Correlated mutations: a hallmark of phenotypic amino acid substitutions.
about
Towards structural systems pharmacology to study complex diseases and personalized medicineMolecular Determinants Underlying Binding Specificities of the ABL Kinase Inhibitors: Combining Alanine Scanning of Binding Hot Spots with Network Analysis of Residue Interactions and CoevolutionRich annotation of DNA sequencing variants by leveraging the Ensembl Variant Effect Predictor with plugins.Recent advances in functional region prediction by using structural and evolutionary information - Remaining problems and future extensionsThe Patterns of Coevolution in Clade B HIV Envelope's N-Glycosylation SitesBioCatNet: A Database System for the Integration of Enzyme Sequences and Biocatalytic Experiments.Identification of catalytic residues using a novel feature that integrates the microenvironment and geometrical location properties of residues.Mapping the mutual information network of enzymatic families in the protein structure to unveil functional features.Computational identification of novel amino-acid interactions in HIV Gag via correlated evolution.Knowledge discovery in variant databases using inductive logic programming.The contribution of coevolving residues to the stability of KDO8P synthase.Whole genome resequencing of black Angus and Holstein cattle for SNP and CNV discoveryFunSAV: predicting the functional effect of single amino acid variants using a two-stage random forest modelMultiscale modeling of the causal functional roles of nsSNPs in a genome-wide association study: application to hypoxia.Did α-Synuclein and Glucocerebrosidase Coevolve? Implications for Parkinson's Disease.Structure-based Markov random field model for representing evolutionary constraints on functional sites.CorNet: Assigning function to networks of co-evolving residues by automated literature mining.Recent advances in rational approaches for enzyme engineering.Robust enzyme design: bioinformatic tools for improved protein stability.The Complementarity Between Protein-Specific and General Pathogenicity Predictors for Amino Acid Substitutions.Molecular Evolutionary Constraints that Determine the Avirulence State of Clostridium botulinum C2 Toxin.Structure of FIV capsid C-terminal domain demonstrates lentiviral evasion of genetic fragility by coevolved substitutions.DIMA 3.0: Domain Interaction MapMustguseal: a Server for Multiple Structure-Guided Sequence Alignment of Protein Families.Reliable and robust detection of coevolving protein residues.Structure-function discrepancy in Clostridium botulinum C3 toxin for its rational prioritization as a subunit vaccine.
P2860
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P2860
Correlated mutations: a hallmark of phenotypic amino acid substitutions.
description
2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Correlated mutations: a hallmark of phenotypic amino acid substitutions.
@ast
Correlated mutations: a hallmark of phenotypic amino acid substitutions.
@en
type
label
Correlated mutations: a hallmark of phenotypic amino acid substitutions.
@ast
Correlated mutations: a hallmark of phenotypic amino acid substitutions.
@en
prefLabel
Correlated mutations: a hallmark of phenotypic amino acid substitutions.
@ast
Correlated mutations: a hallmark of phenotypic amino acid substitutions.
@en
P2093
P2860
P1476
Correlated mutations: a hallmark of phenotypic amino acid substitutions.
@en
P2093
Andreas Kowarsch
Angelika Fuchs
Dmitrij Frishman
Philipp Pagel
P2860
P304
P356
10.1371/JOURNAL.PCBI.1000923
P577
2010-09-16T00:00:00Z