Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria.
about
Three decades of beta-lactamase inhibitorsCharacterization 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 IndiaMechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate modeling and active site mutationsMechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structuresThe Chemical Biology of Human Metallo-β-Lactamase Fold ProteinsQM/MM molecular dynamics studies of metal binding proteinsUse of electron paramagnetic resonance to solve biochemical problemsThe enzymes of bacterial census and censorshipAsp-120 locates Zn2 for optimal metallo-beta-lactamase activitySubstrate-Promoted Formation of a Catalytically Competent Binuclear Center and Regulation of Reactivity in a Glycerophosphodiesterase from Enterobacter aerogenesAdaptive protein evolution grants organismal fitness by improving catalysis and flexibilityHigh-Resolution Crystal Structure of the Subclass B3 Metallo- -Lactamase BJP-1: Rational Basis for Substrate Specificity and Interaction with SulfonamidesMutagenesis of Zinc Ligand Residue Cys221 Reveals Plasticity in the IMP-1 Metallo- -Lactamase Active SiteStructure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-LactamaseMetallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactionsRhodanine hydrolysis leads to potent thioenolate mediated metallo-β-lactamase inhibitionA designed supramolecular protein assembly with in vivo enzymatic activityOvercoming differences: The catalytic mechanism of metallo-β-lactamasesNatural Variants of the KPC-2 Carbapenemase have Evolved Increased Catalytic Efficiency for Ceftazidime Hydrolysis at the Cost of Enzyme StabilityEvolving carbapenemases: can medicinal chemists advance one step ahead of the coming storm?Trapping and characterization of a reaction intermediate in carbapenem hydrolysis by B. cereus metallo-beta-lactamase.VIM-19, a metallo-beta-lactamase with increased carbapenemase activity from Escherichia coli and Klebsiella pneumoniae.Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro EvolutionQM/MM studies of monozinc β-lactamase CphA suggest that the crystal structure of an enzyme-intermediate complex represents a minor pathway.An altered zinc-binding site confers resistance to a covalent inactivator of New Delhi metallo-beta-lactamase-1 (NDM-1) discovered by high-throughput screeningHost-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues.High prevalence of antimicrobial resistance among common bacterial isolates in a tertiary healthcare facility in Rwanda.Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1Metabolome searcher: a high throughput tool for metabolite identification and metabolic pathway mapping directly from mass spectrometry and using genome restrictionNosocomial outbreak of VIM-1-producing Klebsiella pneumoniae isolates of multilocus sequence type 15: molecular basis, clinical risk factors, and outcome.Syntheses and studies of new forms of N-sulfonyloxy β-lactams as potential antibacterial agents and β-lactamase inhibitors.Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.Differential binding of Co(II) and Zn(II) to metallo-beta-lactamase Bla2 from Bacillus anthracis.2-Substituted 4,5-dihydrothiazole-4-carboxylic acids are novel inhibitors of metallo-β-lactamasesStructural and Biochemical Characterization of AidC, a Quorum-Quenching Lactonase with Atypical SelectivityCrystallization and preliminary diffraction studies of GIM-1, a class B carbapenem-hydrolyzing β-lactamase.Exploring the Role of Residue 228 in Substrate and Inhibitor Recognition by VIM Metallo-β-lactamases.Dilution of dipolar interactions in a spin-labeled, multimeric metalloenzyme for DEER studies.Probing the role of Met221 in the unusual metallo-β-lactamase GOB-18.Biochemical characterization of metallo-beta-lactamase VIM-11 from a Pseudomonas aeruginosa clinical strain.
P2860
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P2860
Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria.
@ast
Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria.
@en
type
label
Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria.
@ast
Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria.
@en
prefLabel
Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria.
@ast
Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria.
@en
P2093
P356
P1476
Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria.
@en
P2093
Alejandro J Vila
James Spencer
Michael W Crowder
P304
P356
10.1021/AR0400241
P407
P577
2006-10-01T00:00:00Z