Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation.
about
Molecular chaperones: guardians of the proteome in normal and disease statesDisaggregases, molecular chaperones that resolubilize protein aggregatesChaperone machines for protein folding, unfolding and disaggregationSingle-molecule analyses of the dynamics of heat shock protein 104 (Hsp104) and protein aggregates.Structural 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 chaffeensisQuantifying chaperone-mediated transitions in the proteostasis network of E. coliSpecific Hsp100 Chaperones Determine the Fate of the First Enzyme of the Plastidial Isoprenoid Pathway for Either Refolding or Degradation by the Stromal Clp Protease in ArabidopsisSubstrate 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.Characterization of the molecular chaperone ClpB from the pathogenic spirochaete Leptospira interrogansMetazoan Hsp70 machines use Hsp110 to power protein disaggregationHsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.trans-Acting arginine residues in the AAA+ chaperone ClpB allosterically regulate the activity through inter- and intradomain communication.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 chaperonesFunctional 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.Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency.Structural variants of yeast prions show conformer-specific requirements for chaperone activity.Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System.Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.Functional relevance of J-protein family of rice (Oryza sativa)Schizosaccharomyces pombe disaggregation machinery chaperones support Saccharomyces cerevisiae growth and prion propagation.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.ClpB/Hsp100 proteins and heat stress tolerance in plants.Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.Prions, Chaperones, and Proteostasis in Yeast.Structural basis for the disaggregase activity and regulation of Hsp104.
P2860
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P2860
Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation.
description
2011 nî lūn-bûn
@nan
2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Species-specific collaboration ...... ce and protein disaggregation.
@ast
Species-specific collaboration ...... ce and protein disaggregation.
@en
Species-specific collaboration of heat shock proteins
@nl
type
label
Species-specific collaboration ...... ce and protein disaggregation.
@ast
Species-specific collaboration ...... ce and protein disaggregation.
@en
Species-specific collaboration of heat shock proteins
@nl
prefLabel
Species-specific collaboration ...... ce and protein disaggregation.
@ast
Species-specific collaboration ...... ce and protein disaggregation.
@en
Species-specific collaboration of heat shock proteins
@nl
P2093
P2860
P50
P356
P1476
Species-specific collaboration ...... nce and protein disaggregation
@en
P2093
Daniel C Masison
Danielle M Johnston
Joel R Hoskins
Olivier Genest
Shannon M Doyle
Sue Wickner
P2860
P304
P356
10.1073/PNAS.1102828108
P407
P577
2011-04-07T00:00:00Z