期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 132, 期 41, 页码 14327-14329出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja104393t
关键词
-
资金
- U.S. National Institute of Health [GM086868, RC2CA148354]
- Starr Cancer Consortium
Protein phosphorylation is one of the most common and extensively studied posttranslational modifications (PTMs). Compared to the O-phosphorylation of Ser, Thr, and Tyr residues, our understanding of histidine phosphorylation is relatively limited, particularly in higher eukaryotes, due to technical difficulties stemming from the intrinsic instability and isomerism of phosphohistidine (pHis). We report the design and synthesis of stable and nonisomerizable pHis analogues. These pHis analogues were successfully utilized in solid-phase peptide synthesis and semi-synthesis of histone H4. Significantly, the first antibody that specifically recognizes pHis was obtained using the synthetic peptide as the immunogen.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据