Transient aggregation of nascent thyroglobulin in the endoplasmic reticulum: relationship to the molecular chaperone, BiP.
about
Orchestration of secretory protein folding by ER chaperonesFormation and rearrangement of disulfide bonds during maturation of the Sindbis virus E1 glycoproteinBinding of BiP to the processing enzyme lymphoma proprotein convertase prevents aggregation, but slows down maturationMultiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulumERp29 deficiency affects sensitivity to apoptosis via impairment of the ATF6-CHOP pathway of stress responseA single amino acid change in the acetylcholinesterase-like domain of thyroglobulin causes congenital goiter with hypothyroidism in the cog/cog mouse: a model of human endoplasmic reticulum storage diseasesRegulated increase in folding capacity prevents unfolded protein stress in the ER.Transient covalent interactions of newly synthesized thyroglobulin with oxidoreductases of the endoplasmic reticulumBiP availability distinguishes states of homeostasis and stress in the endoplasmic reticulum of living cells.Role of extracellular molecular chaperones in the folding of oxidized proteins. Refolding of colloidal thyroglobulin by protein disulfide isomerase and immunoglobulin heavy chain-binding protein.Role of thyroglobulin endocytic pathways in the control of thyroid hormone release.Quality control of transmembrane domain assembly in the tetraspanin CD82Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase.Endoplasmic reticulum stress as a novel mechanism in amiodarone-induced destructive thyroiditisMaturation of thyroglobulin protein region I.A mouse model suggests two mechanisms for thyroid alterations in infantile cystinosis: decreased thyroglobulin synthesis due to endoplasmic reticulum stress/unfolded protein response and impaired lysosomal processing.Postoligomerization folding of human cytomegalovirus glycoprotein B: identification of folding intermediates and importance of disulfide bonding.Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum.An endoplasmic reticulum storage disease causing congenital goiter with hypothyroidism.Oxidoreductase interactions include a role for ERp72 engagement with mutant thyroglobulin from the rdw/rdw rat dwarf.Dominant protein interactions that influence the pathogenesis of conformational diseases.Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol.Defective protein folding and intracellular retention of thyroglobulin-R19K mutant as a cause of human congenital goiterCongenital hypothyroid goiter with deficient thyroglobulin. Identification of an endoplasmic reticulum storage disease with induction of molecular chaperones.Perturbations in maturation of secretory proteins and their association with endoplasmic reticulum chaperones in a cell culture model for epithelial ischemia.Endoplasmic reticulum (ER)-associated degradation of misfolded N-linked glycoproteins is suppressed upon inhibition of ER mannosidase I.Site-directed removal of N-glycosylation sites in the bovine cation-dependent mannose 6-phosphate receptor: effects on ligand binding, intracellular targetting and association with binding immunoglobulin protein.Degradation and endoplasmic reticulum retention of unassembled alpha- and beta-subunits of Na,K-ATPase correlate with interaction of BiP.Calnexin acts as a molecular chaperone during the folding of glycoprotein B of human cytomegalovirus.Introduction of an N-glycosylation site increases secretion of heterologous proteins in yeasts.The cholinesterase-like domain of thyroglobulin functions as an intramolecular chaperone.Impaired secretion of a hydrophobic cutinase by Saccharomyces cerevisiae correlates with an increased association with immunoglobulin heavy-chain binding protein (BiP).Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM).VIP21-caveolin, a membrane protein constituent of the caveolar coat, oligomerizes in vivo and in vitroImpaired thyroglobulin (Tg) secretion by FRTL-5 cells transfected with soluble receptor associated protein (RAP): evidence for a role of RAP in the Tg biosynthetic pathway.The acetylcholinesterase homology region is essential for normal conformational maturation and secretion of thyroglobulin.Maturation of lipoprotein lipase in the endoplasmic reticulum. Concurrent formation of functional dimers and inactive aggregates.Protein-disulfide isomerase (PDI) in FRTL5 cells. pH-dependent thyroglobulin/PDI interactions determine a novel PDI function in the post-endoplasmic reticulum of thyrocytes.The dynamic role of GRP78/BiP in the coordination of mRNA translation with protein processing.HLA-DR beta chains enter into an aggregated complex containing GRP-78/BiP prior to their degradation by the pre-Golgi degradative pathway.
P2860
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P2860
Transient aggregation of nascent thyroglobulin in the endoplasmic reticulum: relationship to the molecular chaperone, BiP.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Transient aggregation of nasce ...... the molecular chaperone, BiP.
@ast
Transient aggregation of nasce ...... the molecular chaperone, BiP.
@en
type
label
Transient aggregation of nasce ...... the molecular chaperone, BiP.
@ast
Transient aggregation of nasce ...... the molecular chaperone, BiP.
@en
prefLabel
Transient aggregation of nasce ...... the molecular chaperone, BiP.
@ast
Transient aggregation of nasce ...... the molecular chaperone, BiP.
@en
P2093
P2860
P356
P1476
Transient aggregation of nasce ...... the molecular chaperone, BiP.
@en
P2093
P2860
P304
P356
10.1083/JCB.118.3.541
P407
P577
1992-08-01T00:00:00Z