Proteasome subunits encoded by the major histocompatibility complex are not essential for antigen processing
Article Abstract:
Proteasome subunits encoded by major histocompatibility complex (MHC) are not essential for the stable surface expression of MHC class I molecules. Nor are they required for the presentation of antigenic peptides to the cell surface from influenza virus and from an endogenously synthesized intracellular protein. This is discovered by furnishing a human cell line lacking both transporter and proteasome subunit genes with genes from a rat that encode the MHC-linked transporters.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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Disulphide-isomerase-enabled shedding of tumor-associated NKG2D ligands
Article Abstract:
The soluble major histocompatibility complex class-I-related ligand MICA is associated with endoplasmic reticulum protein 5 (ERp5) on the surface of the tumour cells, which has assisted in the folding of nascent proteins inside cells. The results have revealed a molecular mechanism where the domain-specific deconstruction has regulated MICA protein shedding, promoting tumour immune evasion and identifying surface ERp5 as a strategic target for therapeutic intervention.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
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