Opendata, web and dolomites

jamclay

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

Total Cost €

0

EC-Contrib. €

0

Partnership

0

Views

0

 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.

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

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

Are you the coordinator (or a participant) of this project? Plaese send me more information about the "JAMCLAY" project.

For instance: the website url (it has not provided by EU-opendata yet), the logo, a more detailed description of the project (in plain text as a rtf file or a word file), some pictures (as picture files, not embedded into any word file), twitter account, linkedin page, etc.

Send me an  email (fabio@fabiodisconzi.com) and I put them in your project's page as son as possible.

Thanks. And then put a link of this page into your project's website.

The information about "JAMCLAY" are provided by the European Opendata Portal: CORDIS opendata.

More projects from the same programme (H2020-EU.1.3.2.)

MITafterVIT (2020)

Unravelling maintenance mechanisms of immune tolerance after termination of venom immunotherapy by means of clonal mast cell diseases

Read More  

InBPSOC (2020)

Increases biomass production and soil organic carbon stocks with innovative cropping systems under climate change

Read More  

Extending MEDT (2019)

Extending the Molecular Electron Density Theory

Read More