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Journal Abstract Search


136 related items for PubMed ID: 12431056

  • 1. Sulfamide-based inhibitors for carboxypeptidase A. Novel type transition state analogue inhibitors for zinc proteases.
    Park JD, Kim DH, Kim SJ, Woo JR, Ryu SE.
    J Med Chem; 2002 Nov 21; 45(24):5295-302. PubMed ID: 12431056
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  • 2. Sulfamide derivatives as transition state analogue inhibitors for carboxypeptidase A.
    Park JD, Kim DH.
    Bioorg Med Chem; 2004 May 01; 12(9):2349-56. PubMed ID: 15080932
    [Abstract] [Full Text] [Related]

  • 3. Insight into the stereochemistry in the inhibition of carboxypeptidase A with N-(hydroxyaminocarbonyl)phenylalanine: binding modes of an enantiomeric pair of the inhibitor to carboxypeptidase A.
    Cho JH, Kim DH, Chung SJ, Ha NC, Oh BH, Yong Choi K.
    Bioorg Med Chem; 2002 Jun 01; 10(6):2015-22. PubMed ID: 11937361
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  • 4. N-(Hydroxyaminocarbonyl)phenylalanine: a novel class of inhibitor for carboxypeptidase A.
    Chung SJ, Kim DH.
    Bioorg Med Chem; 2001 Jan 01; 9(1):185-9. PubMed ID: 11197339
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  • 5. Nitro as a novel zinc-binding group in the inhibition of carboxypeptidase A.
    Wang SH, Wang SF, Xuan W, Zeng ZH, Jin JY, Ma J, Tian GR.
    Bioorg Med Chem; 2008 Apr 01; 16(7):3596-601. PubMed ID: 18289863
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  • 17. Gem-dialkyl succinic acids: a novel class of inhibitors for carboxypeptidases.
    Asante-Appiah E, Seetharaman J, Sicheri F, Yang DS, Chan WW.
    Biochemistry; 1997 Jul 22; 36(29):8710-5. PubMed ID: 9220957
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  • 18. Hippuryl-alpha-methylphenylalanine and hippuryl-alpha-methylphenyllactic acid as substrates for carboxypeptidase A. Syntheses, kinetic evaluation and mechanistic implication.
    Lee M, Kim DH.
    Bioorg Med Chem; 2000 Apr 22; 8(4):815-23. PubMed ID: 10819170
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  • 19. Crystal structure of the complex of carboxypeptidase A with a strongly bound phosphonate in a new crystalline form: comparison with structures of other complexes.
    Kim H, Lipscomb WN.
    Biochemistry; 1990 Jun 12; 29(23):5546-55. PubMed ID: 2386784
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  • 20. Design and synthesis of novel imidazole-substituted dipeptide amides as potent and selective inhibitors of Candida albicans myristoylCoA:protein N-myristoyltransferase and identification of related tripeptide inhibitors with mechanism-based antifungal activity.
    Devadas B, Freeman SK, Zupec ME, Lu HF, Nagarajan SR, Kishore NS, Lodge JK, Kuneman DW, McWherter CA, Vinjamoori DV, Getman DP, Gordon JI, Sikorski JA.
    J Med Chem; 1997 Aug 01; 40(16):2609-25. PubMed ID: 9258368
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