Endoplasmic reticulum degradation: reverse protein flow of no return.
about
Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function predictionPerturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasomeE2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell systemThe cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome systemPreviously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation.Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria.Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure.Cue1p is an activator of Ubc7p E2 activity in vitro and in vivo.The PBN1 gene of Saccharomyces cerevisiae: an essential gene that is required for the post-translational processing of the protease B precursorHtm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding.Aggresomes: a cellular response to misfolded proteinsSec61p-independent degradation of the tail-anchored ER membrane protein Ubc6pImmunolocalization of UDP-glucose:glycoprotein glucosyltransferase indicates involvement of pre-Golgi intermediates in protein quality controlElucidation of the molecular logic by which misfolded alpha 1-antitrypsin is preferentially selected for degradation.Complex fate of paralogs.Inefficient quality control of thermosensitive proteins on the plasma membraneIdentification and characterization of endonuclein binding proteins: evidence of modulatory effects on signal transduction and chaperone activityCystic fibrosis as a disease of misprocessing of the cystic fibrosis transmembrane conductance regulator glycoproteinThe proteasome: a macromolecular assembly designed for controlled proteolysisProtective function of von Hippel-Lindau protein against impaired protein processing in renal carcinoma cellsOrganizational diversity among distinct glycoprotein endoplasmic reticulum-associated degradation programsMutant membrane protein of the budding yeast spindle pole body is targeted to the endoplasmic reticulum degradation pathway.Endoplasmic reticulum quality control of oligomeric membrane proteins: topogenic determinants involved in the degradation of the unassembled Na,K-ATPase alpha subunit and in its stabilization by beta subunit assembly.HRD gene dependence of endoplasmic reticulum-associated degradationGolgi apparatus immunolocalization of endomannosidase suggests post-endoplasmic reticulum glucose trimming: implications for quality control.New castanospermine glycoside analogues inhibit breast cancer cell proliferation and induce apoptosis without affecting normal cellsFor whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection.Golgi localization of ERManI defines spatial separation of the mammalian glycoprotein quality control system.Intracellular amyloidogenesis by human islet amyloid polypeptide induces apoptosis in COS-1 cellsThe ubiquitin-proteasome pathway: the complexity and myriad functions of proteins death.The pathway of US11-dependent degradation of MHC class I heavy chains involves a ubiquitin-conjugated intermediateThe unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control.Dissociation from BiP and retrotranslocation of unassembled immunoglobulin light chains are tightly coupled to proteasome activity.The medial-Golgi ion pump Pmr1 supplies the yeast secretory pathway with Ca2+ and Mn2+ required for glycosylation, sorting, and endoplasmic reticulum-associated protein degradation.Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: the role of N-linked glycans and the unfolded protein response.A novel quality control compartment derived from the endoplasmic reticulumDegradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair.Glucose-induced monoubiquitination of the Saccharomyces cerevisiae galactose transporter is sufficient to signal its internalization.ER-golgi traffic is a prerequisite for efficient ER degradation.
P2860
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P2860
Endoplasmic reticulum degradation: reverse protein flow of no return.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Endoplasmic reticulum degradation: reverse protein flow of no return.
@en
type
label
Endoplasmic reticulum degradation: reverse protein flow of no return.
@en
prefLabel
Endoplasmic reticulum degradation: reverse protein flow of no return.
@en
P1433
P1476
Endoplasmic reticulum degradation: reverse protein flow of no return.
@en
P2093
P304
P407
P577
1997-12-01T00:00:00Z