Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.
about
Quality control of inclusion bodies in Escherichia coliThe otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ERStructural and mechanistic studies of VPS4 proteinsA virulence locus of Pseudomonas aeruginosa encodes a protein secretion apparatusSequence determinants of protein aggregation: tools to increase protein solubility.The small heat-shock proteins IbpA and IbpB reduce the stress load of recombinant Escherichia coli and delay degradation of inclusion bodiesMolecular chaperones: guardians of the proteome in normal and disease statesMetazoan Hsp70-based protein disaggregases: emergence and mechanismsDisaggregases, molecular chaperones that resolubilize protein aggregatesChaperone machines for protein folding, unfolding and disaggregationThe Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits.Single-molecule analyses of the dynamics of heat shock protein 104 (Hsp104) and protein aggregates.Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli.Biochemical and Structural Studies of Yeast Vps4 OligomerizationType VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary originStructural basis for intersubunit signaling in a protein disaggregating machineStructure and function of the AAA+ protein CbbX, a red-type Rubisco activaseThe Molecular Mechanism of Hsp100 Chaperone Inhibition by the Prion Curing Agent Guanidinium ChlorideElements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motorHead-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregationSpiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocationSubstrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides.An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteasesFueling type III secretionYeast prions are useful for studying protein chaperones and protein quality controlCooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregationTorsins: not your typical AAA+ ATPasesCHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70Orientation of the amino-terminal domain of ClpB affects the disaggregation of the proteinRoles of conserved arginines in ATP-binding domains of AAA+ chaperone ClpB from Thermus thermophilusType VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actinAggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensisAdaptor protein controlled oligomerization activates the AAA+ protein ClpCSuramin inhibits Hsp104 ATPase and disaggregase activityProteotoxic stress and inducible chaperone networks in neurodegenerative disease and agingQuantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing.FoldEco: a model for proteostasis in E. coli.Role of a conserved pore residue in the formation of a prehydrolytic high substrate affinity state in the AAA+ chaperone ClpAMolecular snapshots of the Pex1/6 AAA+ complex in action.Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study.
P2860
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P2860
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.
description
2004 nî lūn-bûn
@nan
2004 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Thermotolerance requires refol ...... ough the central pore of ClpB.
@ast
Thermotolerance requires refol ...... ough the central pore of ClpB.
@en
Thermotolerance requires refol ...... ough the central pore of ClpB.
@nl
type
label
Thermotolerance requires refol ...... ough the central pore of ClpB.
@ast
Thermotolerance requires refol ...... ough the central pore of ClpB.
@en
Thermotolerance requires refol ...... ough the central pore of ClpB.
@nl
prefLabel
Thermotolerance requires refol ...... ough the central pore of ClpB.
@ast
Thermotolerance requires refol ...... ough the central pore of ClpB.
@en
Thermotolerance requires refol ...... ough the central pore of ClpB.
@nl
P2093
P50
P1433
P1476
Thermotolerance requires refol ...... ough the central pore of ClpB.
@en
P2093
Christian Schlieker
Francis T F Tsai
Hanswalter Zentgraf
Peter Tessarz
Regina Zahn
Sukyeong Lee
Zeljka Maglica
P304
P356
10.1016/J.CELL.2004.11.027
P407
P577
2004-11-01T00:00:00Z