{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T16:47:55Z","timestamp":1762102075509,"version":"3.37.3"},"reference-count":72,"publisher":"Oxford University Press (OUP)","issue":"23","license":[{"start":{"date-parts":[[2017,8,16]],"date-time":"2017-08-16T00:00:00Z","timestamp":1502841600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/about_us\/legal\/notices"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31671369","31270834","61272318","11175224","11121403","31270909","31770775"],"award-info":[{"award-number":["31671369","31270834","61272318","11175224","11121403","31270909","31770775"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2017,12,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:sec>\n                  <jats:title>Motivation<\/jats:title>\n                  <jats:p>Accurate recognition of protein fold types is a key step for template-based prediction of protein structures. The existing approaches to fold recognition mainly exploit the features derived from alignments of query protein against templates. These approaches have been shown to be successful for fold recognition at family level, but usually failed at superfamily\/fold levels. To overcome this limitation, one of the key points is to explore more structurally informative features of proteins. Although residue\u2013residue contacts carry abundant structural information, how to thoroughly exploit these information for fold recognition still remains a challenge.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Results<\/jats:title>\n                  <jats:p>In this study, we present an approach (called DeepFR) to improve fold recognition at superfamily\/fold levels. The basic idea of our approach is to extract fold-specific features from predicted residue\u2013residue contacts of proteins using deep convolutional neural network (DCNN) technique. Based on these fold-specific features, we calculated similarity between query protein and templates, and then assigned query protein with fold type of the most similar template. DCNN has showed excellent performance in image feature extraction and image recognition; the rational underlying the application of DCNN for fold recognition is that contact likelihood maps are essentially analogy to images, as they both display compositional hierarchy. Experimental results on the LINDAHL dataset suggest that even using the extracted fold-specific features alone, our approach achieved success rate comparable to the state-of-the-art approaches. When further combining these features with traditional alignment-related features, the success rate of our approach increased to 92.3%, 82.5% and 78.8% at family, superfamily and fold levels, respectively, which is about 18% higher than the state-of-the-art approach at fold level, 6% higher at superfamily level and 1% higher at family level. An independent assessment on SCOP_TEST dataset showed consistent performance improvement, indicating robustness of our approach. Furthermore, bi-clustering results of the extracted features are compatible with fold hierarchy of proteins, implying that these features are fold-specific. Together, these results suggest that the features extracted from predicted contacts are orthogonal to alignment-related features, and the combination of them could greatly facilitate fold recognition at superfamily\/fold levels and template-based prediction of protein structures.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Availability and implementation<\/jats:title>\n                  <jats:p>Source code of DeepFR is freely available through https:\/\/github.com\/zhujianwei31415\/deepfr, and a web server is available through http:\/\/protein.ict.ac.cn\/deepfr.<\/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\/btx514","type":"journal-article","created":{"date-parts":[[2017,8,9]],"date-time":"2017-08-09T19:13:47Z","timestamp":1502306027000},"page":"3749-3757","source":"Crossref","is-referenced-by-count":47,"title":["Improving protein fold recognition by extracting fold-specific features from predicted residue\u2013residue contacts"],"prefix":"10.1093","volume":"33","author":[{"given":"Jianwei","family":"Zhu","sequence":"first","affiliation":[{"name":"Key Lab of Intelligent Information Processing, Institute of Computing Technology, Chinese Academy of Sciences, Beijing, China"},{"name":"University of Chinese Academy of Sciences, Beijing, China"}]},{"given":"Haicang","family":"Zhang","sequence":"additional","affiliation":[{"name":"Key Lab of Intelligent Information Processing, Institute of Computing Technology, Chinese Academy of Sciences, Beijing, China"}]},{"given":"Shuai Cheng","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Computer Science, City University of Hong Kong, Kowloon, Hong Kong"}]},{"given":"Chao","family":"Wang","sequence":"additional","affiliation":[{"name":"Key Lab of Intelligent Information Processing, Institute of Computing Technology, Chinese Academy of Sciences, Beijing, China"}]},{"given":"Lupeng","family":"Kong","sequence":"additional","affiliation":[{"name":"Key Lab of Intelligent Information Processing, Institute of Computing Technology, Chinese Academy of Sciences, Beijing, China"},{"name":"University of Chinese Academy of Sciences, Beijing, China"}]},{"given":"Shiwei","family":"Sun","sequence":"additional","affiliation":[{"name":"Key Lab of Intelligent Information Processing, Institute of Computing Technology, Chinese Academy of Sciences, Beijing, China"}]},{"given":"Wei-Mou","family":"Zheng","sequence":"additional","affiliation":[{"name":"Institute of Theoretical Physics, Chinese Academy of Sciences, Beijing, China"}]},{"given":"Dongbo","family":"Bu","sequence":"additional","affiliation":[{"name":"Key Lab of Intelligent Information Processing, Institute of Computing Technology, Chinese Academy of Sciences, Beijing, China"}]}],"member":"286","published-online":{"date-parts":[[2017,8,16]]},"reference":[{"key":"2023020207003984800_btx514-B1","doi-asserted-by":"crossref","first-page":"1436","DOI":"10.1002\/prot.24829","article-title":"CONFOLD: residue\u2013residue contact-guided ab initio protein folding","volume":"83","author":"Adhikari","year":"2015","journal-title":"Proteins Struct. 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