Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70.
about
Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradationCytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulumHSP27 is a ubiquitin-binding protein involved in I-kappaBalpha proteasomal degradationGlycosyltransferases and non-alcoholic fatty liver diseaseRecent technical developments in the study of ER-associated degradationThe degradation of apolipoprotein B100: multiple opportunities to regulate VLDL triglyceride production by different proteolytic pathwaysQuality control and fate determination of Hsp90 client proteinsThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyUbr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation.Understanding the role of heat shock protein isoforms in male fertility, aging and apoptosisOverexpression of the tumor autocrine motility factor receptor Gp78, a ubiquitin protein ligase, results in increased ubiquitinylation and decreased secretion of apolipoprotein B100 in HepG2 cellsNascent lipidated apolipoprotein B is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaperones, GRP94, ERp72, BiP, calreticulin, and cyclophilin BGolgi-associated maturation of very low density lipoproteins involves conformational changes in apolipoprotein B, but is not dependent on apolipoprotein EMicrosomal triglyceride transfer protein and its role in apoB-lipoprotein assemblyApolipoprotein B100 quality control and the regulation of hepatic very low density lipoprotein secretion.Cysteine string protein interacts with and modulates the maturation of the cystic fibrosis transmembrane conductance regulator.Uncoupling retro-translocation and degradation in the ER-associated degradation of a soluble protein.HSP90 as a new therapeutic target for cancer therapy: the story unfolds.Complexity in the secretory pathway: the assembly and secretion of apolipoprotein B-containing lipoproteins.A yeast homologue of Hsp70, Ssa1p, regulates turnover of the MFA2 transcript through its AU-rich 3' untranslated regionProtein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substratesDerlin-1 and UBXD8 are engaged in dislocation and degradation of lipidated ApoB-100 at lipid dropletsHsp90 and hepatobiliary transformation during sea lamprey metamorphosis.Intracellular trafficking and secretion of VLDL.Molecular chaperones and heat shock proteins in atherosclerosis.A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase.Analysis of the tau-associated proteome reveals that exchange of Hsp70 for Hsp90 is involved in tau degradationMonogenic hypocholesterolaemic lipid disorders and apolipoprotein B metabolism.The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulum-associated degradation).Carboxyl terminus of hsc70-interacting protein (CHIP) can remodel mature aryl hydrocarbon receptor (AhR) complexes and mediate ubiquitination of both the AhR and the 90 kDa heat-shock protein (hsp90) in vitro.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.The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD)The many intersecting pathways underlying apolipoprotein B secretion and degradationApolipoprotein B100 biogenesis: a complex array of intracellular mechanisms regulating folding, stability, and lipoprotein assembly.Insights from human congenital disorders of intestinal lipid metabolism.p97 functions as an auxiliary factor to facilitate TM domain extraction during CFTR ER-associated degradation.HSP90AB1: Helping the good and the bad.
P2860
Q24297095-C8B65810-14D9-4AF9-B971-AB99443FF7A2Q24643310-A5267649-4F08-4182-8A40-2F7DDE5F05BDQ24679412-27BB8E06-62FD-4F51-8F4A-9D3B0EDFF540Q26764913-EF391838-E2E5-46E9-8372-8DBF1934FC19Q26823514-FBD9B740-B91B-4837-9BF3-B6270202C042Q26824858-4D346CBD-CF20-4835-B92D-D78EB1A4BCDFQ26853052-4374E43F-4480-4116-9841-BB6FE4A00D10Q27015793-21015271-EA64-4FF3-A1E1-784D5BBCCB9DQ27930363-43FAF264-43FD-472E-AB32-590EE34180ECQ27934755-E51428A9-DC69-4262-8FD4-02B8B14F7D1CQ27939982-D49FB06F-C43D-40AD-9268-4BB0AD7AF891Q28080885-564D265E-6709-4E26-B71A-E7A91D1A133DQ28188104-115CA05B-C8C8-49AE-A273-4B3FECFB415CQ28210370-880BA77E-CAD8-4E6F-9352-E0E50AE35D35Q28577984-96E91E27-17F0-4C87-AD68-ED80F6A22D08Q28624200-B6CE06F3-0088-4CD3-8CC6-9FFEB7301624Q33858526-FAEE253A-594A-4035-9653-CA4B290D65D7Q34131032-EB7B4DC9-DDDF-455E-B689-4681125A1374Q34348618-BA7FA3C2-5B0C-4667-9C8A-2B0AC3387AE4Q34482045-9EB69FA8-9778-4EA2-80BA-A714FCB8D986Q34634838-736AEF75-6BDD-42CD-BE38-5EF65E3A23E4Q34889289-2E9080A6-22B5-4E22-952C-B7C72D5709D9Q35756661-DFBD2938-1D42-48C2-9B32-3739DAAE722FQ35790894-26D7EBDC-0A89-4941-ACCD-DFAA94BB6985Q35857968-1F9C6363-CE3E-4A43-8CA7-F20DA37DAD63Q35906628-DDB54443-BAD4-4DB0-B66C-5FD7117052DBQ35964911-E91A387D-E098-4A81-B104-D41760262317Q36322876-36A5D0BD-F400-4EA9-8ADF-E191C8F7DE87Q36335851-31F6F7BB-0D84-448E-9579-036D3E026188Q36359516-98649006-83BC-442E-B4BC-713968A720FCQ36830187-9E141CAF-D316-4A76-9F93-2531F376942EQ36857823-E2ADC6F9-8886-4403-9BDD-FE73F92A54A1Q36947831-8C8B899A-1DB6-41CA-94EA-DF6EA7C25AC8Q36982944-7374C60E-EA6A-47C4-8FFD-74C5B5D62086Q37153569-5437E96E-BD8E-486E-B5F0-3D69A76EADD7Q37240302-97BC2383-6C22-4509-8D36-E03E1931EEB8Q37746984-5C609D2D-4E04-4809-A19A-7DCE3BCA8D93Q38267212-ACC627FA-04E2-4711-8C50-B4C5CA391F28Q38364252-D98AFACF-F08F-46CD-B8D3-C9250875ACE7Q38584468-F7A4EE6A-D774-4305-AAD3-576D50A48B5F
P2860
Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
@zh-hant
name
Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70.
@en
Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70.
@nl
type
label
Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70.
@en
Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70.
@nl
prefLabel
Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70.
@en
Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70.
@nl
P2093
P356
P1476
Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70.
@en
P2093
P304
24891-24900
P356
10.1074/JBC.M100633200
P407
P577
2001-05-01T00:00:00Z