Systematic analysis of metallo-β-lactamases using an automated database.
about
Solution structures of the Bacillus cereus metallo-β-lactamase BcII and its complex with the broad spectrum inhibitor R -thiomandelic acidBioCatNet: A Database System for the Integration of Enzyme Sequences and Biocatalytic Experiments.Draft Genome Sequence of Elizabethkingia meningoseptica Isolated from a Traumatic Wound.New β-lactamase inhibitors: a therapeutic renaissance in an MDR world.Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro EvolutionA standard numbering scheme for thiamine diphosphate-dependent decarboxylases.Biapenem inactivation by B2 metallo β-lactamases: energy landscape of the hydrolysis reaction.Characterization of Halomonas sp. ZM3 isolated from the Zelazny Most post-flotation waste reservoir, with a special focus on its mobile DNA.Computational tools for rational protein engineering of aldolases.Protein variants form a system of networks: microdiversity of IMP metallo-beta-lactamases.How structural and physicochemical determinants shape sequence constraints in a functional enzymeElucidating the Role of Residue 67 in IMP-Type Metallo-β-Lactamase Evolution.Antibiotics as selectors and accelerators of diversity in the mechanisms of resistance: from the resistome to genetic plasticity in the β-lactamases worldDetection of IMP metallo-β-lactamase in carbapenem-nonsusceptible Enterobacteriaceae and non-glucose-fermenting Gram-negative rods by immunochromatography assayNew β-phospholactam as a carbapenem transition state analog: Synthesis of a broad-spectrum inhibitor of metallo-β-lactamasesA variety of roles for versatile zinc in metallo-β-lactamases.Beta-lactamase database (BLDB) - structure and function.The sequence-activity relationship between metallo-β-lactamases IMP-1, IMP-6, and IMP-25 suggests an evolutionary adaptation to meropenem exposure.Network Analysis of Sequence-Function Relationships and Exploration of Sequence Space of TEM β-Lactamases.Identification of 76 novel B1 metallo-β-lactamases through large-scale screening of genomic and metagenomic data.Carbapenemase-Producing Enterobacteriaceae Recovered from the Environment of a Swine Farrow-to-Finish Operation in the United States.Shaping substrate selectivity in a broad spectrum metallo-β-lactamase.Gene Network Analysis of Metallo Beta Lactamase Family Proteins Indicates the Role of Gene Partners in Antibiotic Resistance and Reveals Important Drug Targets.Ceftazidime Is the Key Diversification and Selection Driver of VIM-Type Carbapenemases.Systematic Identification and Classification of β-Lactamases Based on Sequence Similarity Criteria: β-Lactamase Annotation
P2860
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P2860
Systematic analysis of metallo-β-lactamases using an automated database.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Systematic analysis of metallo-β-lactamases using an automated database.
@en
type
label
Systematic analysis of metallo-β-lactamases using an automated database.
@en
prefLabel
Systematic analysis of metallo-β-lactamases using an automated database.
@en
P2093
P2860
P356
P1476
Systematic analysis of metallo-β-lactamases using an automated database.
@en
P2093
Jürgen Pleiss
Michael Widmann
Peter Oelschlaeger
P2860
P304
P356
10.1128/AAC.00255-12
P407
P577
2012-04-30T00:00:00Z