Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin.
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Unfolding the Role of Large Heat Shock Proteins: New Insights and Therapeutic ImplicationsHeat Shock Proteins: A Review of the Molecular Chaperones for Plant ImmunityGRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumOrchestration of secretory protein folding by ER chaperonesEndoplasmic reticulum stress in hepatic steatosis and inflammatory bowel diseasesTargeted mutation of the mouse Grp94 gene disrupts development and perturbs endoplasmic reticulum stress signalingClients and Oncogenic Roles of Molecular Chaperone gp96/grp94Co- and Post-Translational Protein Folding in the ERMapping 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 chaperoneAbcb10 physically interacts with mitoferrin-1 (Slc25a37) to enhance its stability and function in the erythroid mitochondriaExploring the Functional Complementation between Grp94 and Hsp90Mzb1 protein regulates calcium homeostasis, antibody secretion, and integrin activation in innate-like B cellsEndoplasmic Reticulum-resident Heat Shock Protein 90 (HSP90) Isoform Glucose-regulated Protein 94 (GRP94) Regulates Cell Polarity and Cancer Cell Migration by Affecting Intracellular Transport.Heat-shock protein gp96/grp94 is an essential chaperone for the platelet glycoprotein Ib-IX-V complex.The endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?Global miRNA expression analysis identifies novel key regulators of plasma cell differentiation and malignant plasma cell.gp96, an endoplasmic reticulum master chaperone for integrins and Toll-like receptors, selectively regulates early T and B lymphopoiesis.Differential requirement of GRP94 and GRP78 in mammary gland development.Regulatory T cells and Toll-like receptors: what is the missing link?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.The endoplasmic reticulum chaperone protein GRP94 is required for maintaining hematopoietic stem cell interactions with the adult bone marrow niche.Quantitative proteomics reveals that Hsp90 inhibition preferentially targets kinases and the DNA damage response.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 anti-myeloma activity of a novel purine scaffold HSP90 inhibitor PU-H71 is via inhibition of both HSP90A and HSP90B1.Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperoneNovel application for pseudopodia proteomics using excimer laser ablation and two-dimensional difference gel electrophoresis.Antibiotics increase gut metabolism and antioxidant proteins and decrease acute phase response and necrotizing enterocolitis in preterm neonates.Increased expression of Gp96 by HBx-induced NF-κB activation feedback enhances hepatitis B virus productionEffects of glucose-regulated protein94 (Grp94) on Ig secretion from human blood mononuclear cellsSystems biology of vaccination for seasonal influenza in humans.Endoplasmic reticulum heat shock protein gp96 maintains liver homeostasis and promotes hepatocellular carcinogenesis.The BiP cochaperone ERdj4 is required for B cell development and function.High expression of endoplasmic reticulum chaperone grp94 is a novel molecular hallmark of malignant plasma cells in multiple myelomaThe molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domainHeat shock protein gp96 regulates Toll-like receptor 9 proteolytic processing and conformational stability.Chaperone gp96-independent inhibition of endotoxin response by chaperone-based peptide inhibitors.Acute Exposure to Tris(1,3-dichloro-2-propyl) Phosphate (TDCIPP) Causes Hepatic Inflammation and Leads to Hepatotoxicity in Zebrafish.Role of the unfolded protein response, GRP78 and GRP94 in organ homeostasis.Essential roles of grp94 in gut homeostasis via chaperoning canonical Wnt pathway.
P2860
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P2860
Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Endoplasmic reticulum HSP90b1 ...... nd TLR but not immunoglobulin.
@en
type
label
Endoplasmic reticulum HSP90b1 ...... nd TLR but not immunoglobulin.
@en
prefLabel
Endoplasmic reticulum HSP90b1 ...... nd TLR but not immunoglobulin.
@en
P2860
P921
P1433
P1476
Endoplasmic reticulum HSP90b1 ...... nd TLR but not immunoglobulin.
@en
P2093
P2860
P304
P356
10.1182/BLOOD-2008-03-143107
P407
P577
2008-05-28T00:00:00Z