title: IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature.
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.
authors: Faculty of Engineering, Maebashi Institute of Technology, Maebashi, Gunma 371-0816, Japan. sfukuchi@maebashi-it.ac.jp
authors: Satoshi
authors: S
authors: Fukuchi
authors: Shigetaka
authors: S
authors: Sakamoto
authors: Yukiko
authors: Y
authors: Nobe
authors: Seiko D
authors: SD
authors: Murakami
authors: Takayuki
authors: T
authors: Amemiya
authors: Kazuo
authors: K
authors: Hosoda
authors: Ryotaro
authors: R
authors: Koike
authors: Hidekazu
authors: H
authors: Hiroaki
authors: Motonori
authors: M
authors: Ota
mesh_terms: D030562:Databases, Protein; D058977:Molecular Sequence Annotation; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry; D014584:User-Computer Interface
chemical_list: D011506:Proteins