Dissecting glycoprotein quality control in the secretory pathway.
about
The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tractEndoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradationN-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycansHuman EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteinsMajor histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly statusEDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complexAlpha1-antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapyGetting in and out from calnexin/calreticulin cyclesEDEM accelerates ERAD by preventing aberrant dimer formation of misfolded alpha1-antitrypsinA novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradationEDEM1 accelerates the trimming of alpha1,2-linked mannose on the C branch of N-glycansN-linked oligosaccharides play a role in disulphide-dependent dimerization of intestinal mucin Muc2EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimmingElucidation of the molecular logic by which misfolded alpha 1-antitrypsin is preferentially selected for degradation.A Golgi-localized mannosidase (MAN1B1) plays a non-enzymatic gatekeeper role in protein biosynthetic quality control.Energetics of substrate binding and catalysis by class 1 (glycosylhydrolase family 47) alpha-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control.Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexinOrganizational diversity among distinct glycoprotein endoplasmic reticulum-associated degradation programsCharacterization of Schizosaccharomyces pombe ER alpha-mannosidase: a reevaluation of the role of the enzyme on ER-associated degradationContext-dependent effects of asparagine glycosylation on Pin WW folding kinetics and thermodynamics.HIV-1 protein Nef inhibits activity of ATP-binding cassette transporter A1 by targeting endoplasmic reticulum chaperone calnexinA missense mutation in the bovine SLC35A3 gene, encoding a UDP-N-acetylglucosamine transporter, causes complex vertebral malformation.Glycosyltransferase complexes in eukaryotes: long-known, prevalent but still unrecognized.Plasticity-related gene 3 promotes neurite shaft protrusionGlucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo.Reglucosylation by UDP-glucose:glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation.MAN1B1 deficiency: an unexpected CDG-IIRole of calnexin in the glycan-independent quality control of proteolipid protein.For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection.Cellular processing of myocilin.Golgi localization of ERManI defines spatial separation of the mammalian glycoprotein quality control system.Construction of a high-mannose-type glycan library by a renewed top-down chemo-enzymatic approach.Alpha1-antitrypsin deficiency. 4: Molecular pathophysiologyDelta F508 CFTR pool in the endoplasmic reticulum is increased by calnexin overexpression.Approaches toward High-Mannose-Type Glycan Libraries.Endoplasmic Reticulum-Associated rht-PA Processing in CHO Cells: Influence of Mild Hypothermia and Specific Growth Rates in Batch and Chemostat CulturesAAA ATPase p97/VCP: cellular functions, disease and therapeutic potential.Dislocation of a type I membrane protein requires interactions between membrane-spanning segments within the lipid bilayerVersatility of the endoplasmic reticulum protein folding factory.
P2860
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P2860
Dissecting glycoprotein quality control in the secretory pathway.
description
2001 nî lūn-bûn
@nan
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Dissecting glycoprotein quality control in the secretory pathway.
@ast
Dissecting glycoprotein quality control in the secretory pathway.
@en
Dissecting glycoprotein quality control in the secretory pathway.
@nl
type
label
Dissecting glycoprotein quality control in the secretory pathway.
@ast
Dissecting glycoprotein quality control in the secretory pathway.
@en
Dissecting glycoprotein quality control in the secretory pathway.
@nl
prefLabel
Dissecting glycoprotein quality control in the secretory pathway.
@ast
Dissecting glycoprotein quality control in the secretory pathway.
@en
Dissecting glycoprotein quality control in the secretory pathway.
@nl
P2093
P1476
Dissecting glycoprotein quality control in the secretory pathway.
@en
P2093
P304
P356
10.1016/S0968-0004(01)01942-9
P577
2001-10-01T00:00:00Z