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Title: Recognition of proximally phosphorylated tyrosine residues and continuous analysis of phosphatase activity using a stable europium complex
Authors: Hewitt, Sarah H.
Liu, Roanna
Butler, Stephen J.
Keywords: Anion sensing
Enzyme assay
Issue Date: 2017
Publisher: © Taylor and Francis
Citation: HEWITT, S.H., LIU, R. and BUTLER, S.J., 2017. Recognition of proximally phosphorylated tyrosine residues and continuous analysis of phosphatase activity using a stable europium complex. Supramolecular Chemistry, doi: 10.1080/10610278.2017.1410548.
Abstract: The recognition of proteins and their post-translational modifications using synthetic molecules is an active area of research. A common post-translational modification is the phosphorylation of serine, threonine or tyrosine residues. The phosphorylation of proximal tyrosine residues occurs in over 1000 proteins in the human proteome, including in disease-related proteins, so the recognition of this motif is of particular interest. We have developed a luminescent europium(III) complex, [Eu.1] + , capable of the discrimination of proximally phosphorylated tyrosine residues, from analogous mono- and non-phosphorylated tyrosine residues, more distantly-related phosphotyrosine residues and over proximally phosphorylated serine and threonine residues. [Eu.1] + was used to continuously monitor the phosphatase catalysed dephosphorylation of a peptide containing proximally phosphorylated tyrosine residues.
Description: This paper is closed access until 30th November 2018.
Sponsor: This work was supported by a Wellcome Trust Seed Award [grant number 204500/Z/16/Z] and The Royal Society [Research Grant (RG150476)].
Version: Accepted for publication
DOI: 10.1080/10610278.2017.1410548
URI: https://dspace.lboro.ac.uk/2134/28343
Publisher Link: https://doi.org/10.1080/10610278.2017.1410548
ISSN: 1061-0278
Appears in Collections:Closed Access (Chemistry)

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