about
Structural model of ligand-G protein-coupled receptor (GPCR) complex based on experimental double mutant cycle data: MT7 snake toxin bound to dimeric hM1 muscarinic receptorCaught in self-interaction: evolutionary and functional mechanisms of protein homooligomerizationDisordered proteinaceous machinesPredicting protein-protein interface residues using local surface structural similarityParallel dynamics and evolution: Protein conformational fluctuations and assembly reflect evolutionary changes in sequence and structure.Comparative analyses of quaternary arrangements in homo-oligomeric proteins in superfamilies: Functional implications.Functional states of homooligomers: insights from the evolution of glycosyltransferases.Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric statesHomology inference of protein-protein interactions via conserved binding sites.Extent of structural asymmetry in homodimeric proteins: prevalence and relevanceProtein flexibility facilitates quaternary structure assembly and evolution.Coverage of protein domain families with structural protein-protein interactions: current progress and future trends.Evolutionary, physicochemical, and functional mechanisms of protein homooligomerization.Evolutionary meandering of intermolecular interactions along the drift barrier.On the role of electrostatics in protein-protein interactions.Predicted binding site information improves model ranking in protein docking using experimental and computer-generated target structures.Evolution of oligomeric state through geometric coupling of protein interfaces.Structural Perspectives on the Evolutionary Expansion of Unique Protein-Protein Binding Sites.Mechanistic Models Fit to Variable Temperature Calorimetric Data Provide Insights into Cooperativity.Asymmetric ligand binding facilitates conformational transitions in pentameric ligand-gated ion channels.Evolutionary diversification of the multimeric states of proteins.Non-redundant unique interface structures as templates for modeling protein interactionsComputational large-scale mapping of protein-protein interactions using structural complexes.SLG controls grain size and leaf angle by modulating brassinosteroid homeostasis in rice.Raf kinase inhibitor protein (RKIP) dimer formation controls its target switch from Raf1 to G protein-coupled receptor kinase (GRK) 2.Asymmetric configurations in a reengineered homodimer reveal multiple subunit communication pathways in protein allostery.Structural templates for modeling homodimers.Organizational interplay of Golgi N-glycosyltransferases involves organelle microenvironment-dependent transitions between enzyme homo- and heteromers.Protein-protein interactions between proteins of Citrus tristeza virus isolates.The role of the N-terminal tail for the oligomerization, folding and stability of human frataxinWeak conservation of structural features in the interfaces of homologous transient protein-protein complexes.Dimerization of lipocalin allergens.Plant DHDPR forms a dimer with unique secondary structure features that preclude higher-order assembly.Phylogenetic divergence of cell biological features.Cucurbit[8]uril-mediated protein homotetramerization
P2860
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P2860
description
2009 nî lūn-bûn
@nan
2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հոտեմբերին 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
Evolution of protein binding modes in homooligomers.
@ast
Evolution of protein binding modes in homooligomers.
@en
type
label
Evolution of protein binding modes in homooligomers.
@ast
Evolution of protein binding modes in homooligomers.
@en
prefLabel
Evolution of protein binding modes in homooligomers.
@ast
Evolution of protein binding modes in homooligomers.
@en
P2093
P2860
P1476
Evolution of protein binding modes in homooligomers.
@en
P2093
Anna R Panchenko
Benjamin A Shoemaker
Judith E Dayhoff
Stephen H Bryant
P2860
P304
P356
10.1016/J.JMB.2009.10.052
P577
2009-10-30T00:00:00Z