DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.
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Molecular Chaperones as Targets to Circumvent the CFTR Defect in Cystic FibrosisThe human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refoldingHsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiaeComplexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cellsStable transformation of an Arabidopsis cell suspension culture with firefly luciferase providing a cellular system for analysis of chaperone activity in vivoInvestigating the spreading and toxicity of prion-like proteins using the metazoan model organism C. elegansAn essential nonredundant role for mycobacterial DnaK in native protein foldingEscherichia coli Thioredoxin-like Protein YbbN Contains an Atypical Tetratricopeptide Repeat Motif and Is a Negative Regulator of GroELSmall molecule probes to quantify the functional fraction of a specific protein in a cell with minimal folding equilibrium shiftsUbr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum.A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocationThe refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocationThe nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import.Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins.Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo.Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria.The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria.RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpEAllostery in the Hsp70 chaperone proteinsChaperoninsThe ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperoneBiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeastDnaK/DnaJ chaperone system reactivates endogenous E. coli thermostable FBP aldolase in vivo and in vitro; the effect is enhanced by GroE heat shock proteinsIts substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.Role of inducible heat shock protein 70 in radiation-induced cell deathTowards a rigorous network of protein-protein interactions of the model sulfate reducer Desulfovibrio vulgaris HildenboroughIsolation and characterization of a DnaJ-like protein in rats: the C-terminal 10-kDa domain of hsc70 is not essential for stimulating the ATP-hydrolytic activity of hsc70 by a DnaJ-like proteinUse of proteomic analysis to elucidate the role of calcium in acetone-butanol-ethanol fermentation by Clostridium beijerinckii NCIMB 8052Allostery in Hsp70 chaperones is transduced by subdomain rotationsThe HSP70 chaperone machinery: J proteins as drivers of functional specificityQuantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing.Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system.Bacterial proteostasis balances energy and chaperone utilization efficientlyGenome Sequence of Thermoactinomyces daqus H-18, a Novel Thermophilic Species Isolated from High-Temperature DaquChaperone-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.Virus-Induced Chaperone-Enriched (VICE) domains function as nuclear protein quality control centers during HSV-1 infection
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P2860
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
DnaK, DnaJ and GrpE form a cel ...... g heat-induced protein damage.
@en
type
label
DnaK, DnaJ and GrpE form a cel ...... g heat-induced protein damage.
@en
prefLabel
DnaK, DnaJ and GrpE form a cel ...... g heat-induced protein damage.
@en
P2860
P1433
P1476
DnaK, DnaJ and GrpE form a cel ...... ng heat-induced protein damage
@en
P2093
P2860
P304
P356
10.1002/J.1460-2075.1993.TB06097.X
P407
P577
1993-11-01T00:00:00Z