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Volumn 26, Issue 3, 2005, Pages 138-145

Interfacial inhibition of macromolecular interactions: Nature's paradigm for drug discovery

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMANITIN; APHIDICOLIN; BREFELDIN A; CAMPTOTHECIN; CIPROFLOXACIN; COLCHICINE; CYCLOSPORIN; DNA; DNA TOPOISOMERASE INHIBITOR; DOXORUBICIN; ECTEINASCIDIN; EPOTHILONE A; FORSKOLIN; FUSICOCCIN; FUSIDIC ACID; IMMUNOPHILIN; IRINOTECAN; MOCIMYCIN; NALIDIXIC ACID; PACLITAXEL; PROTEIN; PROTEIN INHIBITOR; QUINOLONE DERIVATIVE; RAPAMYCIN; RAZOXANE; TACROLIMUS; THIOSTREPTON; TOPOTECAN; TUBULIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 14644420930     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tips.2005.01.008     Document Type: Review
Times cited : (143)

References (60)
  • 1
    • 0033636402 scopus 로고    scopus 로고
    • Small-molecule inhibitors of cell signaling
    • F. McCormick Small-molecule inhibitors of cell signaling Curr. Opin. Biotechnol. 11 2000 593 597
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 593-597
    • McCormick, F.1
  • 2
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • A.A. Bogan, and K.S. Thorn Anatomy of hot spots in protein interfaces J. Mol. Biol. 280 1998 1 9
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 3
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • M.R. Arkin, and J.A. Wells Small-molecule inhibitors of protein-protein interactions: progressing towards the dream Nat. Rev. Drug Discov. 3 2004 301 317
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 4
    • 0037180432 scopus 로고    scopus 로고
    • The mechanism of topoisomerase I poisoning by a camptothecin analog
    • B.L. Staker The mechanism of topoisomerase I poisoning by a camptothecin analog Proc. Natl. Acad. Sci. U. S. A. 99 2002 15387 15392
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 15387-15392
    • Staker, B.L.1
  • 5
    • 2542425518 scopus 로고    scopus 로고
    • Mechanisms of camptothecin resistance by human topoisomerase I mutations
    • J.E. Chrencik Mechanisms of camptothecin resistance by human topoisomerase I mutations J. Mol. Biol. 339 2004 773 784
    • (2004) J. Mol. Biol. , vol.339 , pp. 773-784
    • Chrencik, J.E.1
  • 6
    • 85030815282 scopus 로고    scopus 로고
    • Structure of three classes of anticancer agents bound to the human topoisomerase I-DNA covalent complex
    • (in press)
    • Staker, B.L. et al. Structure of three classes of anticancer agents bound to the human topoisomerase I-DNA covalent complex. J. Med. Chem. (in press)
    • J. Med. Chem.
    • Staker, B.L.1
  • 7
    • 0034730123 scopus 로고    scopus 로고
    • Binding site of brefeldin a at the interface between the small G protein ADP-ribosylation factor 1 (ARF1) and the nucleotide-exchange factor Sec7 domain
    • S. Robineau Binding site of brefeldin A at the interface between the small G protein ADP-ribosylation factor 1 (ARF1) and the nucleotide-exchange factor Sec7 domain Proc. Natl. Acad. Sci. U. S. A. 97 2000 9913 9918
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9913-9918
    • Robineau, S.1
  • 8
    • 0346243924 scopus 로고    scopus 로고
    • Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor
    • L. Renault Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor Nature 426 2003 525 530
    • (2003) Nature , vol.426 , pp. 525-530
    • Renault, L.1
  • 9
    • 0025027323 scopus 로고
    • Local sequence requirements for DNA cleavage by mammalian topoisomerase II in the presence of doxorubicin
    • G. Capranico Local sequence requirements for DNA cleavage by mammalian topoisomerase II in the presence of doxorubicin Nucleic Acids Res. 18 1990 6611 6619
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6611-6619
    • Capranico, G.1
  • 10
    • 0025719903 scopus 로고
    • Effect of local DNA sequence on topoisomerase I cleavage in the presence or absence of camptothecin
    • C. Jaxel Effect of local DNA sequence on topoisomerase I cleavage in the presence or absence of camptothecin J. Biol. Chem. 266 1991 20418 20423
    • (1991) J. Biol. Chem. , vol.266 , pp. 20418-20423
    • Jaxel, C.1
  • 11
    • 0028896166 scopus 로고
    • Camptothecin and taxol: Discovery to clinic-thirteenth Bruce F. Cain Memorial Award lecture
    • M.E. Wall, and M.C. Wani Camptothecin and taxol: discovery to clinic-thirteenth Bruce F. Cain Memorial Award lecture Cancer Res. 55 1995 753 760
    • (1995) Cancer Res. , vol.55 , pp. 753-760
    • Wall, M.E.1    Wani, M.C.2
  • 12
    • 0022340594 scopus 로고
    • Camptothecin induces protein-linked DNA breaks via mammalian DNA topoisomerase I
    • Y.H. Hsiang Camptothecin induces protein-linked DNA breaks via mammalian DNA topoisomerase I J. Biol. Chem. 260 1985 14873 14878
    • (1985) J. Biol. Chem. , vol.260 , pp. 14873-14878
    • Hsiang, Y.H.1
  • 13
    • 0024305936 scopus 로고
    • Expression of human DNA topoisomerase I in yeast cells lacking yeast DNA topoisomerase I: Restoration of sensitivity of the cells to the antitumor drug camptothecin
    • M-A. Bjornsti Expression of human DNA topoisomerase I in yeast cells lacking yeast DNA topoisomerase I: restoration of sensitivity of the cells to the antitumor drug camptothecin Cancer Res. 49 1989 6318 6323
    • (1989) Cancer Res. , vol.49 , pp. 6318-6323
    • Bjornsti, M.-A.1
  • 14
    • 0033208192 scopus 로고    scopus 로고
    • Topoisomerase I inhibitors: Selectivity and cellular resistance
    • Y. Pommier Topoisomerase I inhibitors: selectivity and cellular resistance Drug Resist. Updat. 2 1999 307 318
    • (1999) Drug Resist. Updat. , vol.2 , pp. 307-318
    • Pommier, Y.1
  • 15
    • 0024560495 scopus 로고
    • Structure-activity study of the actions of camptothecin derivatives on mammalian topoisomerase I: Evidence for a specific receptor site and a relation to antitumor activity
    • C. Jaxel Structure-activity study of the actions of camptothecin derivatives on mammalian topoisomerase I: evidence for a specific receptor site and a relation to antitumor activity Cancer Res. 49 1989 1465 1469
    • (1989) Cancer Res. , vol.49 , pp. 1465-1469
    • Jaxel, C.1
  • 16
    • 0036085460 scopus 로고    scopus 로고
    • Cellular roles of DNA topoisomerases: A molecular perspective
    • J.C. Wang Cellular roles of DNA topoisomerases: a molecular perspective Nat. Rev. Mol. Cell Biol. 3 2002 430 440
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 430-440
    • Wang, J.C.1
  • 17
    • 0034923502 scopus 로고    scopus 로고
    • DNA Topoisomerases: Structure, function, and mechanism
    • J.J. Champoux DNA Topoisomerases: structure, function, and mechanism Annu. Rev. Biochem. 70 2001 369 413
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 369-413
    • Champoux, J.J.1
  • 18
    • 0029081258 scopus 로고
    • Interaction of an alkylating camptothecin derivative with a DNA base at topoisomerase I-DNA cleavage sites
    • Y. Pommier Interaction of an alkylating camptothecin derivative with a DNA base at topoisomerase I-DNA cleavage sites Proc. Natl. Acad. Sci. U. S. A. 92 1995 8861 8865
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 8861-8865
    • Pommier, Y.1
  • 19
    • 0001130199 scopus 로고
    • Decumbin, a new compound from a species of Penicillium
    • V.L. Singleton Decumbin, a new compound from a species of Penicillium Nature 181 1958 1072 1073
    • (1958) Nature , vol.181 , pp. 1072-1073
    • Singleton, V.L.1
  • 20
    • 0021762860 scopus 로고
    • Induction and suppression of phytoalexin biosynthesis in cultured cells of safflower, Carthamus tinctorius L., by metabolites of Alternaria carthami Chowdhury
    • K.G. Tietjen, and U. Matern Induction and suppression of phytoalexin biosynthesis in cultured cells of safflower, Carthamus tinctorius L., by metabolites of Alternaria carthami Chowdhury Arch. Biochem. Biophys. 229 1984 136 144
    • (1984) Arch. Biochem. Biophys. , vol.229 , pp. 136-144
    • Tietjen, K.G.1    Matern, U.2
  • 21
    • 0014247647 scopus 로고
    • Antiviral activity of brefeldin a and verrucarin a
    • G. Tamura Antiviral activity of brefeldin A and verrucarin A J. Antibiot. (Tokyo) 21 1968 160 161
    • (1968) J. Antibiot. (Tokyo) , vol.21 , pp. 160-161
    • Tamura, G.1
  • 22
    • 0033998897 scopus 로고    scopus 로고
    • Elucidation of strict structural requirements of brefeldin a as an inducer of differentiation and apoptosis
    • J.W. Zhu Elucidation of strict structural requirements of brefeldin A as an inducer of differentiation and apoptosis Bioorg. Med. Chem. 8 2000 455 463
    • (2000) Bioorg. Med. Chem. , vol.8 , pp. 455-463
    • Zhu, J.W.1
  • 23
    • 0023008846 scopus 로고
    • Novel blockade by brefeldin a of intracellular transport of secretory proteins in cultured rat hepatocytes
    • Y. Misumi Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes J. Biol. Chem. 261 1986 11398 11403
    • (1986) J. Biol. Chem. , vol.261 , pp. 11398-11403
    • Misumi, Y.1
  • 24
    • 0026746713 scopus 로고
    • Inhibition by brefeldin a of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF
    • J.B. Helms, and J.E. Rothman Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF Nature 360 1992 352 354
    • (1992) Nature , vol.360 , pp. 352-354
    • Helms, J.B.1    Rothman, J.E.2
  • 25
    • 0026677375 scopus 로고
    • Brefeldin a inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein
    • J.G. Donaldson Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein Nature 360 1992 350 352
    • (1992) Nature , vol.360 , pp. 350-352
    • Donaldson, J.G.1
  • 26
    • 0033950864 scopus 로고    scopus 로고
    • Turning on ARF: The Sec7 family of guanine-nucleotide-exchange factors
    • C.L. Jackson, and J.E. Casanova Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors Trends Cell Biol. 10 2000 60 67
    • (2000) Trends Cell Biol. , vol.10 , pp. 60-67
    • Jackson, C.L.1    Casanova, J.E.2
  • 27
    • 0002955384 scopus 로고    scopus 로고
    • Brefeldin a acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: Involvement of specific residues of the Sec7 domain
    • A. Peyroche Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain Mol. Cell 3 1999 275 285
    • (1999) Mol. Cell , vol.3 , pp. 275-285
    • Peyroche, A.1
  • 28
    • 0033574449 scopus 로고    scopus 로고
    • Brefeldin A: The advantage of being uncompetitive
    • P. Chardin, and F. McCormick Brefeldin A: the advantage of being uncompetitive Cell 97 1999 153 155
    • (1999) Cell , vol.97 , pp. 153-155
    • Chardin, P.1    McCormick, F.2
  • 29
    • 0033179296 scopus 로고    scopus 로고
    • GEFs: Structural basis for their activation of small GTP-binding proteins
    • J. Cherfils, and P. Chardin GEFs: structural basis for their activation of small GTP-binding proteins Trends Biochem. Sci. 24 1999 306 311
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 306-311
    • Cherfils, J.1    Chardin, P.2
  • 30
    • 0348047597 scopus 로고    scopus 로고
    • Crystal structure of ARF1*Sec7 complexed with Brefeldin a and its implications for the guanine nucleotide exchange mechanism
    • E. Mossessova Crystal structure of ARF1*Sec7 complexed with Brefeldin A and its implications for the guanine nucleotide exchange mechanism Mol. Cell 12 2003 1403 1411
    • (2003) Mol. Cell , vol.12 , pp. 1403-1411
    • Mossessova, E.1
  • 31
    • 0032538317 scopus 로고    scopus 로고
    • Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide exchange and GTP-myristoyl switching
    • J. Goldberg Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching Cell 95 1998 237 248
    • (1998) Cell , vol.95 , pp. 237-248
    • Goldberg, J.1
  • 32
    • 0028556994 scopus 로고
    • Structure of the human ADP-ribosylation factor 1 complexed with GDP
    • J.C. Amor Structure of the human ADP-ribosylation factor 1 complexed with GDP Nature 372 1994 704 708
    • (1994) Nature , vol.372 , pp. 704-708
    • Amor, J.C.1
  • 33
    • 0033049656 scopus 로고    scopus 로고
    • Structural basis for the inhibitory effect of brefeldin a on guanine nucleotide-exchange proteins for ADP-ribosylation factors
    • M. Sata Structural basis for the inhibitory effect of brefeldin A on guanine nucleotide-exchange proteins for ADP-ribosylation factors Proc. Natl. Acad. Sci. U. S. A. 96 1999 2752 2757
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 2752-2757
    • Sata, M.1
  • 34
    • 0035788652 scopus 로고    scopus 로고
    • A point mutation in an unusual Sec7 domain is linked to brefeldin a resistance in a Plasmodium falciparum line generated by drug selection
    • F. Baumgartner A point mutation in an unusual Sec7 domain is linked to brefeldin A resistance in a Plasmodium falciparum line generated by drug selection Mol. Microbiol. 41 2001 1151 1158
    • (2001) Mol. Microbiol. , vol.41 , pp. 1151-1158
    • Baumgartner, F.1
  • 35
    • 10744233671 scopus 로고    scopus 로고
    • Repair of and checkpoint response to topoisomerase I-mediated DNA damage
    • Y. Pommier Repair of and checkpoint response to topoisomerase I-mediated DNA damage Mutat. Res. 532 2003 173 203
    • (2003) Mutat. Res. , vol.532 , pp. 173-203
    • Pommier, Y.1
  • 36
    • 0030782188 scopus 로고    scopus 로고
    • Golgi tubule traffic and the effects of brefeldin a visualized in living cells
    • N. Sciaky Golgi tubule traffic and the effects of brefeldin A visualized in living cells J. Cell Biol. 139 1997 1137 1155
    • (1997) J. Cell Biol. , vol.139 , pp. 1137-1155
    • Sciaky, N.1
  • 37
    • 2642689663 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS
    • J.J. Tesmer Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS Science 278 1997 1907 1916
    • (1997) Science , vol.278 , pp. 1907-1916
    • Tesmer, J.J.1
  • 38
    • 0033583237 scopus 로고    scopus 로고
    • Structure, mechanism, and regulation of mammalian adenylyl cyclase
    • J.H. Hurley Structure, mechanism, and regulation of mammalian adenylyl cyclase J. Biol. Chem. 274 1999 7599 7602
    • (1999) J. Biol. Chem. , vol.274 , pp. 7599-7602
    • Hurley, J.H.1
  • 39
    • 1642401199 scopus 로고    scopus 로고
    • Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
    • R.B. Ravelli Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain Nature 428 2004 198 202
    • (2004) Nature , vol.428 , pp. 198-202
    • Ravelli, R.B.1
  • 40
    • 0035942226 scopus 로고    scopus 로고
    • The binding conformation of Taxol in beta-tubulin: A model based on electron crystallographic density
    • J.P. Snyder The binding conformation of Taxol in beta-tubulin: a model based on electron crystallographic density Proc. Natl. Acad. Sci. U. S. A. 98 2001 5312 5316
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 5312-5316
    • Snyder, J.P.1
  • 41
    • 3843053396 scopus 로고    scopus 로고
    • The binding mode of epothilone a on alpha,beta-tubulin by electron crystallography
    • J.H. Nettles The binding mode of epothilone A on alpha,beta-tubulin by electron crystallography Science 305 2004 866 869
    • (2004) Science , vol.305 , pp. 866-869
    • Nettles, J.H.1
  • 42
    • 0037022279 scopus 로고    scopus 로고
    • Structural basis of transcription: Alpha-amanitin-RNA polymerase II cocrystal at 2.8 a resolution
    • D.A. Bushnell Structural basis of transcription: alpha-amanitin-RNA polymerase II cocrystal at 2.8 A resolution Proc. Natl. Acad. Sci. U. S. A. 99 2002 1218 1222
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1218-1222
    • Bushnell, D.A.1
  • 43
    • 0033117764 scopus 로고    scopus 로고
    • Structural studies of the translational apparatus
    • R.K. Agrawal, and J. Frank Structural studies of the translational apparatus Curr. Opin. Struct. Biol. 9 1999 215 221
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 215-221
    • Agrawal, R.K.1    Frank, J.2
  • 44
    • 0034602449 scopus 로고    scopus 로고
    • Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site
    • M. Laurberg Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site J. Mol. Biol. 303 2000 593 603
    • (2000) J. Mol. Biol. , vol.303 , pp. 593-603
    • Laurberg, M.1
  • 45
    • 85030811130 scopus 로고    scopus 로고
    • Interaction of thiostrepton and elongation factor-G with the ribosomal protein L11-binding domain
    • (in press)
    • Bowen, W.S. et al. Interaction of thiostrepton and elongation factor-G with the ribosomal protein L11-binding domain. J. Biol. Chem. (in press)
    • J. Biol. Chem.
    • Bowen, W.S.1
  • 46
    • 17944374027 scopus 로고    scopus 로고
    • Antiproliferative activity of ecteinascidin 743 is dependent upon transcription-coupled nucleotide-excision repair
    • Y. Takebayashi Antiproliferative activity of ecteinascidin 743 is dependent upon transcription-coupled nucleotide-excision repair Nat. Med. 7 2001 961 966
    • (2001) Nat. Med. , vol.7 , pp. 961-966
    • Takebayashi, Y.1
  • 48
    • 0037108767 scopus 로고    scopus 로고
    • Crystal structure of human calcineurin complexed with cyclosporin a and human cyclophilin
    • L. Jin, and S.C. Harrison Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin Proc. Natl. Acad. Sci. U. S. A. 99 2002 13522 13526
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 13522-13526
    • Jin, L.1    Harrison, S.C.2
  • 49
    • 0037126026 scopus 로고    scopus 로고
    • Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes
    • Q. Huai Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes Proc. Natl. Acad. Sci. U. S. A. 99 2002 12037 12042
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12037-12042
    • Huai, Q.1
  • 50
    • 0037416221 scopus 로고    scopus 로고
    • Structural view of a fungal toxin acting on a 14-3-3 regulatory complex
    • M. Wurtele Structural view of a fungal toxin acting on a 14-3-3 regulatory complex EMBO J. 22 2003 987 994
    • (2003) EMBO J. , vol.22 , pp. 987-994
    • Wurtele, M.1
  • 51
    • 0028848524 scopus 로고
    • Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex
    • C.R. Kissinger Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex Nature 378 1995 641 644
    • (1995) Nature , vol.378 , pp. 641-644
    • Kissinger, C.R.1
  • 52
    • 0029133116 scopus 로고
    • X-ray structure of calcineurin inhibited by the immunophilin- immunosuppressant FKBP12-FK506 complex
    • J.P. Griffith X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex Cell 82 1995 507 522
    • (1995) Cell , vol.82 , pp. 507-522
    • Griffith, J.P.1
  • 53
    • 0029842109 scopus 로고    scopus 로고
    • Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP
    • J. Choi Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP Science 273 1996 239 242
    • (1996) Science , vol.273 , pp. 239-242
    • Choi, J.1
  • 54
    • 0028345406 scopus 로고
    • Antitumor bisdioxopiperazines inhibit yeast DNA topoisomerase II by trapping the enzyme in the form of a closed protein clamp
    • J. Roca Antitumor bisdioxopiperazines inhibit yeast DNA topoisomerase II by trapping the enzyme in the form of a closed protein clamp Proc. Natl. Acad. Sci. U. S. A. 91 1994 1781 1785
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 1781-1785
    • Roca, J.1
  • 55
    • 0141591551 scopus 로고    scopus 로고
    • Structure of the topoisomerase II ATPase region and its mechanism of inhibition by the chemotherapeutic agent ICRF-187
    • S. Classen Structure of the topoisomerase II ATPase region and its mechanism of inhibition by the chemotherapeutic agent ICRF-187 Proc. Natl. Acad. Sci. U. S. A. 100 2003 10629 10634
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10629-10634
    • Classen, S.1
  • 56
    • 0033736170 scopus 로고    scopus 로고
    • The interaction of drugs with DNA gyrase: A model for the molecular basis of quinolone action
    • J.G. Heddle The interaction of drugs with DNA gyrase: a model for the molecular basis of quinolone action Nucleosides Nucleotides Nucleic Acids 19 2000 1249 1264
    • (2000) Nucleosides Nucleotides Nucleic Acids , vol.19 , pp. 1249-1264
    • Heddle, J.G.1
  • 57
    • 0036720073 scopus 로고    scopus 로고
    • Importance of the fourth alpha-helix within the CAP homology domain of type II topoisomerase for DNA cleavage site recognition and quinolone action
    • D. Strumberg Importance of the fourth alpha-helix within the CAP homology domain of type II topoisomerase for DNA cleavage site recognition and quinolone action Antimicrob. Agents Chemother. 46 2002 2735 2746
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 2735-2746
    • Strumberg, D.1
  • 58
    • 0019435919 scopus 로고
    • New views of the biochemistry of eucaryotic DNA replication revealed by aphidicolin, an unusual inhibitor of DNA polymerase alpha
    • J.A. Huberman New views of the biochemistry of eucaryotic DNA replication revealed by aphidicolin, an unusual inhibitor of DNA polymerase alpha Cell 23 1981 647 648
    • (1981) Cell , vol.23 , pp. 647-648
    • Huberman, J.A.1
  • 59
    • 0034723439 scopus 로고    scopus 로고
    • Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells
    • D.J. Hazuda Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells Science 287 2000 646 650
    • (2000) Science , vol.287 , pp. 646-650
    • Hazuda, D.J.1
  • 60
    • 0041353616 scopus 로고    scopus 로고
    • Metal-dependent inhibition of HIV-1 integrase by {beta}-diketo acids and resistance of the soluble double-mutant (F185K/C280S)
    • C. Marchand Metal-dependent inhibition of HIV-1 integrase by {beta}-diketo acids and resistance of the soluble double-mutant (F185K/C280S) Mol. Pharmacol. 64 2003 600 609
    • (2003) Mol. Pharmacol. , vol.64 , pp. 600-609
    • Marchand, C.1


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