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jamclay

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

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EC-Contrib. €

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 Outcomes and results

 jamclay project word cloud

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

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

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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