A natural polymorphism in beta-lactamase is a global suppressor.
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Compensatory mutations cause excess of antagonistic epistasis in RNA secondary structure foldingThe structural bases of antibiotic resistance in the clinically derived mutant beta-lactamases TEM-30, TEM-32, and TEM-34Genetic and Structural Characterization of an L201P Global Suppressor Substitution in TEM-1 β-LactamaseStructural Bases for Stability–Function Tradeoffs in Antibiotic ResistanceRemoval of the Side Chain at the Active-Site Serine by a Glycine Substitution Increases the Stability of a Wide Range of Serine β-Lactamases by Relieving Steric StrainCrystal Structure of the Pseudomonas aeruginosa BEL-1 Extended-Spectrum β-Lactamase and its Complex with Moxalactam and ImipenemA 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 catalysisExploring the role of a conserved class A residue in the Ω-Loop of KPC-2 β-lactamase: a mechanism for ceftazidime hydrolysisNetwork models of TEM β-lactamase mutations coevolving under antibiotic selection show modular structure and anticipate evolutionary trajectoriesNatural Variants of the KPC-2 Carbapenemase have Evolved Increased Catalytic Efficiency for Ceftazidime Hydrolysis at the Cost of Enzyme StabilityDissecting protein structure and function using directed evolution.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 spaceSusceptibility of beta-lactamase to core amino acid substitutions.Identification and characterization of beta-lactamase inhibitor protein-II (BLIP-II) interactions with beta-lactamases using phage display.Enzyme Efficiency but Not Thermostability Drives Cefotaxime Resistance Evolution in TEM-1 β-Lactamase.Inhibitor-resistant TEM beta-lactamases: phenotypic, genetic and biochemical characteristics.Ceftazidime-resistant Klebsiella pneumoniae and Escherichia coli isolates producing TEM-10 and TEM-43 beta-lactamases from St. Louis, MissouriNovel TEM-type extended-spectrum beta-lactamase, TEM-134, in a Citrobacter koseri clinical isolateEvolution of TEM-type extended-spectrum beta-lactamases in clinical Enterobacteriaceae strains in Poland.Negative feedback in genetic circuits confers evolutionary resilience and capacitance.TEM-72, a new extended-spectrum beta-lactamase detected in Proteus mirabilis and Morganella morganii in Italy.Unexpected enzyme TEM-126: role of mutation Asp179GluTEM-80, a novel inhibitor-resistant beta-lactamase in a clinical isolate of Enterobacter cloacaeCharacterisation of blaTEM genes and types of β-lactamase plasmids in Neisseria gonorrhoeae - the prevalent and conserved blaTEM-135 has not recently evolved and existed in the Toronto plasmid from the origin.Deep sequencing of systematic combinatorial libraries reveals β-lactamase sequence constraints at high resolution.Engineering and characterization of a superfolder green fluorescent protein.Multiple global suppressors of protein stability defects facilitate the evolution of extended-spectrum TEM β-lactamases.A secondary drug resistance mutation of TEM-1 beta-lactamase that suppresses misfolding and aggregation.An analysis of why highly similar enzymes evolve differentlyGenetic constraints on protein evolutionMutational studies on resurrected ancestral proteins reveal conservation of site-specific amino acid preferences throughout evolutionary history.Exploring the potential impact of an expanded genetic code on protein functionA new TEM-derived extended-spectrum beta-lactamase (TEM-91) with an R164C substitution at the omega-loop confers ceftazidime resistanceQuantitative Description of a Protein Fitness Landscape Based on Molecular Features.Activity of ceftazidime/avibactam against isogenic strains of Escherichia coli containing KPC and SHV β-lactamases with single amino acid substitutions in the Ω-loop.Chemical chaperone rescue of mutant human cystathionine beta-synthaseCharacterization of the global stabilizing substitution A77V and its role in the evolution of CTX-M β-lactamases.Mistranslation drives the evolution of robustness in TEM-1 β-lactamase.E240V substitution increases catalytic efficiency toward ceftazidime in a new natural TEM-type extended-spectrum beta-lactamase, TEM-149, from Enterobacter aerogenes and Serratia marcescens clinical isolates.Antibiotics as selectors and accelerators of diversity in the mechanisms of resistance: from the resistome to genetic plasticity in the β-lactamases world
P2860
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P2860
A natural polymorphism in beta-lactamase is a global suppressor.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
A natural polymorphism in beta-lactamase is a global suppressor.
@ast
A natural polymorphism in beta-lactamase is a global suppressor.
@en
type
label
A natural polymorphism in beta-lactamase is a global suppressor.
@ast
A natural polymorphism in beta-lactamase is a global suppressor.
@en
prefLabel
A natural polymorphism in beta-lactamase is a global suppressor.
@ast
A natural polymorphism in beta-lactamase is a global suppressor.
@en
P2860
P356
P1476
A natural polymorphism in beta-lactamase is a global suppressor.
@en
P2093
P2860
P304
P356
10.1073/PNAS.94.16.8801
P407
P577
1997-08-01T00:00:00Z