Stability-mediated epistasis constrains the evolution of an influenza protein - Test2 - elhamkhani - TriplyDB

Stability-mediated epistasis constrains the evolution of an influenza protein

Stability-mediated epistasis constrains the evolution of an influenza protein

http://www.wikidata.org/entity/Q21128791

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Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity Urzymology: experimental access to a key transition in the appearance of enzymes Evolution of drug resistance in tuberculosis: recent progress and implications for diagnosis and therapy Improving pandemic influenza risk assessment.Coordinated Evolution of Influenza A Surface Proteins Functional Sites Induce Long-Range Evolutionary Constraints in Enzymes Both Epistasis and Diversifying Selection Drive the Structural Evolution of the Ebola Virus Glycoprotein Mucin-Like Domain Contingency and entrenchment in protein evolution under purifying selection Convergent adaptation to dangerous prey proceeds through the same first-step mutation in the garter snake Thamnophis sirtalis.Viral factors in influenza pandemic risk assessment.Prediction, dynamics, and visualization of antigenic phenotypes of seasonal influenza viruses.Conserved features of the PB2 627 domain impact influenza virus polymerase function and replication Ethical alternatives to experiments with novel potential pandemic pathogens.Historical contingency and its biophysical basis in glucocorticoid receptor evolution.Mutations to PB2 and NP proteins of an avian influenza virus combine to confer efficient growth in primary human respiratory cells.Viewing protein fitness landscapes through a next-gen lens.Composite Sequence-Structure Stability Models as Screening Tools for Identifying Vulnerable Targets for HIV Drug and Vaccine Development.Potts Hamiltonian models of protein co-variation, free energy landscapes, and evolutionary fitness.Origin of robustness in generating drug-resistant malaria parasites Fitness Inference from Short-Read Data: Within-Host Evolution of a Reassortant H5N1 Influenza Virus The Rodin-Ohno hypothesis that two enzyme superfamilies descended from one ancestral gene: an unlikely scenario for the origins of translation that will not be dismissed.Epistatically interacting substitutions are enriched during adaptive protein evolution Enzyme Efficiency but Not Thermostability Drives Cefotaxime Resistance Evolution in TEM-1 β-Lactamase.Stability-Mediated Epistasis Restricts Accessible Mutational Pathways in the Functional Evolution of Avian Hemoglobin.Inference of Epistatic Effects Leading to Entrenchment and Drug Resistance in HIV-1 Protease.Mistranslation can enhance fitness through purging of deleterious mutations.Causes of molecular convergence and parallelism in protein evolution.Identification of amino acid substitutions with compensational effects in the attachment protein of canine distemper virus.An experimentally determined evolutionary model dramatically improves phylogenetic fit.The inherent mutational tolerance and antigenic evolvability of influenza hemagglutinin.A structural perspective of compensatory evolution An experimentally informed evolutionary model improves phylogenetic fit to divergent lactamase homologs Biophysics of protein evolution and evolutionary protein biophysics Epistatic interactions between neuraminidase mutations facilitated the emergence of the oseltamivir-resistant H1N1 influenza viruses Evolutionary biochemistry: revealing the historical and physical causes of protein properties.Thermodynamic system drift in protein evolution.Evolution of oligomeric state through allosteric pathways that mimic ligand binding Filament-producing mutants of influenza A/Puerto Rico/8/1934 (H1N1) virus have higher neuraminidase activities than the spherical wild-type.Predicting evolution from the shape of genealogical trees The thermostability and specificity of ancient proteins.

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Stability-mediated epistasis constrains the evolution of an influenza protein

http://www.wikidata.org/entity/Q21128791

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2013 nî lūn-bûn

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2013 թուականին հրատարակուած գիտական յօդուած

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Stability-mediated epistasis constrains the evolution of an influenza protein

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Stability-mediated epistasis constrains the evolution of an influenza protein

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Stability-mediated epistasis constrains the evolution of an influenza protein

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Stability-mediated epistasis constrains the evolution of an influenza protein

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Stability-mediated epistasis constrains the evolution of an influenza protein

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Stability-mediated epistasis constrains the evolution of an influenza protein

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Stability-mediated epistasis constrains the evolution of an influenza protein

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Stability-mediated epistasis constrains the evolution of an influenza protein

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Stability-mediated epistasis constrains the evolution of an influenza protein

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Stability-mediated epistasis constrains the evolution of an influenza protein

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Stability-mediated epistasis constrains the evolution of an influenza protein

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Stability-mediated epistasis constrains the evolution of an influenza protein

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Stability-mediated epistasis constrains the evolution of an influenza protein

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Lizhi Ian Gong

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P2860

Historical contingency and the evolution of a key innovation in an experimental population of Escherichia coli

Bayesian phylogenetics with BEAUti and the BEAST 1.7

Protein stability promotes evolvability

The genomic and epidemiological dynamics of human influenza A virus

Crystal structure of an ancient protein: evolution by conformational epistasis

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

The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA

Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine design

An epistatic ratchet constrains the direction of glucocorticoid receptor evolution

Biochemical and Structural Evidence in Support of a Coherent Model for the Formation of the Double-Helical Influenza A Virus Ribonucleoprotein

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10.7554/ELIFE.00631

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Marc A. Suchard

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2013-01-01T00:00:00Z

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protein evolution

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3654441

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