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• W2110976912 abstract "IDEAL, Intrinsically Disordered proteins with Extensive Annotations and Literature (http://www.ideal.force.cs.is.nagoya-u.ac.jp/IDEAL/), is a collection of knowledge on experimentally verified intrinsically disordered proteins. IDEAL contains manual annotations by curators on intrinsically disordered regions, interaction regions to other molecules, post-translational modification sites, references and structural domain assignments. In particular, IDEAL explicitly describes protean segments that can be transformed from a disordered state to an ordered state. Since in most cases they can act as molecular recognition elements upon binding of partner proteins, IDEAL provides a data resource for functional regions of intrinsically disordered proteins. The information in IDEAL is provided on a user-friendly graphical view and in a computer-friendly XML format." @default.
• W2110976912 created "2016-06-24" @default.
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• W2110976912 date "2011-11-08" @default.
• W2110976912 modified "2023-10-01" @default.
• W2110976912 title "IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature" @default.
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• W2110976912 doi "https://doi.org/10.1093/nar/gkr884" @default.
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