{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,16]],"date-time":"2026-01-16T19:09:41Z","timestamp":1768590581857,"version":"3.49.0"},"reference-count":18,"publisher":"Oxford University Press (OUP)","issue":"1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2005,1,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Summary: The Database of Protein Disorder (DisProt) is a curated database that provides structure and function information about proteins that lack a fixed three-dimensional (3D) structure under putatively native conditions, either in their entirety or in part. Starting from the central premise that intrinsic disorder is an important structural class of protein and in order to meet the increasing interest thereof, DisProt is aimed at becoming a central repository of disorder-related information. For each disordered protein, the database includes the name of the protein, various aliases, accession codes, amino acid sequence, location of the disordered region(s), and methods used for structural (disorder) characterization. If applicable, most entries also list the biological function(s) of each disordered region, how each region of disorder is used for function, as well as provide links to PubMed abstracts and major protein databases.<\/jats:p>\n               <jats:p>Availability: \u00a0www.disprot.org<\/jats:p>\n               <jats:p>Contact: \u00a0kedunker@iupui.edu<\/jats:p>","DOI":"10.1093\/bioinformatics\/bth476","type":"journal-article","created":{"date-parts":[[2004,8,14]],"date-time":"2004-08-14T01:32:45Z","timestamp":1092447165000},"page":"137-140","source":"Crossref","is-referenced-by-count":185,"title":["DisProt: a database of protein disorder"],"prefix":"10.1093","volume":"21","author":[{"given":"Slobodan","family":"Vucetic","sequence":"first","affiliation":[]},{"given":"Zoran","family":"Obradovic","sequence":"additional","affiliation":[]},{"given":"Vladimir","family":"Vacic","sequence":"additional","affiliation":[]},{"given":"Predrag","family":"Radivojac","sequence":"additional","affiliation":[]},{"given":"Kang","family":"Peng","sequence":"additional","affiliation":[]},{"given":"Lilia M.","family":"Iakoucheva","sequence":"additional","affiliation":[]},{"given":"Marc S.","family":"Cortese","sequence":"additional","affiliation":[]},{"given":"J. David","family":"Lawson","sequence":"additional","affiliation":[]},{"given":"Celeste J.","family":"Brown","sequence":"additional","affiliation":[]},{"given":"Jason G.","family":"Sikes","sequence":"additional","affiliation":[]},{"given":"Crystal D.","family":"Newton","sequence":"additional","affiliation":[]},{"given":"A. Keith","family":"Dunker","sequence":"additional","affiliation":[]}],"member":"286","published-online":{"date-parts":[[2004,8,13]]},"reference":[{"key":"2023013107192138500_B1","doi-asserted-by":"crossref","unstructured":"Bracken, C. 2001NMR spin relaxation methods for characterization of disorder and folding in proteins. J. Mol. Graph. Model.193\u201312","DOI":"10.1016\/S1093-3263(00)00136-4"},{"key":"2023013107192138500_B2","unstructured":"Daughdrill, G.W., Pielak, G.J., Uversky, V.N., Cortese, M.S., Dunker, A.K. In Buchner, J and Kiefhaber, T.1 (Eds.). 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