Literature DB >> 16937423

Probing, inhibition, and crystallographic characterization of metallo-beta-lactamase (IMP-1) with fluorescent agents containing dansyl and thiol groups.

Hiromasa Kurosaki1, Yoshihiro Yamaguchi, Hisami Yasuzawa, Wanchun Jin, Yuriko Yamagata, Yoshichika Arakawa.   

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Year:  2006        PMID： 16937423     DOI： 10.1002/cmdc.200600115

Source DB:  PubMed          Journal:  ChemMedChem        ISSN： 1860-7179            Impact factor:   3.466


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  10 in total

1.  Crystallization and preliminary X-ray analysis of the subclass B3 metallo-β-lactamase SMB-1 that confers carbapenem resistance.

Authors:  Jun-ichi Wachino; Yoshihiro Yamaguchi; Shigetarou Mori; Yuriko Yamagata; Yoshichika Arakawa; Keigo Shibayama
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2012-02-23

Review 2.  Fragment-based inhibitor discovery against β-lactamase.

Authors:  Derek A Nichols; Adam R Renslo; Yu Chen
Journal:  Future Med Chem       Date:  2014-03       Impact factor: 3.808

3.  Evolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm?

Authors:  Peter Oelschlaeger; Ni Ai; Kevin T Duprez; William J Welsh; Jeffrey H Toney
Journal:  J Med Chem       Date:  2010-04-22       Impact factor: 7.446

4.  A multiscale approach to predict the binding mode of metallo beta-lactamase inhibitors.

Authors:  Silvia Gervasoni; James Spencer; Philip Hinchliffe; Alessandro Pedretti; Franco Vairoletti; Graciela Mahler; Adrian J Mulholland
Journal:  Proteins       Date:  2021-09-20

5.  Structural insights into the design of reversible fluorescent probes for metallo-β-lactamases NDM-1, VIM-2, and IMP-1.

Authors:  Sky Price; Radhika Mehta; Dominique Tan; Abigail Hinojosa; Pei W Thomas; Tawanda Cummings; Walter Fast; Emily L Que
Journal:  J Inorg Biochem       Date:  2022-05-20       Impact factor: 4.336

Review 6.  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

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.  Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.

Authors:  Mahesh Aitha; Amy R Marts; Alex Bergstrom; Abraham Jon Møller; Lindsay Moritz; Lucien Turner; Jay C Nix; Robert A Bonomo; Richard C Page; David L Tierney; Michael W Crowder
Journal:  Biochemistry       Date:  2014-11-13       Impact factor: 3.162

9.  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

10.  Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures.

Authors:  Dali Liu; Jessica Momb; Pei W Thomas; Aaron Moulin; Gregory A Petsko; Walter Fast; Dagmar Ringe
Journal:  Biochemistry       Date:  2008-07-22       Impact factor: 3.162
  10 in total

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