Explore the words cloud of the IDPfun project. It provides you a very rough idea of what is the project "IDPfun" about.
The following table provides information about the project.
UNIVERSITA DEGLI STUDI DI PADOVA
|Coordinator Country||Italy [IT]|
|Total cost||1˙291˙500 €|
|EC max contribution||1˙291˙500 € (100%)|
1. H2020-EU.1.3.3. (Stimulating innovation by means of cross-fertilisation of knowledge)
|Duration (year-month-day)||from 2018-03-01 to 2022-02-28|
Take a look of project's partnership.
|1||UNIVERSITA DEGLI STUDI DI PADOVA||IT (PADOVA)||coordinator||423˙000.00|
|2||EUROPEAN MOLECULAR BIOLOGY LABORATORY||DE (HEIDELBERG)||participant||234˙000.00|
|3||VRIJE UNIVERSITEIT BRUSSEL||BE (BRUSSEL)||participant||234˙000.00|
|4||EOTVOS LORAND TUDOMANYEGYETEM||HU (BUDAPEST)||participant||207˙000.00|
|5||UNIVERSITY COLLEGE DUBLIN, NATIONAL UNIVERSITY OF IRELAND, DUBLIN||IE (DUBLIN)||participant||193˙500.00|
|6||FUNDACION INSTITUTO LELOIR||AR (Buenos Aires)||partner||0.00|
|7||UNIVERSIDAD NACIONAL DE GENERAL SAN MARTIN||AR (SAN MARTIN BUENOS AIRES)||partner||0.00|
|8||UNIVERSIDAD NACIONAL DE QUILMES||AR (BERNAL)||partner||0.00|
Intrinsically 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.
|Symposia Period 1||Other||2020-03-27 11:42:41|
|New version of the Mobi software||Demonstrators, pilots, prototypes||2020-03-11 14:42:16|
|Software for the identification of homologous IDR clusters from sequence databases||Demonstrators, pilots, prototypes||2020-02-12 12:17:39|
|Software package for the automatic extraction of PED entry data from protein ensembles||Demonstrators, pilots, prototypes||2019-09-17 16:46:21|
|Software for automatic detection of IDRs and linear motifs from protein structures||Demonstrators, pilots, prototypes||2019-09-17 16:46:21|
|A software tool for the automatic extraction of IDR relevant information from literature||Demonstrators, pilots, prototypes||2019-09-17 16:46:21|
Take a look to the deliverables list in detail: detailed list of IDPfun deliverables.
|year||authors and title||journal||last update|
Julia Marchetti, Alexander Miguel Monzon, Silvio C.E. Tosatto, Gustavo Parisi, MarÃa Silvina Fornasari
Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution
published pages: 1298-1307, ISSN: 0022-2836, DOI: 10.1016/j.jmb.2019.01.031
|Journal of Molecular Biology 431/6||2019-09-17|
Marco Necci, Damiano Piovesan, Silvio C E Tosatto
Where differences resemble: sequence-feature analysis in curated databases of intrinsically disordered proteins
published pages: , ISSN: 1758-0463, DOI: 10.1093/database/bay127
Pablo Mier, Lisanna Paladin, Stella Tamana, Sophia Petrosian, BorbÃ¡la Hajdu-SoltÃ©sz, Annika Urbanek, Aleksandra Gruca, Dariusz Plewczynski, Marcin Grynberg, Pau BernadÃ³, ZoltÃ¡n GÃ¡spÃ¡ri, Christos A Ouzounis, Vasilis J Promponas, Andrey V Kajava, John M Hancock, Silvio C E Tosatto, Zsuzsanna Dosztanyi, Miguel A Andrade-Navarro
Disentangling the complexity of low complexity proteins
published pages: , ISSN: 1467-5463, DOI: 10.1093/bib/bbz007
|Briefings in Bioinformatics 2019||2019-09-17|
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The information about "IDPFUN" are provided by the European Opendata Portal: CORDIS opendata.
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