## Abstract Osteopontin (OPN) is primarily a secreted phosphoglycoprotein found in a variety of tissues and body fluids. It has a wide range of reported functions, many of which are affected by the degree of postโtranslational modification (PTM) of the protein. These PTMs include phosphorylation, g
Post-translational modifications of naturally processed MHC-binding epitopes
โ Scribed by Victor H Engelhard; Michelle Altrich-Vanlith; Marina Ostankovitch; Angela L Zarling
- Publisher
- Elsevier Science
- Year
- 2006
- Tongue
- English
- Weight
- 165 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0952-7915
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โฆ Synopsis
A variety of different post-translational modifications of peptides displayed by class I and II MHC molecules have now been described. Some modifications promote the binding of peptides to MHC molecules, and might also influence the ability of the peptide to be produced by antigen processing pathways. In some instances, the antigen processing components themselves are actually responsible for generating post-translational modifications. Finally, evidence is accumulating that modifications can be altered as a consequence of inflammation, transformation, apoptosis and aging. This leads to altered repertories of MHC-associated peptides, which may be important in immune responses associated with autoimmune diseases, infection and cancer.
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This mini review is primarily concerned with the biosynthesis of the major outer membrane lipoprotein of Escherichia coli. The lipoprotein is composed of fifty-eight amino acid residues, one glyceride residue and one acyl residue being at the amino terminal cysteine residue. About one-third of the l
## Abstract In a previous review (Bowie, Brinkworth, & Dua (2002); Mass Spectrom Rev 21:87โ107) we described the characteristic backbone cleavages and side chain fragmentations which occur from (MโH)^โ^ parent anions of underivatized peptides. This work is briefly summarized in the present review.