Metallo-β-lactamases and a tug-of-war for the available zinc at the host–pathogen interface

This publication has 60 references indexed in Scilit:

• Zinc Piracy as a Mechanism of Neisseria meningitidis for Evasion of Nutritional Immunity
  PLOS Pathogens, 2013
• Mutagenesis of Zinc Ligand Residue Cys221 Reveals Plasticity in the IMP-1 Metallo-β-Lactamase Active Site
  Antimicrobial Agents and Chemotherapy, 2012
• Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions
  Nature Chemical Biology, 2012
• Structure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-Lactamase
  PLOS ONE, 2011
• Crystal structure of New Delhi metallo‐β‐lactamase reveals molecular basis for antibiotic resistance
  Protein Science, 2011
• Efficacy of Calcium-EDTA as an Inhibitor for Metallo-β-Lactamase in a Mouse Model of Pseudomonas aeruginosa Pneumonia
  Antimicrobial Agents and Chemotherapy, 2010
• Evidence of Adaptability in Metal Coordination Geometry and Active-Site Loop Conformation among B1 Metallo-β-lactamases,
  Biochemistry, 2010
• Secretion of GOB Metallo-β-Lactamase in Escherichia coli Depends Strictly on the Cooperation between the Cytoplasmic DnaK Chaperone System and the Sec Machinery: Completion of Folding and Zn(II) Ion Acquisition Occur in the Bacterial Periplasm
  Antimicrobial Agents and Chemotherapy, 2009
• Metal Ion Binding and Coordination Geometry for Wild Type and Mutants of Metallo-β-lactamase from Bacillus cereus569/H/9 (BcII)
  Journal of Biological Chemistry, 2001
• Kinetic and spectroscopic characterization of native and metal‐substituted β‐lactamase from Aeromonas hydrophila AE036
  FEBS Letters, 2000