Inhibition Studies on the Metallo-β-lactamase L1 from Stenotrophomonas maltophilia
Authors:
- Michael W CrowderMCMichael W Crowder
- 1 August 1999
- journal article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 368 (1) , 1-6
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 å resolution 1 1Edited by K. NagaiJournal of Molecular Biology, 1998
- Crystal Structure of the Zinc-Dependent β-Lactamase from Bacillus cereus at 1.9 Å Resolution: Binuclear Active Site with Features of a Mononuclear Enzyme,Biochemistry, 1998
- Metallo‐β‐Lactamases: A Class ApartClinical Infectious Diseases, 1998
- Spectroscopic Characterization of a Binuclear Metal Site in Bacillus cereus β-Lactamase IIBiochemistry, 1998
- Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-β-lactamaseChemistry & Biology, 1998
- Detection of Noncovalent tRNA·Aminoacyl-tRNA Synthetase Complexes by Matrix-assisted Laser Desorption/Ionization Mass SpectrometryJournal of Biological Chemistry, 1997
- Zn(II) Dependence of the Aeromonas hydrophila AE036 Metallo-β-lactamase Activity and StabilityBiochemistry, 1997
- Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilisStructure, 1996
- Metallo-β-lactamases— new therapeutic challengeJournal of Medical Microbiology, 1993
- The Crisis in Antibiotic ResistanceScience, 1992