Predicting allosteric mutants that increase activity of a major antibiotic resistance enzyme
Author:
Affiliation:
1. Department of Molecular Physiology
2. University of Virginia
3. Charlottesville
4. USA
5. Department of Biomedical Engineering
Abstract
Allosteric mutations increasingkcatin a beta lactamase act by changing conformational ensembles of active-site residues identified by machine learning.
Funder
National Institute of Allergy and Infectious Diseases
Google
Hartwell Foundation
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2017/SC/C7SC02676E
Reference58 articles.
1. Structure, Function, and Inhibition along the Reaction Coordinate of CTX-M β-Lactamases
2. Atomic Resolution Structures of CTX-M β-Lactamases: Extended Spectrum Activities from Increased Mobility and Decreased Stability
3. W. H. Organization , Antimicrobial resistance: global report on surveillance, World Health Organization, 2014
4. Attributable Hospital Cost and Length of Stay Associated with Health Care-Associated Infections Caused by Antibiotic-Resistant Gram-Negative Bacteria
5. qnrB , Another Plasmid-Mediated Gene for Quinolone Resistance
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