Natural evolution of TEM-1 β-lactamase: experimental reconstruction and clinical relevance. - Wikidata - awgldk - TriplyDB

Natural evolution of TEM-1 β-lactamase: experimental reconstruction and clinical relevance.

Natural evolution of TEM-1 β-lactamase: experimental reconstruction and clinical relevance.

http://www.wikidata.org/entity/Q37735903

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Quantifying the adaptive potential of an antibiotic resistance enzyme The genetic code constrains yet facilitates Darwinian evolution Fitness Landscapes of Functional RNAs What can we learn from fitness landscapes?Cytokine reporter mice: the special case of IL-10 A 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 catalysis Network models of TEM β-lactamase mutations coevolving under antibiotic selection show modular structure and anticipate evolutionary trajectories Evolution-Based Functional Decomposition of Proteins A Protocol for Functional Assessment of Whole-Protein Saturation Mutagenesis Libraries Utilizing High-Throughput Sequencing.Enzyme Efficiency but Not Thermostability Drives Cefotaxime Resistance Evolution in TEM-1 β-Lactamase.A comprehensive, high-resolution map of a gene's fitness landscape Emergence and spread of antibiotic resistance: setting a parameter space.Molecular analysis of β-lactamase genes to understand their differential expression in strains of Yersinia enterocolitica biotype 1A Mistranslation can enhance fitness through purging of deleterious mutations.Initial mutations direct alternative pathways of protein evolution The tandem repeats enabling reversible switching between the two phases of β-lactamase substrate spectrum.Circular permutation in the Ω-loop of TEM-1 β-lactamase results in improved activity and altered substrate specificity Twelve positions in a β-lactamase that can expand its substrate spectrum with a single amino acid substitution.Deletion mutations conferring substrate spectrum extension in the class A β-lactamase.Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution Coevolutionary Landscape Inference and the Context-Dependence of Mutations in Beta-Lactamase TEM-1.Multiple global suppressors of protein stability defects facilitate the evolution of extended-spectrum TEM β-lactamases.Identification of TEM-135 β-lactamase in Neisseria gonorrhoeae strains carrying African and Toronto plasmids in Argentina Mutational studies on resurrected ancestral proteins reveal conservation of site-specific amino acid preferences throughout evolutionary history.Role of pleiotropy during adaptation of TEM-1 β-lactamase to two novel antibiotics.Combinatorial active-site variants confer sustained clavulanate resistance in BlaC β-lactamase from Mycobacterium tuberculosis.How structural and physicochemical determinants shape sequence constraints in a functional enzyme Bottlenecks in the transferability of antibiotic resistance from natural ecosystems to human bacterial pathogens.Novel Computational Protocols for Functionally Classifying and Characterising Serine Beta-Lactamases.Comparative analysis of antimicrobial resistance in enterotoxigenic Escherichia coli isolates from two paediatric cohort studies in Lima, Peru.Mistranslation drives the evolution of robustness in TEM-1 β-lactamase.In silico target fishing and pharmacological profiling for the isoquinoline alkaloids of Macleaya cordata (Bo Luo Hui)Antibiotics as selectors and accelerators of diversity in the mechanisms of resistance: from the resistome to genetic plasticity in the β-lactamases world SHV-129: A Gateway to Global Suppressors in the SHV β-Lactamase Family?Capturing the mutational landscape of the beta-lactamase TEM-1.High adaptability of the omega loop underlies the substrate-spectrum-extension evolution of a class A β-lactamase, PenL.Identification of positive selection in genes is greatly improved by using experimentally informed site-specific models.The evolutionary landscape of antifolate resistance in Plasmodium falciparum.The antibiotic resistome: challenge and opportunity for therapeutic intervention.The intrinsic resistome of bacterial pathogens.

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P2860

Natural evolution of TEM-1 β-lactamase: experimental reconstruction and clinical relevance.

http://www.wikidata.org/entity/Q37735903

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2010年学术文章

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2010年学术文章

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2010年學術文章

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2010年學術文章

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Natural evolution of TEM-1 β-l ...... uction and clinical relevance.

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Natural evolution of TEM-1 β-l ...... uction and clinical relevance.

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type

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Natural evolution of TEM-1 β-l ...... uction and clinical relevance.

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Natural evolution of TEM-1 β-l ...... uction and clinical relevance.

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FEMS Microbiology Reviews

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Natural evolution of TEM-1 β-l ...... uction and clinical relevance.

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J Arjan G M De Visser

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Merijn L M Salverda

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Miriam Barlow

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P2860

Thermodynamic prediction of protein neutrality

RAISE: a simple and novel method of generating random insertion and deletion mutations

X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1 beta-lactamase: direct observation of electrostatic modulation in resistance to inactivation by clavulanic acid

Predicting the emergence of antibiotic resistance by directed evolution and structural analysis

An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation

The structural bases of antibiotic resistance in the clinically derived mutant beta-lactamases TEM-30, TEM-32, and TEM-34

Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs

Increased folding stability of TEM-1 beta-lactamase by in vitro selection

Genetic and Structural Characterization of an L201P Global Suppressor Substitution in TEM-1 β-Lactamase

Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases

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1015-1036

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10.1111/J.1574-6976.2010.00222.X

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6

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34

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