NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis
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Kinetics of avibactam inhibition against Class A, C, and D β-lactamasesNew β-Lactamase Inhibitors in the ClinicStructural Insight into Potent Broad-Spectrum Inhibition with Reversible Recyclization Mechanism: Avibactam in Complex with CTX-M-15 and Pseudomonas aeruginosa AmpC -LactamasesTebipenem, a New Carbapenem Antibiotic, Is a Slow Substrate That Inhibits the β-Lactamase from Mycobacterium tuberculosisTargeting Antibiotic ResistanceKinetic and Structural Characterization of the Interaction of 6-Methylidene Penem 2 with the β-Lactamase from Mycobacterium tuberculosisNew β-lactamase inhibitors: a therapeutic renaissance in an MDR world.Ceftazidime-avibactam: a novel cephalosporin/β-lactamase inhibitor combination.Classification of Beta-lactamases and penicillin binding proteins using ligand-centric network models.Inhibition of Klebsiella β-Lactamases (SHV-1 and KPC-2) by Avibactam: A Structural Study.Hydrolysis of clavulanate by Mycobacterium tuberculosis β-lactamase BlaC harboring a canonical SDN motif.Characterization of a Carbapenem-Hydrolyzing Enzyme, PoxB, in Pseudomonas aeruginosa PAO1.Advances in MRSA drug discovery: where are we and where do we need to be?The intrinsic resistome of bacterial pathogens.Resistance in tuberculosis: what do we know and where can we go?Structural and mechanistic insights into the inhibition of class C β-lactamases through the adenylylation of the nucleophilic serine.Ceftazidime-avibactam (CTZ-AVI) as a treatment for hospitalized adult patients with complicated intra-abdominal infections.β-Lactam Resistance Mechanisms: Gram-Positive Bacteria and Mycobacterium tuberculosis.β-Lactamase inhibition by avibactam in Mycobacterium abscessus.Structural/mechanistic insights into the efficacy of non-classical β-lactamase inhibitors against extensively drug resistant Stenotrophomonas maltophilia clinical isolates.Overcoming an Extremely Drug Resistant (XDR) Pathogen: Avibactam Restores Susceptibility to Ceftazidime for Burkholderia cepacia Complex Isolates from Cystic Fibrosis Patients.The discovery of ceftazidime/avibactam as an anti-Mycobacterium avium agent.On 3LEZ, a deep-sea halophilic protein with in vitro class-a β-lactamase activity: molecular-dynamics, docking, and reactivity simulations.Phosphate Promotes the Recovery of Mycobacterium tuberculosis β-Lactamase from Clavulanic Acid Inhibition.Inhibition of β-lactamases of mycobacteria by avibactam and clavulanate.Exploring Additional Dimensions of Complexity in Inhibitor Design for Serine β-Lactamases: Mechanistic and Intra- and Inter-molecular Chemistry Approaches.
P2860
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P2860
NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis
description
2012 nî lūn-bûn
@nan
2012 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis
@ast
NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis
@en
NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis
@nl
type
label
NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis
@ast
NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis
@en
NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis
@nl
prefLabel
NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis
@ast
NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis
@en
NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis
@nl
P2860
P3181
P356
P1433
P1476
NXL104 irreversibly inhibits the β-lactamase from Mycobacterium tuberculosis
@en
P2093
John S Blanchard
P2860
P304
P3181
P356
10.1021/BI300508R
P407
P577
2012-05-22T00:00:00Z