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Data detailing the platelet acetyl-lysine proteome

机译:详细描述血小板乙酰赖氨酸蛋白质组的数据

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Here we detail proteomics data that describe the acetyl-lysine proteome of blood platelets (Aslan et al., 2015 ). 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 ) via with PRIDE partner repository with the dataset identifier http://www.ebi.ac.uk/pride/archive/projects/PXD002332 .
机译:在这里,我们详细描述了血小板的乙酰赖氨酸蛋白质组学的蛋白质组学数据(Aslan等,2015)。亲和纯化–质谱(AP-MS)方法用于鉴定静态,洗涤后的人类血小板中经Nε-赖氨酸乙酰化修饰的蛋白质。数据提供了对蛋白质赖氨酸乙酰化介导的血小板功能潜在调节机制的见解。另外,由于血小板是无核的并且缺乏组蛋白,因此它们提供了独特而有价值的系统来研究赖氨酸乙酰化对胞质蛋白的调控。质谱蛋白质组学数据已通过PRIDE合作伙伴存储库(数据集标识符为http://www.ebi.ac.uk/pride/archive/projects/PXD002332)存放到ProteomeXchange联盟(Vizcaino等,2014)。

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