An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones.
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Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrateEngineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityMolecular chaperones: guardians of the proteome in normal and disease statesNMR Methods to Study Dynamic AllosteryInsights into the molecular mechanism of allostery in Hsp70s.Mechanisms of amyloid formation revealed by solution NMRPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functionsPrinciples of allosteric interactions in cell signalingChaperone machines for protein folding, unfolding and disaggregationModulation of Global Low-Frequency Motions Underlies Allosteric Regulation: Demonstration in CRP/FNR Family Transcription FactorsFunctional analysis of Hsp70 inhibitorsStructural Basis for Protein Antiaggregation Activity of the Trigger Factor ChaperoneStructure and function of Hip, an attenuator of the Hsp70 chaperone cycleStructural basis for the antifolding activity of a molecular chaperoneThe human HSP70 family of chaperones: where do we stand?Structural basis for the inhibition of HSP70 and DnaK chaperones by small-molecule targeting of a C-terminal allosteric pocketSubstrate-binding domain conformational dynamics mediate Hsp70 allosteryClose and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiPIdentification of key hinge residues important for nucleotide-dependent allostery in E. coli Hsp70/DnaKLarge-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 ChaperonesBinding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitroHeterogeneous binding of the SH3 client protein to the DnaK molecular chaperone.HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.Pathways of allosteric regulation in Hsp70 chaperones.Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular MachinesKey features of an Hsp70 chaperone allosteric landscape revealed by ion-mobility native mass spectrometry and double electron-electron resonanceRole of the loop L4,5 in allosteric regulation in mtHsp70s: in vivo significance of domain communication and its implications in protein translocationModeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysisMolecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.The balanced regulation of Hsc70 by DNJ-13 and UNC-23 is required for muscle functionality.The specialized Hsp70 (HscA) interdomain linker binds to its nucleotide-binding domain and stimulates ATP hydrolysis in both cis and trans configurations.Unfolded protein response-regulated Drosophila Fic (dFic) protein reversibly AMPylates BiP chaperone during endoplasmic reticulum homeostasis.Large interdomain rearrangement triggered by suppression of micro- to millisecond dynamics in bacterial Enzyme I.Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation.Common functionally important motions of the nucleotide-binding domain of Hsp70ROS production, intracellular HSP70 levels and their relationship in human neutrophils: effects of ageDecipher the mechanisms of protein conformational changes induced by nucleotide binding through free-energy landscape analysis: ATP binding to Hsp70.ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones.Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.
P2860
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P2860
An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
An interdomain energetic tug-o ...... in Hsp70 molecular chaperones.
@en
type
label
An interdomain energetic tug-o ...... in Hsp70 molecular chaperones.
@en
prefLabel
An interdomain energetic tug-o ...... in Hsp70 molecular chaperones.
@en
P2860
P1433
P1476
An interdomain energetic tug-o ...... in Hsp70 molecular chaperones.
@en
P2093
Eugenia M Clerico
Lila M Gierasch
P2860
P304
P356
10.1016/J.CELL.2012.11.002
P407
P577
2012-12-01T00:00:00Z