A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta
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Copines-1, -2, -3, -6 and -7 show different calcium-dependent intracellular membrane translocation and targetingThe MRH protein Erlectin is a member of the endoplasmic reticulum synexpression group and functions in N-glycan recognitionOS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERADHuman XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiPA dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposalMeprins, membrane-bound and secreted astacin metalloproteinasesA genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins.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.DC-STAMP knock-down deregulates cytokine production and T-cell stimulatory capacity of LPS-matured dendritic cells.Activation of the epithelial sodium channel by the metalloprotease meprin β subunit.Villin and actin in the mouse kidney brush-border membrane bind to and are degraded by meprins, an interaction that contributes to injury in ischemia-reperfusionA 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.Gene expression profile identifies a rare epithelioid variant case of pleomorphic liposarcoma carrying FUS-CHOP transcript.Transport of meprin subunits through the secretory pathway: role of the transmembrane and cytoplasmic domains and oligomerization.Traffic jams II: an update of diseases of intracellular transport.The second C2-domain of copine-2, copine-6 and copine-7 is responsible for their calcium-dependent membrane association.Characterization of the Grp94/OS-9 chaperone-lectin complex.Genomic analysis of the unfolded protein response in Arabidopsis shows its connection to important cellular processes.Targeted disruption of the meprin metalloproteinase beta gene protects against renal ischemia-reperfusion injury in mice.The endoplasmic reticulum-associated protein, OS-9, behaves as a lectin in targeting the immature calcium-sensing receptor.
P2860
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P2860
A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta
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2002 nî lūn-bûn
@nan
2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
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2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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2002年の論文
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2002年論文
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2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
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2002年论文
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name
A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta
@ast
A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta
@en
A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta
@nl
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label
A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta
@ast
A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta
@en
A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta
@nl
prefLabel
A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta
@ast
A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta
@en
A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta
@nl
P2093
P2860
P3181
P356
P1476
A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta
@en
P2093
Elena Friedmann
Larisa Litovchick
Shmuel Shaltiel
P2860
P304
P3181
P356
10.1074/JBC.M203986200
P407
P577
2002-09-13T00:00:00Z