Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats - Wikidata - wikimedia - TriplyDB

Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats

Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats

http://www.wikidata.org/entity/Q28138187

about

Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70 Small glutamine-rich tetratricopeptide repeat-containing protein (SGT) interacts with the ubiquitin-dependent endocytosis (UbE) motif of the growth hormone receptor Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activity Structural and Functional Insights into Small, Glutamine-Rich, Tetratricopeptide Repeat Protein Alpha Crystal structure of the C-terminal 10-kDa subdomain of Hsc70 Crystal Structure of Get4-Get5 Complex and Its Interactions with Sgt2, Get3, and Ydj1 Chaperone ligand-discrimination by the TPR-domain protein Tah1.SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances A brain-specific isoform of small glutamine-rich tetratricopeptide repeat-containing protein binds to Hsc70 and the cysteine string protein Attenuation of the activity of the cAMP-specific phosphodiesterase PDE4A5 by interaction with the immunophilin XAP2 Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes.EEVD motif of heat shock cognate protein 70 contributes to bacterial uptake by trophoblast giant cells Canine REIC/Dkk-3 interacts with SGTA and restores androgen receptor signalling in androgen-independent prostate cancer cell lines.Interaction of intracellular beta amyloid peptide with chaperone proteins.Stress and molecular chaperones in disease.The cochaperone SGTA (small glutamine-rich tetratricopeptide repeat-containing protein alpha) demonstrates regulatory specificity for the androgen, glucocorticoid, and progesterone receptors.Control of steroid receptor dynamics and function by genomic actions of the cochaperones p23 and Bag-1L The co-chaperone SGT of Leishmania donovani is essential for the parasite's viability.Balance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP.The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress.Genome-wide identification of hsp40 genes in channel catfish and their regulated expression after bacterial infection.Arginine methylation of HSP70 regulates retinoid acid-mediated RARβ2 gene activation Intracellular heat shock protein-70 negatively regulates TLR4 signaling in the newborn intestinal epithelium.Temperature desynchronizes sugar and organic acid metabolism in ripening grapevine fruits and remodels their transcriptome Small glutamine-rich tetratricopeptide repeat-containing protein alpha (SGTA), a candidate gene for polycystic ovary syndrome The molecular chaperone Hsp70 activates protein phosphatase 5 (PP5) by binding the tetratricopeptide repeat (TPR) domain.Nutrient-driven O-GlcNAc cycling - think globally but act locally.Neurodegenerative disorders: insights from the nematode Caenorhabditis elegans Hsp70 protein complexes as drug targets.Regulation of molecular chaperones through post-translational modifications: decrypting the chaperone code.SGTA: a new player in the molecular co-chaperone game.Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins.Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity.SGTB Promotes the Caspase-Dependent Apoptosis in Chondrocytes of Osteoarthritis.Prions, Chaperones, and Proteostasis in Yeast.Thermo and pH stable ATP-independent chaperone activity of heat-inducible Hsp70 from Pennisetum glaucum.The cellular chaperone hsc70 is specifically recruited to reovirus viral factories independently of its chaperone function.Tic40, a membrane-anchored co-chaperone homolog in the chloroplast protein translocon Tumor suppressor REIC/DKK-3 and co-chaperone SGTA: Their interaction and roles in the androgen sensitivity.

P2860

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P2860

Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats

http://www.wikidata.org/entity/Q28138187

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

Specific interaction of the 70 ...... the tetratricopeptide repeats

@ast

Specific interaction of the 70 ...... the tetratricopeptide repeats

@en

Specific interaction of the 70 ...... the tetratricopeptide repeats

@nl

type

label

Specific interaction of the 70 ...... the tetratricopeptide repeats

@ast

Specific interaction of the 70 ...... the tetratricopeptide repeats

@en

Specific interaction of the 70 ...... the tetratricopeptide repeats

@nl

prefLabel

Specific interaction of the 70 ...... the tetratricopeptide repeats

@ast

Specific interaction of the 70 ...... the tetratricopeptide repeats

@en

Specific interaction of the 70 ...... the tetratricopeptide repeats

@nl

P1433

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P2860

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P921

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P3181

P356

JBC.274.48.34425

P1433

Journal of Biological Chemistry

P1476

Specific interaction of the 70 ...... the tetratricopeptide repeats

@en

P2093

C D Hsiao

http://www.w3.org/2001/XMLSchema#string

C Wang

http://www.w3.org/2001/XMLSchema#string

F H Liu

http://www.w3.org/2001/XMLSchema#string

S J Wu

http://www.w3.org/2001/XMLSchema#string

S M Hu

http://www.w3.org/2001/XMLSchema#string

P2860

Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein

Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.

Identification and characterization of two novel tetratricopeptide repeat-containing genes

BAG-1 modulates the chaperone activity of Hsp70/Hsc70.

Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90

The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions.

Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

Structural analysis of substrate binding by the molecular chaperone DnaK

Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein

P304

34425-32

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P31

scholarly article

P3181

37062

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P356

10.1074/JBC.274.48.34425

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P407

P433

48

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P478

274

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P577

1999-11-26T00:00:00Z

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P698

10567422

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P921