Correlating protein function and stability through the analysis of single amino acid substitutions.
about
Disease risk of missense mutations using structural inference from predicted functionPredicting disease-associated substitution of a single amino acid by analyzing residue interactions.Between proteins and phenotypes: annotation and interpretation of mutations.PoPMuSiC 2.1: a web server for the estimation of protein stability changes upon mutation and sequence optimalityStructural stability of human protein tyrosine phosphatase ρ catalytic domain: effect of point mutationsEffect of single amino acid substitution observed in cancer on Pim-1 kinase thermodynamic stability and structureNatural polymorphisms and unusual mutations in HIV-1 protease with potential antiretroviral resistance: a bioinformatic analysis.The Loss and Gain of Functional Amino Acid Residues Is a Common Mechanism Causing Human Inherited DiseaseNeutral and weakly nonneutral sequence variants may define individuality.Single-Nucleotide Polymorphism of PPARγ, a Protein at the Crossroads of Physiological and Pathological Processes.Protein stability: a single recorded mutation aids in predicting the effects of other mutations in the same amino acid site.The Complementarity Between Protein-Specific and General Pathogenicity Predictors for Amino Acid Substitutions.Kinetic and thermodynamic studies reveal chemokine homologues CC11 and CC24 with an almost identical tertiary structure have different folding pathways.Understanding pathogenic single-nucleotide polymorphisms in multidomain proteins--studies of isolated domains are not enough.Early Versus Late Diagnosis of Complement Factor I Deficiency: Clinical Consequences Illustrated in Two Families with Novel Homozygous CFI Mutations.Molecular damage in Fabry disease: characterization and prediction of alpha-galactosidase A pathological mutations.A double point mutation at residues Ile14 and Val15 of Bcl-2 uncovers a role for the BH4 domain in both protein stability and function.Polymorphic sites preferentially avoid co-evolving residues in MHC class I proteins.FoldX as Protein Engineering Tool: Better Than Random Based Approaches?
P2860
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P2860
Correlating protein function and stability through the analysis of single amino acid substitutions.
description
2009 nî lūn-bûn
@nan
2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Correlating protein function a ...... ngle amino acid substitutions.
@ast
Correlating protein function a ...... ngle amino acid substitutions.
@en
type
label
Correlating protein function a ...... ngle amino acid substitutions.
@ast
Correlating protein function a ...... ngle amino acid substitutions.
@en
prefLabel
Correlating protein function a ...... ngle amino acid substitutions.
@ast
Correlating protein function a ...... ngle amino acid substitutions.
@en
P2860
P1433
P1476
Correlating protein function a ...... ngle amino acid substitutions.
@en
P2860
P2888
P356
10.1186/1471-2105-10-S8-S8
P478
10 Suppl 8
P577
2009-08-27T00:00:00Z
P6179
1003431907