Mimicking natural evolution in metallo-beta-lactamases through second-shell ligand mutations.
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The molecular basis of glyphosate resistance by an optimized microbial acetyltransferaseAdaptive protein evolution grants organismal fitness by improving catalysis and flexibilityBiocatalytic and structural properties of a highly engineered halohydrin dehalogenasePlastid localization of the key carotenoid enzyme phytoene synthase is altered by isozyme, allelic variation, and activity.Fisher's geometric model of adaptation meets the functional synthesis: data on pairwise epistasis for fitness yields insights into the shape and size of phenotype spaceEvolution of broad spectrum β-lactam resistance in an engineered metallo-β-lactamase.How protein stability and new functions trade offThe role of a second-shell residue in modifying substrate and inhibitor interactions in the SHV beta-lactamase: a study of ambler position Asn276.Single-mutation fitness landscapes for an enzyme on multiple substrates reveal specificity is globally encodedActive site detection by spatial conformity and electrostatic analysis--unravelling a proteolytic function in shrimp alkaline phosphatase.NMR and bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices.A combined molecular dynamics and rapid kinetics approach to identify conserved three-dimensional communication networks in elongation factor TuEvolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro EvolutionHost-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues.How structural and physicochemical determinants shape sequence constraints in a functional enzymeInvestigation of Structural Determinants for the Substrate Specificity in the Zinc-Dependent Alcohol Dehydrogenase CPCR2 from Candida parapsilosis.Meropenem and chromacef intermediates observed in IMP-25 metallo-β-lactamase-catalyzed hydrolysis.Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.Role of Residues W228 and Y233 in the Structure and Activity of Metallo-β-Lactamase GIM-1.X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus.Biochemical characterization of metallo-beta-lactamase VIM-11 from a Pseudomonas aeruginosa clinical strain.B1-Metallo-β-Lactamases: Where Do We Stand?IND-6, a highly divergent IND-type metallo-beta-lactamase from Chryseobacterium indologenes strain 597 isolated in Burkina Faso.Insights into an evolutionary strategy leading to antibiotic resistance.Metallo-β-lactamase structure and function.A variety of roles for versatile zinc in metallo-β-lactamases.Prediction of distal residue participation in enzyme catalysis.Danger lurking in the "unknowns": structure-to-function studies of hypothetical protein Bleg1_2437 from Bacillus lehensis G1 alkaliphile revealed an evolutionary divergent B3 metallo-beta-lactamase.Exploring the conformational and reactive dynamics of biomolecules in solution using an extended version of the glycine reactive force field.Allosteric inhibition of VIM metallo-β-lactamases by a camelid nanobody.Hydrolysis of cephalexin and meropenem by New Delhi metallo-β-lactamase: the substrate protonation mechanism is drug dependent.Optimization of Conformational Dynamics in an Epistatic Evolutionary Trajectory.On the active site of mononuclear B1 metallo β-lactamases: a computational study
P2860
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P2860
Mimicking natural evolution in metallo-beta-lactamases through second-shell ligand mutations.
description
2005 nî lūn-bûn
@nan
2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Mimicking natural evolution in ...... second-shell ligand mutations.
@ast
Mimicking natural evolution in ...... second-shell ligand mutations.
@en
type
label
Mimicking natural evolution in ...... second-shell ligand mutations.
@ast
Mimicking natural evolution in ...... second-shell ligand mutations.
@en
prefLabel
Mimicking natural evolution in ...... second-shell ligand mutations.
@ast
Mimicking natural evolution in ...... second-shell ligand mutations.
@en
P2093
P2860
P356
P1476
Mimicking natural evolution in ...... second-shell ligand mutations.
@en
P2093
Alejandro J Vila
Pablo E Tomatis
Rodolfo M Rasia
P2860
P304
13761-13766
P356
10.1073/PNAS.0503495102
P407
P577
2005-09-19T00:00:00Z