Drosophila glycoprotein 93 Is an ortholog of mammalian heat shock protein gp96 (grp94, HSP90b1, HSPC4) and retains disulfide bond-independent chaperone function for TLRs and integrins.
about
Ixodes scapularis and Ixodes ricinus tick cell lines respond to infection with tick-borne encephalitis virus: transcriptomic and proteomic analysisPotential association between TLR4 and chitinase 3-like 1 (CHI3L1/YKL-40) signaling on colonic epithelial cells in inflammatory bowel disease and colitis-associated cancerGRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumTargeted mutation of the mouse Grp94 gene disrupts development and perturbs endoplasmic reticulum stress signalingClients and Oncogenic Roles of Molecular Chaperone gp96/grp94Mapping the Interactome of a Major Mammalian Endoplasmic Reticulum Heat Shock Protein 90Identification of new protein interactions between dengue fever virus and its hosts, human and mosquitoExploring the Functional Complementation between Grp94 and Hsp90Proteomic plasma membrane profiling reveals an essential role for gp96 in the cell surface expression of LDLR family members, including the LDL receptor and LRP6.Novel application for pseudopodia proteomics using excimer laser ablation and two-dimensional difference gel electrophoresis.Changes in the proteomic profiles of mouse brain after infection with cyst-forming Toxoplasma gondii.The molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domainChaperone gp96-independent inhibition of endotoxin response by chaperone-based peptide inhibitors.Glucose-regulated protein 94 triage of mutant myocilin through endoplasmic reticulum-associated degradation subverts a more efficient autophagic clearance mechanism.Essential roles of grp94 in gut homeostasis via chaperoning canonical Wnt pathway.α7 helix region of αI domain is crucial for integrin binding to endoplasmic reticulum chaperone gp96: a potential therapeutic target for cancer metastasisGRP94 in ER quality control and stress responsesEssential role of the molecular chaperone gp96 in regulating melanogenesis.Drosophila canopy b is a cochaperone of glycoprotein 93.Immune chaperone gp96 drives the contributions of macrophages to inflammatory colon tumorigenesis.GP96 is a GARP chaperone and controls regulatory T cell functions.Gp96 deficiency affects TLR4 functionality and impairs ERK and p38 phosphorylation.The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
P2860
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P2860
Drosophila glycoprotein 93 Is an ortholog of mammalian heat shock protein gp96 (grp94, HSP90b1, HSPC4) and retains disulfide bond-independent chaperone function for TLRs and integrins.
description
2009 nî lūn-bûn
@nan
2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Drosophila glycoprotein 93 Is ...... nction for TLRs and integrins.
@ast
Drosophila glycoprotein 93 Is ...... nction for TLRs and integrins.
@en
type
label
Drosophila glycoprotein 93 Is ...... nction for TLRs and integrins.
@ast
Drosophila glycoprotein 93 Is ...... nction for TLRs and integrins.
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prefLabel
Drosophila glycoprotein 93 Is ...... nction for TLRs and integrins.
@ast
Drosophila glycoprotein 93 Is ...... nction for TLRs and integrins.
@en
P2093
P2860
P921
P356
P1476
Drosophila glycoprotein 93 Is ...... nction for TLRs and integrins.
@en
P2093
P2860
P304
P356
10.4049/JIMMUNOL.0900811
P407
P577
2009-09-28T00:00:00Z