Evaluation of inhibitory action of novel non β-lactam inhibitor against Klebsiella pneumoniae carbapenemase (KPC-2) - Wikidata - awgldk - TriplyDB

Evaluation of inhibitory action of novel non β-lactam inhibitor against Klebsiella pneumoniae carbapenemase (KPC-2)

Evaluation of inhibitory action of novel non β-lactam inhibitor against Klebsiella pneumoniae carbapenemase (KPC-2)

http://www.wikidata.org/entity/Q35284418

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Potential inhibitors designed against NDM-1 type metallo-β-lactamases: an attempt to enhance efficacies of antibiotics against multi-drug-resistant bacteria The analysis of the antibiotic resistome offers new opportunities for therapeutic intervention.

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P2860

Evaluation of inhibitory action of novel non β-lactam inhibitor against Klebsiella pneumoniae carbapenemase (KPC-2)

http://www.wikidata.org/entity/Q35284418

description

2014 nî lūn-bûn

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2014 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

Evaluation of inhibitory actio ...... eumoniae carbapenemase (KPC-2)

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Evaluation of inhibitory actio ...... eumoniae carbapenemase (KPC-2)

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Evaluation of inhibitory actio ...... eumoniae carbapenemase (KPC-2)

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Evaluation of inhibitory actio ...... eumoniae carbapenemase (KPC-2)

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Evaluation of inhibitory actio ...... eumoniae carbapenemase (KPC-2)

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Evaluation of inhibitory actio ...... eumoniae carbapenemase (KPC-2)

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JOURNAL.PONE.0108246

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Evaluation of inhibitory actio ...... eumoniae carbapenemase (KPC-2)

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Arbab Khan

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Asad U Khan

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Mohammad Faheem

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Mohd Danishuddin

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P2860

Novel carbapenem-hydrolyzing beta-lactamase, KPC-1, from a carbapenem-resistant strain of Klebsiella pneumoniae

Updated functional classification of beta-lactamases

Crystal Structure of KPC-2: Insights into Carbapenemase Activity in Class A β-Lactamases † , ‡

Structural and Biochemical Characterization of the Interaction between KPC-2 β-Lactamase and β-Lactamase Inhibitor Protein,

Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction

Efficacy of E. officinalis on the cariogenic properties of Streptococcus mutans: a novel and alternative approach to suppress quorum-sensing mechanism

Biochemical characterization of CTX-M-15 from Enterobacter cloacae and designing a novel non-β-lactam-β-lactamase inhibitor

Inhibitor resistance in the KPC-2 beta-lactamase, a preeminent property of this class A beta-lactamase.

Carbapenem-resistant strain of Klebsiella oxytoca harboring carbapenem-hydrolyzing beta-lactamase KPC-2.

Understanding the molecular determinants of substrate and inhibitor specificities in the Carbapenemase KPC-2: exploring the roles of Arg220 and Glu276.

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e108246

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scholarly article

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10.1371/JOURNAL.PONE.0108246

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9

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9

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2014-09-29T00:00:00Z

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266263976

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25265157

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P921

Klebsiella pneumoniae

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4180753

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