Data detailing the platelet acetyl-lysine proteome

Research output: Contribution to journalArticle

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Abstract

Here we detail proteomics data that describe the acetyl-lysine proteome of blood platelets (Aslan et al., 2015 [1]). An affinity purification - mass spectrometry (AP-MS) approach was used to identify proteins modified by Nε-lysine acetylation in quiescent, washed human platelets. The data provide insights into potential regulatory mechanisms of platelet function mediated by protein lysine acetylation. Additionally, as platelets are anucleate and lack histone proteins, they offer a unique and valuable system to study the regulation of cytosolic proteins by lysine acetylation. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (Vizcaino et al., 2014 [2]) via with PRIDE partner repository with the dataset identifier PXD002332.

Original languageEnglish (US)
Pages (from-to)368-371
Number of pages4
JournalData in Brief
Volume5
DOIs
StatePublished - Dec 1 2015

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Keywords

  • Acetylation
  • Hemostasis
  • Platelets
  • Proteomics

ASJC Scopus subject areas

  • General
  • Education

Cite this

Data detailing the platelet acetyl-lysine proteome. / Aslan, Joseph; David, Larry; McCarty, Owen.

In: Data in Brief, Vol. 5, 01.12.2015, p. 368-371.

Research output: Contribution to journalArticle

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