title: Hypotheses on the physiological role of enzymatic protein methyl esterification using human erythrocytes as a model system.
authors.affiliation: Department of Biochemistry of Macromolecules, 1st Medical School, University of Napoli, Italy.
authors.forename: P
authors.initials: P
authors.lastname: Galletti
authors.forename: C
authors.initials: C
authors.lastname: Manna
authors.forename: D
authors.initials: D
authors.lastname: Ingrosso
authors.forename: P
authors.initials: P
authors.lastname: Iardino
authors.forename: V
authors.initials: V
authors.lastname: Zappia
mesh_terms: D000818:Animals; D001224:Aspartic Acid / Q000378:metabolism; D001798:Blood Proteins / Q000378:metabolism*; D002417:Cattle; D016922:Cellular Senescence; D004905:Erythrocyte Aging; D004910:Erythrocyte Membrane / Q000378:metabolism; D004951:Esterification; D006801:Humans; D007527:Isoenzymes / Q000097:blood / Q000502:physiology; D008565:Membrane Proteins / Q000378:metabolism; D008745:Methylation; D008954:Models, Biological; D026601:Protein D-Aspartate-L-Isoaspartate Methyltransferase; D011496:Protein Methyltransferases / Q000097:blood / Q000502:physiology*; D011499:Protein Processing, Post-Translational; D012260:Ribonucleases / Q000378:metabolism
chemical_list: D001798:Blood Proteins; D007527:Isoenzymes; D008565:Membrane Proteins; D001224:Aspartic Acid; D011496:Protein Methyltransferases; D026601:Protein D-Aspartate-L-Isoaspartate Methyltransferase; D012260:Ribonucleases