{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,6,11]],"date-time":"2025-06-11T05:26:28Z","timestamp":1749619588334},"reference-count":31,"publisher":"Oxford University Press (OUP)","issue":"19","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2013,10,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Summary: Molecular recognition features (MoRFs) are small, intrinsically disordered regions in proteins that undergo a disorder-to-order transition on binding to their partners. MoRFs are involved in protein\u2013protein interactions and may function as the initial step in molecular recognition. The aim of this work was to collect, organize and store all membrane proteins that contain MoRFs. Membrane proteins constitute \u223c30% of fully sequenced proteomes and are responsible for a wide variety of cellular functions. MoRFs were classified according to their secondary structure, after interacting with their partners. We identified MoRFs in transmembrane and peripheral membrane proteins. The position of transmembrane protein MoRFs was determined in relation to a protein\u2019s topology. All information was stored in a publicly available mySQL database with a user-friendly web interface. A Jmol applet is integrated for visualization of the structures. mpMoRFsDB provides valuable information related to disorder-based protein\u2013protein interactions in membrane proteins.<\/jats:p>\n               <jats:p>Availability: \u00a0http:\/\/bioinformatics.biol.uoa.gr\/mpMoRFsDB<\/jats:p>\n               <jats:p>Contact: \u00a0shamodr@biol.uoa.gr<\/jats:p>","DOI":"10.1093\/bioinformatics\/btt427","type":"journal-article","created":{"date-parts":[[2013,7,27]],"date-time":"2013-07-27T06:16:48Z","timestamp":1374905808000},"page":"2517-2518","source":"Crossref","is-referenced-by-count":7,"title":["mpMoRFsDB: a database of molecular recognition features in membrane proteins"],"prefix":"10.1093","volume":"29","author":[{"given":"Foivos","family":"Gypas","sequence":"first","affiliation":[{"name":"Faculty of Biology, Department of Cell Biology and Biophysics, University of Athens, Panepistimiopolis, Athens 157 01, Greece"}]},{"given":"Georgios N.","family":"Tsaousis","sequence":"additional","affiliation":[{"name":"Faculty of Biology, Department of Cell Biology and Biophysics, University of Athens, Panepistimiopolis, Athens 157 01, Greece"}]},{"given":"Stavros J.","family":"Hamodrakas","sequence":"additional","affiliation":[{"name":"Faculty of Biology, Department of Cell Biology and Biophysics, University of Athens, Panepistimiopolis, Athens 157 01, Greece"}]}],"member":"286","published-online":{"date-parts":[[2013,7,26]]},"reference":[{"key":"2023012810471076400_btt427-B1","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1093\/nar\/28.1.235","article-title":"The Protein Data Bank","volume":"28","author":"Berman","year":"2000","journal-title":"Nucleic Acids Res."},{"key":"2023012810471076400_btt427-B2","doi-asserted-by":"crossref","first-page":"13468","DOI":"10.1021\/bi7012273","article-title":"Mining alpha-helix-forming molecular recognition features with cross species sequence alignments","volume":"46","author":"Cheng","year":"2007","journal-title":"Biochemistry"},{"key":"2023012810471076400_btt427-B3","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":"2023012810471076400_btt427-B4","doi-asserted-by":"crossref","first-page":"1042","DOI":"10.1126\/science.1219021","article-title":"The protein-folding problem, 50 years on","volume":"338","author":"Dill","year":"2012","journal-title":"Science"},{"key":"2023012810471076400_btt427-B5","doi-asserted-by":"crossref","first-page":"i75","DOI":"10.1093\/bioinformatics\/bts209","article-title":"MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins","volume":"28","author":"Disfani","year":"2012","journal-title":"Bioinformatics"},{"key":"2023012810471076400_btt427-B6","doi-asserted-by":"crossref","first-page":"2745","DOI":"10.1093\/bioinformatics\/btp518","article-title":"ANCHOR: web server for predicting protein binding regions in disordered proteins","volume":"25","author":"Dosztanyi","year":"2009","journal-title":"Bioinformatics"},{"key":"2023012810471076400_btt427-B7","first-page":"161","article-title":"Intrinsic protein disorder in complete genomes","volume":"11","author":"Dunker","year":"2000","journal-title":"Genome Inform."},{"key":"2023012810471076400_btt427-B8","doi-asserted-by":"crossref","first-page":"D507","DOI":"10.1093\/nar\/gkr884","article-title":"IDEAL: intrinsically disordered proteins with extensive annotations and literature","volume":"40","author":"Fukuchi","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"2023012810471076400_btt427-B9","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1107\/S0021889810030256","article-title":"Jmol \u2013 a paradigm shift in crystallographic visualization","volume":"43","author":"Hanson","year":"2010","journal-title":"J. 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