Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in TEM-1 beta-lactamase.
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Crystal Structure of KPC-2: Insights into Carbapenemase Activity in Class A β-Lactamases † , ‡Saturation mutagenesis of Asn152 reveals a substrate selectivity switch in P99 cephalosporinaseEndothelial galectin-1 binds to specific glycans on nipah virus fusion protein and inhibits maturation, mobility, and function to block syncytia formation.A measure of the broad substrate specificity of enzymes based on 'duplicate' catalytic residuesChimeric β-lactamases: global conservation of parental function and fast time-scale dynamics with increased slow motionsRole of Asp104 in the SHV beta-lactamase.Exploring the potential impact of an expanded genetic code on protein functionHigh tolerance to simultaneous active-site mutations in TEM-1 beta-lactamase: Distinct mutational paths provide more generalized beta-lactam recognitionHigh adaptability of the omega loop underlies the substrate-spectrum-extension evolution of a class A β-lactamase, PenL.The structure of Toho1 β-lactamase in complex with penicillin reveals the role of Tyr105 in substrate recognition.A quantitative and kinetic fusion protein-triggering assay can discern distinct steps in the nipah virus membrane fusion cascadeElucidating the role of Trp105 in the KPC-2 β-lactamase.Functional modulation and directed assembly of an enzyme through designed non-natural post-translation modification.The V4 and V5 Variable Loops of HIV-1 Envelope Glycoprotein Are Tolerant to Insertion of Green Fluorescent Protein and Are Useful Targets for Labeling.Substitutions at position 105 in SHV family β-lactamases decrease catalytic efficiency and cause inhibitor resistance.Predicting allosteric mutants that increase activity of a major antibiotic resistance enzyme.A catalytically and genetically optimized beta-lactamase-matrix based assay for sensitive, specific, and higher throughput analysis of native henipavirus entry characteristics.Amino acid residues that contribute to substrate specificity of class A beta-lactamase SME-1.NMR dynamics of PSE-4 beta-lactamase: an interplay of ps-ns order and mus-ms motions in the active site.The C-terminal residues in the alpha-interacting domain (AID) helix anchor CaV beta subunit interaction and modulation of CaV2.3 channels.NMR investigation of Tyr105 mutants in TEM-1 beta-lactamase: dynamics are correlated with function.Defining the architecture of KPC-2 Carbapenemase: identifying allosteric networks to fight antibiotics resistance
P2860
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P2860
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in TEM-1 beta-lactamase.
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2004 nî lūn-bûn
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name
Site-saturation mutagenesis of ...... ation in TEM-1 beta-lactamase.
@en
Site-saturation mutagenesis of ...... ation in TEM-1 beta-lactamase.
@nl
type
label
Site-saturation mutagenesis of ...... ation in TEM-1 beta-lactamase.
@en
Site-saturation mutagenesis of ...... ation in TEM-1 beta-lactamase.
@nl
prefLabel
Site-saturation mutagenesis of ...... ation in TEM-1 beta-lactamase.
@en
Site-saturation mutagenesis of ...... ation in TEM-1 beta-lactamase.
@nl
P2093
P2860
P356
P1476
Site-saturation mutagenesis of ...... ation in TEM-1 beta-lactamase.
@en
P2093
Joelle N Pelletier
Nicolas Doucet
Pierre-Yves De Wals
P2860
P304
46295-46303
P356
10.1074/JBC.M407606200
P407
P577
2004-08-23T00:00:00Z