{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,10]],"date-time":"2026-04-10T03:32:04Z","timestamp":1775791924827,"version":"3.50.1"},"reference-count":19,"publisher":"Oxford University Press (OUP)","issue":"9","license":[{"start":{"date-parts":[[2017,1,16]],"date-time":"2017-01-16T00:00:00Z","timestamp":1484524800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/about_us\/legal\/notices"}],"funder":[{"DOI":"10.13039\/501100007076","name":"Fondazione Italiana per la Ricerca sul Cancro","doi-asserted-by":"publisher","award":["16621"],"award-info":[{"award-number":["16621"]}],"id":[{"id":"10.13039\/501100007076","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005010","name":"Associazione Italiana per la Ricerca sul Cancro","doi-asserted-by":"publisher","award":["IG17753"],"award-info":[{"award-number":["IG17753"]}],"id":[{"id":"10.13039\/501100005010","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Hungarian Academy of Sciences \u2018Lend\u00fclet\u2019","award":["LP201418\/2016"],"award-info":[{"award-number":["LP201418\/2016"]}]},{"DOI":"10.13039\/501100003549","name":"Hungarian Scientific Research Fund","doi-asserted-by":"crossref","award":["OTKA K 108798"],"award-info":[{"award-number":["OTKA K 108798"]}],"id":[{"id":"10.13039\/501100003549","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2017,5,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:sec>\n                  <jats:title>Motivation<\/jats:title>\n                  <jats:p>Intrinsic disorder (ID) is established as an important feature of protein sequences. Its use in proteome annotation is however hampered by the availability of many methods with similar performance at the single residue level, which have mostly not been optimized to predict long ID regions of size comparable to domains.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Results<\/jats:title>\n                  <jats:p>Here, we have focused on providing a single consensus-based prediction, MobiDB-lite, optimized for highly specific (i.e. few false positive) predictions of long disorder. The method uses eight different predictors to derive a consensus which is then filtered for spurious short predictions. Consensus prediction is shown to outperform the single methods when annotating long ID regions. MobiDB-lite can be useful in large-scale annotation scenarios and has indeed already been integrated in the MobiDB, DisProt and InterPro databases.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Availability and Implementation<\/jats:title>\n                  <jats:p>MobiDB-lite is available as part of the MobiDB database from URL: http:\/\/mobidb.bio.unipd.it\/. An executable can be downloaded from URL: http:\/\/protein.bio.unipd.it\/mobidblite\/.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Supplementary information<\/jats:title>\n                  <jats:p>Supplementary data are available at Bioinformatics online.<\/jats:p>\n               <\/jats:sec>","DOI":"10.1093\/bioinformatics\/btx015","type":"journal-article","created":{"date-parts":[[2017,1,20]],"date-time":"2017-01-20T01:23:50Z","timestamp":1484875430000},"page":"1402-1404","source":"Crossref","is-referenced-by-count":206,"title":["MobiDB-lite: fast and highly specific consensus prediction of intrinsic disorder in proteins"],"prefix":"10.1093","volume":"33","author":[{"given":"Marco","family":"Necci","sequence":"first","affiliation":[{"name":"Department of Biomedical Sciences, University of Padua, Padova, Italy"},{"name":"Fondazione Edmund Mach, San Michele all'Adige, Italy"}]},{"given":"Damiano","family":"Piovesan","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences, University of Padua, Padova, Italy"}]},{"given":"Zsuzsanna","family":"Doszt\u00e1nyi","sequence":"additional","affiliation":[{"name":"MTA-ELTE Lend\u00fclet Bioinformatics Research Group, Department of Biochemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary"},{"name":"Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary"}]},{"given":"Silvio C.E","family":"Tosatto","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences, University of Padua, Padova, Italy"},{"name":"CNR Institute of Neuroscience, Padova, Italy"}]}],"member":"286","published-online":{"date-parts":[[2017,1,16]]},"reference":[{"key":"2023020205032712700_btx015-B1","doi-asserted-by":"crossref","first-page":"2080","DOI":"10.1093\/bioinformatics\/bts327","article-title":"MobiDB: a comprehensive database of intrinsic protein disorder annotations","volume":"28","author":"Di Domenico","year":"2012","journal-title":"Bioinformatics"},{"key":"2023020205032712700_btx015-B2","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1093\/bib\/bbp061","article-title":"Bioinformatical approaches to characterize intrinsically disordered\/unstructured proteins","volume":"11","author":"Doszt\u00e1nyi","year":"2010","journal-title":"Brief. 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