Makwana, M.V., Muimo, R. orcid.org/0000-0003-4242-0188 and Jackson, R.F. (2018) Advances in development of new tools for the study of phosphohistidine. Laboratory Investigation, 98 (3). pp. 291-303. ISSN 0023-6837
Abstract
Protein phosphorylation is an important post-translational modification that is an integral part of cellular function. The O-phosphorylated amino-acid residues, such as phosphoserine (pSer), phosphothreonine (pThr) and phosphotyrosine (pTyr), have dominated the literature while the acid labile N-linked phosphorylated amino acids, such as phosphohistidine (pHis), have largely been historically overlooked because of the acidic conditions routinely used in amino-acid detection and analysis. This review highlights some misinterpretations that have arisen in the existing literature, pinpoints outstanding questions and potential future directions to clarify the role of pHis in mammalian signalling systems. Particular emphasis is placed on pHis isomerization and the hybrid functionality for both pHis and pTyr of the proposed τ-pHis analogue bearing the triazole residue.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2017 Nature Publishing Group. This is an author produced version of a paper subsequently published in Laboratory Investigation. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | Analytical biochemistry; Biomarkers |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Medicine, Dentistry and Health (Sheffield) > Department of Infection, Immunity and Cardiovascular Disease |
Funding Information: | Funder Grant number ENGINEERING AND PHYSICAL SCIENCE RESEARCH COUNCIL (EPSRC) UNSPECIFIED |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 14 Dec 2017 11:21 |
Last Modified: | 21 Dec 2023 11:53 |
Status: | Published |
Publisher: | Nature Publishing Group |
Refereed: | Yes |
Identification Number: | 10.1038/labinvest.2017.126 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:125172 |