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기정민

Kee, Jung-Min
Bioorganic and Chembio Lab.
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Development of stable phosphohistidine analogues

Alternative Title
Development of Stable Phosphohistidine Analogues
Author(s)
Kee, Jung-MinVillani, BryeannaCarpenter, Laura, R.Muir, Tom W.
Issued Date
2010-09
DOI
10.1021/ja104393t
URI
https://scholarworks.unist.ac.kr/handle/201301/13333
Fulltext
http://pubs.acs.org/doi/abs/10.1021/ja104393t
Citation
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, v.132, no.41, pp.14327 - 14328
Abstract
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.
Publisher
AMER CHEMICAL SOC
ISSN
0002-7863

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