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• W2022284744 endingPage "4738" @default.
• W2022284744 startingPage "4734" @default.
• W2022284744 abstract "In the endoplasmic reticulum (ER), newly synthesized subunits of the T-cell antigen receptor (TCR), membrane-bound immunoglobulin (mIg), and major histocompatibility complex (MHC) class I antigens must fold correctly and assemble completely into multimeric protein complexes prior to transport to the cell surface. Although folding and assembly may occur spontaneously, the concept that molecular chaperones facilitate these events is emerging. Here, an intracellular protein of 90-kDa apparent molecular mass, denoted IP90, was shown to be an ER resident protein that associated with partial complexes of the TCR, mIg, and MHC class I proteins but was absent from fully assembled complexes. We speculate that IP90 might participate in folding and assembly processes of these and other multisubunit protein complexes during their transit through the ER." @default.
• W2022284744 created "2016-06-24" @default.
• W2022284744 creator A5000815014 @default.
• W2022284744 creator A5034686039 @default.
• W2022284744 creator A5075556689 @default.
• W2022284744 creator A5088924932 @default.
• W2022284744 date "1992-05-15" @default.
• W2022284744 modified "2023-10-13" @default.
• W2022284744 title "Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T- and B-cell antigen receptors and major histocompatibility complex antigens during their assembly." @default.
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• W2022284744 doi "https://doi.org/10.1073/pnas.89.10.4734" @default.
• W2022284744 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/49158" @default.
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• W2022284744 hasPublicationYear "1992" @default.
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