about
Antimicrobials: a global alliance for optimizing their rational use in intra-abdominal infections (AGORA).Self-resistance in Streptomyces, with Special Reference to β-Lactam AntibioticsThe Chemical Biology of Human Metallo-β-Lactamase Fold ProteinsResistance to antibiotics targeted to the bacterial cell wallSolution structures of the Bacillus cereus metallo-β-lactamase BcII and its complex with the broad spectrum inhibitor R -thiomandelic acidHis224 Alters the R2 Drug Binding Site and Phe218 Influences the Catalytic Efficiency of the Metallo- -Lactamase VIM-7Structural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-β-lactamasesUse of ferrous iron by metallo-β-lactamasesCarbapenem-Resistant Acinetobacter baumannii and Enterobacteriaceae in South and Southeast AsiaIron and zinc exploitation during bacterial pathogenesisStructural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistanceCharacterization of a novel Zn²⁺-dependent intrinsic imipenemase from Pseudomonas aeruginosaEthylmalonic encephalopathy ETHE1 R163W/R163Q mutations alter protein stability and redox properties of the iron centre.Molecular Characterization and Computational Modelling of New Delhi Metallo-β-Lactamase-5 from an Escherichia coli Isolate (KOEC3) of Bovine Origin.New β-lactamase inhibitors: a therapeutic renaissance in an MDR world.Genomic epidemiology of global Klebsiella pneumoniae carbapenemase (KPC)-producing Escherichia coli.Biochemical characterization of New Delhi metallo-β-lactamase variants reveals differences in protein stability.Antibiotic adjuvants: diverse strategies for controlling drug-resistant pathogens.Comparison of Verona Integron-Borne Metallo-β-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition ProfilesProbing the effect of the non-active-site mutation Y229W in New Delhi metallo-β-lactamase-1 by site-directed mutagenesis, kinetic studies, and molecular dynamics simulations.Host-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues.Detection of Metallo-Beta Lactamases Among Carbapenem-Resistant Pseudomonas aeruginosa.Deep Sequencing of Random Mutant Libraries Reveals the Active Site of the Narrow Specificity CphA Metallo-β-Lactamase is Fragile to Mutations.Globally distributed root endophyte Phialocephala subalpina links pathogenic and saprophytic lifestyles.Structural enzymology using X-ray free electron lasers.Conformational dynamics of metallo-β-lactamase CcrA during catalysis investigated by using DEER spectroscopyRole of Residues W228 and Y233 in the Structure and Activity of Metallo-β-Lactamase GIM-1.Multiyear, Multinational Survey of the Incidence and Global Distribution of Metallo-β-Lactamase-Producing Enterobacteriaceae and Pseudomonas aeruginosa.Uncomplicated Urinary Tract Infections and Antibiotic Resistance-Epidemiological and Mechanistic AspectsB1-Metallo-β-Lactamases: Where Do We Stand?Cross-class metallo-β-lactamase inhibition by bisthiazolidines reveals multiple binding modes.Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site.Cyclic Boronates Inhibit All Classes of β-Lactamases.NMR-filtered virtual screening leads to non-metal chelating metallo-β-lactamase inhibitorsProliferation and significance of clinically relevant β-lactamases.Confronting carbapenemase-producing Klebsiella pneumoniae.Fragment-based inhibitor discovery against β-lactamaseA variety of roles for versatile zinc in metallo-β-lactamases.Ceftolozane/tazobactam (CXA 201) for the treatment of intra-abdominal infections.Potential DNA binding and nuclease functions of ComEC domains characterized in silico.
P2860
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P2860
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Metallo-β-lactamase structure and function.
@en
type
label
Metallo-β-lactamase structure and function.
@en
prefLabel
Metallo-β-lactamase structure and function.
@en
P2860
P1476
Metallo-β-lactamase structure and function.
@en
P2093
Timothy Palzkill
P2860
P304
P356
10.1111/J.1749-6632.2012.06796.X
P407
P577
2012-11-16T00:00:00Z