The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner.
about
Molecular chaperones: guardians of the proteome in normal and disease statesDisaggregases, molecular chaperones that resolubilize protein aggregatesSingle-molecule analyses of the dynamics of heat shock protein 104 (Hsp104) and protein aggregates.Structural and Functional Conservation of Mycobacterium tuberculosis GroEL Paralogs Suggests that GroEL1 Is a ChaperoninStructural basis for intersubunit signaling in a protein disaggregating machineThe Molecular Mechanism of Hsp100 Chaperone Inhibition by the Prion Curing Agent Guanidinium ChlorideHead-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregationYeast prions are useful for studying protein chaperones and protein quality controlEngineering enhanced protein disaggregases for neurodegenerative diseaseCooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregationAggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensisSubstrate Discrimination by ClpB and Hsp104.Heat shock protein 104 (Hsp104)-mediated curing of [PSI+] yeast prions depends on both [PSI+] conformation and the properties of the Hsp104 homologs.trans-Acting arginine residues in the AAA+ chaperone ClpB allosterically regulate the activity through inter- and intradomain communication.Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation.Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation.Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104).Aggregate reactivation mediated by the Hsp100 chaperonesBiology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Functional analysis of conserved cis- and trans-elements in the Hsp104 protein disaggregating machineProkaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactionsDnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine.Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling.Structural variants of yeast prions show conformer-specific requirements for chaperone activity.Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate.Functional relevance of J-protein family of rice (Oryza sativa)Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor.Adenosine diphosphate restricts the protein remodeling activity of the Hsp104 chaperone to Hsp70 assisted disaggregationConserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation.The elusive middle domain of Hsp104 and ClpB: location and function.Structural mechanisms of chaperone mediated protein disaggregation.ClpB/Hsp100 proteins and heat stress tolerance in plants.Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.Structural basis for the disaggregase activity and regulation of Hsp104.Ordered assembly of heat shock proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probesOverlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation.Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.ClpB dynamics is driven by its ATPase cycle and regulated by the DnaK system and substrate proteins.Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation.2.4 Å resolution crystal structure of human TRAP1NM, the Hsp90 paralog in the mitochondrial matrix.
P2860
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P2860
The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The M-domain controls Hsp104 p ...... Hsp70/Hsp40-dependent manner.
@ast
The M-domain controls Hsp104 p ...... Hsp70/Hsp40-dependent manner.
@en
The M-domain controls Hsp104 p ...... Hsp70/Hsp40-dependent manner.
@nl
type
label
The M-domain controls Hsp104 p ...... Hsp70/Hsp40-dependent manner.
@ast
The M-domain controls Hsp104 p ...... Hsp70/Hsp40-dependent manner.
@en
The M-domain controls Hsp104 p ...... Hsp70/Hsp40-dependent manner.
@nl
prefLabel
The M-domain controls Hsp104 p ...... Hsp70/Hsp40-dependent manner.
@ast
The M-domain controls Hsp104 p ...... Hsp70/Hsp40-dependent manner.
@en
The M-domain controls Hsp104 p ...... Hsp70/Hsp40-dependent manner.
@nl
P2860
P1476
The M-domain controls Hsp104 p ...... Hsp70/Hsp40-dependent manner.
@en
P2093
Bernhard Sielaff
Francis T F Tsai
P2860
P356
10.1016/J.JMB.2010.07.030
P407
P577
2010-07-21T00:00:00Z