메뉴 건너뛰기




Volumn 365, Issue 1, 2007, Pages 77-89

Crystal Structures of Clinically Relevant Lys103Asn/Tyr181Cys Double Mutant HIV-1 Reverse Transcriptase in Complexes with ATP and Non-nucleoside Inhibitor HBY 097

Author keywords

conformational flexibility; drug design; drug resistance; polymerase

Indexed keywords

ADENOSINE TRIPHOSPHATE; ASPARTIC ACID; MANGANESE; RNA DIRECTED DNA POLYMERASE; TALVIRALINE; THIOL DERIVATIVE;

EID: 33751529192     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.08.097     Document Type: Article
Times cited : (78)

References (62)
  • 1
    • 0033576816 scopus 로고    scopus 로고
    • Efavirenz plus zidovudine and lamivudine, efavirenz plus indinavir, and indinavir plus zidovudine and lamivudine in the treatment of HIV-1 infection in adults
    • Staszewski S., Morales-Ramirez J., Tashima K.T., Rachlis A., Skiest D., Stanford J., et al. Efavirenz plus zidovudine and lamivudine, efavirenz plus indinavir, and indinavir plus zidovudine and lamivudine in the treatment of HIV-1 infection in adults. New Engl. J. Med. 341 (1999) 1865-1873
    • (1999) New Engl. J. Med. , vol.341 , pp. 1865-1873
    • Staszewski, S.1    Morales-Ramirez, J.2    Tashima, K.T.3    Rachlis, A.4    Skiest, D.5    Stanford, J.6
  • 2
    • 0034143429 scopus 로고    scopus 로고
    • Update on highly active antiretroviral therapy: progress and strategies
    • Clumeck N., and De Wit S. Update on highly active antiretroviral therapy: progress and strategies. Biomed. Pharmacother. 54 (2000) 7-12
    • (2000) Biomed. Pharmacother. , vol.54 , pp. 7-12
    • Clumeck, N.1    De Wit, S.2
  • 3
    • 0035141058 scopus 로고    scopus 로고
    • Patterns of resistance mutations to antiretroviral drugs in extensively treated HIV-1-infected patients with failure of highly active antiretroviral therapy
    • Rousseau M.N., Vergne L., Montes B., Peeters M., Reynes J., Delaporte E., and Segondy M. Patterns of resistance mutations to antiretroviral drugs in extensively treated HIV-1-infected patients with failure of highly active antiretroviral therapy. J. Acquir. Immun. Defic. Syndr. 26 (2001) 36-43
    • (2001) J. Acquir. Immun. Defic. Syndr. , vol.26 , pp. 36-43
    • Rousseau, M.N.1    Vergne, L.2    Montes, B.3    Peeters, M.4    Reynes, J.5    Delaporte, E.6    Segondy, M.7
  • 4
    • 0002035867 scopus 로고    scopus 로고
    • Prevalence of HIV-1 resistant to antiretroviral drugs in 81 individuals newly infected by sexual contact or injecting drug use. Investigators of the Quebec Primary Infection Study
    • Salomon H., Wainberg M.A., Brenner B., Quan Y., Rouleau D., Cote P., et al. Prevalence of HIV-1 resistant to antiretroviral drugs in 81 individuals newly infected by sexual contact or injecting drug use. Investigators of the Quebec Primary Infection Study. AIDS 14 (2000) F17-F23
    • (2000) AIDS , vol.14
    • Salomon, H.1    Wainberg, M.A.2    Brenner, B.3    Quan, Y.4    Rouleau, D.5    Cote, P.6
  • 5
    • 0034456474 scopus 로고    scopus 로고
    • Resistance against reverse transcriptase inhibitors
    • O'Brien W.A. Resistance against reverse transcriptase inhibitors. Clin. Infect. Dis. 30 (2000) S185-S192
    • (2000) Clin. Infect. Dis. , vol.30
    • O'Brien, W.A.1
  • 6
    • 9944232661 scopus 로고    scopus 로고
    • Taking aim at a moving target: designing drugs to inhibit drug-resistant HIV-1 reverse transcriptases
    • Sarafianos S.G., Das K., Hughes S.H., and Arnold E. Taking aim at a moving target: designing drugs to inhibit drug-resistant HIV-1 reverse transcriptases. Curr. Opin. Struct. Biol. 14 (2004) 716-730
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 716-730
    • Sarafianos, S.G.1    Das, K.2    Hughes, S.H.3    Arnold, E.4
  • 7
    • 0030708683 scopus 로고    scopus 로고
    • In search of a selective antiviral chemotherapy
    • De Clercq E. In search of a selective antiviral chemotherapy. Clin. Microbiol. Rev. 10 (1997) 674-693
    • (1997) Clin. Microbiol. Rev. , vol.10 , pp. 674-693
    • De Clercq, E.1
  • 8
    • 0032918170 scopus 로고    scopus 로고
    • Perspectives of non-nucleoside reverse transcriptase inhibitors (NNRTIs) in the therapy of HIV-1 infection
    • De Clercq E. Perspectives of non-nucleoside reverse transcriptase inhibitors (NNRTIs) in the therapy of HIV-1 infection. Farmaco 54 (1999) 26-45
    • (1999) Farmaco , vol.54 , pp. 26-45
    • De Clercq, E.1
  • 11
    • 12944314948 scopus 로고    scopus 로고
    • Efavirenz- and adefovir dipivoxil-based salvage therapy in highly treatment-experienced patients: clinical and genotypic predictors of virologic response
    • Shulman N.S., Zolopa A.R., Passaro D.J., Murlidharan U., Israelski D.M., Brosgart C.L., et al. Efavirenz- and adefovir dipivoxil-based salvage therapy in highly treatment-experienced patients: clinical and genotypic predictors of virologic response. J. Acquir. Immune Defic. Syndr. 23 (2000) 221-226
    • (2000) J. Acquir. Immune Defic. Syndr. , vol.23 , pp. 221-226
    • Shulman, N.S.1    Zolopa, A.R.2    Passaro, D.J.3    Murlidharan, U.4    Israelski, D.M.5    Brosgart, C.L.6
  • 12
    • 0030596068 scopus 로고    scopus 로고
    • Crystal structures of 8-Cl and 9-Cl TIBO complexed with wild-type HIV-1 RT and 8-Cl TIBO complexed with the Tyr181Cys HIV-1 RT drug-resistant mutant
    • Das K., Ding J., Hsiou Y., Clark Jr. A.D., Moereels H., Koymans L., et al. Crystal structures of 8-Cl and 9-Cl TIBO complexed with wild-type HIV-1 RT and 8-Cl TIBO complexed with the Tyr181Cys HIV-1 RT drug-resistant mutant. J. Mol. Biol. 264 (1996) 1085-1100
    • (1996) J. Mol. Biol. , vol.264 , pp. 1085-1100
    • Das, K.1    Ding, J.2    Hsiou, Y.3    Clark Jr., A.D.4    Moereels, H.5    Koymans, L.6
  • 13
    • 13144282707 scopus 로고    scopus 로고
    • Structures of Tyr188Leu mutant and wild-type HIV-1 reverse transcriptase complexed with the non-nucleoside inhibitor HBY 097: inhibitor flexibility is a useful design feature for reducing drug resistance
    • Hsiou Y., Das K., Ding J., Clark Jr. A.D., Kleim J.P., Rosner M., et al. Structures of Tyr188Leu mutant and wild-type HIV-1 reverse transcriptase complexed with the non-nucleoside inhibitor HBY 097: inhibitor flexibility is a useful design feature for reducing drug resistance. J. Mol. Biol. 284 (1998) 313-323
    • (1998) J. Mol. Biol. , vol.284 , pp. 313-323
    • Hsiou, Y.1    Das, K.2    Ding, J.3    Clark Jr., A.D.4    Kleim, J.P.5    Rosner, M.6
  • 14
    • 0034435564 scopus 로고    scopus 로고
    • Structural basis for the resilience of efavirenz (DMP-266) to drug resistance mutations in HIV-1 reverse transcriptase
    • Ren J., Milton J., Weaver K.L., Short S.A., Stuart D.I., and Stammers D.K. Structural basis for the resilience of efavirenz (DMP-266) to drug resistance mutations in HIV-1 reverse transcriptase. Struct. Fold. Des. 8 (2000) 1089-1094
    • (2000) Struct. Fold. Des. , vol.8 , pp. 1089-1094
    • Ren, J.1    Milton, J.2    Weaver, K.L.3    Short, S.A.4    Stuart, D.I.5    Stammers, D.K.6
  • 15
    • 0035368238 scopus 로고    scopus 로고
    • The Lys103Asn mutation of HIV-1 RT: a novel mechanism of drug resistance
    • Hsiou Y., Ding J., Das K., Clark Jr. A.D., Boyer P.L., Lewi P., et al. The Lys103Asn mutation of HIV-1 RT: a novel mechanism of drug resistance. J. Mol. Biol. 309 (2001) 437-445
    • (2001) J. Mol. Biol. , vol.309 , pp. 437-445
    • Hsiou, Y.1    Ding, J.2    Das, K.3    Clark Jr., A.D.4    Boyer, P.L.5    Lewi, P.6
  • 16
    • 0036229823 scopus 로고    scopus 로고
    • Structural basis for the inhibitory efficacy of efavirenz (DMP-266), MSC194 and PNU142721 towards the HIV-1 RT K103N mutant
    • Lindberg J., Sigurdsson S., Lowgren S., Andersson H.O., Sahlberg C., Noreen R., et al. Structural basis for the inhibitory efficacy of efavirenz (DMP-266), MSC194 and PNU142721 towards the HIV-1 RT K103N mutant. Eur. J. Biochem. 269 (2002) 1670-1677
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1670-1677
    • Lindberg, J.1    Sigurdsson, S.2    Lowgren, S.3    Andersson, H.O.4    Sahlberg, C.5    Noreen, R.6
  • 17
    • 0842289678 scopus 로고    scopus 로고
    • Crystal structures of HIV-1 reverse transcriptases mutated at codons 100, 106 and 108 and mechanisms of resistance to non-nucleoside inhibitors
    • Ren J., Nichols C.E., Chamberlain P.P., Weaver K.L., Short S.A., and Stammers D.K. Crystal structures of HIV-1 reverse transcriptases mutated at codons 100, 106 and 108 and mechanisms of resistance to non-nucleoside inhibitors. J. Mol. Biol. 336 (2004) 569-578
    • (2004) J. Mol. Biol. , vol.336 , pp. 569-578
    • Ren, J.1    Nichols, C.E.2    Chamberlain, P.P.3    Weaver, K.L.4    Short, S.A.5    Stammers, D.K.6
  • 18
    • 4344683266 scopus 로고    scopus 로고
    • 2004: which HIV-1 drug resistance mutations are common in clinical practice?
    • Cheung P.K., Wynhoven B., and Harrigan P.R. 2004: which HIV-1 drug resistance mutations are common in clinical practice?. AIDS Rev. 6 (2004) 107-116
    • (2004) AIDS Rev. , vol.6 , pp. 107-116
    • Cheung, P.K.1    Wynhoven, B.2    Harrigan, P.R.3
  • 20
    • 0031052425 scopus 로고    scopus 로고
    • HIV-1 drug susceptibilities and reverse transcriptase mutations in patients receiving combination therapy with didanosine and delavirdine
    • Demeter L.M., Meehan P.M., Morse G., Gerondelis P., Dexter A., Berrios L., et al. HIV-1 drug susceptibilities and reverse transcriptase mutations in patients receiving combination therapy with didanosine and delavirdine. J. Acquir. Immun. Defic. Syndr. Hum. Retrovirol. 14 (1997) 136-144
    • (1997) J. Acquir. Immun. Defic. Syndr. Hum. Retrovirol. , vol.14 , pp. 136-144
    • Demeter, L.M.1    Meehan, P.M.2    Morse, G.3    Gerondelis, P.4    Dexter, A.5    Berrios, L.6
  • 21
    • 0033994776 scopus 로고    scopus 로고
    • Non-nucleoside reverse transcriptase inhibitor resistance among patients failing a nevirapine plus protease inhibitor-containing regimen
    • Casado J.L., Hertogs K., Ruiz L., Dronda F., Van Cauwenberge A., Arno A., et al. Non-nucleoside reverse transcriptase inhibitor resistance among patients failing a nevirapine plus protease inhibitor-containing regimen. AIDS 14 (2000) F1-F7
    • (2000) AIDS , vol.14
    • Casado, J.L.1    Hertogs, K.2    Ruiz, L.3    Dronda, F.4    Van Cauwenberge, A.5    Arno, A.6
  • 22
    • 0034928482 scopus 로고    scopus 로고
    • Distribution of K103N and/or Y181C HIV-1 mutations by exposure to zidovudine and non-nucleoside reverse transcriptase inhibitors
    • Torti C., Pozniak A., Nelson M., Hertogs K., and Gazzard B.G. Distribution of K103N and/or Y181C HIV-1 mutations by exposure to zidovudine and non-nucleoside reverse transcriptase inhibitors. J. Antimicrob. Chemother. 48 (2001) 113-116
    • (2001) J. Antimicrob. Chemother. , vol.48 , pp. 113-116
    • Torti, C.1    Pozniak, A.2    Nelson, M.3    Hertogs, K.4    Gazzard, B.G.5
  • 23
    • 0032585902 scopus 로고    scopus 로고
    • Efavirenz: resistance and cross-resistance
    • Clotet B. Efavirenz: resistance and cross-resistance. Int. J. Clin. Pract. Suppl. 103 (1999) 21-25
    • (1999) Int. J. Clin. Pract. Suppl. , vol.103 , pp. 21-25
    • Clotet, B.1
  • 24
  • 25
    • 0034002944 scopus 로고    scopus 로고
    • Delavirdine susceptibilities and associated reverse transcriptase mutations in human immunodeficiency virus type 1 isolates from patients in a phase I/II trial of delavirdine monotherapy (ACTG 260)
    • Demeter L.M., Shafer R.W., Meehan P.M., Holden-Wiltse J., Fischl M.A., Freimuth W.W., et al. Delavirdine susceptibilities and associated reverse transcriptase mutations in human immunodeficiency virus type 1 isolates from patients in a phase I/II trial of delavirdine monotherapy (ACTG 260). Antimicrob. Agents Chemother. 44 (2000) 794-797
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 794-797
    • Demeter, L.M.1    Shafer, R.W.2    Meehan, P.M.3    Holden-Wiltse, J.4    Fischl, M.A.5    Freimuth, W.W.6
  • 26
    • 20144372481 scopus 로고    scopus 로고
    • In search of a novel anti-HIV drug: multidisciplinary coordination in the discovery of 4-[[4-[[4-[(1E)-2-Cyanoethenyl]-2,6-dimethylphenyl]amino]-2-pyrimidinyl] amino]benzonitrile (R278474, Rilpivirine)
    • Janssen P.A., Lewi P.J., Arnold E., Daeyaert F., de Jonge M., Heeres J., et al. In search of a novel anti-HIV drug: multidisciplinary coordination in the discovery of 4-[[4-[[4-[(1E)-2-Cyanoethenyl]-2,6-dimethylphenyl]amino]-2-pyrimidinyl] amino]benzonitrile (R278474, Rilpivirine). J. Med. Chem. 48 (2005) 1901-1909
    • (2005) J. Med. Chem. , vol.48 , pp. 1901-1909
    • Janssen, P.A.1    Lewi, P.J.2    Arnold, E.3    Daeyaert, F.4    de Jonge, M.5    Heeres, J.6
  • 27
    • 9744258219 scopus 로고    scopus 로고
    • Crystallography and the design of anti-AIDS drugs: conformational flexibility and positional adaptability are important in the design of non-nucleoside HIV-1 reverse transcriptase inhibitors
    • Das K., Lewi P.J., Hughes S.H., and Arnold E. Crystallography and the design of anti-AIDS drugs: conformational flexibility and positional adaptability are important in the design of non-nucleoside HIV-1 reverse transcriptase inhibitors. Prog. Biophys. Mol. Biol. 88 (2005) 209-231
    • (2005) Prog. Biophys. Mol. Biol. , vol.88 , pp. 209-231
    • Das, K.1    Lewi, P.J.2    Hughes, S.H.3    Arnold, E.4
  • 28
    • 0029147651 scopus 로고
    • Preclinical evaluation of HBY 097, a new nonnucleoside reverse transcriptase inhibitor of human immunodeficiency virus type 1 replication
    • Kleim J.P., Bender R., Kirsch R., Meichsner C., Paessens A., Rosner M., et al. Preclinical evaluation of HBY 097, a new nonnucleoside reverse transcriptase inhibitor of human immunodeficiency virus type 1 replication. Antimicrob. Agents Chemother. 39 (1995) 2253-2257
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2253-2257
    • Kleim, J.P.1    Bender, R.2    Kirsch, R.3    Meichsner, C.4    Paessens, A.5    Rosner, M.6
  • 29
    • 0032030658 scopus 로고    scopus 로고
    • Retention of marked sensitivity to (S)-4-isopropoxycarbonyl-6-methoxy-3-(methylthiomethyl)-3,4-di hydroquin oxaline-2(1H)-thione (HBY 097) by an azidothymidine (AZT)-resistant human immunodeficiency virus type 1 (HIV-1) strain subcultured in the combined presence of quinoxaline HBY 097 and 2′,3′-dideoxy-3′-thiacytidine (lamivudine)
    • Balzarini J., Pelemans H., Riess G., Roesner M., Winkler I., De Clercq E., and Kleim J.P. Retention of marked sensitivity to (S)-4-isopropoxycarbonyl-6-methoxy-3-(methylthiomethyl)-3,4-di hydroquin oxaline-2(1H)-thione (HBY 097) by an azidothymidine (AZT)-resistant human immunodeficiency virus type 1 (HIV-1) strain subcultured in the combined presence of quinoxaline HBY 097 and 2′,3′-dideoxy-3′-thiacytidine (lamivudine). Biochem. Pharmacol. 55 (1998) 617-625
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 617-625
    • Balzarini, J.1    Pelemans, H.2    Riess, G.3    Roesner, M.4    Winkler, I.5    De Clercq, E.6    Kleim, J.P.7
  • 30
  • 31
    • 0030586090 scopus 로고    scopus 로고
    • Structure of unliganded HIV-1 reverse transcriptase at 2.7 Å resolution: implications of conformational changes for polymerization and inhibition mechanisms
    • Hsiou Y., Ding J., Das K., Clark Jr. A.D., Hughes S.H., and Arnold E. Structure of unliganded HIV-1 reverse transcriptase at 2.7 Å resolution: implications of conformational changes for polymerization and inhibition mechanisms. Structure 4 (1996) 853-860
    • (1996) Structure , vol.4 , pp. 853-860
    • Hsiou, Y.1    Ding, J.2    Das, K.3    Clark Jr., A.D.4    Hughes, S.H.5    Arnold, E.6
  • 32
    • 0041886575 scopus 로고    scopus 로고
    • Activity predictions for efavirenz analogues with the K103N mutant of HIV reverse transcriptase
    • Udier-Blagovic M., Watkins E.K., Tirado-Rives J., and Jorgensen W.L. Activity predictions for efavirenz analogues with the K103N mutant of HIV reverse transcriptase. Bioorg. Med. Chem. Letters 13 (2003) 3337-3340
    • (2003) Bioorg. Med. Chem. Letters , vol.13 , pp. 3337-3340
    • Udier-Blagovic, M.1    Watkins, E.K.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 33
    • 2342620790 scopus 로고    scopus 로고
    • Roles of conformational and positional adaptability in structure-based design of TMC125-R165335 (Etravirine) and related non-nucleoside reverse transcriptase inhibitors that are highly potent and effective against wild-type and drug-rresistant HIV-1 variants
    • Das K., Clark Jr. A.D., Lewi P.J., Heeres J., de Jonge M.R., et al. Roles of conformational and positional adaptability in structure-based design of TMC125-R165335 (Etravirine) and related non-nucleoside reverse transcriptase inhibitors that are highly potent and effective against wild-type and drug-rresistant HIV-1 variants. J. Med. Chem. 47 (2004) 2550-2560
    • (2004) J. Med. Chem. , vol.47 , pp. 2550-2560
    • Das, K.1    Clark Jr., A.D.2    Lewi, P.J.3    Heeres, J.4    de Jonge, M.R.5
  • 34
    • 0030926748 scopus 로고    scopus 로고
    • In vitro selection for different mutational patterns in the HIV-1 reverse transcriptase using high and low selective pressure of the nonnucleoside reverse transcriptase inhibitor HBY 097
    • Kleim J.P., Winkler I., Rosner M., Kirsch R., Rubsamen-Waigmann H., Paessens A., and Riess G. In vitro selection for different mutational patterns in the HIV-1 reverse transcriptase using high and low selective pressure of the nonnucleoside reverse transcriptase inhibitor HBY 097. Virology 231 (1997) 112-118
    • (1997) Virology , vol.231 , pp. 112-118
    • Kleim, J.P.1    Winkler, I.2    Rosner, M.3    Kirsch, R.4    Rubsamen-Waigmann, H.5    Paessens, A.6    Riess, G.7
  • 35
    • 0032506055 scopus 로고    scopus 로고
    • Phenotypic mechanism of HIV-1 resistance to 3′-azido-3′-deoxythymidine (AZT): increased polymerization processivity and enhanced sensitivity to pyrophosphate of the mutant viral reverse transcriptase
    • Arion D., Kaushik N., McS. Cormick G., and Borkow M.A. Phenotypic mechanism of HIV-1 resistance to 3′-azido-3′-deoxythymidine (AZT): increased polymerization processivity and enhanced sensitivity to pyrophosphate of the mutant viral reverse transcriptase. Biochemistry 37 (1998) 15908-15917
    • (1998) Biochemistry , vol.37 , pp. 15908-15917
    • Arion, D.1    Kaushik, N.2    McS. Cormick, G.3    Borkow, M.A.4
  • 36
    • 0032506228 scopus 로고    scopus 로고
    • Unblocking of chain-terminated primer by HIV-1 reverse transcriptase through a nucleotide-dependent mechanism
    • Meyer P.R., Matsuura S.E., So A.G., and Scott W.A. Unblocking of chain-terminated primer by HIV-1 reverse transcriptase through a nucleotide-dependent mechanism. Proc. Natl Acad. Sci. USA 95 (1998) 13471-13476
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13471-13476
    • Meyer, P.R.1    Matsuura, S.E.2    So, A.G.3    Scott, W.A.4
  • 37
    • 0035031936 scopus 로고    scopus 로고
    • Selective excision of AZTMP by drug-resistant human immunodeficiency virus reverse transcriptase
    • Boyer P.L., Sarafianos S.G., Arnold E., and Hughes S.H. Selective excision of AZTMP by drug-resistant human immunodeficiency virus reverse transcriptase. J. Virol. 75 (2001) 4832-4842
    • (2001) J. Virol. , vol.75 , pp. 4832-4842
    • Boyer, P.L.1    Sarafianos, S.G.2    Arnold, E.3    Hughes, S.H.4
  • 38
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance
    • Huang H., Chopra R., Verdine G.L., and Harrison S.C. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance. Science 282 (1998) 1669-1675
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 40
    • 0032509101 scopus 로고    scopus 로고
    • Structure and functional implications of the polymerase active site region in a complex of HIV-1 RT with a double-stranded DNA template-primer and an antibody Fab fragment at 2.8 Å resolution
    • Ding J., Das K., Hsiou Y., Sarafianos S.G., Clark Jr. A.D., Jacobo-Molina A., et al. Structure and functional implications of the polymerase active site region in a complex of HIV-1 RT with a double-stranded DNA template-primer and an antibody Fab fragment at 2.8 Å resolution. J. Mol. Biol. 284 (1998) 1095-1111
    • (1998) J. Mol. Biol. , vol.284 , pp. 1095-1111
    • Ding, J.1    Das, K.2    Hsiou, Y.3    Sarafianos, S.G.4    Clark Jr., A.D.5    Jacobo-Molina, A.6
  • 41
    • 0030930760 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: evidence for an induced fit mechanism
    • Sawaya M.R., Prasad R., Wilson S.H., Kraut J., and Pelletier H. Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: evidence for an induced fit mechanism. Biochemistry 36 (1997) 11205-11215
    • (1997) Biochemistry , vol.36 , pp. 11205-11215
    • Sawaya, M.R.1    Prasad, R.2    Wilson, S.H.3    Kraut, J.4    Pelletier, H.5
  • 42
  • 43
    • 0032535528 scopus 로고    scopus 로고
    • Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation
    • Li Y., Korolev S., and Waksman G. Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation. EMBO J. 17 (1998) 7514-7525
    • (1998) EMBO J. , vol.17 , pp. 7514-7525
    • Li, Y.1    Korolev, S.2    Waksman, G.3
  • 44
    • 0033133780 scopus 로고    scopus 로고
    • Touching the heart of HIV-1 drug resistance: the fingers close down on the dNTP at the polymerase active site
    • Sarafianos S.G., Das K., Ding J., Boyer P.L., Hughes S.H., and Arnold E. Touching the heart of HIV-1 drug resistance: the fingers close down on the dNTP at the polymerase active site. Chem. Biol. 6 (1999) R137-R146
    • (1999) Chem. Biol. , vol.6
    • Sarafianos, S.G.1    Das, K.2    Ding, J.3    Boyer, P.L.4    Hughes, S.H.5    Arnold, E.6
  • 45
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: structural diversity and common mechanisms
    • Steitz T.A. DNA polymerases: structural diversity and common mechanisms. J. Biol. Chem. 274 (1999) 17395-17398
    • (1999) J. Biol. Chem. , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 46
    • 0037388383 scopus 로고    scopus 로고
    • Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations
    • Johnson S.J., Taylor J.S., and Beese L.S. Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Proc. Natl Acad. Sci. USA 100 (2003) 3895-3900
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 3895-3900
    • Johnson, S.J.1    Taylor, J.S.2    Beese, L.S.3
  • 47
    • 13744256975 scopus 로고    scopus 로고
    • Functional roles of carboxylate residues comprising the DNA polymerase active site triad of Ty3 reverse transcriptase
    • Bibillo A., Lener D., Klarmann G.J., and Le Grice S.F. Functional roles of carboxylate residues comprising the DNA polymerase active site triad of Ty3 reverse transcriptase. Nucl. Acids Res. 33 (2005) 171-181
    • (2005) Nucl. Acids Res. , vol.33 , pp. 171-181
    • Bibillo, A.1    Lener, D.2    Klarmann, G.J.3    Le Grice, S.F.4
  • 48
    • 18744365757 scopus 로고    scopus 로고
    • Structures of HIV-1 reverse transcriptase with pre- and post-translocation AZTMP-terminated DNA
    • Sarafianos S.G., Clark Jr. A.D., Das K., Tuske S., Birktoft J.J., Ilankumaran P., et al. Structures of HIV-1 reverse transcriptase with pre- and post-translocation AZTMP-terminated DNA. EMBO J. 21 (2002) 6614-6624
    • (2002) EMBO J. , vol.21 , pp. 6614-6624
    • Sarafianos, S.G.1    Clark Jr., A.D.2    Das, K.3    Tuske, S.4    Birktoft, J.J.5    Ilankumaran, P.6
  • 49
    • 0026019625 scopus 로고
    • Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism
    • Beese L.S., and Steitz T.A. Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism. EMBO J. 10 (1991) 25-33
    • (1991) EMBO J. , vol.10 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 51
    • 0029150042 scopus 로고
    • Human immunodeficiency virus reverse transcriptase substrate-induced conformational changes and the mechanism of inhibition by nonnucleoside inhibitors
    • Rittinger K., Divita G., and Goody R.S. Human immunodeficiency virus reverse transcriptase substrate-induced conformational changes and the mechanism of inhibition by nonnucleoside inhibitors. Proc. Natl Acad. Sci. USA 92 (1995) 8046-8049
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8046-8049
    • Rittinger, K.1    Divita, G.2    Goody, R.S.3
  • 52
    • 0028925773 scopus 로고
    • Mechanism of inhibition of HIV-1 reverse transcriptase by nonnucleoside inhibitors
    • Spence R.A., Kati W.M., Anderson K.S., and Johnson K.A. Mechanism of inhibition of HIV-1 reverse transcriptase by nonnucleoside inhibitors. Science 267 (1995) 988-993
    • (1995) Science , vol.267 , pp. 988-993
    • Spence, R.A.1    Kati, W.M.2    Anderson, K.S.3    Johnson, K.A.4
  • 53
    • 3242657912 scopus 로고    scopus 로고
    • Structure of HIV-1 reverse transcriptase bound to an inhibitor active against mutant reverse transcriptases resistant to other nonnucleoside inhibitors
    • Pata J.D., Stirtan W.G., Goldstein S.W., and Steitz T.A. Structure of HIV-1 reverse transcriptase bound to an inhibitor active against mutant reverse transcriptases resistant to other nonnucleoside inhibitors. Proc. Natl Acad. Sci. USA 101 (2004) 10548-10553
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 10548-10553
    • Pata, J.D.1    Stirtan, W.G.2    Goldstein, S.W.3    Steitz, T.A.4
  • 54
    • 28144445329 scopus 로고    scopus 로고
    • Crystal structures for HIV-1 reverse transcriptase in complexes with three pyridinone derivatives: a new class of non-nucleoside inhibitors effective against a broad range of drug-resistant strains
    • Himmel D.M., Das K., Clark Jr. A.D., Hughes S.H., Benjahad A., Oumouch S., et al. Crystal structures for HIV-1 reverse transcriptase in complexes with three pyridinone derivatives: a new class of non-nucleoside inhibitors effective against a broad range of drug-resistant strains. J. Med. Chem. 48 (2005) 7582-7591
    • (2005) J. Med. Chem. , vol.48 , pp. 7582-7591
    • Himmel, D.M.1    Das, K.2    Clark Jr., A.D.3    Hughes, S.H.4    Benjahad, A.5    Oumouch, S.6
  • 55
    • 0028924567 scopus 로고
    • Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors
    • Esnouf R., Ren J., Ross C., Jones Y., Stammers D., and Stuart D. Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors. Nature Struct. Biol. 2 (1995) 303-308
    • (1995) Nature Struct. Biol. , vol.2 , pp. 303-308
    • Esnouf, R.1    Ren, J.2    Ross, C.3    Jones, Y.4    Stammers, D.5    Stuart, D.6
  • 56
    • 0028172345 scopus 로고
    • Locations of anti-AIDS drug binding sites and resistance mutations in the three-dimensional structure of HIV-1 reverse transcriptase. Implications for mechanisms of drug inhibition and resistance
    • Tantillo C., Ding J., Jacobo-Molina A., Nanni R.G., Boyer P.L., Hughes S.H., et al. Locations of anti-AIDS drug binding sites and resistance mutations in the three-dimensional structure of HIV-1 reverse transcriptase. Implications for mechanisms of drug inhibition and resistance. J. Mol. Biol. 243 (1994) 369-387
    • (1994) J. Mol. Biol. , vol.243 , pp. 369-387
    • Tantillo, C.1    Ding, J.2    Jacobo-Molina, A.3    Nanni, R.G.4    Boyer, P.L.5    Hughes, S.H.6
  • 57
    • 0026572005 scopus 로고
    • Structure of HIV-1 reverse transcriptase/DNA complex at 7 Å resolution showing active site locations
    • Arnold E., Jacobo-Molina A., Nanni R.G., Williams R.L., Lu X., Ding J., et al. Structure of HIV-1 reverse transcriptase/DNA complex at 7 Å resolution showing active site locations. Nature 357 (1992) 85-89
    • (1992) Nature , vol.357 , pp. 85-89
    • Arnold, E.1    Jacobo-Molina, A.2    Nanni, R.G.3    Williams, R.L.4    Lu, X.5    Ding, J.6
  • 58
    • 0028806233 scopus 로고
    • Crystallization of human immunodeficiency virus type 1 reverse transcriptase with and without nucleic acid substrates, inhibitors and an antibody Fab fragment
    • Clark A.D.J., Jacobo-Molina A., Clark P., Hughes S.H., and Arnold E. Crystallization of human immunodeficiency virus type 1 reverse transcriptase with and without nucleic acid substrates, inhibitors and an antibody Fab fragment. Methods Enzymol. 262 (1995) 171-185
    • (1995) Methods Enzymol. , vol.262 , pp. 171-185
    • Clark, A.D.J.1    Jacobo-Molina, A.2    Clark, P.3    Hughes, S.H.4    Arnold, E.5
  • 60
    • 84889120137 scopus 로고
    • Improved methods for binding 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. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A 47 (1991) 110-119
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 61
    • 0344541116 scopus 로고    scopus 로고
    • Recent developments for the efficient crystallographic refinement of macromolecular structures
    • Brunger A.T., Adams P.D., and Rice L.M. Recent developments for the efficient crystallographic refinement of macromolecular structures. Curr. Opin. Struct. Biol. 8 (1998) 606-611
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 606-611
    • Brunger, A.T.1    Adams, P.D.2    Rice, L.M.3
  • 62
    • 0026319199 scopus 로고
    • Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., and Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11 (1991) 281-296
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.