Crystal structures of VIM‐1 complexes explain active site heterogeneity in VIM‐class metallo‐β‐lactamases-Reference-Cited by-同舟云学术

Crystal structures of VIM‐1 complexes explain active site heterogeneity in VIM‐class metallo‐β‐lactamases

Published:2018-11-23 Issue:1 Volume:286 Page:169-183
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:FEBS J

Author:

Salimraj Ramya¹,Hinchliffe Philip¹,Kosmopoulou Magda¹,Tyrrell Jonathan M.²,Brem Jürgen³,Berkel Sander S.³,Verma Anil⁴,Owens Raymond J.⁴,McDonough Michael A.³,Walsh Timothy R.²,Schofield Christopher J.³,Spencer James¹

Affiliation:

1. School of Cellular and Molecular Medicine University of Bristol UK

2. Institute of Infection and Immunity Cardiff University UK

3. Department of Chemistry University of Oxford UK

4. Oxford Protein Production Facility UK Rutherford Appleton Laboratory Oxfordshire UK

Funder

Medical Research Council

FP7 Joint Technology Initiatives

National Institute of Allergy and Infectious Diseases

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.14695

Reference61 articles.

1. DaviesSC(2013)Infections and the rise of antimicrobial resistance.Annual Report of the Chief Medical Officer Volume 2 2011 Department of Health London.

2. The threat of antibiotic resistance in Gram-negative pathogenic bacteria: β-lactams in peril!

3. Industrial production of β-lactam antibiotics

4. Beta-lactamases and bacterial resistance to antibiotics

5. beta-Lactamases in laboratory and clinical resistance

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