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Journal Abstract Search

120 related items for PubMed ID: 15187432

  • 1. Comparative study of the inhibition of metallo-beta-lactamases (IMP-1 and VIM-2) by thiol compounds that contain a hydrophobic group.
    Jin W, Arakawa Y, Yasuzawa H, Taki T, Hashiguchi R, Mitsutani K, Shoga A, Yamaguchi Y, Kurosaki H, Shibata N, Ohta M, Goto M.
    Biol Pharm Bull; 2004 Jun; 27(6):851-6. PubMed ID: 15187432
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  • 2. Spectroscopic and biochemical characterization of metallo-β-lactamase IMP-1 with dicarboxylic, sulfonyl, and thiol inhibitors.
    Zhang H, Yang K, Cheng Z, Thomas C, Steinbrunner A, Pryor C, Vulcan M, Kemp C, Orea D, Paththamperuma C, Chen AY, Cohen SM, Page RC, Tierney DL, Crowder MW.
    Bioorg Med Chem; 2021 Jun 15; 40():116183. PubMed ID: 33965839
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  • 6. Carbapenem derivatives as potential inhibitors of various beta-lactamases, including class B metallo-beta-lactamases.
    Nagano R, Adachi Y, Imamura H, Yamada K, Hashizume T, Morishima H.
    Antimicrob Agents Chemother; 1999 Oct 15; 43(10):2497-503. PubMed ID: 10508031
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  • 7. Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor.
    Concha NO, Janson CA, Rowling P, Pearson S, Cheever CA, Clarke BP, Lewis C, Galleni M, Frère JM, Payne DJ, Bateson JH, Abdel-Meguid SS.
    Biochemistry; 2000 Apr 18; 39(15):4288-98. PubMed ID: 10757977
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  • 10. Synthesis and SAR of thioester and thiol inhibitors of IMP-1 metallo-beta-lactamase.
    Greenlee ML, Laub JB, Balkovec JM, Hammond ML, Hammond GG, Pompliano DL, Epstein-Toney JH.
    Bioorg Med Chem Lett; 1999 Sep 06; 9(17):2549-54. PubMed ID: 10498206
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  • 11. Probing, inhibition, and crystallographic characterization of metallo-beta-lactamase (IMP-1) with fluorescent agents containing dansyl and thiol groups.
    Kurosaki H, Yamaguchi Y, Yasuzawa H, Jin W, Yamagata Y, Arakawa Y.
    ChemMedChem; 2006 Sep 06; 1(9):969-72. PubMed ID: 16937423
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  • 12. Approved Drugs Containing Thiols as Inhibitors of Metallo-β-lactamases: Strategy To Combat Multidrug-Resistant Bacteria.
    Klingler FM, Wichelhaus TA, Frank D, Cuesta-Bernal J, El-Delik J, Müller HF, Sjuts H, Göttig S, Koenigs A, Pos KM, Pogoryelov D, Proschak E.
    J Med Chem; 2015 Apr 23; 58(8):3626-30. PubMed ID: 25815530
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  • 18. Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases.
    Lassaux P, Hamel M, Gulea M, Delbrück H, Mercuri PS, Horsfall L, Dehareng D, Kupper M, Frère JM, Hoffmann K, Galleni M, Bebrone C.
    J Med Chem; 2010 Jul 08; 53(13):4862-76. PubMed ID: 20527888
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  • 20. Crystallographic investigation of the inhibition mode of a VIM-2 metallo-beta-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor.
    Yamaguchi Y, Jin W, Matsunaga K, Ikemizu S, Yamagata Y, Wachino J, Shibata N, Arakawa Y, Kurosaki H.
    J Med Chem; 2007 Dec 27; 50(26):6647-53. PubMed ID: 18052313
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