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Kee, Jung-Min
Bioorganic and Chembio Lab
Research Interests
  • Chemical biology, organic synthesis, peptide chemistry, synthetic protein chemistry

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Development of stable phosphohistidine analogues

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Title
Development of stable phosphohistidine analogues
Other Titles
Development of Stable Phosphohistidine Analogues
Author
Kee, Jung-MinVillani, BryeannaCarpenter, Laura, R.Muir, Tom W.
Keywords
NUCLEOSIDE DIPHOSPHATE KINASE; PROTEIN HISTIDINE PHOSPHORYLATION; LABILE HISTONE PHOSPHATES; RAT-LIVER; CYCLOADDITION; LIGATION; FRACTIONS; CHEMISTRY; MECHANISM; ALKYNES
Issue Date
2010-09
Publisher
AMER CHEMICAL SOC
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.
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DOI
10.1021/ja104393t
ISSN
0002-7863
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PHY_Journal Papers
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