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Volumn 7, Issue 3, 2001, Pages 200-204

Examination of the reduced affinity of the thymidylate synthase G52S mutation for FdUMP by Ab initio and semi-empirical studies

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ENZYME INHIBITOR; FLOXURIDINE PHOSPHATE; THYMIDYLATE SYNTHASE;

EID: 0035288608     PISSN: 10761551     EISSN: None     Source Type: Journal    
DOI: 10.1007/bf03401954     Document Type: Article
Times cited : (3)

References (10)
  • 1
    • 0033579809 scopus 로고    scopus 로고
    • Crystal structures of rat thymidylate synthase inhibited by Tomudex, a potent anticancer drug
    • 1a. Sotelo-Mundo RR, Ciesla J, Dzik JM, et al. (1999) Crystal structures of rat thymidylate synthase inhibited by Tomudex, a potent anticancer drug. Biochemistry 38: 1087-1094.
    • (1999) Biochemistry , vol.38 , pp. 1087-1094
    • Sotelo-Mundo, R.R.1    Ciesla, J.2    Dzik, J.M.3
  • 2
    • 0025307988 scopus 로고
    • Single amino acid substitution defines a naturally occurring genetic variant of human thymidylate synthase
    • 1b. Barbour KW, Berger SH, Berger FG. (1990) Single amino acid substitution defines a naturally occurring genetic variant of human thymidylate synthase. Mol. Pharmacol. 37: 515-518.
    • (1990) Mol. Pharmacol. , vol.37 , pp. 515-518
    • Barbour, K.W.1    Berger, S.H.2    Berger, F.G.3
  • 3
    • 0027081148 scopus 로고
    • A naturally occurring tyrosine to histidine replacement at residue 33 of human thymidylate synthase confers resistance to 5-fluoro-2′-deoxyuridine in mammalian and bacterial cells
    • 1c. Barbour KW, Hoganson DK, Berger SH, Berger FG. (1992) A naturally occurring tyrosine to histidine replacement at residue 33 of human thymidylate synthase confers resistance to 5-fluoro-2′-deoxyuridine in mammalian and bacterial cells. Mol. Pharmacol. 42: 242-248.
    • (1992) Mol. Pharmacol. , vol.42 , pp. 242-248
    • Barbour, K.W.1    Hoganson, D.K.2    Berger, S.H.3    Berger, F.G.4
  • 4
    • 0027275831 scopus 로고
    • Functional effects of a naturally occurring amino acid substitution in human thymidylate synthase
    • 1d. Hughey CT, Barbour KW, Berger FG, Berger SH. (1993) Functional effects of a naturally occurring amino acid substitution in human thymidylate synthase. Mol. Pharmacol. 44: 316-323.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 316-323
    • Hughey, C.T.1    Barbour, K.W.2    Berger, F.G.3    Berger, S.H.4
  • 6
    • 0032813224 scopus 로고    scopus 로고
    • Ab initio studies of some amino acid residue complexes with 4-mercaptopyridine as a model for thymitaq (AG337), an inhibitor of thymidylate synthase
    • Sapse SD, Tong Y, Bertino JR, Sapse AM. (1999) Ab initio studies of some amino acid residue complexes with 4-mercaptopyridine as a model for thymitaq (AG337), an inhibitor of thymidylate synthase. Cancer Invest. 17: 396-401.
    • (1999) Cancer Invest. , vol.17 , pp. 396-401
    • Sapse, S.D.1    Tong, Y.2    Bertino, J.R.3    Sapse, A.M.4
  • 7
    • 0032496226 scopus 로고    scopus 로고
    • Isolation and characterization of Thymitaq (AG337) and 5-fluoro-2-deoxyuridylate-resistant mutants of human thymidylate synthase from ethyl methanesulfonate-exposed human sarcoma HT1080 cells
    • Tong Y, Xinyue L-C, Ercikan-Abali EA, Capiaux GM, Zhao S-C, Banerjee D, Bertino JR. (1998) Isolation and characterization of Thymitaq (AG337) and 5-fluoro-2-deoxyuridylate-resistant mutants of human thymidylate synthase from ethyl methanesulfonate-exposed human sarcoma HT1080 cells. J Biol. Chem. 273: 11611-11618.
    • (1998) J Biol. Chem. , vol.273 , pp. 11611-11618
    • Tong, Y.1    Xinyue, L.-C.2    Ercikan-Abali, E.A.3    Capiaux, G.M.4    Zhao, S.-C.5    Banerjee, D.6    Bertino, J.R.7
  • 8
    • 0027171350 scopus 로고
    • Refined structures of substrate-bound and phosphate-bound thymidylate synthase from Lactobacillus casei
    • Finer-Moore J, Fauman EB, Foster PG, Perry KM, Santi DV, Stroud RM. (1993) Refined structures of substrate-bound and phosphate-bound thymidylate synthase from Lactobacillus casei. J. Mol. Biol. 232: 1101-1116.
    • (1993) J. Mol. Biol. , vol.232 , pp. 1101-1116
    • Finer-Moore, J.1    Fauman, E.B.2    Foster, P.G.3    Perry, K.M.4    Santi, D.V.5    Stroud, R.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.