Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution
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Three decades of beta-lactamase inhibitorsCrystal structure of the carbapenemase OXA-24 reveals insights into the mechanism of carbapenem hydrolysisTriplet nucleotide removal at random positions in a target gene: the tolerance of TEM-1 beta-lactamase to an amino acid deletion.The crystal structure of a penicilloyl-serine transferase of intermediate penicillin sensitivity. The DD-transpeptidase of streptomyces K15Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-A resolutionEstB from Burkholderia gladioli: A novel esterase with a β-lactamase fold reveals steric factors to discriminate between esterolytic and β-lactam cleaving activityThe structural bases of antibiotic resistance in the clinically derived mutant beta-lactamases TEM-30, TEM-32, and TEM-34Acyl-intermediate structures of the extended-spectrum class A beta-lactamase, Toho-1, in complex with cefotaxime, cephalothin, and benzylpenicillinGenetic and Structural Insights into the Dissemination Potential of the Extremely Broad-Spectrum Class A -Lactamase KPC-2 Identified in an Escherichia coli Strain and an Enterobacter cloacae Strain Isolated from the Same Patient in FranceCrystal Structures of Penicillin-Binding Protein 6 from Escherichia coliStructural and Biochemical Evidence That a TEM-1 -Lactamase N170G Active Site Mutant Acts via Substrate-assisted CatalysisAn Antibiotic-Resistance Enzyme from a Deep-Sea BacteriumEngineering an allosteric binding site for aminoglycosides into TEM1-β-LactamaseStructure of the extended-spectrum β-lactamase TEM-72 inhibited by citrateCan Inhibitor-Resistant Substitutions in the Mycobacterium tuberculosis -Lactamase BlaC Lead to Clavulanate Resistance?: a Biochemical Rationale for the Use of -Lactam- -Lactamase Inhibitor CombinationsCrystal Structure of Carbapenemase OXA-58 from Acinetobacter baumanniiX-ray analysis of the NMC-A beta-lactamase at 1.64-A resolution, a class A carbapenemase with broad substrate specificityA Review of SHV Extended-Spectrum β-Lactamases: Neglected Yet UbiquitousA triple mutant in the Ω-loop of TEM-1 β-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysisThe catalytic mechanism of beta-lactamases: NMR titration of an active-site lysine residue of the TEM-1 enzymeNetwork models of TEM β-lactamase mutations coevolving under antibiotic selection show modular structure and anticipate evolutionary trajectoriesInvestigating protein structural plasticity by surveying the consequence of an amino acid deletion from TEM-1 beta-lactamase.Alanine-stretch scanning mutagenesis: a simple and efficient method to probe protein structure and function.Time-lapse imaging of a dynamic phosphorylation-dependent protein-protein interaction in mammalian cellsDesign of generic biosensors based on green fluorescent proteins with allosteric sites by directed evolution.Susceptibility of beta-lactamase to core amino acid substitutions.Novel ceftazidime-resistance beta-lactamases generated by a codon-based mutagenesis method and selection.Library analysis of SCHEMA-guided protein recombination.Engineering a regulatable enzyme for homogeneous immunoassays.Roles of amino acids 161 to 179 in the PSE-4 omega loop in substrate specificity and in resistance to ceftazidimeCharacterization of a PSE-4 mutant with different properties in relation to penicillanic acid sulfones: importance of residues 216 to 218 in class A beta-lactamases.Active TEM-1 beta-lactamase mutants with random peptides inserted in three contiguous surface loops.Linking the functions of unrelated proteins using a novel directed evolution domain insertion methodExpanded molecular diversity generation during directed evolution by trinucleotide exchange (TriNEx).Random dissection to select for protein split sites and its application in protein fragment complementationEnzyme Efficiency but Not Thermostability Drives Cefotaxime Resistance Evolution in TEM-1 β-Lactamase.Inhibitor-resistant TEM beta-lactamases: phenotypic, genetic and biochemical characteristics.The role of a second-shell residue in modifying substrate and inhibitor interactions in the SHV beta-lactamase: a study of ambler position Asn276.Kinship and diversification of bacterial penicillin-binding proteins and beta-lactamases.Discriminatory detection of inhibitor-resistant beta-lactamases in Escherichia coli by single-strand conformation polymorphism-PCR.
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P2860
Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution
description
1993 nî lūn-bûn
@nan
1993 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution
@ast
Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution
@en
Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution
@nl
type
label
Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution
@ast
Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution
@en
Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution
@nl
prefLabel
Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution
@ast
Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution
@en
Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution
@nl
P2093
P2860
P3181
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Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution
@en
P2093
P2860
P304
P3181
P356
10.1002/PROT.340160406
P407
P577
1993-08-01T00:00:00Z