Bringing Intrinsically Disordered Proteins to Biomedical Applications

Widening ParticipationHORIZON-CSAID: 101160233
EC Contribution
€12,447
Consortium Size
4 orgs
Start Year
2024
Summary

The IDP2Biomed twinning program is aimed at strengthening the scientific excellence and innovation capacity at the interface between Chemistry and Biology of the Faculty of Science of Eötvös Loránd University (ELTE). Researchers from ELTE will be working closely together with three leading European research groups in the field of intrinsically disordered proteins (IDPs). This partnership will provide an ideal platform to enable ELTE to increase its ability to generate scientific innovation and clinical translation. This objective will be achieved by focusing on IDPs that are directly involved in diseases with great socio-economic importance, such as neurodegenerative diseases and rare diseases. IDP2Biomed will integrate IDP-related information with biomedical data, advance the understanding of the function of IDPs in normal and disease states and explore new avenues to alter their behaviour in pathological states. The impact of this program will be maximised by fostering cooperation with academic and industrial partners locally and across the EU.

Consortium (4)

Project Results (12)

Source: CORDIS, the EU research results database.

Publications (12)
DisProt in 2026: enhancing intrinsically disordered proteins accessibility, deposition, and annotation
Nucleic Acids Research· 2026DOI
Maria Victoria Nugnes, Kamel Eddine Adel Bouhraoua, Mehdi Zoubiri, Rita Pancsa, Erzsébet Fichó, null null, Alexander M Monzon, Ana M Melo, Edoardo Salladini, Emanuela Leonardi, Federica Quaglia, Daniyal Nasiribavil, Hamidreza Ghafouri, Gobeill Julien, Emilie Pasche, Patrick Ruch, Paul Van Rijen, László Dobson, Marco Schiavina, Trinidad Cordero, Zsófia E Kálmán, Ximena Castro, Valentín Iglesias, István Reményi, Mahta Mehdiabadi, Gábor Erdős, Zsuzsanna Dosztányi, Peter Tompa, Damiano Piovesan, Silvio C E Tosatto, Maria Cristina Aspromonte
<scp>DR</scp> and <scp>SPIT</scp>: Statistical approaches for identifying transient structure in intrinsically disordered proteins via <scp>NMR</scp> chemical shifts
Protein Science· 2025DOI
Dániel Kovács; Andrea Bodor
AIUPred - Binding: energy embedding to identify disordered binding regions
Journal of Molecular Biology· 2025DOI
Gábor Erdős, Norbert Deutsch, Zsuzsanna Dosztányi
Critical Assessment of Protein Intrinsic Disorder Round 3 ‐ Predicting Disorder in the Era of Protein Language Models
Proteins: Structure, Function, and Bioinformatics· 2025DOI
Mahta Mehdiabadi, Alessio Del Conte, Maria Victoria Nugnes, Maria Cristina Aspromonte, Silvio C. E. Tosatto, Damiano Piovesan
Fine‐tuned interactions between globular and disordered regions of single‐stranded <scp>DNA</scp> binding (<scp>SSB</scp>) protein are required for dynamic condensation under physiological conditions
Protein Science· 2025DOI
Zoltán J. Kovács; Péter Ecsédi; Gábor M. Harami; János Pálinkás; Mina Botros; Lamiya Mahmudova; Viktoria Katran; Dávid Érfalvy; Miklós Cervenak; László Smeller; Mihály Kovács
GeomeTRe: accurate calculation of geometrical descriptors of tandem repeat proteins
Bioinformatics· 2025DOI
Osmanli, Zarifa; Ferrero, Elisa; Monzon, Alexander Miguel; Tosatto, Silvio C E; Piovesan, Damiano
Phase transition drives bacterial single-stranded DNA binding (SSB) protein mobilization during stress response and metabolic adaptation
bioRxiv· 2025DOI
Péter Ecsédi1 , Júlia Szittyai1 , János Pálinkás1,2, Bálint Jezsó1,2, Viktoria Katran1 , Zoltán J. Kovács1,2, Henriett Halász3 , Tasvilla Sonallya4 , Tünde Juhász4 , Tamás Beke-Somfai4 , Szilvia Barkó3 , Edina Szabó-Meleg3 , and Mihály Kovács1,2
Selective engineering of condensation properties of single-stranded DNA binding (SSB) protein via its intrinsically disordered linker region
Nucleic Acids Research· 2025DOI
Péter Ecsédi; Dávid Érfalvy; Zoltán J Kovács; Viktoria Katran; János Pálinkás; Miklós Cervenak; Rita Pancsa; Gábor M Harami; László Smeller; Mihály Kovács
Towards a Unified Framework for Determining Conformational Ensembles of Disordered Proteins
arXiv· 2025DOI
Hamidreza Ghafouri, Pavel Kadeřávek, Ana M Melo, Maria Cristina Aspromonte, Pau Bernadó, Juan Cortes, Zsuzsanna Dosztányi, Gabor Erdos, Michael Feig, Giacomo Janson, Kresten Lindorff-Larsen, Frans A. A. Mulder, Peter Nagy, Richard Pestell, Damiano Piovesa
Deep learning for intrinsically disordered proteins: From improved predictions to deciphering conformational ensembles
Current Opinion in Structural Biology· 2024DOI
Gábor Erdős, Zsuzsanna Dosztányi
DRMAAtic: dramatically improve your cluster potential
Bioinformatics Advances· 2024DOI
Del Conte, Alessio; Ghafouri, Hamidreza; Clementel, Damiano; Mičetić, Ivan; Piovesan, Damiano; Tosatto, Silvio C E; Monzon, Alexander Miguel
MOBIDB in 2025: integrating ensemble properties and function annotations for intrinsically disordered proteins
Nucleic Acids Research· 2024DOI
Damiano Piovesan; Alessio Del Conte; Mahta Mehdiabadi; Maria Cristina Aspromonte; Matthias Blum; Giulio Tesei; Sören von Bülow; Kresten Lindorff-Larsen; Silvio C E Tosatto