BROWSE

Related Researcher

Author's Photo

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

ITEM VIEW & DOWNLOAD

Chasing Phosphohistidine, an Elusive Sibling in the Phosphoamino Acid Family

Cited 35 times inthomson ciCited 37 times inthomson ci
Title
Chasing Phosphohistidine, an Elusive Sibling in the Phosphoamino Acid Family
Other Titles
Chasing Phosphohistidine, an Elusive Sibling in the Phosphoamino Acid Fa mily
Author
Kee, Jung-MinMuir, Tom W.
Keywords
Posttranslational modification (PTM); Phosphoproteomics; Histidine phosphorylation; Phosphoramidate; Histidine kinase; Two-component signaling system; Phosphohistidine analogue; Protein semisynthesis
Issue Date
2012-01
Publisher
AMER CHEMICAL SOC
Citation
ACS CHEMICAL BIOLOGY, v.7, no.1, pp.44 - 51
Abstract
This year (2012) marks the 50th anniversary of the discovery of protein histidine phosphorylation. Phosphorylation of histidine (pHis) is now widely recognized as being critical to signaling processes in prokaryotes and lower eukaryotes. However, the modification is also becoming more widely reported in mammalian cellular processes and implicated in certain human disease states such as cancer and inflammation. Nonetheless, much remains to be understood about the role and extent of the modification in mammalian cell biology. Studying the functional role of pHis in signaling, either in vitro or in vivo, has proven devilishly hard, largely due to the chemical instability of the modification. As a consequence, we are currently handicapped by a chronic lack of chemical and biochemical tools with which to study histidine phosphorylation. Here, we discuss the challenges associated with studying the chemical biology of pHis and review recent., progress that offers some hope that long-awaited biochemical reagents for studying this elusive posttranslational modification (PTM) might soon be available
URI
Go to Link
DOI
10.1021/cb200445w
ISSN
1554-8929
Appears in Collections:
PHY_Journal Papers
Files in This Item:
cb200445w.pdf Download

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show full item record

qrcode

  • mendeley

    citeulike

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

MENU