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000839466 005__ 20230210112507.0
000839466 0247_ $$2CORDIS$$aG:(EU-Grant)778247$$d778247
000839466 0247_ $$2CORDIS$$aG:(EU-Call)H2020-MSCA-RISE-2017$$dH2020-MSCA-RISE-2017
000839466 0247_ $$2originalID$$acorda__h2020::778247
000839466 035__ $$aG:(EU-Grant)778247
000839466 150__ $$aDriving the functional characterization of intrinsically disordered proteins$$y2018-03-01 - 2023-08-31
000839466 371__ $$aUNIVERSITY COLLEGE DUBLIN, NATIONAL UNIVERSITY OF IRELAND, DUBLIN$$bNUID UCD$$dIreland$$ehttp://www.ucd.ie$$vCORDIS
000839466 371__ $$aEUROPEAN MOLECULAR BIOLOGY LABORATORY$$bEMBL$$dGermany$$ehttp://www.embl.org$$vCORDIS
000839466 371__ $$aVrije Universiteit Brussel$$bVUB$$dBelgium$$ehttp://www.vub.ac.be/en/$$vCORDIS
000839466 371__ $$aEötvös Loránd University$$bELTE$$dHungary$$ehttps://www.elte.hu/en$$vCORDIS
000839466 371__ $$aUniversity of Padua$$bUNIPD$$dItaly$$ehttp://www.unipd.it/en/home-page$$vCORDIS
000839466 372__ $$aH2020-MSCA-RISE-2017$$s2018-03-01$$t2023-08-31
000839466 450__ $$aIDPfun$$wd$$y2018-03-01 - 2023-08-31
000839466 5101_ $$0I:(DE-588b)5098525-5$$2CORDIS$$aEuropean Union
000839466 680__ $$aIntrinsically disordered proteins (IDPs), characterized by high conformational variability and interaction promiscuity, defy the classic protein structure-function paradigm. IDPs cover almost half of the residues in Eukaryotic proteomes. Growing evidence suggests that IDPs, interacting with multiple partners, are major players in cellular regulation and involved in numerous human diseases. Computational methods have contributed to the identification of IDPs from sequence and recently published curated IDP databases provide a starting point. However, functional knowledge for IDPs remains very limited.
IDPfun is an international consortium aiming to extend our knowledge on the functions of IDPs. Starting from available state of the art computational tools and databases, which have been mostly developed by IDPfun participants, it aims drive a new level of IDP characterization leverage the complementary expertise of 5 EU MS and 3 TC institutions in Argentina, the latter providing useful complementary expertises. IDPfun will create a collaborative environment for research on novel ways to detect and characterize different IDP phenomena in their evolutionary context. It will develop an ontology and classification facilitating the comprehension of IDP complexity and aims to understand IDP functional mechanisms. The gained knowledge will be translated into major international protein databases for the benefit of the wider scientific community. Periodic meetings and symposia will generate a continuous knowledge exchange to be disseminated by open training schools and conferences. IDPfun will foster particularly young researchers, through dedicated activities and by ensuring adherence to the highest quality, ethics and gender balance standards. It is expected that IDPfun will strengthen overseas collaborations, focusing and coordinating research, leading to the creation of a sustainable international IDP community, driving knowledge and infrastructure in bioinformatics.
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000839466 970__ $$aoai:dnet:corda__h2020::67e871140dad0028f7ab7bb3b3431e72
000839466 980__ $$aG
000839466 980__ $$aCORDIS
000839466 980__ $$aAUTHORITY