Literature DB >> 10509927

Structure-activity relationships of biphenyl tetrazoles as metallo-beta-lactamase inhibitors.

J H Toney1, K A Cleary, G G Hammond, X Yuan, W J May, S M Hutchins, W T Ashton, D E Vanderwall.   

Abstract

Resistance to carbapenem antibiotics in gram-negative bacteria is due, in part, to expression of a wide spectrum metallo-beta-lactamase, which renders the drug inactive. Biphenyl tetrazoles containing 3-n-butyl-1-phenylpyrazole-5-carboxylates or the corresponding 5-ethyl esters were found to inhibit metallo-beta-lactamases as well as renal dehydropeptidase I to a lesser extent.

Entities:  

Mesh:

Substances:

Year:  1999        PMID: 10509927     DOI: 10.1016/s0960-894x(99)00458-8

Source DB:  PubMed          Journal:  Bioorg Med Chem Lett        ISSN: 0960-894X            Impact factor:   2.823


  8 in total

1.  Antifungal properties of substituted 1-phenyl-5-mercaptotetrazoles and their oxidation product, 5-bis-(1-phenyltetrazolyl)disulfide.

Authors:  K Nesmĕrák; M Pospísek; I Nĕmec; K Waisser; J Gabriel
Journal:  Folia Microbiol (Praha)       Date:  2000       Impact factor: 2.099

Review 2.  Metallo-beta-lactamases: the quiet before the storm?

Authors:  Timothy R Walsh; Mark A Toleman; Laurent Poirel; Patrice Nordmann
Journal:  Clin Microbiol Rev       Date:  2005-04       Impact factor: 26.132

3.  N-arylsulfonyl hydrazones as inhibitors of IMP-1 metallo-beta-lactamase.

Authors:  Stefan Siemann; Darryl P Evanoff; Laura Marrone; Anthony J Clarke; Thammaiah Viswanatha; Gary I Dmitrienko
Journal:  Antimicrob Agents Chemother       Date:  2002-08       Impact factor: 5.191

Review 4.  Diversity and Proliferation of Metallo-β-Lactamases: a Clarion Call for Clinically Effective Metallo-β-Lactamase Inhibitors.

Authors:  Anou M Somboro; John Osei Sekyere; Daniel G Amoako; Sabiha Y Essack; Linda A Bester
Journal:  Appl Environ Microbiol       Date:  2018-08-31       Impact factor: 4.792

5.  Probing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis.

Authors:  Anne L Carenbauer; James D Garrity; Gopal Periyannan; Robert B Yates; Michael W Crowder
Journal:  BMC Biochem       Date:  2002-02-13       Impact factor: 4.059

6.  An Update on the Status of Potent Inhibitors of Metallo-β-Lactamases.

Authors:  Nazar Ul Islam
Journal:  Sci Pharm       Date:  2013-03-28

7.  Solution structures of the Bacillus cereus metallo-β-lactamase BcII and its complex with the broad spectrum inhibitor R-thiomandelic acid.

Authors:  Andreas Ioannis Karsisiotis; Christian F Damblon; Gordon C K Roberts
Journal:  Biochem J       Date:  2013-12-15       Impact factor: 3.857

8.  Structural and Kinetic Studies of the Potent Inhibition of Metallo-β-lactamases by 6-Phosphonomethylpyridine-2-carboxylates.

Authors:  Philip Hinchliffe; Carol A Tanner; Anthony P Krismanich; Geneviève Labbé; Valerie J Goodfellow; Laura Marrone; Ahmed Y Desoky; Karina Calvopiña; Emily E Whittle; Fanxing Zeng; Matthew B Avison; Niels C Bols; Stefan Siemann; James Spencer; Gary I Dmitrienko
Journal:  Biochemistry       Date:  2018-03-09       Impact factor: 3.162

  8 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.