71 , Issue.8 , pp. 5723-5732
    • Sheng, N.1    Pettit, S.C.2    Tritch, R.J.3    Ozturk, D.H.4    Rayner, M.M.5    Swanstrom, R.6    Erickson-Viitanen, S.7
  • 97
    • 84862291648 scopus 로고    scopus 로고
    • Identification of HIV-1 inhibitors targeting the nucleocapsid protein
    • Breuer, S., Chang, M. W., Yuan, J., and Torbett, B. E. (2012) Identification of HIV-1 inhibitors targeting the nucleocapsid protein. J. Med. Chem. 55, 4968-4977
    • (2012) J. Med. Chem. , vol.55 , pp. 4968-4977
    • Breuer, S.1    Chang, M.W.2    Yuan, J.3    Torbett, B.E.4
  • 98
    • 79956196738 scopus 로고    scopus 로고
    • A cleavage enzyme-cytometric bead array provides biochemical profiling of resistance mutations in HIV-1 Gag and protease
    • Breuer, S., Sepulveda, H., Chen, Y., Trotter, J., and Torbett, B. E. (2011) A cleavage enzyme-cytometric bead array provides biochemical profiling of resistance mutations in HIV-1 Gag and protease. Biochemistry 50, 4371-4381
    • (2011) Biochemistry , vol.50 , pp. 4371-4381
    • Breuer, S.1    Sepulveda, H.2    Chen, Y.3    Trotter, J.4    Torbett, B.E.5
  • 99
    • 77950927781 scopus 로고    scopus 로고
    • A simple fluorescence based assay for quantification of human immunodeficiency virus particle release
    • Hermle, J., Anders, M., Heuser, A. M., and Müller, B. (2010) A simple fluorescence based assay for quantification of human immunodeficiency virus particle release. BMC Biotechnol. 10, 32
    • (2010) BMC Biotechnol. , vol.10 , pp. 32
    • Hermle, J.1    Anders, M.2    Heuser, A.M.3    Müller, B.4
  • 100
    • 2942750655 scopus 로고
    • Identification of a large polypeptide precursor of avian oncornavirus proteins
    • Vogt, V. M., and Eisenman, R. (1973) Identification of a large polypeptide precursor of avian oncornavirus proteins. Proc. Natl. Acad. Sci. U.S.A. 70, 1734-1738
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 1734-1738
    • Vogt, V.M.1    Eisenman, R.2
  • 101
    • 5444247213 scopus 로고    scopus 로고
    • Combating susceptibility to drug resistance: Lessons from HIV-1 protease
    • DOI 10.1016/j.chembiol.2004.08.010, PII S1074552104002431
    • King, N. M., Prabu-Jeyabalan, M., Nalivaika, E. A., and Schiffer, C. (2004) Combating susceptibility to drug resistance: lessons from HIV-1 protease. Chem. Biol. 11, 1333-1338 (Pubitemid 39351371)
    • (2004) Chemistry and Biology , vol.11 , Issue.10 , pp. 1333-1338
    • King, N.M.1    Prabu-Jeyabalan, M.2    Nalivaika, E.A.3    Schiffer, C.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.