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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2015
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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. |
format | Online Article Text |
id | pubmed-4726637 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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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