Epistatically interacting substitutions are enriched during adaptive protein evolution
about
Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityCoordinated Evolution of Influenza A Surface ProteinsStrong Selection Significantly Increases Epistatic Interactions in the Long-Term Evolution of a ProteinEpistasis constrains mutational pathways of hemoglobin adaptation in high-altitude pikasViral factors in influenza pandemic risk assessment.Viewing protein fitness landscapes through a next-gen lens.Single-mutation fitness landscapes for an enzyme on multiple substrates reveal specificity is globally encodedScaffoldSeq: Software for characterization of directed evolution populations.The inherent mutational tolerance and antigenic evolvability of influenza hemagglutinin.Transient Darwinian selection in Salmonella enterica serovar Paratyphi A during 450 years of global spread of enteric fever.Coupling high-throughput genetics with phylogenetic information reveals an epistatic interaction on the influenza A virus M segment.The Mutational Robustness of Influenza A Virus.The effective rate of influenza reassortment is limited during human infectionPositive Selection in CD8+ T-Cell Epitopes of Influenza Virus Nucleoprotein Revealed by a Comparative Analysis of Human and Swine Viral Lineages.Experimental Evolution of Escherichia coli Harboring an Ancient Translation ProteinExtensive Positive Selection Drives the Evolution of Nonstructural Proteins in Lineage C Betacoronaviruses.The population genetics of drug resistance evolution in natural populations of viral, bacterial and eukaryotic pathogensLong-term adaptation of the influenza A virus by escaping cytotoxic T-cell recognition.K-Pax2: Bayesian identification of cluster-defining amino acid positions in large sequence datasetsSynthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Detecting Adaptation in Protein-Coding Genes Using a Bayesian Site-Heterogeneous Mutation-Selection Codon Substitution Model.Selection on non-antigenic gene segments of seasonal influenza A virus and its impact on adaptive evolution.Diminishing-returns epistasis decreases adaptability along an evolutionary trajectory.Sequence entropy of folding and the absolute rate of amino acid substitutions.Optimization of Conformational Dynamics in an Epistatic Evolutionary Trajectory.Pairwise and higher-order genetic interactions during the evolution of a tRNA
P2860
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P2860
Epistatically interacting substitutions are enriched during adaptive protein evolution
description
2014 nî lūn-bûn
@nan
2014 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Epistatically interacting substitutions are enriched during adaptive protein evolution
@ast
Epistatically interacting substitutions are enriched during adaptive protein evolution
@en
Epistatically interacting substitutions are enriched during adaptive protein evolution.
@nl
type
label
Epistatically interacting substitutions are enriched during adaptive protein evolution
@ast
Epistatically interacting substitutions are enriched during adaptive protein evolution
@en
Epistatically interacting substitutions are enriched during adaptive protein evolution.
@nl
prefLabel
Epistatically interacting substitutions are enriched during adaptive protein evolution
@ast
Epistatically interacting substitutions are enriched during adaptive protein evolution
@en
Epistatically interacting substitutions are enriched during adaptive protein evolution.
@nl
P2860
P1433
P1476
Epistatically interacting substitutions are enriched during adaptive protein evolution
@en
P2093
Lizhi Ian Gong
P2860
P304
P356
10.1371/JOURNAL.PGEN.1004328
P577
2014-05-08T00:00:00Z