Crystal structure of the Mycobacterium fortuitum class A beta-lactamase: structural basis for broad substrate specificity.
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Detection of protein catalytic residues at high precision using local network properties.A measure of the broad substrate specificity of enzymes based on 'duplicate' catalytic residuesVariations within class-A β-lactamase physiochemical properties reflect evolutionary and environmental patterns, but not antibiotic specificityImpact of β-lactamase inhibition on the activity of ceftaroline against Mycobacterium tuberculosis and Mycobacterium abscessus.Hydrolysis of clavulanate by Mycobacterium tuberculosis β-lactamase BlaC harboring a canonical SDN motif.A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes.Irreversible inhibition of the Mycobacterium tuberculosis beta-lactamase by clavulanate.A programme to create short-course chemotherapy for pulmonary Mycobacterium avium disease based on pharmacokinetics/pharmacodynamics and mathematical forecasting.The discovery of ceftazidime/avibactam as an anti-Mycobacterium avium agent.A Tyrosine Residue Along with a Glutamic Acid of the Omega-Like Loop Governs the Beta-Lactamase Activity of MSMEG_4455 in Mycobacterium smegmatis.
P2860
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P2860
Crystal structure of the Mycobacterium fortuitum class A beta-lactamase: structural basis for broad substrate specificity.
description
2006 nî lūn-bûn
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name
Crystal structure of the Mycob ...... r broad substrate specificity.
@en
type
label
Crystal structure of the Mycob ...... r broad substrate specificity.
@en
prefLabel
Crystal structure of the Mycob ...... r broad substrate specificity.
@en
P2093
P2860
P356
P1476
Crystal structure of the Mycob ...... r broad substrate specificity.
@en
P2093
Birgit Quinting
Eric Sauvage
Eveline Fonzé
Jean-Marie Frère
Moreno Galleni
Paulette Charlier
P2860
P304
P356
10.1128/AAC.01226-05
P407
P577
2006-07-01T00:00:00Z