about
Mechanisms of CFTR Folding at the Endoplasmic ReticulumInhibition 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.Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone systemBag6 complex contains a minimal tail-anchor-targeting module and a mock BAG domainCloning and functional analysis of FLJ20420: a novel transcription factor for the BAG-1 promoterShort peptides derived from the BAG-1 C-terminus inhibit the interaction between BAG-1 and HSC70 and decrease breast cancer cell growthHuman Fas-associated factor 1 interacts with heat shock protein 70 and negatively regulates chaperone activityInteraction of the Hsp90 cochaperone cyclophilin 40 with Hsc70Protein kinase CK2 phosphorylates Hsp105 alpha at Ser509 and modulates its functionMeaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactionsp53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1.The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesisHsp27 as a negative regulator of cytochrome C release.Biological activities of HAP46/BAG-1. The HAP46/BAG-1 protein: regulator of HSP70 chaperones, DNA-binding protein and stimulator of transcription.Tumor necrosis factor receptor 1 is an ATPase regulated by silencer of death domainReversible inhibition of Hsp70 chaperone function by Scythe and ReaperHsp70-RAP46 interaction in downregulation of DNA binding by glucocorticoid receptorSIAH-1 promotes apoptosis and tumor suppression through a network involving the regulation of protein folding, unfolding, and trafficking: identification of common effectors with p53 and p21(Waf1)Human BAG-1 proteins bind to the cellular stress response protein GADD34 and interfere with GADD34 functionsActivities of the cochaperones Hap46/BAG-1M and Hap50/BAG-1L and isoformsA nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activityAnopheles gambiae heat shock protein cognate 70B impedes o'nyong-nyong virus replicationBAG4/SODD protein contains a short BAG domainCrystal structure of the C-terminal 10-kDa subdomain of Hsc70SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteinsA lysine-rich region within fungal BAG domain-containing proteins mediates a novel association with ribosomes.Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.A novel protein modification pathway related to the ubiquitin system.Stable association of 70-kDa heat shock protein induces latent multisite specificity of a unisite-specific endonuclease in yeast mitochondria.Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeatsCAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-gamma and Hsp70/Hsc70Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cellsA mouse homologue of the Drosophila tumor suppressor l(2)tid gene defines a novel Ras GTPase-activating protein (RasGAP)-binding proteinThe ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasomeHuman DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70BAG1L enhances trans-activation function of the vitamin D receptorMolecular chaperone targeting and regulation by BAG family proteinsCAIR-1/BAG-3 abrogates heat shock protein-70 chaperone complex-mediated protein degradation: accumulation of poly-ubiquitinated Hsp90 client proteins
P2860
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P2860
description
1997 nî lūn-bûn
@nan
1997 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
BAG-1 modulates the chaperone activity of Hsp70/Hsc70
@nl
BAG-1 modulates the chaperone activity of Hsp70/Hsc70.
@ast
BAG-1 modulates the chaperone activity of Hsp70/Hsc70.
@en
BAG-1 modulates the chaperone activity of Hsp70/Hsc70.
@en-gb
type
label
BAG-1 modulates the chaperone activity of Hsp70/Hsc70
@nl
BAG-1 modulates the chaperone activity of Hsp70/Hsc70.
@ast
BAG-1 modulates the chaperone activity of Hsp70/Hsc70.
@en
BAG-1 modulates the chaperone activity of Hsp70/Hsc70.
@en-gb
prefLabel
BAG-1 modulates the chaperone activity of Hsp70/Hsc70
@nl
BAG-1 modulates the chaperone activity of Hsp70/Hsc70.
@ast
BAG-1 modulates the chaperone activity of Hsp70/Hsc70.
@en
BAG-1 modulates the chaperone activity of Hsp70/Hsc70.
@en-gb
P2093
P2860
P3181
P356
P1433
P1476
BAG-1 modulates the chaperone activity of Hsp70/Hsc70.
@en
P2093
B C Freeman
C Aime-Sempe
D N Bimston
R I Morimoto
S Matsuzawa
S Takayama
P2860
P304
P3181
P356
10.1093/EMBOJ/16.16.4887
P407
P577
1997-08-01T00:00:00Z