about
Stability-mediated epistasis constrains the evolution of an influenza proteinEvolution favors protein mutational robustness in sufficiently large populationsIn the light of directed evolution: pathways of adaptive protein evolutionWeak selection and protein evolutionRobustness and evolvabilityMerging molecular mechanism and evolution: theory and computation at the interface of biophysics and evolutionary population geneticsThe interface of protein structure, protein biophysics, and molecular evolutionGenome-wide functional divergence after the symbiosis of proteobacteria with insects unraveled through a novel computational approachContingency and entrenchment in protein evolution under purifying selectionWhy does a protein's evolutionary rate vary over time?Neutrality and robustness in evo-devo: emergence of lateral inhibitionLethal mutagenesis of bacteriaImprovisation in evolution of genes and genomes: whose structure is it anyway?Dynamic New World: Refining Our View of Protein Structure, Function and EvolutionBiophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence.The Role of Evolutionary Selection in the Dynamics of Protein Structure Evolution.A computational-experimental approach identifies mutations that enhance surface expression of an oseltamivir-resistant influenza neuraminidase.Evolutionary dynamics on protein bi-stability landscapes can potentially resolve adaptive conflicts.Neutral genetic drift can alter promiscuous protein functions, potentially aiding functional evolution.A first-principles model of early evolution: emergence of gene families, species, and preferred protein folds.How protein stability and new functions trade offInferring stabilizing mutations from protein phylogenies: application to influenza hemagglutinin.Interplay between pleiotropy and secondary selection determines rise and fall of mutators in stress response.Why genes evolve faster on secondary chromosomes in bacteriaMutation bias favors protein folding stability in the evolution of small populationsPoPMuSiC 2.1: a web server for the estimation of protein stability changes upon mutation and sequence optimalityAn experimentally determined evolutionary model dramatically improves phylogenetic fit.A measure of the promiscuity of proteins and characteristics of residues in the vicinity of the catalytic site that regulate promiscuity.An experimentally informed evolutionary model improves phylogenetic fit to divergent lactamase homologsBiophysics of protein evolution and evolutionary protein biophysicsBringing molecules back into molecular evolution.Evolutionary biochemistry: revealing the historical and physical causes of protein properties.Reconstructed Ancestral Enzymes Impose a Fitness Cost upon Modern Bacteria Despite Exhibiting Favourable Biochemical Properties.Epistasis increases the rate of conditionally neutral substitution in an adapting population.Evolution on neutral networks accelerates the ticking rate of the molecular clockVariations within class-A β-lactamase physiochemical properties reflect evolutionary and environmental patterns, but not antibiotic specificityA biophysical protein folding model accounts for most mutational fitness effects in viruses.Protein folding absent selection.Biophysical fitness landscapes for transcription factor binding sitesChanging folding and binding stability in a viral coat protein: a comparison between substitutions accessible through mutation and those fixed by natural selection.
P2860
Q21128791-276F9A9A-3F56-4519-BCB3-4D7A2CEC725CQ21245352-631FA2DE-937F-479E-988B-F6F97BB609E0Q22066327-5476C7AF-DF1D-4A04-A03C-CB5E71643C16Q22305972-9E0B9C53-C6E7-40F2-BC63-29D8E0BD0D25Q24634833-92B516B9-A19C-41E9-9FF2-6DF3AA5F683AQ26861515-D6D56426-4C97-4ECA-B6B1-3842A5538852Q26863623-655FDF7D-FB1D-48FB-8C7C-AA032100FD2AQ28475165-EC1DD221-264C-4DFD-B5B2-2BD6423B05BDQ28647800-756D42F1-4AEA-4A46-9BBE-08FD501FDBF0Q28709176-87CC2419-0F7A-42F5-B699-1B0F8A000B62Q28756627-6693F81E-B9A3-4105-961E-782BBE9E4B19Q28756839-D6948630-F725-4AF9-AA5D-84A468BDB7FBQ30369479-06CBAC74-6CDF-4829-9BF9-369C66E68F09Q30399262-41279626-EC8A-4C12-B2F2-CC68665F082EQ30399998-11080277-073E-4C15-853D-0BAD13476FD3Q30401012-0A4EE815-1337-4D20-B81E-41DE7135B6CBQ30405350-9405A2D1-3342-4AC0-AAA1-821127A1A53EQ30421817-2651A1BA-2477-418A-92DD-A407FA0FC8A1Q30479736-4127FBFC-D00D-41B7-B215-3876162A8A05Q33290829-9B9FF441-3991-40A2-94FF-1F8D81273F2DQ33332450-7EC99D86-6ECA-469A-8BA4-387D5F88F78AQ33432709-555D74AA-305E-4376-A051-4CFC5CAFDCDAQ33543179-32D6939B-BBEF-4DE6-A80B-7E1FD2ECB8C5Q33549713-46932965-5424-48AC-80BE-9049C5258DF1Q33576690-6F83DDD9-FDA4-43BE-8671-DC95F4903165Q33898999-9674A983-6B7A-40A2-9397-DBEB7429A8A9Q33923545-A3D4365E-5E72-4660-A5E5-281480473EB1Q34168526-500545CD-C627-4C7F-8124-BCE5C8634B6DQ34201879-1A53989F-4C4A-4DC2-AA77-1F492870F2CAQ34311852-CC1FC7E3-8EE5-486E-9CDC-56D5C2E3616DQ34325465-0825CA41-D287-48B3-960B-455806B62236Q34358160-5ED36182-9C0D-4C0F-B659-DDED056B3A90Q34493140-A1C2BF43-9C6E-44F0-963B-70852DE5A4DCQ34760482-31997973-3D32-4408-BBEA-4E3763EE6586Q34775302-7456A8B9-DF27-4677-BB29-254A3366B932Q34845380-ED6D48B0-D2D4-4273-862D-0E8FAC8F224AQ35049281-9F4C87F1-C772-408B-BF8B-27D140A27B2FQ35141919-DBD5EFB2-9D24-41BE-A4D6-59632E267C46Q35204371-8064BCC9-E28A-42A8-B7A9-5F1D6411C0BDQ35432114-E51EF14E-15F9-4B4C-9B58-FCD1EC4C05B0
P2860
description
2007 nî lūn-bûn
@nan
2007 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Thermodynamics of neutral protein evolution
@ast
Thermodynamics of neutral protein evolution
@en
Thermodynamics of neutral protein evolution
@nl
type
label
Thermodynamics of neutral protein evolution
@ast
Thermodynamics of neutral protein evolution
@en
Thermodynamics of neutral protein evolution
@nl
prefLabel
Thermodynamics of neutral protein evolution
@ast
Thermodynamics of neutral protein evolution
@en
Thermodynamics of neutral protein evolution
@nl
P2860
P3181
P1433
P1476
Thermodynamics of neutral protein evolution
@en
P2093
Alpan Raval
P2860
P304
P3181
P356
10.1534/GENETICS.106.061754
P407
P577
2007-01-01T00:00:00Z
P5875
P698
P818
q-bio/0605041