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What is IDEAL ?
IDEAL provides a collection of knowledge of experimentally verified intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs), along with manually curated annotations of IDPs on both structural and functional aspects.
References
S. Fukuchi, T. Amemiya, S. Sakamoto, Y. Nobe, K. Hosoda, Y. Kado, S. D. Murakami, R. Koike, H. Hiroaki and M. Ota.,  "IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners",  2014, Nucleic Acids Res., 42, D320-D325.,  PMID: 24178034DOI: 10.1093/nar/gkt1010

S. Fukuchi, S. Sakamoto, Y. Nobe, S. D. Murakami, T. Amemiya, K. Hosoda, R. Koike, H. Hiroaki and M. Ota.,  "IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature",  2012, Nucleic Acids Res., 40, D507-D511.,  PMID: 22067451DOI: 10.1093/nar/gkr884
Collaboration
IDEAL in RDF was implemented by the collaboration with Tokyo City University and Database Center for Life Science (DBCLS).
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