{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,4]],"date-time":"2026-08-04T00:04:13Z","timestamp":1785801853714,"version":"3.56.0"},"reference-count":22,"publisher":"Oxford University Press (OUP)","issue":"22-23","license":[{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"name":"European Union\u2019s Horizon 2020 research and innovation programme"},{"name":"Marie Sk\u0142odowska-Curie","award":["778247"],"award-info":[{"award-number":["778247"]}]},{"name":"Italian Ministry of University and Research","award":["2017483NH8"],"award-info":[{"award-number":["2017483NH8"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,4,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:sec>\n                  <jats:title>Motivation<\/jats:title>\n                  <jats:p>The earlier version of MobiDB-lite is currently used in large-scale proteome annotation platforms to detect intrinsic disorder. However, new theoretical models allow for the classification of intrinsically disordered regions into subtypes from sequence features associated with specific polymeric properties or compositional bias.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Results<\/jats:title>\n                  <jats:p>MobiDB-lite 3.0 maintains its previous speed and performance but also provides a finer classification of disorder by identifying regions with characteristics of polyolyampholytes, positive or negative polyelectrolytes, low-complexity regions or enriched in cysteine, proline or glycine or polar residues. Subregions are abundantly detected in IDRs of the human proteome. The new version of MobiDB-lite represents a new step for the proteome level analysis of protein disorder.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Availability and implementation<\/jats:title>\n                  <jats:p>Both the MobiDB-lite 3.0 source code and a docker container are available from the GitHub repository: https:\/\/github.com\/BioComputingUP\/MobiDB-lite<\/jats:p>\n               <\/jats:sec>","DOI":"10.1093\/bioinformatics\/btaa1045","type":"journal-article","created":{"date-parts":[[2020,12,8]],"date-time":"2020-12-08T03:55:05Z","timestamp":1607399705000},"page":"5533-5534","source":"Crossref","is-referenced-by-count":77,"title":["MobiDB-lite 3.0: fast consensus annotation of intrinsic disorder flavors in proteins"],"prefix":"10.1093","volume":"36","author":[{"given":"Marco","family":"Necci","sequence":"first","affiliation":[{"name":"Department of Biomedical Sciences, University of Padua , 35121 Padova, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Damiano","family":"Piovesan","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences, University of Padua , 35121 Padova, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Damiano","family":"Clementel","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences, University of Padua , 35121 Padova, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zsuzsanna","family":"Doszt\u00e1nyi","sequence":"additional","affiliation":[{"name":"MTA-ELTE Lend\u00fclet Bioinformatics Research Group, Department of Biochemistry, ELTE E\u00f6tv\u00f6s Lor\u00e1nd University , Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4525-7793","authenticated-orcid":false,"given":"Silvio C E","family":"Tosatto","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences, University of Padua , 35121 Padova, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2020,12,16]]},"reference":[{"key":"2023062708410124200_btaa1045-B1","doi-asserted-by":"crossref","first-page":"13392","DOI":"10.1073\/pnas.1304749110","article-title":"Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues","volume":"110","author":"Das","year":"2013","journal-title":"Proc. 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