{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,5]],"date-time":"2026-07-05T04:10:21Z","timestamp":1783224621900,"version":"3.54.6"},"reference-count":18,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2017,10,9]],"date-time":"2017-10-09T00:00:00Z","timestamp":1507507200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"DOI":"10.13039\/100004410","name":"European Molecular Biology Organization","doi-asserted-by":"publisher","award":["ALTF 702-2015"],"award-info":[{"award-number":["ALTF 702-2015"]}],"id":[{"id":"10.13039\/100004410","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003549","name":"OTKA","doi-asserted-by":"publisher","award":["K115698"],"award-info":[{"award-number":["K115698"]}],"id":[{"id":"10.13039\/501100003549","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003549","name":"OTKA","doi-asserted-by":"publisher","award":["OTKA K108798"],"award-info":[{"award-number":["OTKA K108798"]}],"id":[{"id":"10.13039\/501100003549","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003825","name":"Hungarian Academy of Sciences","doi-asserted-by":"publisher","award":["LP2014-18"],"award-info":[{"award-number":["LP2014-18"]}],"id":[{"id":"10.13039\/501100003825","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2018,2,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:sec>\n                  <jats:title>Motivation<\/jats:title>\n                  <jats:p>Intrinsically Disordered Proteins (IDPs) mediate crucial protein\u2013protein interactions, most notably in signaling and regulation. As their importance is increasingly recognized, the detailed analyses of specific IDP interactions opened up new opportunities for therapeutic targeting. Yet, large scale information about IDP-mediated interactions in structural and functional details are lacking, hindering the understanding of the mechanisms underlying this distinct binding mode.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Results<\/jats:title>\n                  <jats:p>Here, we present DIBS, the first comprehensive, curated collection of complexes between IDPs and ordered proteins. DIBS not only describes by far the highest number of cases, it also provides the dissociation constants of their interactions, as well as the description of potential post-translational modifications modulating the binding strength and linear motifs involved in the binding. Together with the wide range of structural and functional annotations, DIBS will provide the cornerstone for structural and functional studies of IDP complexes.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Availability and implementation<\/jats:title>\n                  <jats:p>DIBS is freely accessible at http:\/\/dibs.enzim.ttk.mta.hu\/. The DIBS application is hosted by Apache web server and was implemented in PHP. To enrich querying features and to enhance backend performance a MySQL database was also created.<\/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\/btx640","type":"journal-article","created":{"date-parts":[[2017,10,6]],"date-time":"2017-10-06T19:12:01Z","timestamp":1507317121000},"page":"535-537","source":"Crossref","is-referenced-by-count":90,"title":["DIBS: a repository of disordered binding sites mediating interactions with ordered proteins"],"prefix":"10.1093","volume":"34","author":[{"given":"Eva","family":"Schad","sequence":"first","affiliation":[{"name":"Research Centre for Natural Sciences, Institute of Enzymology, Hungarian Academy of Sciences, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erzs\u00e9bet","family":"Fich\u00f3","sequence":"additional","affiliation":[{"name":"Research Centre for Natural Sciences, Institute of Enzymology, Hungarian Academy of Sciences, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rita","family":"Pancsa","sequence":"additional","affiliation":[{"name":"MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Istv\u00e1n","family":"Simon","sequence":"additional","affiliation":[{"name":"Research Centre for Natural Sciences, Institute of Enzymology, Hungarian Academy of Sciences, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zsuzsanna","family":"Doszt\u00e1nyi","sequence":"additional","affiliation":[{"name":"MTA-ELTE Momentum Bioinformatics Research Group, Department of Biochemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B\u00e1lint","family":"M\u00e9sz\u00e1ros","sequence":"additional","affiliation":[{"name":"Research Centre for Natural Sciences, Institute of Enzymology, Hungarian Academy of Sciences, Budapest, Hungary"},{"name":"MTA-ELTE Momentum Bioinformatics Research Group, Department of Biochemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2017,10,9]]},"reference":[{"key":"2023012712320965000_btx640-B1","doi-asserted-by":"crossref","first-page":"e1003782","DOI":"10.1371\/journal.pcbi.1003782","article-title":"Specificity and affinity quantification of flexible recognition from underlying energy landscape topography","volume":"10","author":"Chu","year":"2014","journal-title":"PLoS Comput. 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