{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,23]],"date-time":"2025-10-23T20:53:12Z","timestamp":1761252792397},"reference-count":34,"publisher":"World Scientific Pub Co Pte Lt","issue":"02","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Bioinform. Comput. Biol."],"published-print":{"date-parts":[[2013,4]]},"abstract":"<jats:p> This is a study on the precision of four known protein disorder predictors, ranked among the best-performing ones: DISOPRED2, PONDR VSL2B, IUPred and ESpritz. We address here the problem of a systematic overestimation of the number of disordered proteins recognized through the use of these predictors, considered as a standard. Some of these predictors, used with their default setting, have a low precision, implying a tendency to overestimate the occurrence of disordered proteins in genome-wide surveys. Moreover, different predictors often disagree on the evaluation of individual proteins. To cope with this problem and in order to propose a simple procedure that enhances precision based on precision-recall curves, we re-tuned the discriminative thresholds of the predictors by training and cross-validating their performance on a cured dataset. After re-tuning, both the disagreement among predictors and the tendency to overestimate the occurrence of disordered proteins are reduced. This is shown in a dedicated study over the human proteome and a set of cancer-related human proteins, with no a priori disorder annotation. Simple quantitative estimates suggest that the occurrence of disorder among cancer-related proteins and other similar large-scale surveys has been overestimated in the past. <\/jats:p>","DOI":"10.1142\/s0219720012500230","type":"journal-article","created":{"date-parts":[[2012,10,2]],"date-time":"2012-10-02T09:40:57Z","timestamp":1349170857000},"page":"1250023","source":"Crossref","is-referenced-by-count":3,"title":["TUNING THE PRECISION OF PREDICTORS TO REDUCE OVERESTIMATION OF PROTEIN DISORDER OVER LARGE DATASETS"],"prefix":"10.1142","volume":"11","author":[{"given":"ANTONIO","family":"DEIANA","sequence":"first","affiliation":[{"name":"Physics Department, Sapienza University of Rome, Rome, Italy"}]},{"given":"ANDREA","family":"GIANSANTI","sequence":"additional","affiliation":[{"name":"Physics Department, Sapienza University of Rome, Rome, Italy"},{"name":"INFN, Sezione di Roma1, Roma, 00185, Italy"}]}],"member":"219","published-online":{"date-parts":[[2013,4,21]]},"reference":[{"key":"rf1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbapap.2010.01.017"},{"key":"rf2","volume-title":"Structure and Function of Intrinsically Disordered Proteins","author":"Tompa P.","year":"2010"},{"key":"rf3","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2164-9-S2-S1"},{"key":"rf4","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biophys.37.032807.125924"},{"key":"rf5","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2164-10-S1-S7"},{"key":"rf6","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(02)00969-5"},{"key":"rf7","doi-asserted-by":"publisher","DOI":"10.1021\/bi060981d"},{"key":"rf8","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0005566"},{"key":"rf9","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2164-10-S1-S12"},{"key":"rf10","doi-asserted-by":"publisher","DOI":"10.2174\/156720508784533312"},{"key":"rf11","doi-asserted-by":"publisher","DOI":"10.1002\/9783527619498.ch41"},{"key":"rf12","doi-asserted-by":"publisher","DOI":"10.1002\/prot.21075"},{"key":"rf13","first-page":"225","volume":"2","author":"Dosztanyi Z.","journal-title":"Brief. 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