Structural Insight into Potent Broad-Spectrum Inhibition with Reversible Recyclization Mechanism: Avibactam in Complex with CTX-M-15 and Pseudomonas aeruginosa AmpC -Lactamases - Wikidata - wikimedia - TriplyDB

Structural Insight into Potent Broad-Spectrum Inhibition with Reversible Recyclization Mechanism: Avibactam in Complex with CTX-M-15 and Pseudomonas aeruginosa AmpC -Lactamases

Structural Insight into Potent Broad-Spectrum Inhibition with Reversible Recyclization Mechanism: Avibactam in Complex with CTX-M-15 and Pseudomonas aeruginosa AmpC -Lactamases

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Kinetics of avibactam inhibition against Class A, C, and D β-lactamases New β-Lactamase Inhibitors in the Clinic Pseudomonas aeruginosa ventilator-associated pneumonia management The β-Lactams Strike Back: Ceftazidime-Avibactam Structure of the extended-spectrum class C β-lactamase ADC-1 fromAcinetobacter baumannii Avibactam and Class C -Lactamases: Mechanism of Inhibition, Conservation of the Binding Pocket, and Implications for Resistance OP0595, a new diazabicyclooctane: mode of action as a serine β-lactamase inhibitor, antibiotic and β-lactam 'enhancer'Crystal Structure of the Pseudomonas aeruginosa BEL-1 Extended-Spectrum β-Lactamase and its Complex with Moxalactam and Imipenem Targeting Antibiotic Resistance Investigations on recyclisation and hydrolysis in avibactam mediated serine β-lactamase inhibition Recent contributions of structure-based drug design to the development of antibacterial compounds.Structural and Functional Aspects of Class A Carbapenemases.New β-lactamase inhibitors: a therapeutic renaissance in an MDR world.Reclaiming the efficacy of β-lactam-β-lactamase inhibitor combinations: avibactam restores the susceptibility of CMY-2-producing Escherichia coli to ceftazidime.Effect of asparagine substitutions in the YXN loop of a class C β-lactamase of Acinetobacter baumannii on substrate and inhibitor kinetics.Unexpected challenges in treating multidrug-resistant Gram-negative bacteria: resistance to ceftazidime-avibactam in archived isolates of Pseudomonas aeruginosa.Classification of Beta-lactamases and penicillin binding proteins using ligand-centric network models.Variants of β-lactamase KPC-2 that are resistant to inhibition by avibactam.Avibactam and inhibitor-resistant SHV β-lactamases Inhibition of Klebsiella β-Lactamases (SHV-1 and KPC-2) by Avibactam: A Structural Study.In vitro selection of ceftazidime-avibactam resistance in Enterobacteriaceae with KPC-3 carbapenemase.Structure-based approach for identification of novel phenylboronic acids as serine-β-lactamase inhibitors.Characterization of a Carbapenem-Hydrolyzing Enzyme, PoxB, in Pseudomonas aeruginosa PAO1.β-Lactam Antibiotics Renaissance.In vitro activity of ceftaroline-avibactam against gram-negative and gram-positive pathogens isolated from patients in Canadian hospitals from 2010 to 2012: results from the CANWARD surveillance study A kinetic analysis of the inhibition of FOX-4 β-lactamase, a plasmid-mediated AmpC cephalosporinase, by monocyclic β-lactams and carbapenems Cyclic Boronates Inhibit All Classes of β-Lactamases.Fragment-based inhibitor discovery against β-lactamase β-lactam/β-lactamase inhibitor combinations: from then to now.Antimicrobial activity of ceftazidime-avibactam against Gram-negative organisms collected from U.S. medical centers in 2012.New promising β-lactamase inhibitors for clinical use.Ceftazidime-avibactam for the treatment of complicated urinary tract infections and complicated intra-abdominal infections.Recent developments in antibiotic agents for the treatment of complicated intra-abdominal infections.One ring to rule them all: Current trends in combating bacterial resistance to the β-lactams The road to avibactam: the first clinically useful non-β-lactam working somewhat like a β-lactam.Emerging drugs for nosocomial pneumonia.Recent Advances in the Rational Design and Optimization of Antibacterial Agents.Identification of Novel VEB β-Lactamase Enzymes and Their Impact on Avibactam Inhibition.Structural/mechanistic insights into the efficacy of non-classical β-lactamase inhibitors against extensively drug resistant Stenotrophomonas maltophilia clinical isolates.Avibactam Restores the Susceptibility of Clinical Isolates of Stenotrophomonas maltophilia to Aztreonam.

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Structural Insight into Potent Broad-Spectrum Inhibition with Reversible Recyclization Mechanism: Avibactam in Complex with CTX-M-15 and Pseudomonas aeruginosa AmpC -Lactamases

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2013 nî lūn-bûn

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2013 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2013年の論文

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Structural Insight into Potent ...... s aeruginosa AmpC -Lactamases

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Structural Insight into Potent ...... s aeruginosa AmpC -Lactamases

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Gautam Sanyal

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Sushmita D Lahiri

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Thomas Durand-Reville

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P2860

Three decades of beta-lactamase inhibitors

Mechanistic insights into the inhibition of serine proteases by monocyclic lactams

An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation

Structural milestones in the reaction pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase

Structural basis for imipenem inhibition of class C beta-lactamases.

Structural aspects for evolution of beta-lactamases from penicillin-binding proteins

Exploiting structure similarity in refinement: automated NCS and target-structure restraints in BUSTER

NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis

Coot: model-building tools for molecular graphics

Protein production by auto-induction in high density shaking cultures

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2496-505

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10.1128/AAC.02247-12

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6

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57

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Manuela Benvenuti

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Jean-Denis Docquier

Filomena De Luca

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2013-06-01T00:00:00Z

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23439634

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Pseudomonas aeruginosa

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3716117

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