Chaperone-assisted protein folding in the cell cytoplasm.
about
The diverse members of the mammalian HSP70 machine show distinct chaperone-like activitiesBleach activates a redox-regulated chaperone by oxidative protein unfoldingExtracellular Release and Signaling by Heat Shock Protein 27: Role in Modifying Vascular InflammationA new native EcHsp31 structure suggests a key role of structural flexibility for chaperone functionHeat shock proteins (HSPs) in the homeostasis of regulatory T cells (Tregs)Selective contribution of eukaryotic prefoldin subunits to actin and tubulin bindingMicrocompartments and protein machines in prokaryotesIdentification of a potential hydrophobic peptide binding site in the C-terminal arm of trigger factor.Ischemic preconditioning induces chaperone hsp70 expression and inhibits protein aggregation in the CA1 neurons of ratsLoss of Hsp70 in Drosophila is pleiotropic, with effects on thermotolerance, recovery from heat shock and neurodegeneration.Genotoxic stress/p53-induced DNAJB9 inhibits the pro-apoptotic function of p53.Increased persistence in Escherichia coli caused by controlled expression of toxins or other unrelated proteinsStrain engineering for improved expression of recombinant proteins in bacteriaGenome-wide identification of hsp40 genes in channel catfish and their regulated expression after bacterial infection.4-Tertiary butyl phenol exposure sensitizes human melanocytes to dendritic cell-mediated killing: relevance to vitiligo.The inner cavity of Escherichia coli DegP protein is not essential for molecular chaperone and proteolytic activity.Gap1 functions as a molecular chaperone to stabilize its interactive partner Gap3 during biogenesis of serine-rich repeat bacterial adhesinChaperone proteins and brain tumors: potential targets and possible therapeutics.Intracellular heat shock protein-70 negatively regulates TLR4 signaling in the newborn intestinal epithelium.Pharmacologic rescue of conformationally-defective proteins: implications for the treatment of human disease.Alterations in the proteome of pulmonary alveolar type II cells in the rat after hepatic ischemia-reperfusion.Transport capabilities of eleven gram-positive bacteria: comparative genomic analyses.Utility of the Trypanosoma cruzi sequence database for identification of potential vaccine candidates by in silico and in vitro screening.Hsp60 exerts a tumor suppressor function by inducing cell differentiation and inhibiting invasion in hepatocellular carcinoma.Global gene expression responses to cadmium toxicity in Escherichia coli.Transcriptome of enterohemorrhagic Escherichia coli O157 adhering to eukaryotic plasma membranes.The microbial genomics of arsenic.Alphab-crystallin-assisted reactivation of glucose-6-phosphate dehydrogenase upon refolding.Translational control analysis by translationally active RNA capture/microarray analysis (TrIP-Chip).The Pih1-Tah1 cochaperone complex inhibits Hsp90 molecular chaperone ATPase activity.clpB, a class III heat-shock gene regulated by CtsR, is involved in thermotolerance and virulence of Enterococcus faecalis.Large nucleotide-dependent movement of the N-terminal domain of the ClpX chaperone.NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: implications for the allosteric mechanism.Chaperonin GroEL/GroES Over-Expression Promotes Aminoglycoside Resistance and Reduces Drug Susceptibilities in Escherichia coli Following Exposure to Sublethal Aminoglycoside Doses.Design of affinity peptides from natural protein ligands: A study of the cardiac troponin complex.Complementation studies of the DnaK-DnaJ-GrpE chaperone machineries from Vibrio harveyi and Escherichia coli, both in vivo and in vitro.ZraP is a periplasmic molecular chaperone and a repressor of the zinc-responsive two-component regulator ZraSR.Identification and changes in the seasonal concentrations of heat shock proteins in roe deer (Capreolus capreolus) epididymides.Bacterial inactivation by plasma treated water enhanced by reactive nitrogen species
P2860
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P2860
Chaperone-assisted protein folding in the cell cytoplasm.
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Chaperone-assisted protein folding in the cell cytoplasm.
@ast
Chaperone-assisted protein folding in the cell cytoplasm.
@en
Chaperone-assisted protein folding in the cell cytoplasm.
@nl
type
label
Chaperone-assisted protein folding in the cell cytoplasm.
@ast
Chaperone-assisted protein folding in the cell cytoplasm.
@en
Chaperone-assisted protein folding in the cell cytoplasm.
@nl
prefLabel
Chaperone-assisted protein folding in the cell cytoplasm.
@ast
Chaperone-assisted protein folding in the cell cytoplasm.
@en
Chaperone-assisted protein folding in the cell cytoplasm.
@nl
P356
P1476
Chaperone-assisted protein folding in the cell cytoplasm.
@en
P2093
P304
P356
10.2174/1389203013381134
P577
2001-09-01T00:00:00Z