Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan
about
Repetitive Ser-Gly sequences enhance heparan sulfate assembly in proteoglycansInsight into the biology of macrophage migration inhibitory factor (MIF) revealed by the cloning of its cell surface receptorThe PA-TM-RING protein RING finger protein 13 is an endosomal integral membrane E3 ubiquitin ligase whose RING finger domain is released to the cytoplasm by proteolysisIdentification of the glycosaminoglycan-attachment site of mouse invariant-chain proteoglycan core protein by site-directed mutagenesisThe invariant chain forms complexes with class II major histocompatibility complex molecules and antigenic peptides "in vivo".Structure and function of aggrecan.Defective intracellular transport as a common mechanism limiting expression of inappropriately paired class II major histocompatibility complex alpha/beta chains.Efficient endosomal localization of major histocompatibility complex class II-invariant chain complexes requires multimerization of the invariant chain targeting sequence.Efficient cell surface expression of class II MHC molecules in the absence of associated invariant chain.The human invariant chain is the core protein of the human class II-associated proteoglycan.Uncoupling of chondroitin sulfate glycosaminoglycan synthesis by brefeldin A.Gene expression of the chondroitin sulfate proteoglycan core protein PG19.Relationship between elevated soluble CD74 and severity of experimental and clinical ALI/ARDSTrafficking and proteolytic processing of RNF13, a model PA-TM-RING family endosomal membrane ubiquitin ligase.CD74: an emerging opportunity as a therapeutic target in cancer and autoimmune disease.Invariant Chain Complexes and Clusters as Platforms for MIF Signaling.Role of protein glycosylation in immune regulation.Proteoglycans in macrophages: characterization and possible role in the cellular uptake of lipoproteins.The chondroitin sulfate form of invariant chain trimerizes with conventional invariant chain and these complexes are rapidly transported from the trans-Golgi network to the cell surface.Matrix metalloproteinase-9 in a unique proteoglycan form in avian embryonic growth plate cartilage.Proteoglycan synthesis in human erythroleukaemia (HEL) cellsExpression and enhanced secretion of proteochondroitin sulphate in a metastatic variant of a mouse lymphoma cell line.
P2860
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P2860
Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan
description
1985 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1985 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1985
@ast
im Dezember 1985 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1985/12/01)
@sk
vědecký článek publikovaný v roce 1985
@cs
wetenschappelijk artikel (gepubliceerd op 1985/12/01)
@nl
наукова стаття, опублікована в грудні 1985
@uk
مقالة علمية (نشرت في ديسمبر 1985)
@ar
name
Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan
@ast
Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan
@en
Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan
@nl
type
label
Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan
@ast
Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan
@en
Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan
@nl
prefLabel
Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan
@ast
Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan
@en
Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan
@nl
P2093
P2860
P356
P1476
Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan
@en
P2093
A. J. Sant
B. D. Schwartz
K. S. Giacoletto
S. E. Cullen
P2860
P304
P356
10.1084/JEM.162.6.1916
P407
P577
1985-12-01T00:00:00Z