about
Structure-guided recombination creates an artificial family of cytochromes P450.Evolution favors protein mutational robustness in sufficiently large populationsIn the light of directed evolution: pathways of adaptive protein evolutionAn integrated view of protein evolutionProtein stability promotes evolvabilityOn the conservative nature of intragenic recombinationThermodynamic prediction of protein neutralityImplications of genetic heterogeneity in cancerExploring protein fitness landscapes by directed evolutionSimple evolutionary pathways to complex proteinsA reverse genetic screen in Drosophila using a deletion-inducing mutagenSeqDoC: rapid SNP and mutation detection by direct comparison of DNA sequence chromatogramsUtility of Synechocystis sp. PCC 6803 glutaredoxin A as a platform to study high-resolution mutagenesis of proteinsProbing the role of highly conserved residues in triosephosphate isomerase--analysis of site specific mutants at positions 64 and 75 in the Plasmodial enzymeE Pluribus Unum: 50 Years of Research, Millions of Viruses, and One Goal--Tailored Acceleration of AAV EvolutionThermodynamics of neutral protein evolutionDirected evolution: tailoring biocatalysts for industrial applicationsHow much of protein sequence space has been explored by life on Earth?Prevalence of epistasis in the evolution of influenza A surface proteinsSelection on Network Dynamics Drives Differential Rates of Protein Domain EvolutionA decade and a half of protein intrinsic disorder: biology still waits for physicsLethal mutagenesis of bacteriaNovel protein folds and their nonsequential structural analogsPrediction of mutational tolerance in HIV-1 protease and reverse transcriptase using flexible backbone protein designMutagenesis-based definitions and probes of residue burial in proteins.High-throughput profiling of influenza A virus hemagglutinin gene at single-nucleotide resolutionCharacterization of all possible single-nucleotide change caused amino acid substitutions in the kinase domain of Bruton tyrosine kinase.Translationally optimal codons associate with structurally sensitive sites in proteinsIn planta mutagenesis determines the functional regions of the wheat puroindoline proteinsEffects of point mutations on protein structure are nonexponentially distributed.GSAFold: a new application of GSA to protein structure prediction.Software for the analysis and visualization of deep mutational scanning data.Fold designability, distribution, and diseaseHighly tolerated amino acid substitutions increase the fidelity of Escherichia coli DNA polymerase I.Neutral evolution of protein-protein interactions: a computational study using simple models.How protein stability and new functions trade offSubstrate binding pocket residues of human alkyladenine-DNA glycosylase critical for methylating agent survivalCreating context for the use of DNA adduct data in cancer risk assessment: I. Data organization.Revisiting the myths of protein interior: studying proteins with mass-fractal hydrophobicity-fractal and polarizability-fractal dimensionsHuman cancers express mutator phenotypes: origin, consequences and targeting.
P2860
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P2860
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Protein tolerance to random amino acid change
@ast
Protein tolerance to random amino acid change
@en
Protein tolerance to random amino acid change
@nl
type
label
Protein tolerance to random amino acid change
@ast
Protein tolerance to random amino acid change
@en
Protein tolerance to random amino acid change
@nl
prefLabel
Protein tolerance to random amino acid change
@ast
Protein tolerance to random amino acid change
@en
Protein tolerance to random amino acid change
@nl
P2860
P3181
P356
P1476
Protein tolerance to random amino acid change
@en
P2093
Lawrence A Loeb
P2860
P304
P3181
P356
10.1073/PNAS.0403255101
P407
P577
2004-06-14T00:00:00Z