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RAPID-KDM

Application of peptide screening technology for identification of substrates of the Jumonji-C histone demethylases

Total Cost €

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EC-Contrib. €

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Partnership

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 RAPID-KDM project word cloud

Explore the words cloud of the RAPID-KDM project. It provides you a very rough idea of what is the project "RAPID-KDM" about.

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Project "RAPID-KDM" data sheet

The following table provides information about the project.

Coordinator
THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD 

Organization address
address: WELLINGTON SQUARE UNIVERSITY OFFICES
city: OXFORD
postcode: OX1 2JD
website: www.ox.ac.uk

contact info
title: n.a.
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surname: n.a.
function: n.a.
email: n.a.
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fax: n.a.

 Coordinator Country United Kingdom [UK]
 Project website http://schofield.chem.ox.ac.uk/
 Total cost 270˙271 €
 EC max contribution 270˙271 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2014
 Funding Scheme MSCA-IF-GF
 Starting year 2015
 Duration (year-month-day) from 2015-10-01   to  2018-09-30

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD UK (OXFORD) coordinator 270˙271.00
2    NATIONAL UNIVERSITY CORPORATION THEUNIVERSITY OF TOKYO JP (TOKYO) partner 0.00

Map

 Project objective

In recent years it has become evident that the functional human proteome is vastly expanded by post-translational modifications (PTMs) that modify protein function and gene expression in a time- and context-dependent manner. Misregulation of these modifications leads to developmental disorders and often contributes to disease biogenesis. However, with the possible exception of protein phosphorylation, the full roles and regulation of these modifications remain poorly understood. Currently, in particular, arginine methylation is proposed to be largely stable and irreversible. Building on my exciting preliminary data that demonstrate that Jumonji C histone demethylases (JmjC KDMs) can catalyse removal of arginine methylation, this proposal aims to identify biologically relevant methylarginine substrates of the JmjC KDM. Cutting-edge mRNA display-based peptide screening technology will be adapted for use as a substrate identification assay in collaboration with Prof Hiroaki Suga at the University of Tokyo. Consensus sequences identified using this novel methodology will be used to identify biologically relevant peptide sequences by bioinformatic searches. On the return to the UK, results with isolated proteins will be correlated with in-cell studies and the functional consequences of these reactions assessed. Given the high level of interest in the post-translational modification field, the results of this study will be of interest to a very wide-range of scientists including other academic researchers in the field of epigenetics and beyond, and major biotechnology and pharmaceutical companies studying JmjC KDMs as drug targets. The fellowship will provide training in state-of-the-art techniques. The collaboration between the University of Oxford and the University of Tokyo will enhance the research capabilities of the European Union, promote cross-fertilisation of knowledge and strengthen research ties with Japan.

 Publications

year authors and title journal last update
List of publications.
2018 Louise J. Walport, Richard J. Hopkinson, Rasheduzzaman Chowdhury, Yijia Zhang, Joanna Bonnici, Rachel Schiller, Akane Kawamura, Christopher J. Schofield
Mechanistic and structural studies of KDM-catalysed demethylation of histone 1 isotype 4 at lysine 26
published pages: 3264-3273, ISSN: 0014-5793, DOI: 10.1002/1873-3468.13231
FEBS Letters 592/19 2019-04-19
2017 Louise J Walport, Richard Obexer, Hiroaki Suga
Strategies for transitioning macrocyclic peptides to cell-permeable drug leads
published pages: 242-250, ISSN: 0958-1669, DOI: 10.1016/j.copbio.2017.07.007
Current Opinion in Biotechnology 48 2019-06-13
2017 Richard Obexer, Louise J Walport, Hiroaki Suga
Exploring sequence space: harnessing chemical and biological diversity towards new peptide leads
published pages: 52-61, ISSN: 1367-5931, DOI: 10.1016/j.cbpa.2017.02.020
Current Opinion in Chemical Biology 38 2019-06-13

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