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


Chasing Phosphohistidine, an Elusive Sibling in the Phosphoamino Acid Family

DC Field Value Language Kee, Jung-Min ko Muir, Tom W. ko 2015-08-05T00:25:59Z - 2015-08-04 ko 2012-01 ko
dc.identifier.citation ACS CHEMICAL BIOLOGY, v.7, no.1, pp.44 - 51 ko
dc.identifier.issn 1554-8929 ko
dc.identifier.uri -
dc.description.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 ko
dc.description.statementofresponsibility close -
dc.language 영어 ko
dc.publisher AMER CHEMICAL SOC ko
dc.title Chasing Phosphohistidine, an Elusive Sibling in the Phosphoamino Acid Family ko
dc.title.alternative Chasing Phosphohistidine, an Elusive Sibling in the Phosphoamino Acid Fa mily ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-84856158810 ko
dc.identifier.wosid 000299241300006 ko
dc.type.rims ART ko
dc.description.wostc 35 *
dc.description.scopustc 37 * 2015-12-28 * 2015-11-04 *
dc.identifier.doi 10.1021/cb200445w ko
dc.identifier.url ko
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