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针对天冬氨酸和谷氨酸 ADP-核糖基化蛋白质组的特异性研究。

Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome.

机构信息

Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas, USA.

出版信息

Nat Methods. 2013 Oct;10(10):981-4. doi: 10.1038/nmeth.2603. Epub 2013 Aug 18.

DOI:10.1038/nmeth.2603
PMID:23955771
Abstract

Poly(ADP-ribosyl)ation is catalyzed by a family of enzymes known as PARPs. We describe a method to characterize the human aspartic acid- and glutamic acid-ADP-ribosylated proteome. We identified 1,048 ADP-ribosylation sites on 340 proteins involved in a wide array of nuclear functions; among these were many previously unknown PARP downstream targets whose ADP-ribosylation was sensitive to PARP inhibitor treatment. We also confirmed that iniparib had a negligible effect on PARP activity in intact cells.

摘要

聚(ADP-核糖)化由一组称为 PARP 的酶催化。我们描述了一种鉴定人类天冬氨酸和谷氨酸 ADP-核糖基化蛋白质组的方法。我们在 340 种参与广泛核功能的蛋白质上鉴定了 1048 个 ADP-核糖基化位点;其中包括许多以前未知的 PARP 下游靶标,其 ADP-核糖基化对 PARP 抑制剂处理敏感。我们还证实,在完整细胞中,尼拉帕尼对 PARP 活性几乎没有影响。

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The zinc-finger domains of PARP1 cooperate to recognize DNA strand breaks.PARP1 的锌指结构域协同识别 DNA 链断裂。
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Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1.DNA 损伤依赖性聚(ADP-核糖)化的人 PARP-1 的结构基础。
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