<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Dowal L</submitter><funding>NHLBI NIH HHS</funding><pagination>e62-73</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3186346</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>118(13)</volume><pubmed_abstract>Protein palmitoylation is a dynamic process that regulates membrane targeting of proteins and protein-protein interactions. We have previously demonstrated a critical role for protein palmitoylation in platelet activation and have identified palmitoylation machinery in platelets. Using a novel proteomic approach, Palmitoyl Protein Identification and Site Characterization, we have begun to characterize the human platelet palmitoylome. Palmitoylated proteins were enriched from membranes isolated from resting platelets using acyl-biotinyl exchange chemistry, followed by identification using liquid chromatography-tandem mass spectrometry. This global analysis identified > 1300 proteins, of which 215 met criteria for significance and represent the platelet palmitoylome. This collection includes</pubmed_abstract><journal>Blood</journal><pubmed_title>Proteomic analysis of palmitoylated platelet proteins.</pubmed_title><pmcid>PMC3186346</pmcid><funding_grant_id>T32 HL07917</funding_grant_id><funding_grant_id>T32 HL007917</funding_grant_id><funding_grant_id>HL87203</funding_grant_id><funding_grant_id>P01 HL087203</funding_grant_id><pubmed_authors>Yang W</pubmed_authors><pubmed_authors>Flaumenhaft R</pubmed_authors><pubmed_authors>Freeman MR</pubmed_authors><pubmed_authors>Steen H</pubmed_authors><pubmed_authors>Dowal L</pubmed_authors></additional><is_claimable>false</is_claimable><name>Proteomic analysis of palmitoylated platelet proteins.</name><description>Protein palmitoylation is a dynamic process that regulates membrane targeting of proteins and protein-protein interactions. We have previously demonstrated a critical role for protein palmitoylation in platelet activation and have identified palmitoylation machinery in platelets. Using a novel proteomic approach, Palmitoyl Protein Identification and Site Characterization, we have begun to characterize the human platelet palmitoylome. Palmitoylated proteins were enriched from membranes isolated from resting platelets using acyl-biotinyl exchange chemistry, followed by identification using liquid chromatography-tandem mass spectrometry. This global analysis identified > 1300 proteins, of which 215 met criteria for significance and represent the platelet palmitoylome. This collection includes</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Sep</publication><modification>2026-06-03T10:52:10.485Z</modification><creation>2026-04-28T03:11:04.814Z</creation></dates><accession>S-EPMC3186346</accession><cross_references><pubmed>21813449</pubmed><doi>10.1182/blood-2011-05-353078</doi></cross_references></HashMap>