Heat-shock protein gp96/grp94 is an essential chaperone for the platelet glycoprotein Ib-IX-V complex.
about
GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumOrchestration of secretory protein folding by ER chaperonesClients and Oncogenic Roles of Molecular Chaperone gp96/grp94Mapping the Interactome of a Major Mammalian Endoplasmic Reticulum Heat Shock Protein 90Murine but not human basophil undergoes cell-specific proteolysis of a major endoplasmic reticulum chaperonePlatelets with a W127X mutation in GPIX express sufficient residual amounts of GPIbα to support adhesion to von Willebrand factor and collagen.Proteomic plasma membrane profiling reveals an essential role for gp96 in the cell surface expression of LDLR family members, including the LDL receptor and LRP6.The organizing principle of the platelet glycoprotein Ib-IX-V complex.Increased expression of Gp96 by HBx-induced NF-κB activation feedback enhances hepatitis B virus productionEndoplasmic reticulum heat shock protein gp96 maintains liver homeostasis and promotes hepatocellular carcinogenesis.GP96 interacts with HHV-6 during viral entry and directs it for cellular degradation.Blockage of conformational changes of heat shock protein gp96 on cell membrane by a α-helix peptide inhibits HER2 dimerization and signaling in breast cancerThe molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domainThe Interleukin-2-mTORc1 Kinase Axis Defines the Signaling, Differentiation, and Metabolism of T Helper 1 and Follicular B Helper T Cells.Prioritizing genetic variants for causality on the basis of preferential linkage disequilibrium.Heat shock protein 70 regulates platelet integrin activation, granule secretion and aggregation.Essential roles of grp94 in gut homeostasis via chaperoning canonical Wnt pathway.A Human Variant of Glucose-Regulated Protein 94 That Inefficiently Supports IGF Production.α7 helix region of αI domain is crucial for integrin binding to endoplasmic reticulum chaperone gp96: a potential therapeutic target for cancer metastasisThe ER membrane-anchored ubiquitin ligase Hrd1 is a positive regulator of T-cell immunity.Serum Gp96 is a chaperone of complement-C3 during graft-versus-host disease.Essential role of the molecular chaperone gp96 in regulating melanogenesis.Accessory molecules for Toll-like receptors and their function.Platelets subvert T cell immunity against cancer via GARP-TGFβ axis.Analysis of inter-subunit contacts reveals the structural malleability of extracellular domains in platelet glycoprotein Ib-IX complex.Gut homeostasis and regulatory T cell induction depend on molecular chaperone gp96 in CD11c+ cells.GP96 is a GARP chaperone and controls regulatory T cell functions.GRP94 is an Essential Regulator of Pancreatic β Cell Development, Mass and Function in Male Mice.The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
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P2860
Heat-shock protein gp96/grp94 is an essential chaperone for the platelet glycoprotein Ib-IX-V complex.
description
2011 nî lūn-bûn
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2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2011年の論文
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2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
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name
Heat-shock protein gp96/grp94 ...... glycoprotein Ib-IX-V complex.
@ast
Heat-shock protein gp96/grp94 ...... glycoprotein Ib-IX-V complex.
@en
type
label
Heat-shock protein gp96/grp94 ...... glycoprotein Ib-IX-V complex.
@ast
Heat-shock protein gp96/grp94 ...... glycoprotein Ib-IX-V complex.
@en
prefLabel
Heat-shock protein gp96/grp94 ...... glycoprotein Ib-IX-V complex.
@ast
Heat-shock protein gp96/grp94 ...... glycoprotein Ib-IX-V complex.
@en
P2093
P2860
P1433
P1476
Heat-shock protein gp96/grp94 ...... glycoprotein Ib-IX-V complex.
@en
P2093
Aleksandra Stojanovic
Matthew Staron
Robert Bona
Xiaoping Du
P2860
P304
P356
10.1182/BLOOD-2011-01-330464
P407
P577
2011-05-16T00:00:00Z