메뉴 건너뛰기




Volumn 43, Issue 38, 2004, Pages 12141-12151

Comparing the accumulation of active- and nonactive-site mutations in the HIV-1 protease

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CATALYSIS; CRYSTAL STRUCTURE; DYNAMICS;

EID: 4644353680     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049459m     Document Type: Article
Times cited : (72)

References (57)
  • 1
    • 0037047028 scopus 로고    scopus 로고
    • Amplification of the effects of drug resistance mutations by background polymorphisms in HIV-1 protease from African subtypes
    • Velazquez-Campoy, A., Vega, S., and Freire, E. (2002) Amplification of the effects of drug resistance mutations by background polymorphisms in HIV-1 protease from African subtypes, Biochemistry 41, 8613-8619.
    • (2002) Biochemistry , vol.41 , pp. 8613-8619
    • Velazquez-Campoy, A.1    Vega, S.2    Freire, E.3
  • 2
    • 0031006664 scopus 로고    scopus 로고
    • Identification of a loop outside the active site cavity of the human immunodeficiency virus proteases which confers inhibitor specificity
    • Towler, E. M., Thompson, S. K., Tomaszek, T., and Debouck, C. (1997) Identification of a loop outside the active site cavity of the human immunodeficiency virus proteases which confers inhibitor specificity, Biochemistry 36, 5128-5133.
    • (1997) Biochemistry , vol.36 , pp. 5128-5133
    • Towler, E.M.1    Thompson, S.K.2    Tomaszek, T.3    Debouck, C.4
  • 3
    • 0032483034 scopus 로고    scopus 로고
    • Structural role of the 30's loop in determining the ligand specificity of the human immunodeficiency virus protease
    • Swairjo, M. A., Towler, E. M., Debouck, C., and Abdel-Meguid, S. S. (1998) Structural role of the 30's loop in determining the ligand specificity of the human immunodeficiency virus protease, Biochemistry 37, 10928-10936.
    • (1998) Biochemistry , vol.37 , pp. 10928-10936
    • Swairjo, M.A.1    Towler, E.M.2    Debouck, C.3    Abdel-Meguid, S.S.4
  • 5
    • 0033588178 scopus 로고    scopus 로고
    • Nonactive site changes elicit broad-based cross-resistance of the HIV-1 protease to inhibitors
    • Olsen, D. B., Stahlhut, M. W., Rutkowski, C. A., Schock, H. B., van Olden, A. L., and Kuo, L. C. (1999) Nonactive site changes elicit broad-based cross-resistance of the HIV-1 protease to inhibitors, J. Biol. Chem. 274, 23699-23701.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23699-23701
    • Olsen, D.B.1    Stahlhut, M.W.2    Rutkowski, C.A.3    Schock, H.B.4    Van Olden, A.L.5    Kuo, L.C.6
  • 6
    • 0029795041 scopus 로고    scopus 로고
    • Human immunodeficiency virus protease ligand specificity conferred by residues outside of the active site cavity
    • Hoog, S. S., Towler, E. M., Zhao, B., Doyle, M. L., Debouck, C., and Abdel-Meguid, S. S. (1996) Human immunodeficiency virus protease ligand specificity conferred by residues outside of the active site cavity, Biochemistry 35, 10279-10286.
    • (1996) Biochemistry , vol.35 , pp. 10279-10286
    • Hoog, S.S.1    Towler, E.M.2    Zhao, B.3    Doyle, M.L.4    Debouck, C.5    Abdel-Meguid, S.S.6
  • 7
    • 0034615571 scopus 로고    scopus 로고
    • Structural and biochemical studies of retroviral proteases
    • Wlodawer, A., and Gustchina, A. (2000) Structural and biochemical studies of retroviral proteases, Biochim. Biophys. Acta 1477, 16-34.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 16-34
    • Wlodawer, A.1    Gustchina, A.2
  • 8
    • 0034615554 scopus 로고    scopus 로고
    • Targeting the HIV-protease in AIDS therapy: A current clinical perspective
    • Tomasselli, A. G., and Heinrikson, R. L. (2000) Targeting the HIV-protease in AIDS therapy: A current clinical perspective, Biochim. Biophys. Acta 1477, 189-214.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 189-214
    • Tomasselli, A.G.1    Heinrikson, R.L.2
  • 9
    • 0038732585 scopus 로고    scopus 로고
    • Anatomy and pathology of HIV-1 peptidase
    • Dunn, B. M. (2002) Anatomy and pathology of HIV-1 peptidase, Essays Biochem. 38, 113-127.
    • (2002) Essays Biochem. , vol.38 , pp. 113-127
    • Dunn, B.M.1
  • 11
    • 0033827606 scopus 로고    scopus 로고
    • Baseline human immunodeficiency virus type 1 phenotype, genotype, and RNA response after switching from long-term hard-capsule saquinavir to indinavir or soft-gel-capsule saquinavir in AIDS clinical trials group protocol 333
    • Para, M. F., Glidden, D. V., Coombs, R. W., Collier, A. C., Condra, J. H., Craig, C., Bassett, R., Leavitt, R., Snyder, S., McAuliffe, V., and Boucher, C. (2000) Baseline human immunodeficiency virus type 1 phenotype, genotype, and RNA response after switching from long-term hard-capsule saquinavir to indinavir or soft-gel-capsule saquinavir in AIDS clinical trials group protocol 333, J. Infect. Dis. 182, 733-743.
    • (2000) J. Infect. Dis. , vol.182 , pp. 733-743
    • Para, M.F.1    Glidden, D.V.2    Coombs, R.W.3    Collier, A.C.4    Condra, J.H.5    Craig, C.6    Bassett, R.7    Leavitt, R.8    Snyder, S.9    McAuliffe, V.10    Boucher, C.11
  • 12
    • 0033534115 scopus 로고    scopus 로고
    • HIV-1 genotypic resistance patterns predict response to saquinavir-ritonavir therapy in patients in whom previous protease inhibitor therapy had failed
    • Zolopa, A. R., Shafer, R. W., Warford, A., Montoya, J. G., Hsu, P., Katzenstein, D., Merigan, T. C., and Efron, B. (1999) HIV-1 genotypic resistance patterns predict response to saquinavir-ritonavir therapy in patients in whom previous protease inhibitor therapy had failed, Ann. Intern. Med. 131, 813-821.
    • (1999) Ann. Intern. Med. , vol.131 , pp. 813-821
    • Zolopa, A.R.1    Shafer, R.W.2    Warford, A.3    Montoya, J.G.4    Hsu, P.5    Katzenstein, D.6    Merigan, T.C.7    Efron, B.8
  • 13
    • 0033827608 scopus 로고    scopus 로고
    • Drug resistance and predicted virologic responses to human immunodeficiency virus type 1 protease inhibitor therapy
    • Condra, J. H., Petropoulos, C. J., Ziermann, R., Schleif, W. A., Shivaprakash, M., and Emini, E. A. (2000) Drug resistance and predicted virologic responses to human immunodeficiency virus type 1 protease inhibitor therapy, J. Infect. Dis. 182, 758-765.
    • (2000) J. Infect. Dis. , vol.182 , pp. 758-765
    • Condra, J.H.1    Petropoulos, C.J.2    Ziermann, R.3    Schleif, W.A.4    Shivaprakash, M.5    Emini, E.A.6
  • 15
    • 0026325601 scopus 로고
    • Kinetic studies of human immunodeficiency virus type 1 protease and its active-site hydrogen bond mutant A28S
    • Ido, E., Man, H. P., Kezdy, F. J., and Tang, J. (1991) Kinetic studies of human immunodeficiency virus type 1 protease and its active-site hydrogen bond mutant A28S, J. Biol. Chem. 266, 24359-24366.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24359-24366
    • Ido, E.1    Man, H.P.2    Kezdy, F.J.3    Tang, J.4
  • 16
    • 0036056291 scopus 로고    scopus 로고
    • Naturally occurring amino acid polymorphisms in human immunodeficiency virus type 1 (HIV-1) Gag p7(NC) and the C-cleavage site impact Gag-Pol processing by HIV-1 protease
    • Goodenow, M. M., Bloom, G., Rose, S. L., Pomeroy, S. M., O'Brien, P. O., Perez, E. E., Sleasman, J. W., and Dunn, B. M. (2002) Naturally occurring amino acid polymorphisms in human immunodeficiency virus type 1 (HIV-1) Gag p7(NC) and the C-cleavage site impact Gag-Pol processing by HIV-1 protease, Virology 292, 137-149.
    • (2002) Virology , vol.292 , pp. 137-149
    • Goodenow, M.M.1    Bloom, G.2    Rose, S.L.3    Pomeroy, S.M.4    O'Brien, P.O.5    Perez, E.E.6    Sleasman, J.W.7    Dunn, B.M.8
  • 18
    • 0346333382 scopus 로고    scopus 로고
    • Secondary mutations M36I and A71V in the human immunodeficiency virus type 1 protease can provide an advantage for the emergence of the primary mutation D30N
    • Clemente, J. C., Hemrajani, R., Blum, L. E., Goodenow, M. M., and Dunn, B. M. (2003) Secondary mutations M36I and A71V in the human immunodeficiency virus type 1 protease can provide an advantage for the emergence of the primary mutation D30N, Biochemistry 42, 15029-15035.
    • (2003) Biochemistry , vol.42 , pp. 15029-15035
    • Clemente, J.C.1    Hemrajani, R.2    Blum, L.E.3    Goodenow, M.M.4    Dunn, B.M.5
  • 20
    • 0034452113 scopus 로고    scopus 로고
    • Chimeric aspartic proteinases and active site binding
    • Bhatt, D., and Dunn, B. M. (2000) Chimeric aspartic proteinases and active site binding, Bioorg. Chem. 28, 374-393.
    • (2000) Bioorg. Chem. , vol.28 , pp. 374-393
    • Bhatt, D.1    Dunn, B.M.2
  • 23
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron-density maps and the location of errors in these models, Acta Crystallogr., Sect. A 47, 110-119.
    • (1991) Acta Crystallogr., Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 24
    • 4644281272 scopus 로고    scopus 로고
    • note
    • DeLano, W. L. (2002) DeLano Scientific, San Carlos, CA.
  • 25
    • 0242446287 scopus 로고    scopus 로고
    • Characterisation of protein-ligand interfaces: Separating surfaces
    • Keil, M., Exner, T., and Brickmann, J. (1998) Characterisation of protein-ligand interfaces: Separating surfaces, J. Mol. Model. 4, 335-339.
    • (1998) J. Mol. Model. , vol.4 , pp. 335-339
    • Keil, M.1    Exner, T.2    Brickmann, J.3
  • 26
    • 0038592455 scopus 로고    scopus 로고
    • Identification of substrate channels and protein cavities
    • Exner, T., Keil, M., Moeckel, G., and Brickmann, J. (1998) Identification of substrate channels and protein cavities, J. Mol. Model. 4, 340-343.
    • (1998) J. Mol. Model. , vol.4 , pp. 340-343
    • Exner, T.1    Keil, M.2    Moeckel, G.3    Brickmann, J.4
  • 27
    • 0028927329 scopus 로고
    • Effect of point mutations on the kinetics and the inhibition of human immunodeficiency virus type 1 protease: Relationship to drug resistance
    • Lin, Y., Lin, X., Hong, L., Foundling, S., Heinrikson, R. L., Thaisrivongs, S., Leelamanit, W., Raterman, D., Shah, M., Dunn, B. M., and et al. (1995) Effect of point mutations on the kinetics and the inhibition of human immunodeficiency virus type 1 protease: Relationship to drug resistance, Biochemistry 34, 1143-1152.
    • (1995) Biochemistry , vol.34 , pp. 1143-1152
    • Lin, Y.1    Lin, X.2    Hong, L.3    Foundling, S.4    Heinrikson, R.L.5    Thaisrivongs, S.6    Leelamanit, W.7    Raterman, D.8    Shah, M.9    Dunn, B.M.10
  • 28
    • 0037469148 scopus 로고    scopus 로고
    • A major role for a set of non-active site mutations in the development of HIV-1 protease drug resistance
    • Muzammil, S., Ross, P., and Freire, E. (2003) A major role for a set of non-active site mutations in the development of HIV-1 protease drug resistance, Biochemistry 42, 631-638.
    • (2003) Biochemistry , vol.42 , pp. 631-638
    • Muzammil, S.1    Ross, P.2    Freire, E.3
  • 33
    • 0032990257 scopus 로고    scopus 로고
    • Clinical resistance patterns and responses to two sequential protease inhibitor regimens in saquinavir and reverse transcriptase inhibitor-experienced persons
    • Lawrence, J., Schapiro, J., Winters, M., Montoya, J., Zolopa, A., Pesano, R., Efron, B., Winslow, D., and Merigan, T. C. (1999) Clinical resistance patterns and responses to two sequential protease inhibitor regimens in saquinavir and reverse transcriptase inhibitor-experienced persons, J. Infect. Dis. 179, 1356-1364.
    • (1999) J. Infect. Dis. , vol.179 , pp. 1356-1364
    • Lawrence, J.1    Schapiro, J.2    Winters, M.3    Montoya, J.4    Zolopa, A.5    Pesano, R.6    Efron, B.7    Winslow, D.8    Merigan, T.C.9
  • 34
    • 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 Krausslich, 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.
    • (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
  • 35
    • 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.
    • (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
  • 36
    • 0029001258 scopus 로고
    • Host strain selection for bacterial expression of toxic proteins
    • Chen, E. (1994) Host strain selection for bacterial expression of toxic proteins, Methods Enzymol. 241, 29-46.
    • (1994) Methods Enzymol. , vol.241 , pp. 29-46
    • Chen, E.1
  • 37
    • 0032500125 scopus 로고    scopus 로고
    • Activity of a ritonavir plus saquinavir-containing regimen in patients with virologic evidence of indinavir or ritonavir failure
    • Deeks, S. G., Grant, R. M., Beatty, G. W., Horton, C., Detmer, J., and Eastman, S. (1998) Activity of a ritonavir plus saquinavir-containing regimen in patients with virologic evidence of indinavir or ritonavir failure, AIDS 12, F97-F102.
    • (1998) AIDS , vol.12
    • Deeks, S.G.1    Grant, R.M.2    Beatty, G.W.3    Horton, C.4    Detmer, J.5    Eastman, S.6
  • 38
    • 0342906635 scopus 로고    scopus 로고
    • The cumulative occurrence of resistance mutations in the HIV-1 protease gene is associated with failure of salvage therapy with ritonavir and saquinavir in protease inhibitor-experienced patients
    • Karmochkine, M., Si Mohamed, A., Piketty, C., Ginsburg, C., Raguin, G., Schneider-Fauveau, V., Gutmann, L., Kazatchkine, M. D., and Belec, L. (2000) The cumulative occurrence of resistance mutations in the HIV-1 protease gene is associated with failure of salvage therapy with ritonavir and saquinavir in protease inhibitor-experienced patients, Antiviral. Res. 47, 179-188.
    • (2000) Antiviral. Res. , vol.47 , pp. 179-188
    • Karmochkine, M.1    Si Mohamed, A.2    Piketty, C.3    Ginsburg, C.4    Raguin, G.5    Schneider-Fauveau, V.6    Gutmann, L.7    Kazatchkine, M.D.8    Belec, L.9
  • 39
    • 0029896360 scopus 로고    scopus 로고
    • Kinetic characterization of human immunodeficiency virus type-1 protease-resistant variants
    • Pazhanisamy, S., Stuver, C. M., Cullinan, A. B., Margolin, N., Rao, B. G., and Livingston, D. J. (1996) Kinetic characterization of human immunodeficiency virus type-1 protease-resistant variants, J. Biol. Chem. 271, 17979-17985.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17979-17985
    • Pazhanisamy, S.1    Stuver, C.M.2    Cullinan, A.B.3    Margolin, N.4    Rao, B.G.5    Livingston, D.J.6
  • 41
    • 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., Yoshimura, K., Kavlick, M. F., Nagashima, K., Gorelick, R. J., Mardy, S., Tang, C., Summers, M. F., and Mitsuya, H. (2002) 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. 277, 5952-5961.
    • (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
  • 43
    • 0141571239 scopus 로고    scopus 로고
    • Covariation of amino acid positions in HIV-1 protease
    • Hoffman, N. G., Schiffer, C. A., and Swanstrom, R. (2003) Covariation of amino acid positions in HIV-1 protease, Virology 314, 536-548.
    • (2003) Virology , vol.314 , pp. 536-548
    • Hoffman, N.G.1    Schiffer, C.A.2    Swanstrom, R.3
  • 44
    • 0344823654 scopus 로고    scopus 로고
    • Multidrug resistance to HIV-1 protease inhibition requires cooperative coupling between distal mutations
    • Ohtaka, H., Schon, A., and Freire, E. (2003) Multidrug resistance to HIV-1 protease inhibition requires cooperative coupling between distal mutations, Biochemistry 42, 13659-13666.
    • (2003) Biochemistry , vol.42 , pp. 13659-13666
    • Ohtaka, H.1    Schon, A.2    Freire, E.3
  • 45
    • 0034056585 scopus 로고    scopus 로고
    • An alternate binding site for the P1-P3 group of a class of potent HIV-1 protease inhibitors as a result of concerted structural change in the 80s loop of the protease
    • Munshi, S., Chen, Z., Yan, Y., Li, Y., Olsen, D. B., Schock, H. B., Galvin, B. B., Dorsey, B., and Kuo, L. C. (2000) An alternate binding site for the P1-P3 group of a class of potent HIV-1 protease inhibitors as a result of concerted structural change in the 80s loop of the protease, Acta. Crystallogr., Sect. D 56 (Part 4), 381-388.
    • (2000) Acta Crystallogr., Sect. D , vol.56 , Issue.PART 4 , pp. 381-388
    • Munshi, S.1    Chen, Z.2    Yan, Y.3    Li, Y.4    Olsen, D.B.5    Schock, H.B.6    Galvin, B.B.7    Dorsey, B.8    Kuo, L.C.9
  • 46
    • 0028842828 scopus 로고
    • Trans-dominant inhibitory human immunodeficiency virus type 1 protease monomers prevent protease activation and virion maturation
    • Babe, L. M., Rose, J., and Craik, C. S. (1995) Trans-dominant inhibitory human immunodeficiency virus type 1 protease monomers prevent protease activation and virion maturation, Proc. Natl. Acad. Sci. U.S.A. 92, 10069-10073.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 10069-10073
    • Babe, L.M.1    Rose, J.2    Craik, C.S.3
  • 47
    • 0029966228 scopus 로고    scopus 로고
    • Engineering human immunodeficiency virus 1 protease heterodimers as macromolecular inhibitors of viral maturation
    • McPhee, F., Good, A. C., Kuntz, I. D., and Craik, C. S. (1996) Engineering human immunodeficiency virus 1 protease heterodimers as macromolecular inhibitors of viral maturation, Proc. Natl. Acad. Sci. U.S.A. 93, 11477-11481.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 11477-11481
    • McPhee, F.1    Good, A.C.2    Kuntz, I.D.3    Craik, C.S.4
  • 48
    • 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
  • 49
    • 2442558308 scopus 로고    scopus 로고
    • A structural and thermodynamic escape mechanism from a drug resistant mutation of the HIV-1 protease
    • Vega, S., Kang, L. W., Velazquez-Campoy, A., Kiso, Y., Amzel, L. M., and Freire, E. (2004) A structural and thermodynamic escape mechanism from a drug resistant mutation of the HIV-1 protease, Proteins 55, 594-602.
    • (2004) Proteins , vol.55 , pp. 594-602
    • Vega, S.1    Kang, L.W.2    Velazquez-Campoy, A.3    Kiso, Y.4    Amzel, L.M.5    Freire, E.6
  • 50
    • 0032483034 scopus 로고    scopus 로고
    • Structural role of the 30's loop in determining the ligand specificity of the human immunodeficiency virus protease
    • Swairjo, M. A., Towler, E. M., Debouck, C., and Abdel-Meguid, S. S. (1998) Structural role of the 30's loop in determining the ligand specificity of the human immunodeficiency virus protease, Biochemistry 37, 10928-10936.
    • (1998) Biochemistry , vol.37 , pp. 10928-10936
    • Swairjo, M.A.1    Towler, E.M.2    Debouck, C.3    Abdel-Meguid, S.S.4
  • 51
    • 0031552351 scopus 로고    scopus 로고
    • The 80's loop (residues 78-85) is important for the differential activity of retroviral proteases
    • Stebbins, J., Towler, E. M., Tennant, M. G., Deckman, I. C., and Debouck, C. (1997) The 80's loop (residues 78-85) is important for the differential activity of retroviral proteases, J. Mol. Biol. 267, 467-475.
    • (1997) J. Mol. Biol. , vol.267 , pp. 467-475
    • Stebbins, J.1    Towler, E.M.2    Tennant, M.G.3    Deckman, I.C.4    Debouck, C.5
  • 52
    • 0030468331 scopus 로고    scopus 로고
    • Human immunodeficiency virus. Mutations in the viral protease that confer resistance to saquinavir increase the dissociation rate constant of the protease-saquinavir complex
    • Maschera, B., Darby, G., Palu, G., Wright, L. L., Tisdale, M., Myers, R., Blair, E. D., and Furfine, E. S. (1996) Human immunodeficiency virus. Mutations in the viral protease that confer resistance to saquinavir increase the dissociation rate constant of the protease-saquinavir complex, J. Biol. Chem. 271, 33231-33235.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33231-33235
    • Maschera, B.1    Darby, G.2    Palu, G.3    Wright, L.L.4    Tisdale, M.5    Myers, R.6    Blair, E.D.7    Furfine, E.S.8
  • 53
    • 0038058949 scopus 로고    scopus 로고
    • Elucidation of HIV-1 protease resistance by characterization of interaction kinetics between inhibitors and enzyme variants
    • Shuman, C. F., Markgren, P. O., Hamalainen, M., and Danielson, U. H. (2003) Elucidation of HIV-1 protease resistance by characterization of interaction kinetics between inhibitors and enzyme variants, Antiviral Res. 58, 235-242.
    • (2003) Antiviral Res. , vol.58 , pp. 235-242
    • Shuman, C.F.1    Markgren, P.O.2    Hamalainen, M.3    Danielson, U.H.4
  • 54
    • 0035903001 scopus 로고    scopus 로고
    • Impact of baseline polymorphisms in RT and protease on outcome of highly active antiretroviral therapy in HIV-1-infected African patients
    • Prater, A. J., Beardall, A., Ariyoshi, K., Churchill, D., Galpin, S., Clarke, J. R., Weber, J. N., and McClure, M. O. (2001) Impact of baseline polymorphisms in RT and protease on outcome of highly active antiretroviral therapy in HIV-1-infected African patients, AIDS 15, 1493-1502.
    • (2001) AIDS , vol.15 , pp. 1493-1502
    • Prater, A.J.1    Beardall, A.2    Ariyoshi, K.3    Churchill, D.4    Galpin, S.5    Clarke, J.R.6    Weber, J.N.7    McClure, M.O.8
  • 56
    • 0031883581 scopus 로고    scopus 로고
    • Drug susceptibility of subtypes A, B, C, D, and E human immunodeficiency virus type 1 primary isolates
    • Palmer, S., Alaeus, A., Albert, J., and Cox, S. (1998) Drug susceptibility of subtypes A, B, C, D, and E human immunodeficiency virus type 1 primary isolates, AIDS Res. Hum. Retroviruses 14, 157-162.
    • (1998) AIDS Res. Hum. Retroviruses , vol.14 , pp. 157-162
    • Palmer, S.1    Alaeus, A.2    Albert, J.3    Cox, S.4
  • 57
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C., Laskowski, R. A., and Thornton, J. M. (1995) LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions, Protein Eng. 8, 127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.