In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved.
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3did: identification and classification of domain-based interactions of known three-dimensional structureA De Novo Protein Binding Pair By Computational Design and Directed EvolutionArchitecture of the flagellar rotorStructural insight into the low affinity between Thermotoga maritima CheA and CheB compared to their Escherichia coli/Salmonella typhimurium counterpartsThe 3.2 Å Resolution Structure of a Receptor:CheA:CheW Signaling Complex Defines Overlapping Binding Sites and Key Residue Interactions within Bacterial Chemosensory ArraysSolution Structure of a Complex of the Histidine Autokinase CheA with Its Substrate CheYStructure of FliM provides insight into assembly of the switch complex in the bacterial flagella motorA Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.CheA Kinase of bacterial chemotaxis: chemical mapping of four essential docking sites.The many faces of protein-protein interactions: A compendium of interface geometry.The two active sites of Thermotoga maritima CheA dimers bind ATP with dramatically different affinitiesA selection that reports on protein-protein interactions within a thermophilic bacterium.Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy.Alternative protein-protein interfaces are frequent exceptions.Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways.Identification of methylation sites in Thermotoga maritima chemotaxis receptors.Combining random gene fission and rational gene fusion to discover near-infrared fluorescent protein fragments that report on protein-protein interactions.Coevolved Mutations Reveal Distinct Architectures for Two Core Proteins in the Bacterial Flagellar MotorStructural systems biology: modelling protein interactions.Conformational Transitions that Enable Histidine Kinase Autophosphorylation and Receptor Array Integration.3DIANA: 3D Domain Interaction Analysis: A Toolbox for Quaternary Structure Modeling.Characterization of the Thermotoga maritima chemotaxis methylation system that lacks pentapeptide-dependent methyltransferase CheR:MCP tethering.Comparative genomic and protein sequence analyses of a complex system controlling bacterial chemotaxisOn the binding affinity of macromolecular interactions: daring to ask why proteins interact.Conformational dynamics as a key factor of signaling mediated by the receiver domain of sensor histidine kinase from Arabidopsis thaliana.3did Update: domain-domain and peptide-mediated interactions of known 3D structure.Building interacting partner predictors using co-varying residue pairs between histidine kinase and response regulator pairs of 48 bacterial two-component systems.Comparative structural bioinformatics analysis of Bacillus amyloliquefaciens chemotaxis proteins within Bacillus subtilis group
P2860
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P2860
In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 02 August 2004
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
In different organisms, the mo ...... is not necessarily conserved.
@en
In different organisms, the mo ...... is not necessarily conserved.
@nl
type
label
In different organisms, the mo ...... is not necessarily conserved.
@en
In different organisms, the mo ...... is not necessarily conserved.
@nl
prefLabel
In different organisms, the mo ...... is not necessarily conserved.
@en
In different organisms, the mo ...... is not necessarily conserved.
@nl
P2093
P2860
P356
P1476
In different organisms, the mo ...... is not necessarily conserved.
@en
P2093
Alexandrine M Bilwes
Brian R Crane
Bryan D Beel
Melvin I Simon
Sang-Youn Park
P2860
P304
11646-11651
P356
10.1073/PNAS.0401038101
P407
P577
2004-08-02T00:00:00Z