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Recognition of proximally phosphorylated tyrosine residues and continuous analysis of phosphatase activity using a stable europium complex

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journal contribution
posted on 01.02.2018 by Sarah Hewitt, Roanna Liu, Stephen Butler
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.

Funding

This work was supported by a Wellcome Trust Seed Award [grant number 204500/Z/16/Z] and The Royal Society [Research Grant (RG150476)].

History

School

  • Science

Department

  • Chemistry

Published in

Supramolecular Chemistry

Volume

30

Issue

9

Pages

765 - 771

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, 30 (9), pp. 765-771.

Publisher

© Taylor and Francis

Version

AM (Accepted Manuscript)

Publisher statement

This work is made available according to the conditions of the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) licence. Full details of this licence are available at: https://creativecommons.org/licenses/by-nc-nd/4.0/

Acceptance date

16/11/2017

Publication date

2017-11-30

Copyright date

2018

Notes

This is an Accepted Manuscript of an article published by Taylor & Francis in Supramolecular Chemistry on 30 November 2017, available online: http://www.tandfonline.com/10.1080/10610278.2017.1410548.

ISSN

1061-0278

eISSN

1029-0478

Language

en

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