The molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domain
about
Functions of heat shock proteins in pathways of the innate and adaptive immune systemClients and Oncogenic Roles of Molecular Chaperone gp96/grp94Co- and Post-Translational Protein Folding in the ERExploring the Functional Complementation between Grp94 and Hsp90Regulation of Toll-like receptor 2 interaction with Ecgp96 controls Escherichia coli K1 invasion of brain endothelial cellsThe stress protein/chaperone Grp94 counteracts muscle disuse atrophy by stabilizing subsarcolemmal neuronal nitric oxide synthase.OS-9 facilitates turnover of nonnative GRP94 marked by hyperglycosylation.Identification of minimum carbohydrate moiety in N-glycosylation sites of brain endothelial cell glycoprotein 96 for interaction with Escherichia coli K1 outer membrane protein AExtracellular IgC2 constant domains of CEACAMs mediate PI3K sensitivity during uptake of pathogens.Endoplasmic reticulum heat shock protein gp96 maintains liver homeostasis and promotes hepatocellular carcinogenesis.Blockage of conformational changes of heat shock protein gp96 on cell membrane by a α-helix peptide inhibits HER2 dimerization and signaling in breast cancerHigh expression of endoplasmic reticulum chaperone grp94 is a novel molecular hallmark of malignant plasma cells in multiple myelomaInteraction of Toll-Like Receptors with the Molecular Chaperone Gp96 Is Essential for Its Activation of Cytotoxic T Lymphocyte Response.The role of glycoprotein 96 in the persistent inflammation of rheumatoid arthritis.Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.Essential roles of grp94 in gut homeostasis via chaperoning canonical Wnt pathway.Grp94 Protein Delivers γ-Aminobutyric Acid Type A (GABAA) Receptors to Hrd1 Protein-mediated Endoplasmic Reticulum-associated Degradation.α7 helix region of αI domain is crucial for integrin binding to endoplasmic reticulum chaperone gp96: a potential therapeutic target for cancer metastasisToll-like receptor polymorphisms, inflammatory and infectious diseases, allergies, and cancer.Development of Glucose Regulated Protein 94-Selective Inhibitors Based on the BnIm and Radamide ScaffoldElucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone.Grp94 in complexes with IgG is a soluble diagnostic marker of gastrointestinal tumors and displays immune-stimulating activity on peripheral blood immune cells.Identification of a novel protein binding motif within the T-synthase for the molecular chaperone Cosmc.Retrospective Proteomic Screening of 100 Breast Cancer Tissues.Leukocyte integrin α4β7 associates with heat shock protein 70.Molecular regulation of macrophages in unleashing cancer-related inflammation.Immune chaperone gp96 drives the contributions of macrophages to inflammatory colon tumorigenesis.Heat-Shock Protein gp96 Enhances T Cell Responses and Protective Potential to Bacillus Calmette-Guérin Vaccine.Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site.Autologous heat-shock protein vaccinesGP96 is a GARP chaperone and controls regulatory T cell functions.Surface Expression of TGFβ Docking Receptor GARP Promotes Oncogenesis and Immune Tolerance in Breast Cancer.GRP94 is an Essential Regulator of Pancreatic β Cell Development, Mass and Function in Male Mice.Resorcinol-Based Grp94-Selective Inhibitors.Second Generation Grp94-Selective Inhibitors Provide Opportunities for the Inhibition of Metastatic Cancer.Immunoregulatory functions and the therapeutic implications of GARP-TGF-β in inflammation and cancer.Gp96 deficiency affects TLR4 functionality and impairs ERK and p38 phosphorylation.TLR folding by chaperones GP96 and CNPY3The significance of heat-shock protein gp96 and its receptors' CD91 and Toll-like receptor 4 expression at the maternal foetal interface.The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
P2860
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P2860
The molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domain
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
The molecular chaperone gp96/G ...... C-terminal hydrophobic domain
@ast
The molecular chaperone gp96/G ...... C-terminal hydrophobic domain
@en
type
label
The molecular chaperone gp96/G ...... C-terminal hydrophobic domain
@ast
The molecular chaperone gp96/G ...... C-terminal hydrophobic domain
@en
prefLabel
The molecular chaperone gp96/G ...... C-terminal hydrophobic domain
@ast
The molecular chaperone gp96/G ...... C-terminal hydrophobic domain
@en
P2093
P2860
P921
P356
P1476
The molecular chaperone gp96/G ...... C-terminal hydrophobic domain
@en
P2093
P2860
P304
P356
10.1074/JBC.M111.309526
P407
P577
2012-01-05T00:00:00Z