DisProt: the Database of Disordered Proteins.

@article{citeulike:1245533, abstract = {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.}, address = {Department of Biochemistry and Molecular Biology, Center for Computational Biology and Bioinformatics, Indiana University School of Medicine, Indianapolis, IN 46202, USA.}, author = {Sickmeier, M. and Hamilton, J. A. and LeGall, T. and Vacic, V. and Cortese, M. S. and Tantos, A. and Szabo, B. and Tompa, P. and Chen, J. and Uversky, V. N. and Obradovic, Z. and Dunker, A. K. }, citeulike-article-id = {1245533}, issn = {1362-4962}, journal = {Nucleic Acids Res}, keywords = {protein-folding, protein-interaction, web-server}, month = {January}, number = {Database issue}, posted-at = {2008-05-30 06:37:27}, priority = {3}, title = {DisProt: the Database of Disordered Proteins.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/17145717}, volume = {35}, year = {2007} }

TY - JOUR ID - citeulike:1245533 L3 - citeulike-article-id:1245533 TI - DisProt: the Database of Disordered Proteins. JF - Nucleic Acids Res VL - 35 IS - Database issue AD - Department of Biochemistry and Molecular Biology, Center for Computational Biology and Bioinformatics, Indiana University School of Medicine, Indianapolis, IN 46202, USA. SN - 1362-4962 N2 - 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. KW - protein-folding KW - protein-interaction KW - web-server AU - Sickmeier, M AU - Hamilton, JA AU - LeGall, T AU - Vacic, V AU - Cortese, MS AU - Tantos, A AU - Szabo, B AU - Tompa, P AU - Chen, J AU - Uversky, VN AU - Obradovic, Z AU - Dunker, AK PY - 2007/01// UR - http://view.ncbi.nlm.nih.gov/pubmed/17145717 ER -