Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins
about
Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation stepsFolding-competent and folding-defective forms of ricin A chain have different fates after retrotranslocation from the endoplasmic reticulumIdentification of new protein interactions between dengue fever virus and its hosts, human and mosquitoSuppression subtractive hybridization analysis of low-protein diet- and vitamin D-induced gene expression from rat kidney inner medullary baseThe critical role of membralin in postnatal motor neuron survival and diseaseEDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog.Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates.The function of hypoxia-inducible factor (HIF) is independent of the endoplasmic reticulum protein OS-9Identification of cellular proteins interacting with equine infectious anemia virus S2 protein.A Novel Role of OS-9 in the Maintenance of Intestinal Barrier Function from Hypoxia-induced Injury via p38-dependent Pathway.OS9 Protein Interacts with Na-K-2Cl Co-transporter (NKCC2) and Targets Its Immature Form for the Endoplasmic Reticulum-associated Degradation Pathway.Hypoxia Associated Proteolytic Processing of OS-9 by the Metalloproteinase Meprin β.Protein disulfide isomerase A6 controls the decay of IRE1α signaling via disulfide-dependent associationGRP94 in ER quality control and stress responsesSorting things out through endoplasmic reticulum quality control.Specificity and regulation of the endoplasmic reticulum-associated degradation machinery.Glycosylation-directed quality control of protein folding.The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation.ERAD of proteins containing aberrant transmembrane domains requires ubiquitylation of cytoplasmic lysine residues.A highly conserved motif at the COOH terminus dictates endoplasmic reticulum exit and cell surface expression of NKCC2.The endoplasmic reticulum-associated protein, OS-9, behaves as a lectin in targeting the immature calcium-sensing receptor.OS9:SEL1:ERAD E3 ligase:DERL2 ubiquitinates unfolded protein:(GlcNAc)2 (Man)9-5OS9:SEL1:ERAD E3 ligase:DERL2 transports Ub-unfolded protein:(GlcNAc)2 (Man)9-5 from ERQC to cytosolRedundant and Antagonistic Roles of XTP3B and OS9 in Decoding Glycan and Non-glycan Degrons in ER-Associated Degradation.
P2860
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P2860
Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins
description
2009 nî lūn-bûn
@nan
2009 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Mammalian OS-9 is upregulated ...... ion of misfolded glycoproteins
@ast
Mammalian OS-9 is upregulated ...... ion of misfolded glycoproteins
@en
Mammalian OS-9 is upregulated ...... ion of misfolded glycoproteins
@en-gb
Mammalian OS-9 is upregulated ...... ion of misfolded glycoproteins
@nl
type
label
Mammalian OS-9 is upregulated ...... ion of misfolded glycoproteins
@ast
Mammalian OS-9 is upregulated ...... ion of misfolded glycoproteins
@en
Mammalian OS-9 is upregulated ...... ion of misfolded glycoproteins
@en-gb
Mammalian OS-9 is upregulated ...... ion of misfolded glycoproteins
@nl
prefLabel
Mammalian OS-9 is upregulated ...... ion of misfolded glycoproteins
@ast
Mammalian OS-9 is upregulated ...... ion of misfolded glycoproteins
@en
Mammalian OS-9 is upregulated ...... ion of misfolded glycoproteins
@en-gb
Mammalian OS-9 is upregulated ...... ion of misfolded glycoproteins
@nl
P921
P3181
P1476
Mammalian OS-9 is upregulated ...... ion of misfolded glycoproteins
@en
P2093
Eileithyia Swanton
Felicity Alcock
P304
P3181
P356
10.1016/J.JMB.2008.11.045
P407
P577
2008-11-30T00:00:00Z