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Volumn 40, Issue 1, 1997, Pages 4-8

Rationally designed inhibitors of inosine monophosphate dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; INOSINATE DEHYDROGENASE; INOSINE PHOSPHATE;

EID: 0031022626     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm960732v     Document Type: Article
Times cited : (20)

References (24)
  • 1
    • 0014546166 scopus 로고
    • The inhibition of nucleic acid synthesis by mycophenolic acid
    • Franklin, T. J.; Cook, T. M. The inhibition of nucleic acid synthesis by mycophenolic acid. Biochem. J. 1969, 113, 515-524.
    • (1969) Biochem. J. , vol.113 , pp. 515-524
    • Franklin, T.J.1    Cook, T.M.2
  • 2
    • 0027786826 scopus 로고
    • Immunosuppressive and other effects of mycophenolic acid and an ester prodrug, mycophenolate mofetil
    • Allison, A. C.; Eugui, E. M. Immunosuppressive and other effects of mycophenolic acid and an ester prodrug, mycophenolate mofetil. Immunol. Rev. 1993 136, 5-28.
    • (1993) Immunol. Rev. , vol.136 , pp. 5-28
    • Allison, A.C.1    Eugui, E.M.2
  • 3
    • 0025063949 scopus 로고
    • Synthesis and immunosuppressive activity of some side-chain variants of mycophenolic acid
    • Nelson, P. H.; Eugui, E.; Wang, C. C.; Allison, A. C. Synthesis and immunosuppressive activity of some side-chain variants of mycophenolic acid. J. Med. Chem. 1990, 33, 833-838.
    • (1990) J. Med. Chem. , vol.33 , pp. 833-838
    • Nelson, P.H.1    Eugui, E.2    Wang, C.C.3    Allison, A.C.4
  • 4
    • 34249770076 scopus 로고
    • Mycophenolate mofetil: Molecular mechanisms of action
    • Wyvratt, M. J.; Sigal, N. H., Eds.; ESCOM Science Publishers: Leiden
    • Wu, J. C. Mycophenolate mofetil: Molecular mechanisms of action. in Perspectives in Drug Discovery and Design; Wyvratt, M. J.; Sigal, N. H., Eds.; ESCOM Science Publishers: Leiden, 1994; Vol. 2, pp 185-204.
    • (1994) Perspectives in Drug Discovery and Design , vol.2 , pp. 185-204
    • Wu, J.C.1
  • 5
    • 0028216317 scopus 로고
    • Human IMP dehydrogenase catalyzes the dehalogenation of 2-fluoro- and 2-chloroinosine 5′-monophosphate in the absence of NAD
    • Antonino, L. C.; Wu, J. C. Human IMP dehydrogenase catalyzes the dehalogenation of 2-fluoro- and 2-chloroinosine 5′-monophosphate in the absence of NAD. Biochemistry 1994, 33, 1753-1759.
    • (1994) Biochemistry , vol.33 , pp. 1753-1759
    • Antonino, L.C.1    Wu, J.C.2
  • 6
    • 0025103320 scopus 로고
    • Mycophenolic acid and thiazole adenine dinucleotide inhibition of Tritrichomonas foetus inosine 5′-monophosphate dehydrogenase: Implications on enzme mechanism
    • Hedstrom, L.; Wang, C. C. Mycophenolic acid and thiazole adenine dinucleotide inhibition of Tritrichomonas foetus inosine 5′-monophosphate dehydrogenase: Implications on enzme mechanism. Biochemistry 1990, 29, 849-854.
    • (1990) Biochemistry , vol.29 , pp. 849-854
    • Hedstrom, L.1    Wang, C.C.2
  • 7
    • 0029670363 scopus 로고    scopus 로고
    • Trapping of an IMP-dehydrogenase-substrate covalent intermediate by mycophenolic acid
    • Link, J.; Straub, K. Trapping of an IMP-dehydrogenase-substrate covalent intermediate by mycophenolic acid. J. Am. Chem. Soc. 1996, 118, 2091-2092.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2091-2092
    • Link, J.1    Straub, K.2
  • 8
    • 0028231758 scopus 로고
    • Probing the active site of human IMP dehydrogenase using halogenated purine riboside 5′-monophosphates and covalent modification reagents
    • Antonino, L. C.; Straub, K.; Wu, J. C. Probing the active site of human IMP dehydrogenase using halogenated purine riboside 5′-monophosphates and covalent modification reagents. Biochemistry 1994, 33, 1760-1765.
    • (1994) Biochemistry , vol.33 , pp. 1760-1765
    • Antonino, L.C.1    Straub, K.2    Wu, J.C.3
  • 9
    • 0028808281 scopus 로고
    • Identification of the IMP binding site in the IMP dehydrogenase from Tritrichomonas foetus
    • Huete-Perez, J. A.; Wu, J. C.; Whitby, F. G.; Wang, C. C. Identification of the IMP binding site in the IMP dehydrogenase from Tritrichomonas foetus. Biochemistry 1995, 34, 13889-13894.
    • (1995) Biochemistry , vol.34 , pp. 13889-13894
    • Huete-Perez, J.A.1    Wu, J.C.2    Whitby, F.G.3    Wang, C.C.4
  • 10
    • 0021252025 scopus 로고
    • Inhibitors of inosinic acid dehydrogenase. 2-substituted inosinic acids
    • Wong, C. G.; Meyer, R. B., Jr. Inhibitors of inosinic acid dehydrogenase. 2-substituted inosinic acids. J. Med. Chem. 1984, 27, 429-432.
    • (1984) J. Med. Chem. , vol.27 , pp. 429-432
    • Wong, C.G.1    Meyer Jr., R.B.2
  • 11
    • 8044260534 scopus 로고    scopus 로고
    • note
    • 50 values, with the exception of the 2-styryl derivative, which will be discussed later.
  • 12
    • 33947336041 scopus 로고
    • A simple method for the synthesis of inosine, 2-alkylinosine, and xanthosine from 5-amino-1-β-D-ribofuranosyl-4-imidazolecarboxamide
    • Yamasaki, A.; Kumashiro, I.; Takenishi, T. A simple method for the synthesis of inosine, 2-alkylinosine, and xanthosine from 5-amino-1-β-D-ribofuranosyl-4-imidazolecarboxamide. J. Org. Chem. 1967, 32, 3258-3260.
    • (1967) J. Org. Chem. , vol.32 , pp. 3258-3260
    • Yamasaki, A.1    Kumashiro, I.2    Takenishi, T.3
  • 13
    • 0001635779 scopus 로고
    • Studies of phosphorylation. III. Selective phosphorylation of unprotected nucleosides
    • Yoshikana, M.; Kato, T.; Takenishi, T. Studies of phosphorylation. III. Selective phosphorylation of unprotected nucleosides. Bull. Chem. Soc. Jpn. 1969, 43, 3505-3508.
    • (1969) Bull. Chem. Soc. Jpn. , vol.43 , pp. 3505-3508
    • Yoshikana, M.1    Kato, T.2    Takenishi, T.3
  • 14
    • 0030065820 scopus 로고    scopus 로고
    • A Short Synthesis of 2-Vinylinosine
    • Zhang, H.-Z.; Fried, J. A Short Synthesis of 2-Vinylinosine. Synth. Commun. 1996, 26, 351-355.
    • (1996) Synth. Commun. , vol.26 , pp. 351-355
    • Zhang, H.-Z.1    Fried, J.2
  • 15
    • 0016904563 scopus 로고
    • Transition state analog inhibitors and enzyme catalysis
    • Wolfenden, R. Transition state analog inhibitors and enzyme catalysis. Ann. Rev. Biophys. Bioeng. 1976, 5, 271-306.
    • (1976) Ann. Rev. Biophys. Bioeng. , vol.5 , pp. 271-306
    • Wolfenden, R.1
  • 16
    • 0022746525 scopus 로고
    • Inhibition of serine proteases by peptidyl fluoromethyl ketones
    • Imperiali, B.; Abeles, R. H. Inhibition of serine proteases by peptidyl fluoromethyl ketones. Biochemistry 1986, 25, 3760-3767.
    • (1986) Biochemistry , vol.25 , pp. 3760-3767
    • Imperiali, B.1    Abeles, R.H.2
  • 17
    • 0002903441 scopus 로고
    • Analog approaches to the structure of the transition state in enzyme reactions
    • Wolfenden, R. Analog approaches to the structure of the transition state in enzyme reactions. Acc. Chem. Res. 1972, 5, 10-18.
    • (1972) Acc. Chem. Res. , vol.5 , pp. 10-18
    • Wolfenden, R.1
  • 18
    • 0024370607 scopus 로고
    • Novel unsaturated purine nucleosides
    • Nair, V.; Lyons, A. G. Novel unsaturated purine nucleosides. Tetrahedron 1989, 45, 3653-3662.
    • (1989) Tetrahedron , vol.45 , pp. 3653-3662
    • Nair, V.1    Lyons, A.G.2
  • 19
    • 0015911768 scopus 로고
    • Use of peptide aldehydes to generate transition-state analogs of elastase
    • Thompson, R. C. Use of peptide aldehydes to generate transition-state analogs of elastase. Biochemistry 1973, 12, 47-51.
    • (1973) Biochemistry , vol.12 , pp. 47-51
    • Thompson, R.C.1
  • 20
    • 0015524151 scopus 로고
    • Aldehydes as inhibitors of papain
    • Westerik, J. O.; Wolfenden, R. Aldehydes as inhibitors of papain. J. Biol. Chem. 1972, 247, 8195-8197.
    • (1972) J. Biol. Chem. , vol.247 , pp. 8195-8197
    • Westerik, J.O.1    Wolfenden, R.2
  • 21
    • 77956913442 scopus 로고
    • Chemical modification of active-site-directed reagents
    • Boyer, P., Ed.; Acdemic Pess: New York
    • Shaw, E. Chemical modification of active-site-directed reagents. In The Enzymes, 3rd ed.; Boyer, P., Ed.; Acdemic Pess: New York, 1970; Vol. 1, pp 91-137.
    • (1970) The Enzymes, 3rd Ed. , vol.1 , pp. 91-137
    • Shaw, E.1
  • 24
    • 0027717956 scopus 로고
    • Characterization of human type I and type II IMP Dehydrogenases
    • Carr, S. F.; Papp, E.; Wu, J. C.; Natsumeda, Y. Characterization of human type I and type II IMP Dehydrogenases. J. Biol. Chem. 1993, 268, 27286-27290.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27286-27290
    • Carr, S.F.1    Papp, E.2    Wu, J.C.3    Natsumeda, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.