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. 1997 Jul;6(7):1405–1411. doi: 10.1002/pro.5560060704

Synthesis and characterization of histidine-phosphorylated peptides.

K F Medzihradszky 1, N J Phillipps 1, L Senderowicz 1, P Wang 1, C W Turck 1
PMCID: PMC2143754  PMID: 9232641

Abstract

Posttranslational phosphorylation of proteins is an important event in many cellular processes. Whereas phosphoesters of serine, threonine, and tyrosine have been studied extensively, only limited information is available for other amino acids modified by a phosphate group. The formation of phosphohistidine residues in proteins was discovered originally in prokaryotic organisms, but also has been found recently in eukaryotic cells. We describe methods for the synthesis and analysis of phosphohistidine-containing peptides, a prerequisite for the investigation of the role of this posttranslational modification in cellular processes.

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Selected References

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