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

Abbreviation:IDEAL

General Information
IDEAL provides a collection of knowledge on experimentally verified intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDRs). IDEAL contains manually curated annotations on IDPs in locations, structures, and functional sites such as protein binding regions and posttranslational modification sites together with references and structural domain assignments.

Homepage http://www.ideal.force.cs.is.nagoya-u.ac.jp/IDEAL/

Developed in Japan

Created in 2011

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How to cite this record FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: 10.25504/FAIRsharing.h3y42f; Last edited: Feb. 22, 2018, 2:43 p.m.; Last accessed: Jun 24 2018 2:08 a.m.


Record updated: Jan. 12, 2018, 2:23 p.m. by The FAIRsharing Team.




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Data Release

quarterly release No link recorded

Data Curation

manual curation No link recorded

Data Access

file download(XML) No link recorded
browse http://www.ideal.force.cs.is.nagoya-u.ac.jp/IDEAL/ideal.php
download http://www.ideal.force.cs.is.nagoya-u.ac.jp/IDEAL/download/



Publications

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

View Paper (PubMed) View Paper (DOI)

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

View Paper (PubMed) View Paper (DOI)

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