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jamclay

Chemical Tools to Probe the Role of Bromodomains in the Parasite Trypanosoma cruzi

Total Cost €

0

EC-Contrib. €

0

Partnership

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 jamclay project word cloud

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clinical    led    explosion    species    roles    modules    lysine    equally    containing    dissecting    tcbdf1    parasite    proteins    ing    bet    modification    histone    terminal    acetylated    protein    cells    probes    rapid    invaluable    bromodomain    prevent    translational    potent    play    transferases    found    exist    regulation    ultimately    environment    atherosclerosis    inhibitors    hdacs    cancer    fundamental    biology    cloned    treatment    function    discovered    ptm    trials    chagas    post    bind    inflammation    interactions    despite    compounds    interaction    prof    modulate    acetylation    trypanosoma    progress    causes    antiproliferative    collaborator    domain    serra    acetyl    reversing    played    bcps    humans    hats    bromodomains    cruzi    small    disease    deacetlyases    pocket    hypothesise    transcriptional    cellular    poorly    kac    binding    dynamic    molecule    mediate    plasmids    ligands    hence    acetylating    human    organisms    lines    mediated    understand    extra    contain    larger   

Project "jamclay" 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.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country United Kingdom [UK]
 Project website http://conway.chem.ox.ac.uk
 Total cost 183˙454 €
 EC max contribution 183˙454 € (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-EF-ST
 Starting year 2016
 Duration (year-month-day) from 2016-03-24   to  2018-03-23

 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 183˙454.00

Map

 Project objective

Lysine acetylation is a key protein post-translational modification (PTM) found throughout the cellular environment and across the range of species. This PTM is dynamic, with histone acetyl transferases (HATs) acetylating lysine, and histone deacetlyases (HDACs) reversing the modification. In addition, proteins modules bromodomains, have been identified that bind to acetylated lysine (KAc) and mediate protein-protein interactions. In humans, bromodomains exist as part of larger proteins, many of which are involved in transcriptional regulation. Bromodomains contain a KAc-binding pocket for which small molecule ligands have been identified. These ligands prevent the interaction of bromodomains with KAc and have been invaluable in dissecting the fundamental biology mediated by bromodomain-containing proteins (BCPs). We and others have developed potent ligands for the human bromodomain and extra C-terminal domain (BET) bromodomains. These compounds have antiproliferative effects in cancer cells lines and modulate inflammation and atherosclerosis. This work led to an explosion of interest in developing BET bromodomain inhibitors, resulting in 5 compounds in clinical trials. Despite rapid progress in understanding the role of human bromodomains, their function in other species is poorly understood. Given the fundamental role played by bromodomains in humans, we hypothesise that BCPs will play equally important roles in other organisms.

To understand the role of non-human bromodomains we will develop small molecule probes to study the function of BCPs in the parasite Trypanosoma cruzi. We have selected T. cruzi for two reasons: 1. Four BCPs (TcBDF1-4) have been discovered in T. cruzi; our collaborator Prof. Serra has cloned these proteins and we have the plasmids; 2. T. cruzi is the parasite that causes Chagas Disease and hence bromodomain ligands might ultimately represent a novel method of treatment for this disease.

 Publications

year authors and title journal last update
List of publications.
2018 Laura E. Jennings, Matthias Schiedel, David S. Hewings, Sarah Picaud, Corentine M.C. Laurin, Paul A. Bruno, Joseph P. Bluck, Amy R. Scorah, Larissa See, Jessica K. Reynolds, Mustafa Moroglu, Ishna N. Mistry, Amy Hicks, Pavel Guzanov, James Clayton, Charles N.G. Evans, Giulia Stazi, Philip C. Biggin, Anna K. Mapp, Ester M. Hammond, Philip G. Humphreys, Panagis Filippakopoulos, Stuart J. Conway
BET bromodomain ligands: Probing the WPF shelf to improve BRD4 bromodomain affinity and metabolic stability
published pages: , ISSN: 0968-0896, DOI: 10.1016/j.bmc.2018.05.003
Bioorganic & Medicinal Chemistry 2020-01-24

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