期刊
NUCLEIC ACIDS RESEARCH
卷 45, 期 D1, 页码 D219-D227出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkw1056
关键词
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资金
- COST Action BM1405 NGP-net
- ELIXIR-IIB
- Hungarian Academy of Sciences [LP2014-16]
- Hungarian Scientific Research Fund [OTKA K 108798]
- AIRC Research Fellowship
- Spanish Ministerio de Educacion Cultura i Deporte PhD Fellowship
- Mexican National Council for Science and Technology (CONACYT) [215503]
- Grant PortoNeuroDRIve@i3S - Norte Portugal Regional Operational Programme (NORTE), under the PORTUGAL Partnership Agreement, through the European Regional Development Fund (ERDF)
- Direction Generale des Armees
- Aix-Marseille University PhD Fellowship
- OTKA Grant [PD-OTKA 108772]
- French Ministry of National Education, Research and Technology PhD Fellowship
- Ministry of Education, Science and Technological Development of the Republic of Serbia [173001, 173049]
- ICREAAcademia Award
- Odysseus Grant from Research Foundation Flanders (FWO) [G.0029.12]
- AIRC IG Grant [17753]
- Italian Ministry of Health [GR-2011-02347754, GR-2011-02346845]
- Swedish Research Council Grant [VR-NT 2012-5046]
The Database of Protein Disorder (DisProt, URL: www.disprot.org) has been significantly updated and upgraded since its last major renewal in 2007. The current release holds information on more than 800 entries of IDPs/IDRs, i.e. intrinsically disordered proteins or regions that exist and function without a well-defined three-dimensional structure. We have re-curated previous entries to purge DisProt from conflicting cases, and also upgraded the functional classification scheme to reflect continuous advance in the field in the past 10 years or so. We define IDPs as proteins that are disordered along their entire sequence, i.e. entirely lack structural elements, and IDRs as regions that are at least five consecutive residues without well-defined structure. We base our assessment of disorder strictly on experimental evidence, such as X-ray crystallography and nuclear magnetic resonance ( primary techniques) and a broad range of other experimental approaches (secondary techniques). Confident and ambiguous annotations are highlighted separately. DisProt 7.0 presents classified knowledge regarding the experimental characterization and functional annotations of IDPs/IDRs, and is intended to provide an invaluable resource for the research community for a better understanding structural disorder and for developing better computational tools for studying disordered proteins.
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