Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity.
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Unfolding the Role of Large Heat Shock Proteins: New Insights and Therapeutic ImplicationsMetazoan Hsp70-based protein disaggregases: emergence and mechanismsHigh molecular weight stress proteins: Identification, cloning and utilisation in cancer immunotherapyHsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins.Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashionAn asymmetric interface between the regulatory and core particles of the proteasomeHeat shock proteins: cellular and molecular mechanisms in the central nervous system.Integrating mass spectrometry of intact protein complexes into structural proteomicsCoordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.Metazoan Hsp70 machines use Hsp110 to power protein disaggregationRole of Hsc70 binding cycle in CFTR folding and endoplasmic reticulum-associated degradation.HSP105 recruits protein phosphatase 2A to dephosphorylate β-catenin.Dancing through Life: Molecular Dynamics Simulations and Network-Centric Modeling of Allosteric Mechanisms in Hsp70 and Hsp110 Chaperone Proteins.Computational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and CommunicationCytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeastAdenosine diphosphate restricts the protein remodeling activity of the Hsp104 chaperone to Hsp70 assisted disaggregationMutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding.Pharmacological targeting of the Hsp70 chaperone.Mechanisms of the Hsp70 chaperone system.The control of spindle length by Hsp70 and Hsp110 molecular chaperones.Expression of a mutant HSP110 sensitizes colorectal cancer cells to chemotherapy and improves disease prognosis.Targeting Allosteric Control Mechanisms in Heat Shock Protein 70 (Hsp70).The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110.Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activitySubstrate binding by the yeast Hsp110 nucleotide exchange factor and molecular chaperone Sse1 is not obligate for its biological activities.Interactions between Kar2p and its nucleotide exchange factors Sil1p and Lhs1p are mechanistically distinct.Structural analysis of the ribosome-associated complex (RAC) reveals an unusual Hsp70/Hsp40 interaction.Nucleotide Exchange Factors for Hsp70 Chaperones.Nucleotide exchange factors Fes1 and HspBP1 mimic substrate to release misfolded proteins from Hsp70.High Throughput Screen for Inhibitors of Protein-Protein Interactions in a Reconstituted Heat Shock Protein 70 (Hsp70) Complex.Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces.Advantage of HSP110 (T17) marker inclusion for microsatellite instability (MSI) detection in colorectal cancer patients.
P2860
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P2860
Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Insights into the structural d ...... nucleotide exchange activity.
@en
type
label
Insights into the structural d ...... nucleotide exchange activity.
@en
prefLabel
Insights into the structural d ...... nucleotide exchange activity.
@en
P2860
P50
P356
P1476
Insights into the structural d ...... nucleotide exchange activity.
@en
P2093
Claes Andréasson
Heike Rampelt
P2860
P304
16519-16524
P356
10.1073/PNAS.0804187105
P407
P577
2008-10-23T00:00:00Z