Disentangling direct from indirect co-evolution of residues in protein alignments
about
Dissecting the specificity of protein-protein interaction in bacterial two-component signaling: orphans and crosstalksProtein 3D structure computed from evolutionary sequence variationDirect-coupling analysis of residue coevolution captures native contacts across many protein familiesThree-dimensional structures of membrane proteins from genomic sequencingCauses of evolutionary rate variation among protein sitesInferring Pairwise Interactions from Biological Data Using Maximum-Entropy Probability ModelsIntegrated analysis of residue coevolution and protein structure in ABC transportersFrom residue coevolution to protein conformational ensembles and functional dynamics.Molecular replacement: tricks and treatsPrediction of contact residue pairs based on co-substitution between sites in protein structuresLarge-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 ChaperonesProtein structure prediction from sequence variationPconsFold: improved contact predictions improve protein modelsEvaluation of residue-residue contact prediction in CASP10Identification of specificity determining residues in peptide recognition domains using an information theoretic approach applied to large-scale binding mapsPredicting functionally informative mutations in Escherichia coli BamA using evolutionary covariance analysis.Network deconvolution as a general method to distinguish direct dependencies in networksProtein modeling: what happened to the "protein structure gap"?Fast and accurate multivariate Gaussian modeling of protein families: predicting residue contacts and protein-interaction partnersH2rs: deducing evolutionary and functionally important residue positions by means of an entropy and similarity based analysis of multiple sequence alignments.Predicting evolutionary site variability from structure in viral proteins: buriedness, packing, flexibility, and design.Protein contact prediction by integrating joint evolutionary coupling analysis and supervised learning.Amino acid positions subject to multiple coevolutionary constraints can be robustly identified by their eigenvector network centrality scoresCombining Evolutionary Information and an Iterative Sampling Strategy for Accurate Protein Structure Prediction.Residue proximity information and protein model discrimination using saturation-suppressor mutagenesisCritical assessment of methods of protein structure prediction: Progress and new directions in round XI.Benchmarking Inverse Statistical Approaches for Protein Structure and Design with Exactly Solvable Models.Residue contacts predicted by evolutionary covariance extend the application of ab initio molecular replacement to larger and more challenging protein folds.NeBcon: Protein contact map prediction using neural network training coupled with naïve Bayes classifiers.Correlated mutations via regularized multinomial regression.Accurate de novo structure prediction of large transmembrane protein domains using fragment-assembly and correlated mutation analysis.Deep architectures for protein contact map predictionFrom principal component to direct coupling analysis of coevolution in proteins: low-eigenvalue modes are needed for structure predictionInference of Epistatic Effects Leading to Entrenchment and Drug Resistance in HIV-1 Protease.Correlated evolution of nearby residues in Drosophilid proteinsStructural constraints on the covariance matrix derived from multiple aligned protein sequencesA three-dimensional topology of complex I inferred from evolutionary correlations.Improving contact prediction along three dimensions.Accurate simulation and detection of coevolution signals in multiple sequence alignments.Prediction of disulfide connectivity in proteins with machine-learning methods and correlated mutations.
P2860
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P2860
Disentangling direct from indirect co-evolution of residues in protein alignments
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունվարին 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
Disentangling direct from indirect co-evolution of residues in protein alignments
@ast
Disentangling direct from indirect co-evolution of residues in protein alignments
@en
Disentangling direct from indirect co-evolution of residues in protein alignments
@en-gb
Disentangling direct from indirect co-evolution of residues in protein alignments
@nl
type
label
Disentangling direct from indirect co-evolution of residues in protein alignments
@ast
Disentangling direct from indirect co-evolution of residues in protein alignments
@en
Disentangling direct from indirect co-evolution of residues in protein alignments
@en-gb
Disentangling direct from indirect co-evolution of residues in protein alignments
@nl
altLabel
Disentangling Direct from Indirect Co-Evolution of Residues in Protein Alignments
@en
prefLabel
Disentangling direct from indirect co-evolution of residues in protein alignments
@ast
Disentangling direct from indirect co-evolution of residues in protein alignments
@en
Disentangling direct from indirect co-evolution of residues in protein alignments
@en-gb
Disentangling direct from indirect co-evolution of residues in protein alignments
@nl
P2860
P3181
P1476
Disentangling direct from indirect co-evolution of residues in protein alignments
@en
P2093
Lukas Burger
P2860
P304
P3181
P356
10.1371/JOURNAL.PCBI.1000633
P407
P577
2010-01-01T00:00:00Z