Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
about
Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding proteinAn evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulatorsIdentification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.Human cyclophilin 40 is a heat shock protein that exhibits altered intracellular localization following heat shockMolecular markers of early Parkinson's disease based on gene expression in bloodThe Ras signaling inhibitor LOX-PP interacts with Hsp70 and c-Raf to reduce Erk activation and transformed phenotype of breast cancer cellsChaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by HipBAG-1 modulates the chaperone activity of Hsp70/Hsc70.Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptorHuman Fas-associated factor 1 interacts with heat shock protein 70 and negatively regulates chaperone activityRegulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPKInteraction of the Hsp90 cochaperone cyclophilin 40 with Hsc70Protein kinase CK2 phosphorylates Hsp105 alpha at Ser509 and modulates its functionHsp70 regulates the interaction between the peroxisome targeting signal type 1 (PTS1)-receptor Pex5p and PTS1BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP.FANCC interacts with Hsp70 to protect hematopoietic cells from IFN-gamma/TNF-alpha-mediated cytotoxicity.Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53.GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1Reversible inhibition of Hsp70 chaperone function by Scythe and ReaperThe human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refoldingSmall glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activityMolecular chaperones as HSF1-specific transcriptional repressorsCytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulumNot all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactionsHsp70 chaperones: cellular functions and molecular mechanismHsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and traffickingMutational analysis of the hsp70-interacting protein HipComplexes 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 vivoA nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activityRole of Heat-Shock Proteins in Cellular Function and in the Biology of FungiThe nucleotide exchange factors of Hsp70 molecular chaperonesMolecular chaperones and co-chaperones in Parkinson diseaseCrystal structure of the C-terminal 10-kDa subdomain of Hsc70Structure and function of Hip, an attenuator of the Hsp70 chaperone cycleChaperone ligand-discrimination by the TPR-domain protein Tah1.Saccharomyces cerevisiae Rot1p is an ER-localized membrane protein that may function with BiP/Kar2p in protein folding.Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1pProtein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.
P2860
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P2860
Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
description
1995 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1995
@ast
im November 1995 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1995/11/17)
@sk
vědecký článek publikovaný v roce 1995
@cs
wetenschappelijk artikel (gepubliceerd op 1995/11/17)
@nl
наукова стаття, опублікована в листопаді 1995
@uk
مقالة علمية (نشرت في 17-11-1995)
@ar
name
Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
@ast
Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
@en
Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
@nl
type
label
Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
@ast
Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
@en
Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
@nl
prefLabel
Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
@ast
Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
@en
Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
@nl
P3181
P1433
P1476
Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
@en
P2093
P304
P3181
P356
10.1016/0092-8674(95)90099-3
P407
P577
1995-11-17T00:00:00Z