Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are now recognised as major determinants in cellular regulation. This white paper presents a roadmap for future e-infrastructure developments in the field of IDP research within the ELIXIR framework. The goal of these developments is to drive the creation of high-quality tools and resources to support the identification, analysis and functional characterisation of IDPs. The roadmap is the result of a workshop titled "An intrinsically disordered protein user community proposal for ELIXIR" held at the University of Padua. The workshop, and further consultation with the members of the wider IDP community, identified the key priority areas for the roadmap inclu...
All proteomes contain both proteins and polypeptide segments that don't form a defined three-dimensi...
Intrinsically Disordered Proteins (IDPs) lack stable tertiary and secondary structures and are exten...
<p>(A) Cellular localizations of fully folded proteins and IDPs according to their UniProt annotatio...
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are now recogni...
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are now recogni...
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are now recogni...
It is now clearly established that some proteins or protein regions are devoid of any stable seconda...
The Database of Protein Disorder (DisProt) links structure and function information for intrinsicall...
The Database of Protein Disorder (DisProt) links structure and function information for intrinsicall...
Abstract Background Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (I...
The Database of Intrinsically Disordered Proteins (DisProt, URL: https://disprot.org) is the major r...
Intrinsically disordered proteins (IDPs) are proteins that usually do not adopt well-defined native ...
Intrinsically disordered proteins (IDPs) now serve as important nodes in biological signaling networ...
International audienceThe Database of Intrinsically Disordered Proteins (DisProt, URL: https://dispr...
Intrinsically disordered proteins (IDPs) and regions (IDRs) are a class of functionally important pr...
All proteomes contain both proteins and polypeptide segments that don't form a defined three-dimensi...
Intrinsically Disordered Proteins (IDPs) lack stable tertiary and secondary structures and are exten...
<p>(A) Cellular localizations of fully folded proteins and IDPs according to their UniProt annotatio...
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are now recogni...
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are now recogni...
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are now recogni...
It is now clearly established that some proteins or protein regions are devoid of any stable seconda...
The Database of Protein Disorder (DisProt) links structure and function information for intrinsicall...
The Database of Protein Disorder (DisProt) links structure and function information for intrinsicall...
Abstract Background Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (I...
The Database of Intrinsically Disordered Proteins (DisProt, URL: https://disprot.org) is the major r...
Intrinsically disordered proteins (IDPs) are proteins that usually do not adopt well-defined native ...
Intrinsically disordered proteins (IDPs) now serve as important nodes in biological signaling networ...
International audienceThe Database of Intrinsically Disordered Proteins (DisProt, URL: https://dispr...
Intrinsically disordered proteins (IDPs) and regions (IDRs) are a class of functionally important pr...
All proteomes contain both proteins and polypeptide segments that don't form a defined three-dimensi...
Intrinsically Disordered Proteins (IDPs) lack stable tertiary and secondary structures and are exten...
<p>(A) Cellular localizations of fully folded proteins and IDPs according to their UniProt annotatio...