databases > DOI:10.25504/FAIRsharing.h3y42f
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ready Intrinsically Disordered proteins with Extensive Annotations and Literature

Abbreviation:IDEAL

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IDEAL (Intrinsically Disordered proteins with Extensive Annotations and Literature) is a collection of experimentally-verified intrinsically disordered proteins (IDPs) that cannot adopt stable globular structures under physiological conditions. IDEAL contains manually curated annotations on IDPs in locations, structures, and functional sites such as protein binding regions and post-translational modification sites together with references and structural domain assignments.




How to cite this record FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Sep 25 2021 4:01 a.m.

Publication for citation  IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners. Fukuchi S,Amemiya T,Sakamoto S,Nobe Y,Hosoda K,Kado Y,Murakami SD,Koike R,Hiroaki H,Ota M; Nucleic Acids Res ; 2013; 10.1093/nar/gkt1010;


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Record updated: Jan. 30, 2020, 9:48 a.m. by The FAIRsharing Team.

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IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners.

Fukuchi S,Amemiya T,Sakamoto S,Nobe Y,Hosoda K,Kado Y,Murakami SD,Koike R,Hiroaki H,Ota M
Nucleic Acids Res 2013

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