The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
DisProt: the Database of Disordered Proteins
Open accessAbstract
The Database of Protein Disorder (DisProt) links structure and function information for intrinsically disordered proteins (IDPs). Intrinsically disordered proteins do not form a fixed three-dimensional structure under physiological conditions, either in their entireties or in segments or regions. We define IDP as a protein that contains at least one experimentally determined disordered region. Although lacking fixed structure, IDPs and regions carry out important biological functions, being typically involved in regulation, signaling and control. Such functions can involve high-specificity low-affinity interactions, the multiple binding of one protein to many partners and the multiple binding of many proteins to one partner. These three features are all enabled and enhanced by protein intrinsic disorder. One of the major hindrances in the study of IDPs has been the lack of organized information. DisProt was developed to enable IDP research by collecting and organizing knowledge regarding the experimental characterization and the functional associations of IDPs. In addition to being a unique source of biological information, DisProt opens doors for a plethora of bioinformatics studies. DisProt is openly available at http://www.disprot.org.
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Cites
Intrinsic Disorder and Protein Function
Dunker, A. K., Brown, C. J., Lawson, J. D., Iakoucheva, L. M., & Obradović, Z. (2002) · Biochemistry · doi:10.1021/bi012159+ · Cited by 1,731
Self-citationThe protein trinity—linking function and disorder
Dunker, A. K., & Obradovic, Z. (2001) · Nature Biotechnology · doi:10.1038/nbt0901-805 · Cited by 581
Self-citationRomero, P. R., Zaidi, S., Fang, Y. Y., Uversky, V. N., Radivojac, P., Oldfield, C. J., Cortese, M. S., Sickmeier, M., LeGall, T., Obradovic, Z., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507916103 · Cited by 480
Self-citationLinear motifs: Evolutionary interaction switches
Neduva, V., & Russell, R. B. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.04.005 · Cited by 352
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Oldfield, C. J., & Dunker, A. K. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-164947 · Cited by 1,057
Self-citationD2P2: database of disordered protein predictions
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Self-citationMolecular Dynamics Simulations in Drug Discovery and Pharmaceutical Development
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Metadata
- Authors
- Sickmeier, M., Hamilton, J. A., LeGall, T., Vacic, V., Cortese, M. S., Tantos, A., Szabo, B., Tompa, P., Chen, J., Uversky, V. N., Obradovic, Z., & Dunker, A. K.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2007-01-03
- Volume
- 35
- Issue
- Database
- Pages
- D786-D793
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2144252381
- Cited by
- 797
- References
- 4
- FWCI
- 13.26
- Type
- journal article
- Language
- en
- Open access
- gold
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- Sickmeier, M., Hamilton, J. A., LeGall, T., Vacic, V., Cortese, M. S., Tantos, A., Szabo, B., Tompa, P., Chen, J., Uversky, V. N., Obradovic, Z., & Dunker, A. K. (2007). DisProt: the Database of Disordered Proteins. Nucleic Acids Research. https://doi.org/10.1093/nar/gkl893
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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