Name
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. |
Year | DOI | Venue |
|---|---|---|
2012 | 10.1093/nar/gkr884 | NUCLEIC ACIDS RESEARCH |
Keywords | Field | DocType |
proteins,protein conformation | XML,Biology,Molecular recognition,Intrinsically disordered proteins,Bioinformatics,Computational biology,Genetics,Molecular Sequence Annotation,Protein structure | Journal |
Volume | Issue | ISSN |
40 | D1 | 0305-1048 |
Citations | PageRank | References |
14 | 0.85 | 9 |
Authors | ||
9 | ||
Name | Order | Citations | PageRank |
|---|---|---|---|
| Satoshi Fukuchi | 1 | 44 | 8.93 |
| Shigetaka Sakamoto | 2 | 25 | 2.30 |
| Yukiko Nobe | 3 | 19 | 1.42 |
| Seiko D Murakami | 4 | 19 | 1.42 |
| Takayuki Amemiya | 5 | 32 | 3.25 |
| Kazuo Hosoda | 6 | 19 | 1.42 |
| Ryotaro Koike | 7 | 33 | 3.66 |
| H Hiroaki | 8 | 19 | 2.10 |
| Motonori Ota | 9 | 135 | 29.12 |