메뉴 건너뛰기




Volumn 7, Issue 11, 2012, Pages 1866-1872

In vivo validation of thymidylate kinase (TMK) with a rationally designed, selective antibacterial compound

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; BACTERIAL DNA; BACTERIAL ENZYME; THYMIDINE PHOSPHATE; THYMIDYLATE KINASE; TK 666; UNCLASSIFIED DRUG;

EID: 84869438365     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb300316n     Document Type: Article
Times cited : (37)

References (21)
  • 1
    • 69549111337 scopus 로고    scopus 로고
    • Antibiotics for emerging pathogens
    • Fischbach, M. A. and Walsh, C. T. (2009) Antibiotics for emerging pathogens Science 325, 1089-1093
    • (2009) Science , vol.325 , pp. 1089-1093
    • Fischbach, M.A.1    Walsh, C.T.2
  • 2
    • 33845903833 scopus 로고    scopus 로고
    • Drugs for bad bugs: Confronting the challenges of antibacterial discovery
    • Payne, D. J., Gwynn, M. N., Holmes, D. J., and Pompliano, D. L. (2007) Drugs for bad bugs: confronting the challenges of antibacterial discovery Nat. Rev. Drug Discovery 6, 29-40
    • (2007) Nat. Rev. Drug Discovery , vol.6 , pp. 29-40
    • Payne, D.J.1    Gwynn, M.N.2    Holmes, D.J.3    Pompliano, D.L.4
  • 7
    • 4344593930 scopus 로고    scopus 로고
    • Preclinical evaluation of novel antibacterial agents by microbiological and molecular techniques
    • O'Neill, A. J. and Chopra, I. (2004) Preclinical evaluation of novel antibacterial agents by microbiological and molecular techniques Expert Opin. Investig. Drugs 13, 1045-1063
    • (2004) Expert Opin. Investig. Drugs , vol.13 , pp. 1045-1063
    • O'Neill, A.J.1    Chopra, I.2
  • 8
    • 0036566484 scopus 로고    scopus 로고
    • Characterization of Streptococcus pneumoniae thymidylate kinase: Steady-state kinetics of the forward reaction and isothermal titration calorimetry
    • Petit, C. M. and Koretke, K. K. (2002) Characterization of Streptococcus pneumoniae thymidylate kinase: steady-state kinetics of the forward reaction and isothermal titration calorimetry Biochem. J. 363, 825-831
    • (2002) Biochem. J. , vol.363 , pp. 825-831
    • Petit, C.M.1    Koretke, K.K.2
  • 9
    • 33644761270 scopus 로고    scopus 로고
    • Use of thymine limitation and thymine starvation to study bacterial physiology and cytology
    • Zaritsky, A., Woldringh, C. L., Einav, M., and Alexeeva, S. (2006) Use of thymine limitation and thymine starvation to study bacterial physiology and cytology J. Bacteriol. 188, 1667-1679
    • (2006) J. Bacteriol. , vol.188 , pp. 1667-1679
    • Zaritsky, A.1    Woldringh, C.L.2    Einav, M.3    Alexeeva, S.4
  • 10
    • 9744241646 scopus 로고    scopus 로고
    • Discovery of bicyclic thymidine analogues as selective and high-affinity inhibitors of Mycobacterium tuberculosis thymidine monophosphate kinase
    • Vanheusden, V., Munier-Lehmann, H., Froeyen, M., Busson, R., Rozenski, J., Herdewijn, P., and Calenbergh, S. V. (2004) Discovery of bicyclic thymidine analogues as selective and high-affinity inhibitors of Mycobacterium tuberculosis thymidine monophosphate kinase J. Med. Chem. 47, 6187-6194
    • (2004) J. Med. Chem. , vol.47 , pp. 6187-6194
    • Vanheusden, V.1    Munier-Lehmann, H.2    Froeyen, M.3    Busson, R.4    Rozenski, J.5    Herdewijn, P.6    Calenbergh, S.V.7
  • 12
  • 13
    • 33645508875 scopus 로고    scopus 로고
    • Structures of S. aureus thymidylate kinase reveal an atypical active site configuration and an intermediate conformational state upon substrate binding
    • Kotaka, M., Dhaliwal, B., Ren, J., Nichols, C. E., Angell, R., Lockyer, M., Hawkins, A. R., and Stammers, D. K. (2006) Structures of S. aureus thymidylate kinase reveal an atypical active site configuration and an intermediate conformational state upon substrate binding Protein Sci. 15, 774-784
    • (2006) Protein Sci. , vol.15 , pp. 774-784
    • Kotaka, M.1    Dhaliwal, B.2    Ren, J.3    Nichols, C.E.4    Angell, R.5    Lockyer, M.6    Hawkins, A.R.7    Stammers, D.K.8
  • 14
    • 0034660675 scopus 로고    scopus 로고
    • Insights into the phosphoryltransfer mechanism of human thymidylate kinase gained from the crystal structures of enzyme complexes along the reaction coordinate
    • Ostermann, N., Schlichting, I., Brundiers, R., Konrad, M., Reinstein, J., Veit, T., Goody, R. S., and Lavie, A. (2000) Insights into the phosphoryltransfer mechanism of human thymidylate kinase gained from the crystal structures of enzyme complexes along the reaction coordinate Structure 8, 629-642
    • (2000) Structure , vol.8 , pp. 629-642
    • Ostermann, N.1    Schlichting, I.2    Brundiers, R.3    Konrad, M.4    Reinstein, J.5    Veit, T.6    Goody, R.S.7    Lavie, A.8
  • 15
    • 0032564339 scopus 로고    scopus 로고
    • Structural basis for efficient phosphorylation of 3′-azidothymidine monophosphate by Escherichia coli thymidylate kinase
    • Lavie, A., Ostermann, N., Brundiers, R., Goody, R. S., Reinstein, J., Konrad, M., and Schlichting, I. (1998) Structural basis for efficient phosphorylation of 3′-azidothymidine monophosphate by Escherichia coli thymidylate kinase Proc. Natl. Acad. Sci. U.S.A. 95, 14045-14050
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 14045-14050
    • Lavie, A.1    Ostermann, N.2    Brundiers, R.3    Goody, R.S.4    Reinstein, J.5    Konrad, M.6    Schlichting, I.7
  • 18
    • 1642311135 scopus 로고    scopus 로고
    • Clinical relevance of bacteriostatic versus bactericidal mechanisms of action in the treatment of Gram-positive bacterial infections
    • Pankey, G. A. and Sabath, L. D. (2004) Clinical relevance of bacteriostatic versus bactericidal mechanisms of action in the treatment of Gram-positive bacterial infections Clin. Infect. Dis. 38, 864-870
    • (2004) Clin. Infect. Dis. , vol.38 , pp. 864-870
    • Pankey, G.A.1    Sabath, L.D.2
  • 19
    • 0032807458 scopus 로고    scopus 로고
    • Multiple mechanisms of action for inhibitors of histidine protein kinases from bacterial two-component systems
    • Hilliard, J. J., Goldschmidt, R. M., Licata, L., Baum, E. Z., and Bush, K. (1999) Multiple mechanisms of action for inhibitors of histidine protein kinases from bacterial two-component systems Antimicrob. Agents Chemother. 43, 1693-1697
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1693-1697
    • Hilliard, J.J.1    Goldschmidt, R.M.2    Licata, L.3    Baum, E.Z.4    Bush, K.5
  • 21
    • 4644267929 scopus 로고    scopus 로고
    • Effective dosing regimen of 1-aminobenzotriazole for inhibition of antipyrine clearance in guinea pigs and mice using serial sampling
    • Balani, S. K., Li, P., Nguyen, J., Cardoza, K., Zeng, H., Mu, D.-X., Wu, J.-T., Gan, L.-S., and Lee, F. W. (2004) Effective dosing regimen of 1-aminobenzotriazole for inhibition of antipyrine clearance in guinea pigs and mice using serial sampling Drug Metab. Dispos. 32, 1092-1095
    • (2004) Drug Metab. Dispos. , vol.32 , pp. 1092-1095
    • Balani, S.K.1    Li, P.2    Nguyen, J.3    Cardoza, K.4    Zeng, H.5    Mu, D.-X.6    Wu, J.-T.7    Gan, L.-S.8    Lee, F.W.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.