Assay platform for clinically relevant metallo-β-lactamases. - Test2 - elhamkhani - TriplyDB

Assay platform for clinically relevant metallo-β-lactamases.

Assay platform for clinically relevant metallo-β-lactamases.

http://www.wikidata.org/entity/Q41832679

about

Substrate Deconstruction and the Nonadditivity of Enzyme Recognition Rhodanine hydrolysis leads to potent thioenolate mediated metallo-β-lactamase inhibition Use of ferrous iron by metallo-β-lactamases Biochemical characterization of New Delhi metallo-β-lactamase variants reveals differences in protein stability.Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy.Structural Basis of Metallo-β-Lactamase Inhibition by Captopril Stereoisomers Comparison of Verona Integron-Borne Metallo-β-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition Profiles Interaction of Avibactam with Class B Metallo-β-Lactamases.Exploring the Role of Residue 228 in Substrate and Inhibitor Recognition by VIM Metallo-β-lactamases.Cyclic Boronates Inhibit All Classes of β-Lactamases.NMR-filtered virtual screening leads to non-metal chelating metallo-β-lactamase inhibitors Fragment-based inhibitor discovery against β-lactamase New Delhi metallo-β-lactamase-1: structure, inhibitors and detection of producers.Structural/mechanistic insights into the efficacy of non-classical β-lactamase inhibitors against extensively drug resistant Stenotrophomonas maltophilia clinical isolates.Monitoring conformational changes in the NDM-1 metallo-β-lactamase by 19F NMR spectroscopy.19 F-NMR Reveals the Role of Mobile Loops in Product and Inhibitor Binding by the São Paulo Metallo-β-Lactamase.Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates.Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1†Electronic supplementary information (ESI) available: Procedures for protein expression and purification, 19F-labelling, crystallisation, data collection, and structure de Role for dithiolopyrrolones in disrupting bacterial metal homeostasis.13C-Carbamylation as a mechanistic probe for the inhibition of class D β-lactamases by avibactam and halide ions.Structure activity relationship studies on rhodanines and derived enethiol inhibitors of metallo-β-lactamases.Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-β-lactamase inhibition.Structural and Kinetic Studies of the Potent Inhibition of Metallo-β-lactamases by 6-Phosphonomethylpyridine-2-carboxylates.Chromophore-linked substrate (CLS405): probing metallo-β-lactamase activity and inhibition.

P2860

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P2860

Assay platform for clinically relevant metallo-β-lactamases.

http://www.wikidata.org/entity/Q41832679

description

2013 nî lūn-bûn

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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2013年论文

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2013年论文

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name

Assay platform for clinically relevant metallo-β-lactamases.

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Assay platform for clinically relevant metallo-β-lactamases.

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Assay platform for clinically relevant metallo-β-lactamases.

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Assay platform for clinically relevant metallo-β-lactamases.

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Assay platform for clinically relevant metallo-β-lactamases.

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Assay platform for clinically relevant metallo-β-lactamases.

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2-s2.0-84884245033

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Journal of Medicinal Chemistry

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Assay platform for clinically relevant metallo-β-lactamases.

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Anil Verma

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James Spencer

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Jürgen Brem

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Raymond J Owens

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Sander S van Berkel

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P2860

Carbapenems: past, present, and future

Updated functional classification of beta-lactamases

Three decades of beta-lactamase inhibitors

Characterization of a new metallo-beta-lactamase gene, bla(NDM-1), and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India

Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase

The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form

Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols

A structural view of the antibiotic degradation enzyme NDM-1 from a superbug

Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism

Structure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-Lactamase

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17

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56

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Christopher J. Schofield

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2013-08-16T00:00:00Z

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