Proteolysis, proteasomes and antigen presentation
- 1 June 1992
- journal article
- review article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 357 (6377), 375-379
- https://doi.org/10.1038/357375a0
Abstract
Proteins presented to the immune system must first be cleaved to small peptides by intracellular proteinases. Proteasomes are proteolytic complexes that degrade cytosolic and nuclear proteins. These particles have been implicated in ATP-ubiquitin-dependent proteolysis and in the processing of intracellular antigens for cytolytic immune responses.Keywords
This publication has 63 references indexed in Scilit:
- Electron microscopy of 26 S complex containing 20 S proteasomeFEBS Letters, 1991
- Cloning and sequencing of the gene encoding the large (α‐) subunit of the proteasome from Thermoplasma acidophilumFEBS Letters, 1991
- Isolation of an endogenously processed immunodominant viral peptide from the class I H–2Kb moleculeNature, 1990
- Proteinase yscE of yeast shows homology with the 20 S cylinder particles of Xenopus laevisFEBS Letters, 1988
- Molecular organization of a high molecular weight multi-protease complex from rat liverJournal of Molecular Biology, 1988
- Introduction of soluble protein into the class I pathway of antigen processing and presentationCell, 1988
- Size and shape of the multicatalytic proteinase from rat skeletal muscleBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- The LMP antigens: A stable MHC-controlled multisubunit protein complexHuman Immunology, 1986
- Role for the Adenosine Triphosphate-Dependent Proteolytic Pathway in Reticulocyte MaturationScience, 1982
- CYTOPLASMIC PARTICLES AND AMINOACYL TRANSFERASE I ACTIVITYThe Journal of cell biology, 1970