The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG
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Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrateBacterial Heat Shock Protein ActivityAllosteric Coupling between the Lid and Interdomain Linker in DnaK Revealed by Inhibitor Binding StudiesSolution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrateSubstrate-binding domain conformational dynamics mediate Hsp70 allosteryAllostery in the Hsp70 chaperone proteinsDomain architecture and activity of human Pex19p, a chaperone-like protein for intracellular trafficking of peroxisomal membrane proteinsUsing steered molecular dynamics to predict and assess Hsp70 substrate-binding domain mutants that alter prion propagationAllostery in Hsp70 chaperones is transduced by subdomain rotationsFatty acyl benzamido antibacterials based on inhibition of DnaK-catalyzed protein folding.Pathways of allosteric regulation in Hsp70 chaperones.Ionic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics.Small molecule DnaK modulators targeting the beta-domain.Accurate prediction of DnaK-peptide binding via homology modelling and experimental data.Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK)Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.Effect of hsp70 chaperone on the folding and misfolding of polypeptides modeling an elongating protein chainTangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.Dancing through Life: Molecular Dynamics Simulations and Network-Centric Modeling of Allosteric Mechanisms in Hsp70 and Hsp110 Chaperone Proteins.Mapping the conformation of a client protein through the Hsp70 functional cycle.Enhanced J-protein interaction and compromised protein stability of mtHsp70 variants lead to mitochondrial dysfunction in Parkinson's diseaseComputational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and CommunicationNanomechanics of the substrate binding domain of Hsp70 determine its allosteric ATP-induced conformational change.Experimentally biased model structure of the Hsc70/auxilin complex: substrate transfer and interdomain structural changeDynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.Conformational heterogeneity in the Hsp70 chaperone-substrate ensemble: identified from analysis of NMR-detected titration data.Heat shock protein 70 inhibitors. 1. 2,5'-thiodipyrimidine and 5-(phenylthio)pyrimidine acrylamides as irreversible binders to an allosteric site on heat shock protein 70Targeting Allosteric Control Mechanisms in Heat Shock Protein 70 (Hsp70).Molecular cloning and functional analysis of the drought tolerance gene MsHSP70 from alfalfa (Medicago sativa L.).Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles.Tracking the interplay between bound peptide and the lid domain of DnaK, using molecular dynamics.NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: implications for the allosteric mechanism.Development of fluorescence polarization assays for the molecular chaperone Hsp70 family members: Hsp72 and DnaK.The allosteric transition in DnaK probed by infrared difference spectroscopy. Concerted ATP-induced rearrangement of the substrate binding domain.A stromal heat shock protein 70 system functions in protein import into chloroplasts in the moss Physcomitrella patens.Preferential substrate binding orientation by the molecular chaperone HscA.Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU.Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states.The β6/β7 region of the Hsp70 substrate-binding domain mediates heat-shock response and prion propagation.The lid subdomain of DnaK is required for the stabilization of the substrate-binding site.
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The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG
description
2003 nî lūn-bûn
@nan
2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
The solution structure of the ...... mplex with the peptide NRLLLTG
@ast
The solution structure of the ...... mplex with the peptide NRLLLTG
@en
The solution structure of the ...... mplex with the peptide NRLLLTG
@nl
type
label
The solution structure of the ...... mplex with the peptide NRLLLTG
@ast
The solution structure of the ...... mplex with the peptide NRLLLTG
@en
The solution structure of the ...... mplex with the peptide NRLLLTG
@nl
prefLabel
The solution structure of the ...... mplex with the peptide NRLLLTG
@ast
The solution structure of the ...... mplex with the peptide NRLLLTG
@en
The solution structure of the ...... mplex with the peptide NRLLLTG
@nl
P2093
P2860
P356
P1433
P1476
The solution structure of the ...... mplex with the peptide NRLLLTG
@en
P2093
Erik R P Zuiderweg
Shawn Y Stevens
P2860
P304
P356
10.1110/PS.03269103
P577
2003-11-01T00:00:00Z