title: [Functional proteome analysis of human platelets].
abstract: Platelets are anucleated cells and therefore ideal research objects for modern proteome analyses. Despite their importance in thrombosis and hemostasis the protein content of platelets is still poorly characterized in major parts. In preparation for bioinformatic and functional studies a series of proteomic analyses was conducted for platelet subproteomes as well as for posttranslational modifications. Thereby, the identification of 489 proteins, over 550 phosphorylations and 326 N-glycosylation sites was possible, which were not identified in previous proteome studies of platelets. Those results represent new research possibilities for functional characterization of platelet proteins as well as their modifications.
authors.affiliation: Rudolf-Virchow-Zentrum für Experimentelle Biomedizin, Universität Würzburg.
authors.forename: U
authors.initials: U
authors.lastname: Lewandrowski
authors.forename: R P
authors.initials: RP
authors.lastname: Zahedi
authors.forename: J
authors.initials: J
authors.lastname: Moebius
authors.forename: A
authors.initials: A
authors.lastname: Sickmann
mesh_terms: D001792:Blood Platelets / Q000502:physiology*; D001798:Blood Proteins / Q000235:genetics* / Q000378:metabolism; D006487:Hemostasis; D006801:Humans; D008565:Membrane Proteins / Q000097:blood / Q000235:genetics; D011499:Protein Processing, Post-Translational; D020543:Proteome; D040901:Proteomics / Q000379:methods*; D013927:Thrombosis / Q000097:blood
chemical_list: D001798:Blood Proteins; D008565:Membrane Proteins; D020543:Proteome