| Autor: |
Fukuchi S; Faculty of Engineering, Maebashi Institute of Technology, Maebashi, Gunma 371-0816, Japan. sfukuchi@maebashi-it.ac.jp, Sakamoto S, Nobe Y, Murakami SD, Amemiya T, Hosoda K, Koike R, Hiroaki H, Ota M |
| Jazyk: |
angličtina |
| Zdroj: |
Nucleic acids research [Nucleic Acids Res] 2012 Jan; Vol. 40 (Database issue), pp. D507-11. Date of Electronic Publication: 2011 Nov 08. |
| DOI: |
10.1093/nar/gkr884 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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