Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.
about
Large-scale identification of protein-protein interaction of Escherichia coli K-12Hsp70 chaperones: cellular functions and molecular mechanismA new heat shock gene, AgsA, which encodes a small chaperone involved in suppressing protein aggregation in Salmonella enterica serovar typhimuriumCharacterization of the Staphylococcus aureus heat shock, cold shock, stringent, and SOS responses and their effects on log-phase mRNA turnoverUnscrambling an egg: protein disaggregation by AAA+ proteinsSequence 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 bodiesCharacterization of the aggregates formed during recombinant protein expression in bacteriaMolecular 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 disaggregationInvestigating the spreading and toxicity of prion-like proteins using the metazoan model organism C. elegansSingle-molecule analyses of the dynamics of heat shock protein 104 (Hsp104) and protein aggregates.Structural basis for intersubunit signaling in a protein disaggregating machineHead-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregationAnalysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding.A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase.Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides.Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregationCatalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulinHow high G+C Gram-positive bacteria and in particular bifidobacteria cope with heat stress: protein players and regulatorsAllostery in the Hsp70 chaperone proteinsCooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants.DnaK/DnaJ chaperone system reactivates endogenous E. coli thermostable FBP aldolase in vivo and in vitro; the effect is enhanced by GroE heat shock proteinsOrientation 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 thermophilusThe alternative sigma factor SigH regulates major components of oxidative and heat stress responses in Mycobacterium tuberculosisAggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensisSpecific 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 ArabidopsisUnfolding and translocation pathway of substrate protein controlled by structure in repetitive allosteric cycles of the ClpY ATPase.Pathways of allosteric regulation in Hsp70 chaperones.YSK2 Type Dehydrin (SbDhn1) from Sorghum bicolor Showed Improved Protection under High Temperature and Osmotic Stress Condition.The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli.Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coliA genome-scale proteomic screen identifies a role for DnaK in chaperoning of polar autotransporters in Shigella.The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion.Synergistic cooperation between two ClpB isoforms in aggregate reactivation.Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region.Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.
P2860
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P2860
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Sequential mechanism of solubi ...... ates by a bichaperone network.
@ast
Sequential mechanism of solubi ...... ates by a bichaperone network.
@en
Sequential mechanism of solubi ...... ates by a bichaperone network.
@nl
type
label
Sequential mechanism of solubi ...... ates by a bichaperone network.
@ast
Sequential mechanism of solubi ...... ates by a bichaperone network.
@en
Sequential mechanism of solubi ...... ates by a bichaperone network.
@nl
prefLabel
Sequential mechanism of solubi ...... ates by a bichaperone network.
@ast
Sequential mechanism of solubi ...... ates by a bichaperone network.
@en
Sequential mechanism of solubi ...... ates by a bichaperone network.
@nl
P2093
P2860
P356
P1476
Sequential mechanism of solubi ...... ates by a bichaperone network.
@en
P2093
P2860
P304
13732-13737
P356
10.1073/PNAS.96.24.13732
P407
P577
1999-11-01T00:00:00Z