The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin.
about
150-kDa oxygen-regulated protein (ORP150) suppresses hypoxia-induced apoptotic cell death150-kDa oxygen-regulated protein (ORP150) functions as a novel molecular chaperone in MDCK cellsA subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.Lack of glucose recycling between endoplasmic reticulum and cytoplasm underlies cellular dysfunction in glucose-6-phosphatase-beta-deficient neutrophils in a congenital neutropenia syndromeUnfolding the Role of Large Heat Shock Proteins: New Insights and Therapeutic ImplicationsBiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functionsThe role of glucosamine-induced ER stress in diabetic atherogenesisHigh molecular weight stress proteins: Identification, cloning and utilisation in cancer immunotherapyOrchestration of secretory protein folding by ER chaperonesThe Endoplasmic Reticulum Chaperone GRP170: From Immunobiology to Cancer TherapeuticsJPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifsMultiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulumThe effect of hypoxia on the expression of 150 kDa oxygen-regulated protein (ORP 150) in HeLa cellspERp1 is significantly up-regulated during plasma cell differentiation and contributes to the oxidative folding of immunoglobulinMechanisms of glucosamine-induced suppression of the hepatic assembly and secretion of apolipoprotein B-100-containing lipoproteinsRabbit cardiac and skeletal myocytes differ in constitutive and inducible expression of the glucose-regulated protein GRP94Proteomic profiles of induced hepatotoxicity at the subcellular level.The endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradationThe hsp110 and Grp1 70 stress proteins: newly recognized relatives of the Hsp70s.Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress.Superior antitumor response induced by large stress protein chaperoned protein antigen compared with peptide antigen.Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulumMitochondrial monolysocardiolipin acyltransferase is elevated in the surviving population of H9c2 cardiac myoblast cells exposed to 2-deoxyglucose-induced apoptosis.Tumour secreted grp170 chaperones full-length protein substrates and induces an adaptive anti-tumour immune response in vivoSil1, a nucleotide exchange factor for BiP, is not required for antibody assembly or secretionGene expression profiling in tibial muscular dystrophy reveals unfolded protein response and altered autophagy.Proteome mapping of epidermal growth factor induced hepatocellular carcinomas identifies novel cell metabolism targets and mitogen activated protein kinase signalling events.Impaired neutrophil activity and increased susceptibility to bacterial infection in mice lacking glucose-6-phosphatase-beta.Endoplasmic reticulum retention signal-dependent glycylation of the Hsp70/Grp170-related Pgp1p in Tetrahymena.Glucose-6-phosphatase-β, implicated in a congenital neutropenia syndrome, is essential for macrophage energy homeostasis and functionality.Versatility of the endoplasmic reticulum protein folding factory.Identification of tropoelastin as a ligand for the 65-kD FK506-binding protein, FKBP65, in the secretory pathway.Mechanisms linking diabetes mellitus to the development of atherosclerosis: a role for endoplasmic reticulum stress and glycogen synthase kinase-3.Neutrophil stress and apoptosis underlie myeloid dysfunction in glycogen storage disease type IbEndoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin.The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channelThe activities and function of molecular chaperones in the endoplasmic reticulum.Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol.Mycobacterium tuberculosis evades macrophage defenses by inhibiting plasma membrane repair.
P2860
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P2860
The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
The 170-kDa glucose-regulated ...... ein that binds immunoglobulin.
@en
The 170-kDa glucose-regulated ...... ein that binds immunoglobulin.
@nl
type
label
The 170-kDa glucose-regulated ...... ein that binds immunoglobulin.
@en
The 170-kDa glucose-regulated ...... ein that binds immunoglobulin.
@nl
prefLabel
The 170-kDa glucose-regulated ...... ein that binds immunoglobulin.
@en
The 170-kDa glucose-regulated ...... ein that binds immunoglobulin.
@nl
P2093
P2860
P356
P1476
The 170-kDa glucose-regulated ...... ein that binds immunoglobulin.
@en
P2093
P2860
P304
P356
10.1091/MBC.4.11.1109
P577
1993-11-01T00:00:00Z