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Sequence co-evolution gives 3D contacts and structures of protein complexesSequence co-evolutionary information is a natural partner to minimally-frustrated models of biomolecular dynamicsMetabolomics and systems pharmacology: why and how to model the human metabolic network for drug discoveryFrom residue coevolution to protein conformational ensembles and functional dynamics.Connecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial EnzymeLarge-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 ChaperonesMolecular Determinants Underlying Binding Specificities of the ABL Kinase Inhibitors: Combining Alanine Scanning of Binding Hot Spots with Network Analysis of Residue Interactions and CoevolutionOrigin of a folded repeat protein from an intrinsically disordered ancestorProgress and challenges in predicting protein interfacesThe vgll3 Locus Controls Age at Maturity in Wild and Domesticated Atlantic Salmon (Salmo salar L.) MalesProtein structure determination by combining sparse NMR data with evolutionary couplingsFreeContact: fast and free software for protein contact prediction from residue co-evolutionEvaluation of residue-residue contact prediction in CASP10Critical assessment of methods of protein structure prediction (CASP)--round xConstructing sequence-dependent protein models using coevolutionary information.Exploring bacterial organelle interactomes: a model of the protein-protein interaction network in the Pdu microcompartment.Protein modeling: what happened to the "protein structure gap"?BCov: a method for predicting β-sheet topology using sparse inverse covariance estimation and integer programming.CASP10 results compared to those of previous CASP experimentsCoevolutionary signals across protein lineages help capture multiple protein conformations.Emerging Computational Methods for the Rational Discovery of Allosteric Drugs.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.Structural bioinformatics of the interactome.Accurate De Novo Prediction of Protein Contact Map by Ultra-Deep Learning ModelMetaPSICOV: combining coevolution methods for accurate prediction of contacts and long range hydrogen bonding in proteins.Improving accuracy of protein contact prediction using balanced network deconvolution.Algorithmic approaches to protein-protein interaction site prediction.Protein contact prediction by integrating joint evolutionary coupling analysis and supervised learning.CoeViz: a web-based tool for coevolution analysis of protein residues.HotSpot Wizard 2.0: automated design of site-specific mutations and smart libraries in protein engineering.Benchmarking Inverse Statistical Approaches for Protein Structure and Design with Exactly Solvable Models.Simultaneous identification of specifically interacting paralogs and interprotein contacts by direct coupling analysis.A large-scale comparative assessment of methods for residue-residue contact prediction.Potts Hamiltonian models of protein co-variation, free energy landscapes, and evolutionary fitness.A unified statistical model of protein multiple sequence alignment integrating direct coupling and insertions.Correlated Mutation in the Evolution of Catalysis in Uracil DNA Glycosylase SuperfamilyApplications of contact predictions to structural biologyFrom principal component to direct coupling analysis of coevolution in proteins: low-eigenvalue modes are needed for structure predictionCoevolution of axon guidance molecule Slit and its receptor Robo.
P2860
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P2860
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Emerging methods in protein co-evolution.
@en
type
label
Emerging methods in protein co-evolution.
@en
prefLabel
Emerging methods in protein co-evolution.
@en
P356
P1476
Emerging methods in protein co-evolution.
@en
P2093
David de Juan
Florencio Pazos
P2888
P304
P356
10.1038/NRG3414
P577
2013-03-05T00:00:00Z
P5875
P6179
1037155505