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Data detailing the platelet acetyl-lysine proteome

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 in...

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Detalles Bibliográficos
Autores principales: Aslan, Joseph E., David, Larry L., McCarty, Owen J.T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4726637/
https://www.ncbi.nlm.nih.gov/pubmed/26904711
http://dx.doi.org/10.1016/j.dib.2015.09.020
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author Aslan, Joseph E.
David, Larry L.
McCarty, Owen J.T.
author_facet Aslan, Joseph E.
David, Larry L.
McCarty, Owen J.T.
author_sort Aslan, Joseph E.
collection PubMed
description 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.
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spelling pubmed-47266372016-02-22 Data detailing the platelet acetyl-lysine proteome Aslan, Joseph E. David, Larry L. McCarty, Owen J.T. Data Brief Data Article 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. Elsevier 2015-10-09 /pmc/articles/PMC4726637/ /pubmed/26904711 http://dx.doi.org/10.1016/j.dib.2015.09.020 Text en © 2015 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Aslan, Joseph E.
David, Larry L.
McCarty, Owen J.T.
Data detailing the platelet acetyl-lysine proteome
title Data detailing the platelet acetyl-lysine proteome
title_full Data detailing the platelet acetyl-lysine proteome
title_fullStr Data detailing the platelet acetyl-lysine proteome
title_full_unstemmed Data detailing the platelet acetyl-lysine proteome
title_short Data detailing the platelet acetyl-lysine proteome
title_sort data detailing the platelet acetyl-lysine proteome
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4726637/
https://www.ncbi.nlm.nih.gov/pubmed/26904711
http://dx.doi.org/10.1016/j.dib.2015.09.020
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