메뉴 건너뛰기




Volumn 336, Issue 3, 2004, Pages 569-578

Crystal Structures of HIV-1 Reverse Transcriptases Mutated at Codons 100, 106 and 108 and Mechanisms of Resistance to Non-nucleoside Inhibitors

Author keywords

DNA polymerase; Drug resistance mechanism; HIV 1; Reverse transcriptase mutants; X ray crystallography

Indexed keywords

ALANINE; ISOLEUCINE; LEUCINE; N [4 CHLORO 3 (3 METHYL 2 BUTENYLOXY)PHENYL] 2 METHYL 3 FURANCARBOTHIOAMIDE; NEVIRAPINE; RNA DIRECTED DNA POLYMERASE; RNA DIRECTED DNA POLYMERASE INHIBITOR; TNK 651; TYROSINE; UNCLASSIFIED DRUG; VALINE;

EID: 0842289678     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.12.055     Document Type: Article
Times cited : (71)

References (42)
  • 1
    • 0028120730 scopus 로고
    • HIV resistance to reverse transcriptase inhibitors
    • De Clercq E. HIV resistance to reverse transcriptase inhibitors. Biochem. Pharmacol. 47:1994;155-169.
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 155-169
    • De Clercq, E.1
  • 2
    • 0034083833 scopus 로고    scopus 로고
    • Mutations in retroviral genes associated with drug resistance
    • Schinazi R.F., Larder B.A., Mellors J.W. Mutations in retroviral genes associated with drug resistance. Int. Antivir. News. 8:2000;65-91.
    • (2000) Int. Antivir. News , vol.8 , pp. 65-91
    • Schinazi, R.F.1    Larder, B.A.2    Mellors, J.W.3
  • 3
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt L.A., Wang J., Friedman J.M., Rice P.A., Steitz T.A. Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science. 256:1992;1783-1790.
    • (1992) Science , vol.256 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steitz, T.A.5
  • 5
    • 0029644484 scopus 로고
    • Structure of HIV-1 reverse transcriptase in a complex with the non-nucleoside inhibitor a-APA R 95845 at 2.8 Å resolution
    • Ding J., Das K., Tantillo C., Zhang W., Clark A.D.J., Jessen S., Lu X., et al. Structure of HIV-1 reverse transcriptase in a complex with the non-nucleoside inhibitor a-APA R 95845 at 2.8 Å resolution. Structure. 3:1995;365-379.
    • (1995) Structure , vol.3 , pp. 365-379
    • Ding, J.1    Das, K.2    Tantillo, C.3    Zhang, W.4    Clark, A.D.J.5    Jessen, S.6    Lu, X.7
  • 6
    • 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., 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
  • 7
    • 0028925773 scopus 로고
    • Mechanism of inhibition of HIV-1 reverse transcriptase by nonnucleoside inhibitors
    • Spence R.A., Kati W.M., Anderson K.S., 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
  • 8
    • 0027957791 scopus 로고
    • Nevirapine resistance mutations of human immunodeficiency virus type 1 selected during therapy
    • Richman D.D., Havlir D., Corbeil J., Looney D., Ignacio C., Spector S.A., Sullivan J., et al. Nevirapine resistance mutations of human immunodeficiency virus type 1 selected during therapy. J. Virol. 68:1994;1660-1666.
    • (1994) J. Virol. , vol.68 , pp. 1660-1666
    • Richman, D.D.1    Havlir, D.2    Corbeil, J.3    Looney, D.4    Ignacio, C.5    Spector, S.A.6    Sullivan, J.7
  • 9
    • 0026756720 scopus 로고
    • Functional analysis of HIV-1 reverse transcriptase amino acids involved in resistance to multiple nonnucleoside inhibitors
    • Sardana V.V., Emini E.A., Gotlib L., Graham D.J., Lineberger D.W., Long W.J., Wolfgang J.A., et al. Functional analysis of HIV-1 reverse transcriptase amino acids involved in resistance to multiple nonnucleoside inhibitors. J. Biol. Chem. 267:1992;17526-17530.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17526-17530
    • Sardana, V.V.1    Emini, E.A.2    Gotlib, L.3    Graham, D.J.4    Lineberger, D.W.5    Long, W.J.6    Wolfgang, J.A.7
  • 10
    • 0026543676 scopus 로고
    • Structure-activity relationships of 1-[(2-hydroxyethoxy)methyl]-6- (phenylthio)thymine analogues: Effects of substituents at the C-6 phenyl ring and at the C-5 position on anti-HIV-1 activity
    • Tanaka H., Takashima H., Ubasawa M., Sekiya K., Nitta I., Baba M., Shigeta S., et al. Structure-activity relationships of 1-[(2-hydroxyethoxy) methyl]-6-(phenylthio)thymine analogues: effects of substituents at the C-6 phenyl ring and at the C-5 position on anti-HIV-1 activity. J. Med. Chem. 35:1992;337-345.
    • (1992) J. Med. Chem. , vol.35 , pp. 337-345
    • Tanaka, H.1    Takashima, H.2    Ubasawa, M.3    Sekiya, K.4    Nitta, I.5    Baba, M.6    Shigeta, S.7
  • 11
    • 0029976422 scopus 로고    scopus 로고
    • Complexes of HIV-1 reverse transcriptase with inhibitors of the HEPT series reveal conformational changes relevant to the design of potent non-nucleoside inhibitors
    • Hopkins A.L., Ren J., Esnouf R.M., Willcox B.E., Jones E.Y., Ross C., Miyasaka T., et al. Complexes of HIV-1 reverse transcriptase with inhibitors of the HEPT series reveal conformational changes relevant to the design of potent non-nucleoside inhibitors. J. Med. Chem. 39:1996;1589-1600.
    • (1996) J. Med. Chem. , vol.39 , pp. 1589-1600
    • Hopkins, A.L.1    Ren, J.2    Esnouf, R.M.3    Willcox, B.E.4    Jones, E.Y.5    Ross, C.6    Miyasaka, T.7
  • 12
    • 0028785708 scopus 로고
    • L-743, 726 (DMP-266): A novel, highly potent nonnucleoside inhibitor of the human immunodeficiency virus type 1 reverse transcriptase
    • Young S.D., Britcher S.F., Tran L.O., Payne L.S., Lumma W.C., Lyle T.A., et al. L-743, 726 (DMP-266): a novel, highly potent nonnucleoside inhibitor of the human immunodeficiency virus type 1 reverse transcriptase. Antimicrob. Agents Chemother. 39:1995;2602-2605.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2602-2605
    • Young, S.D.1    Britcher, S.F.2    Tran, L.O.3    Payne, L.S.4    Lumma, W.C.5    Lyle, T.A.6
  • 13
    • 0029809694 scopus 로고    scopus 로고
    • Highly favorable antiviral activity and resistance profile of the novel thiocarboxanilide pentenyloxy ether derivatives UC-781 and UC-82 as inhibitors of human immunodeficiency virus type 1 replication
    • Balzarini J., Pelemans H., Aquaro S., Perno C.F., Witvrouw M., Schols D., et al. Highly favorable antiviral activity and resistance profile of the novel thiocarboxanilide pentenyloxy ether derivatives UC-781 and UC-82 as inhibitors of human immunodeficiency virus type 1 replication. Mol. Pharmacol. 50:1996;394-401.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 394-401
    • Balzarini, J.1    Pelemans, H.2    Aquaro, S.3    Perno, C.F.4    Witvrouw, M.5    Schols, D.6
  • 14
    • 0031805095 scopus 로고    scopus 로고
    • S-1153 inhibits replication of known drug-resistant strains of human immunodeficiency virus type 1
    • Fujiwara T., Sato A., el-Farrash M., Miki S., Abe K., Isaka Y., et al. S-1153 inhibits replication of known drug-resistant strains of human immunodeficiency virus type 1. Antimicrob. Agents Chemother. 42:1998;1340-1345.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1340-1345
    • Fujiwara, T.1    Sato, A.2    El-Farrash, M.3    Miki, S.4    Abe, K.5    Isaka, Y.6
  • 15
    • 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., 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
  • 16
    • 0027318776 scopus 로고
    • Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 Å resolution shows bent DNA
    • Jacobo-Molina A., Ding J.P., Nanni R.G., Clark A.D.J., Lu X., Tantillo C., et al. Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 Å resolution shows bent DNA. Proc. Natl Acad. Sci. USA. 90:1993;6320-6324.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6320-6324
    • Jacobo-Molina, A.1    Ding, J.P.2    Nanni, R.G.3    Clark, A.D.J.4    Lu, X.5    Tantillo, C.6
  • 17
    • 11544277817 scopus 로고    scopus 로고
    • 3'-azido-3'-deoxythymidine drug resistance mutations in HIV-1 reverse transcriptase can induce long range conformational changes
    • Ren J., Esnouf R.M., Hopkins A.L., Jones E.Y., Kirby I., Keeling J., et al. 3'-azido-3'-deoxythymidine drug resistance mutations in HIV-1 reverse transcriptase can induce long range conformational changes. Proc. Natl Acad. Sci. USA. 95:1998;9518-9523.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9518-9523
    • Ren, J.1    Esnouf, R.M.2    Hopkins, A.L.3    Jones, E.Y.4    Kirby, I.5    Keeling, J.6
  • 18
    • 0036776359 scopus 로고    scopus 로고
    • Crystal structures of Zidovudine- or Lamivudine-resistant human immunodeficiency virus type 1 reverse transcriptases containing mutations at codons 41, 184, and 215
    • Chamberlain P.P., Ren J., Nichols C.E., Douglas L., Lennerstrand J., Larder B.A., et al. Crystal structures of Zidovudine- or Lamivudine-resistant human immunodeficiency virus type 1 reverse transcriptases containing mutations at codons 41, 184, and 215. J. Virol. 76:2002;10015-10019.
    • (2002) J. Virol. , vol.76 , pp. 10015-10019
    • Chamberlain, P.P.1    Ren, J.2    Nichols, C.E.3    Douglas, L.4    Lennerstrand, J.5    Larder, B.A.6
  • 19
    • 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 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, A.D.4    Moereels, H.5    Koymans, L.6
  • 20
    • 0035965124 scopus 로고    scopus 로고
    • Structural mechanisms of drug resistance for mutations at codons 181 and 188 in HIV-1 reverse transcriptase and the improved resilience of second generation non-nucleoside inhibitors
    • Ren J., Nichols C., Bird L., Chamberlain P., Weaver K., Short S., et al. Structural mechanisms of drug resistance for mutations at codons 181 and 188 in HIV-1 reverse transcriptase and the improved resilience of second generation non-nucleoside inhibitors. J. Mol. Biol. 312:2001;795-805.
    • (2001) J. Mol. Biol. , vol.312 , pp. 795-805
    • Ren, J.1    Nichols, C.2    Bird, L.3    Chamberlain, P.4    Weaver, K.5    Short, S.6
  • 21
    • 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., 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
  • 23
    • 13144282707 scopus 로고    scopus 로고
    • 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 A.D., Kleim J.-P., Rosner M., et al. 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, A.D.4    Kleim, J.-P.5    Rosner, M.6
  • 24
    • 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 A.D. Jr, 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
  • 25
    • 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., Sigurosson 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    Sigurosson, S.2    Lowgren, S.3    Andersson, H.O.4    Sahlberg, C.5    Noreen, R.6
  • 26
    • 0031578901 scopus 로고    scopus 로고
    • Resistance to nevirapine of HIV-1 reverse transcriptase mutants: Loss of stabilizing interactions and thermodynamic or steric barriers are induced by different single amino acid substitutions
    • Maga G., Amacker M., Ruel N., Hubscher U., Spadari S. Resistance to nevirapine of HIV-1 reverse transcriptase mutants: loss of stabilizing interactions and thermodynamic or steric barriers are induced by different single amino acid substitutions. J. Mol. Biol. 274:1997;738-747.
    • (1997) J. Mol. Biol. , vol.274 , pp. 738-747
    • Maga, G.1    Amacker, M.2    Ruel, N.3    Hubscher, U.4    Spadari, S.5
  • 27
    • 8244226649 scopus 로고    scopus 로고
    • Highly potent oxathiin carboxanilide derivatives with efficacy against nonnucleoside reverse transcriptase inhibitor-resistant human immunodeficiency virus isolates
    • Buckheit R.W., Snow M.J., Fliakas-Boltz V., Kinjerski T.L., Russell J.D., Pallansch L.A., et al. Highly potent oxathiin carboxanilide derivatives with efficacy against nonnucleoside reverse transcriptase inhibitor-resistant human immunodeficiency virus isolates. Antimicrob. Agents. Chemother. 41:1997;831-837.
    • (1997) Antimicrob. Agents. Chemother. , vol.41 , pp. 831-837
    • Buckheit, R.W.1    Snow, M.J.2    Fliakas-Boltz, V.3    Kinjerski, T.L.4    Russell, J.D.5    Pallansch, L.A.6
  • 28
    • 0030860860 scopus 로고    scopus 로고
    • Cross-resistance analysis and molecular modeling of nonnucleoside reverse transcriptase inhibitors targeting drug-resistance mutations in the reverse transcriptase of human immunodeficiency virus
    • Yang S.S., Pattabiraman N., Gussio R., Pallansch L., Buckheit R.W., Bader J.P. Cross-resistance analysis and molecular modeling of nonnucleoside reverse transcriptase inhibitors targeting drug-resistance mutations in the reverse transcriptase of human immunodeficiency virus. Leukemia. 11:1997;89-92.
    • (1997) Leukemia , vol.11 , pp. 89-92
    • Yang, S.S.1    Pattabiraman, N.2    Gussio, R.3    Pallansch, L.4    Buckheit, R.W.5    Bader, J.P.6
  • 29
    • 0028838466 scopus 로고
    • Structure-activity and cross-resistance evaluations of a series of human immunodeficiency virus type-1-specific compounds related to oxathiin carboxanilide
    • Buckheit R.W., Kinjerski T.L., Fliakas-Boltz V., Russell J.D., Stup T.L., Pallansch L.A., et al. Structure-activity and cross-resistance evaluations of a series of human immunodeficiency virus type-1-specific compounds related to oxathiin carboxanilide. Antimicrob. Agents Chemother. 39:1995;2718-2727.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2718-2727
    • Buckheit, R.W.1    Kinjerski, T.L.2    Fliakas-Boltz, V.3    Russell, J.D.4    Stup, T.L.5    Pallansch, L.A.6
  • 30
    • 0029904239 scopus 로고    scopus 로고
    • Identification of novel thiocarboxanilide derivatives that suppress a variety of drug-resistant mutant human immunodeficiency virus type 1 strains at a potency similar to that for wild-type virus
    • Balzarini J., Brouwer W.G., Dao D.C., Osika E.M., De Clercq E. Identification of novel thiocarboxanilide derivatives that suppress a variety of drug-resistant mutant human immunodeficiency virus type 1 strains at a potency similar to that for wild-type virus. Antimicrob. Agents Chemother. 40:1996;1454-1466.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 1454-1466
    • Balzarini, J.1    Brouwer, W.G.2    Dao, D.C.3    Osika, E.M.4    De Clercq, E.5
  • 31
    • 0029079399 scopus 로고
    • Suppression of the breakthrough of human immunodeficiency virus type 1 (HIV-1) in cell culture by thiocarboxanilide derivatives when used individually or in combination with other HIV-1-specific inhibitors (i.e. TSAO derivatives)
    • Balzarini J., Perez-Perez M.J., Velazquez S., San-Felix A., Camarasa M.J., De Clercq E., Karlsson A. Suppression of the breakthrough of human immunodeficiency virus type 1 (HIV-1) in cell culture by thiocarboxanilide derivatives when used individually or in combination with other HIV-1-specific inhibitors (i.e. TSAO derivatives). Proc. Natl Acad. Sci. USA. 92:1995;5470-5474.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5470-5474
    • Balzarini, J.1    Perez-Perez, M.J.2    Velazquez, S.3    San-Felix, A.4    Camarasa, M.J.5    De Clercq, E.6    Karlsson, A.7
  • 32
    • 0029075207 scopus 로고
    • Structure of HIV-1 RT/TIBO R 86183 complex reveals similarity in the binding of diverse nonnucleoside inhibitors
    • Ding J., Das K., Moereels H., Koymans L., Andries K., Janssen P.A.J., et al. Structure of HIV-1 RT/TIBO R 86183 complex reveals similarity in the binding of diverse nonnucleoside inhibitors. Nature Struct. Biol. 2:1995;407-415.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 407-415
    • Ding, J.1    Das, K.2    Moereels, H.3    Koymans, L.4    Andries, K.5    Janssen, P.A.J.6
  • 35
    • 0032167707 scopus 로고    scopus 로고
    • Continuous and discontinuous changes in the unit cell of HIV-1 reverse transcriptase crystals on dehydration
    • Esnouf R.M., Ren J., Garman E.F., Somers D.O.N., Ross C.K., Jones E.Y., et al. Continuous and discontinuous changes in the unit cell of HIV-1 reverse transcriptase crystals on dehydration. Acta Crystallog. sect. D. 54:1998;938-954.
    • (1998) Acta Crystallog. Sect. D , vol.54 , pp. 938-954
    • Esnouf, R.M.1    Ren, J.2    Garman, E.F.3    Somers, D.O.N.4    Ross, C.K.5    Jones, E.Y.6
  • 36
    • 0000293676 scopus 로고
    • X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation
    • Sakabe N. X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation. Nucl. Instrum. Methods Phys. Res. 303:1991;448-463.
    • (1991) Nucl. Instrum. Methods Phys. Res. , vol.303 , pp. 448-463
    • Sakabe, N.1
  • 37
    • 0027358894 scopus 로고
    • Weissenberg data collection for macromolecular crystallography
    • Stuart D.I., Jones E.Y. Weissenberg data collection for macromolecular crystallography. Curr. Opin. Struct. Biol. 3:1993;737-740.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 737-740
    • Stuart, D.I.1    Jones, E.Y.2
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1996;307-326.
    • (1996) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 40
    • 0029645409 scopus 로고
    • The structure of HIV-1 reverse transcriptase complexed with 9-chloro-TIBO: Lessons for inhibitor design
    • Ren J., Esnouf R., Hopkins A., Ross C., Jones Y., Stammers D., Stuart D. The structure of HIV-1 reverse transcriptase complexed with 9-chloro-TIBO: lessons for inhibitor design. Structure. 3:1995;915-926.
    • (1995) Structure , vol.3 , pp. 915-926
    • Ren, J.1    Esnouf, R.2    Hopkins, A.3    Ross, C.4    Jones, Y.5    Stammers, D.6    Stuart, D.7
  • 41
    • 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., Kjeldgaard M. Improved methods for building 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    Kjeldgaard, M.4
  • 42
    • 0018792428 scopus 로고
    • The crystal structure of cat pyruvate kinase at a resolution of 2.6 Å
    • Stuart D.I., Levine M., Muirhead H., Stammers D.K. The crystal structure of cat pyruvate kinase at a resolution of 2.6 Å J. Mol. Biol. 134:1979;109-142.
    • (1979) J. Mol. Biol. , vol.134 , pp. 109-142
    • Stuart, D.I.1    Levine, M.2    Muirhead, H.3    Stammers, D.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.