Analysis of covariation in an SH3 domain sequence alignment: applications in tertiary contact prediction and the design of compensating hydrophobic core substitutions.
about
Consensus-derived structural determinants of the ankyrin repeat motifThe ankyrin repeat as molecular architecture for protein recognitionGenome-wide hepatitis C virus amino acid covariance networks can predict response to antiviral therapy in humansStructural, Functional, and Bioinformatic Studies Demonstrate the Crucial Role of an Extended Peptide Binding Site for the SH3 Domain of Yeast Abp1pProtein sectors: evolutionary units of three-dimensional structureDistinguishing functional amino acid covariation from background linkage disequilibrium in HIV protease and reverse transcriptaseComputational protein design quantifies structural constraints on amino acid covariationIdentification of specificity determining residues in peptide recognition domains using an information theoretic approach applied to large-scale binding mapsTransactivation of Abl by the Crk II adapter protein requires a PNAY sequence in the Crk C-terminal SH3 domain.Transition states for protein folding have native topologies despite high structural variability.The identification of conserved interactions within the SH3 domain by alignment of sequences and structures.CRASP: a program for analysis of coordinated substitutions in multiple alignments of protein sequences.Recent advances in functional region prediction by using structural and evolutionary information - Remaining problems and future extensionsH2rs: deducing evolutionary and functionally important residue positions by means of an entropy and similarity based analysis of multiple sequence alignments.Covariation Is a Poor Measure of Molecular Coevolution.CoeViz: a web-based tool for coevolution analysis of protein residues.Use of mutual information arrays to predict coevolving sites in the full length HIV gp120 protein for subtypes B and C.Computational identification of novel amino-acid interactions in HIV Gag via correlated evolution.H2r: identification of evolutionary important residues by means of an entropy based analysis of multiple sequence alignments.Distinguishing HIV-1 drug resistance, accessory, and viral fitness mutations using conditional selection pressure analysis of treated versus untreated patient samples.FamClash: a method for ranking the activity of engineered enzymes.Positive and negative design in stability and thermal adaptation of natural proteinsLeveraging hierarchical population structure in discrete association studies.Coevolution in defining the functional specificity.Analysing the origin of long-range interactions in proteins using lattice models.Correlated mutations: a hallmark of phenotypic amino acid substitutions.FunSAV: predicting the functional effect of single amino acid variants using a two-stage random forest modelAn integrated system for studying residue coevolution in proteins.Improving computational protein design by using structure-derived sequence profile.Development of scoring functions for antibody sequence assessment and optimization.EpiSweep: Computationally Driven Reengineering of Therapeutic Proteins to Reduce Immunogenicity While Maintaining Function.Simulation-based fitting of protein-protein interaction potentials to SAXS experimentsMultidrug efflux pumps: the structures of prokaryotic ATP-binding cassette transporter efflux pumps and implications for our understanding of eukaryotic P-glycoproteins and homologues.Detecting coevolving positions in a molecule: why and how to account for phylogeny.Thoroughly sampling sequence space: large-scale protein design of structural ensembles.Mutation patterns and structural correlates in human immunodeficiency virus type 1 protease following different protease inhibitor treatmentsRRCRank: a fusion method using rank strategy for residue-residue contact predictionIdentification of residues in ABCG2 affecting protein trafficking and drug transport, using co-evolutionary analysis of ABCG sequences.Genome-wide networks of amino acid covariances are common among viruses.A conserved Asn in transmembrane helix 7 is an on/off switch in the activation of the thyrotropin receptor.
P2860
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P2860
Analysis of covariation in an SH3 domain sequence alignment: applications in tertiary contact prediction and the design of compensating hydrophobic core substitutions.
description
2000 nî lūn-bûn
@nan
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Analysis of covariation in an ...... ydrophobic core substitutions.
@ast
Analysis of covariation in an ...... ydrophobic core substitutions.
@en
type
label
Analysis of covariation in an ...... ydrophobic core substitutions.
@ast
Analysis of covariation in an ...... ydrophobic core substitutions.
@en
prefLabel
Analysis of covariation in an ...... ydrophobic core substitutions.
@ast
Analysis of covariation in an ...... ydrophobic core substitutions.
@en
P2093
P356
P1476
Analysis of covariation in an ...... ydrophobic core substitutions.
@en
P2093
Davidson AR
Di Nardo AA
P304
P356
10.1006/JMBI.2000.4146
P407
P577
2000-10-01T00:00:00Z