Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases
about
New β-Lactamase Inhibitors in the ClinicA structural view of the antibiotic degradation enzyme NDM-1 from a superbugStructural Insights into the Subclass B3 Metallo- -Lactamase SMB-1 and the Mode of Inhibition by the Common Metallo- -Lactamase Inhibitor MercaptoacetateCrystal Structure of the Mobile Metallo- -Lactamase AIM-1 from Pseudomonas aeruginosa: Insights into Antibiotic Binding and the Role of Gln157Solution structures of the Bacillus cereus metallo-β-lactamase BcII and its complex with the broad spectrum inhibitor R -thiomandelic acidMolecular basis of NDM-1, a new antibiotic resistance determinantComparison of Verona Integron-Borne Metallo-β-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition ProfilesBiochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.Conformational dynamics of metallo-β-lactamase CcrA during catalysis investigated by using DEER spectroscopyCross-class metallo-β-lactamase inhibition by bisthiazolidines reveals multiple binding modes.New β-phospholactam as a carbapenem transition state analog: Synthesis of a broad-spectrum inhibitor of metallo-β-lactamasesAn Update on the Status of Potent Inhibitors of Metallo-β-Lactamases.Fragment-based inhibitor discovery against β-lactamaseA variety of roles for versatile zinc in metallo-β-lactamases.Progress toward inhibitors of metallo-β-lactamases.Carbamylmethyl Mercaptoacetate Thioether: A Novel Scaffold for the Development of L1 Metallo-β-lactamase Inhibitors.1,2,4-Triazole-3-thione Compounds as Inhibitors of Dizinc Metallo-β-lactamases.Decarbonylative Phosphorylation of Amides by Palladium and Nickel Catalysis: The Hirao Cross-Coupling of Amide Derivatives.Rhodium(iii)-catalyzed ortho-olefination of aryl phosphonates.Structure activity relationship studies on rhodanines and derived enethiol inhibitors of metallo-β-lactamases.Structural and Kinetic Studies of the Potent Inhibition of Metallo-β-lactamases by 6-Phosphonomethylpyridine-2-carboxylates.Binding site residues in β-lactamases: role in non-classical interactions and metal bindingDiversity and Proliferation of Metallo-β-Lactamases: a Clarion Call for Clinically Effective Metallo-β-Lactamase Inhibitors
P2860
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P2860
Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases
description
2010 nî lūn-bûn
@nan
2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases
@ast
Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases
@en
Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases
@nl
type
label
Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases
@ast
Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases
@en
Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases
@nl
prefLabel
Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases
@ast
Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases
@en
Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases
@nl
P2093
P50
P356
P1476
Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases
@en
P2093
Dominique Dehareng
Heinrich Delbrück
Kurt Hoffmann
Matthieu Hamel
Michaël Kupper
Paola Sandra Mercuri
P304
P356
10.1021/JM100213C
P407
P577
2010-07-08T00:00:00Z