The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control.
about
Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell deathPER1 is required for GPI-phospholipase A2 activity and involved in lipid remodeling of GPI-anchored proteinsActivation of hepatitis B virus S promoter by a cell type-restricted IRE1-dependent pathway induced by endoplasmic reticulum stressDistinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein responseCharacterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ.Inhibition of p97-dependent protein degradation by Eeyarestatin IGene expression profiling in the human pathogenic dermatophyte Trichophyton rubrum during growth on proteinsOne step at a time: endoplasmic reticulum-associated degradationIRE1-independent gain control of the unfolded protein responseThe stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiaeFlavivirus Infection Activates the XBP1 Pathway of the Unfolded Protein Response To Cope with Endoplasmic Reticulum StressEndoplasmic Reticulum-associated Degradation of Pca1p, a Polytopic Protein, via Interaction with the Proteasome at the MembraneZinc and the Msc2 zinc transporter protein are required for endoplasmic reticulum function.Genome-wide analysis identifies MYND-domain protein Mub1 as an essential factor for Rpn4 ubiquitylation.ERAD and protein import defects in a sec61 mutant lacking ER-lumenal loop 7.The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation.Pbn1p: an essential endoplasmic reticulum membrane protein required for protein processing in the endoplasmic reticulum of budding yeast.SCS3 and YFT2 link transcription of phospholipid biosynthetic genes to ER stress and the UPR.Futile protein folding cycles in the ER are terminated by the unfolded protein O-mannosylation pathway.Hos2p/Set3p deacetylase complex signals secretory stress through the Mpk1p cell integrity pathwayADD66, a gene involved in the endoplasmic reticulum-associated degradation of alpha-1-antitrypsin-Z in yeast, facilitates proteasome activity and assembly.Suppression of Rft1 expression does not impair the transbilayer movement of Man5GlcNAc2-P-P-dolichol in sealed microsomes from yeast.Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins.The membrane stress response buffers lethal effects of lipid disequilibrium by reprogramming the protein homeostasis network.Pga1 is an essential component of Glycosylphosphatidylinositol-mannosyltransferase II of Saccharomyces cerevisiae.Sel1p/Ubx2p participates in a distinct Cdc48p-dependent endoplasmic reticulum-associated degradation pathway.INSIG: a broadly conserved transmembrane chaperone for sterol-sensing domain proteinsThe unfolded protein response represses differentiation through the RPD3-SIN3 histone deacetylaseThe Saccharomyces cerevisiae YFR041C/ERJ5 gene encoding a type I membrane protein with a J domain is required to preserve the folding capacity of the endoplasmic reticulum.Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein.Genomewide analysis reveals novel pathways affecting endoplasmic reticulum homeostasis, protein modification and quality control.Distinct flippases translocate glycerophospholipids and oligosaccharide diphosphate dolichols across the endoplasmic reticulum.Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p.Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding.HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins.BcR-induced apoptosis involves differential regulation of C16 and C24-ceramide formation and sphingolipid-dependent activation of the proteasomeAAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradationGenomic analysis of the secretion stress response in the enzyme-producing cell factory Aspergillus niger.An RNA-dependent protein kinase is involved in tunicamycin-induced apoptosis and Alzheimer's disease.BiP clustering facilitates protein folding in the endoplasmic reticulum
P2860
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P2860
The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
2000年學術文章
@zh
2000年學術文章
@zh-hant
name
The unfolded protein response ...... mic reticulum quality control.
@ast
The unfolded protein response ...... mic reticulum quality control.
@en
type
label
The unfolded protein response ...... mic reticulum quality control.
@ast
The unfolded protein response ...... mic reticulum quality control.
@en
prefLabel
The unfolded protein response ...... mic reticulum quality control.
@ast
The unfolded protein response ...... mic reticulum quality control.
@en
P2093
P2860
P356
P1476
The unfolded protein response ...... mic reticulum quality control.
@en
P2093
P2860
P356
10.1083/JCB.150.1.77
P407
P577
2000-07-01T00:00:00Z