GRP94, an ER chaperone with protein and peptide binding properties.
about
Hsp90: a specialized but essential protein-folding toolHeat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha.Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophagesIslet amyloid in type 2 diabetes, and the toxic oligomer hypothesisTargeted mutation of the mouse Grp94 gene disrupts development and perturbs endoplasmic reticulum stress signalingCo- and Post-Translational Protein Folding in the ERModulation of α(2C) adrenergic receptor temperature-sensitive trafficking by HSP90Identification of cisplatin-binding proteins using agarose conjugates of platinum compoundsLocalization of RNAs to the mitochondrial cloud in Xenopus oocytes through entrapment and association with endoplasmic reticulum.SHEPHERD is the Arabidopsis GRP94 responsible for the formation of functional CLAVATA proteinsThe stress protein/chaperone Grp94 counteracts muscle disuse atrophy by stabilizing subsarcolemmal neuronal nitric oxide synthase.The endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?Correlation between clinicopathology and expression of heat shock protein 72 and glycoprotein 96 in human esophageal squamous cell carcinomaLeishmania LPG3 encodes a GRP94 homolog required for phosphoglycan synthesis implicated in parasite virulence but not viabilityThe carboxy-terminal domain of Grp94 binds to protein kinase CK2 alpha but not to CK2 holoenzyme.Expression and significance of heat shock protein 70 and glucose-regulated protein 94 in human esophageal carcinomaHSP90 as a new therapeutic target for cancer therapy: the story unfolds.Correlation between clinicopathology and expression of heat shock protein 70 and glucose-regulated protein 94 in human colonic adenocarcinoma.Protective effects of transforming growth factor β2 in intestinal epithelial cells by regulation of proteins associated with stress and endotoxin responses.Pre-M phase-promoting factor associates with annulate lamellae in Xenopus oocytes and egg extracts.Macrocyclic inhibitors of hsp90Is all of the endoplasmic reticulum created equal? The effects of the heterogeneous distribution of endoplasmic reticulum Ca2+-handling proteins.Chaperone proteins and brain tumors: potential targets and possible therapeutics.Expression of Human DNAJ (Heat Shock Protein-40) B3 in Humanized UDP-glucuronosyltransferase 1 MiceXRab40 and XCullin5 form a ubiquitin ligase complex essential for the noncanonical Wnt pathwayThe Prognostic Impact of Heat Shock Proteins Expression in Patients with Esophageal Cancer: A Meta-Analysis.Versatility of the endoplasmic reticulum protein folding factory.Endoplasmic reticulum stress and the making of a professional secretory cell.Heat-shock protein 90 inhibitors in cancer therapy: 17AAG and beyond.Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.Listeria monocytogenes triggers the cell surface expression of Gp96 protein and interacts with its N terminus to support cellular infectionEndoplasmic reticulum (ER) stress response and its physiological roles in plants.Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin.Effect of starvation on transcriptomes of brain and liver in adult female zebrafish (Danio rerio).Rab5 modulates aggregation and toxicity of mutant huntingtin through macroautophagy in cell and fly models of Huntington disease.The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivationProtein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol.Discovery and development of heat shock protein 90 inhibitors.GRP94 in ER quality control and stress responsesNovel molecular events in oral carcinogenesis via integrative approaches.
P2860
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P2860
GRP94, an ER chaperone with protein and peptide binding properties.
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին 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
GRP94, an ER chaperone with protein and peptide binding properties.
@ast
GRP94, an ER chaperone with protein and peptide binding properties.
@en
type
label
GRP94, an ER chaperone with protein and peptide binding properties.
@ast
GRP94, an ER chaperone with protein and peptide binding properties.
@en
prefLabel
GRP94, an ER chaperone with protein and peptide binding properties.
@ast
GRP94, an ER chaperone with protein and peptide binding properties.
@en
P356
P1476
GRP94, an ER chaperone with protein and peptide binding properties.
@en
P2093
P304
P356
10.1006/SCDB.1999.0320
P577
1999-10-01T00:00:00Z