{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,17]],"date-time":"2026-07-17T12:20:58Z","timestamp":1784290858382,"version":"3.55.0"},"reference-count":60,"publisher":"Oxford University Press (OUP)","issue":"20","license":[{"start":{"date-parts":[[2021,5,12]],"date-time":"2021-05-12T00:00:00Z","timestamp":1620777600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["62072199"],"award-info":[{"award-number":["62072199"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31670724"],"award-info":[{"award-number":["31670724"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003397","name":"Huazhong University of Science and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003397","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,10,25]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Motivation<\/jats:title>\n                    <jats:p>Advances in microscopy instruments and image processing algorithms have led to an increasing number of Cryo-electron microscopy (cryo-EM) maps. However, building accurate models for the EM maps at 3\u20135\u2009\u00c5 resolution remains a challenging and time-consuming process. With the rapid growth of deposited EM maps, there is an increasing gap between the maps and reconstructed\/modeled three-dimensional (3D) structures. Therefore, automatic reconstruction of atomic-accuracy full-atom structures from EM maps is pressingly needed.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>We present a semi-automatic de novo structure determination method using a deep learning-based framework, named as DeepMM, which builds atomic-accuracy all-atom models from cryo-EM maps at near-atomic resolution. In our method, the main-chain and C\u03b1 positions as well as their amino acid and secondary structure types are predicted in the EM map using Densely Connected Convolutional Networks. DeepMM was extensively validated on 40 simulated maps at 5\u2009\u00c5 resolution and 30 experimental maps at 2.6\u20134.8\u2009\u00c5 resolution as well as an Electron Microscopy Data Bank-wide dataset of 2931 experimental maps at 2.6\u20134.9\u2009\u00c5 resolution, and compared with state-of-the-art algorithms including RosettaES, MAINMAST and Phenix. Overall, our DeepMM algorithm obtained a significant improvement over existing methods in terms of both accuracy and coverage in building full-length protein structures on all test sets, demonstrating the efficacy and general applicability of DeepMM.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Availability and implementation<\/jats:title>\n                    <jats:p>http:\/\/huanglab.phys.hust.edu.cn\/DeepMM.<\/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\/btab357","type":"journal-article","created":{"date-parts":[[2021,5,8]],"date-time":"2021-05-08T08:33:38Z","timestamp":1620462818000},"page":"3480-3490","source":"Crossref","is-referenced-by-count":36,"title":["Full-length\n                    <i>de novo<\/i>\n                    protein structure determination from cryo-EM maps using deep learning"],"prefix":"10.1093","volume":"37","author":[{"given":"Jiahua","family":"He","sequence":"first","affiliation":[{"name":"School of Physics, Huazhong University of Science and Technology , Wuhan, Hubei 430074, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4209-4565","authenticated-orcid":false,"given":"Sheng-You","family":"Huang","sequence":"additional","affiliation":[{"name":"School of Physics, Huazhong University of Science and Technology , Wuhan, Hubei 430074, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2021,5,12]]},"reference":[{"key":"2023051609024775400_btab357-B1","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"2023051609024775400_btab357-B2","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1107\/S2059798318006551","article-title":"Real-space refinement in PHENIX for cryo-EM and crystallography","volume":"74","author":"Afonine","year":"2018","journal-title":"Acta Crystallogr. D Struct. Biol"},{"key":"2023051609024775400_btab357-B3","doi-asserted-by":"crossref","first-page":"814","DOI":"10.1107\/S2059798318009324","article-title":"New tools for the analysis and validation of cryo-EM maps and atomic models","volume":"74","author":"Afonine","year":"2018","journal-title":"Acta Crystallogr. D Struct. Biol"},{"key":"2023051609024775400_btab357-B4","doi-asserted-by":"crossref","first-page":"82","DOI":"10.3390\/molecules25010082","article-title":"Advances in structure modeling methods for cryo-electron microscopy maps","volume":"25","author":"Alnabati","year":"2019","journal-title":"Molecules (Basel, Switzerland)"},{"key":"2023051609024775400_btab357-B5","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/j.jsb.2011.01.015","article-title":"Modeling protein structure at near atomic resolutions with Gorgon","volume":"174","author":"Baker","year":"2011","journal-title":"J. Struct. Biol"},{"key":"2023051609024775400_btab357-B6","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/j.str.2012.01.008","article-title":"Constructing and validating initial C\u03b1 models from subnanometer resolution density maps with Pathwalking","volume":"20","author":"Baker","year":"2012","journal-title":"Structure (London, England: 1993)"},{"key":"2023051609024775400_btab357-B7","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":"2023051609024775400_btab357-B8","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1002\/jcc.20290","article-title":"The Amber biomolecular simulation programs","volume":"26","author":"Case","year":"2005","journal-title":"J. Comput. Chem"},{"key":"2023051609024775400_btab357-B9","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/j.jsb.2016.06.004","article-title":"De novo modeling in cryo-EM density maps with Pathwalking","volume":"196","author":"Chen","year":"2016","journal-title":"J. Struct. Biol"},{"key":"2023051609024775400_btab357-B10","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1038\/nmeth.4405","article-title":"Convolutional neural networks for automated annotation of cellular cryo-electron tomograms","volume":"14","author":"Chen","year":"2017","journal-title":"Nat. Methods"},{"key":"2023051609024775400_btab357-B11","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1016\/j.jsb.2018.09.005","article-title":"Automation and assessment of de novo modeling with pathwalking in near atomic resolution cryoEM density maps","volume":"204","author":"Chen","year":"2018","journal-title":"J. Struct. Biol"},{"key":"2023051609024775400_btab357-B12","doi-asserted-by":"crossref","first-page":"876","DOI":"10.1126\/science.aat4346","article-title":"Single-particle cryo-EM-How did it get here and where will it go","volume":"361","author":"Cheng","year":"2018","journal-title":"Science (New York, N.Y.)"},{"key":"2023051609024775400_btab357-B13","doi-asserted-by":"crossref","first-page":"D304","DOI":"10.1093\/nar\/gkt1240","article-title":"SCOPe: structural classification of proteins\u2014extended, integrating SCOP and ASTRAL data and classification of new structures","volume":"42","author":"Fox","year":"2014","journal-title":"Nucleic Acids Res"},{"key":"2023051609024775400_btab357-B14","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1038\/nprot.2017.004","article-title":"Advances in the field of single-particle cryo-electron microscopy over the last decade","volume":"12","author":"Frank","year":"2017","journal-title":"Nat. Protoc"},{"key":"2023051609024775400_btab357-B15","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1038\/nmeth.4340","article-title":"RosettaES: a sampling strategy enabling automated interpretation of difficult cryo-EM maps","volume":"14","author":"Frenz","year":"2017","journal-title":"Nat. Methods"},{"key":"2023051609024775400_btab357-B16","doi-asserted-by":"crossref","first-page":"3150","DOI":"10.1093\/bioinformatics\/bts565","article-title":"CD-HIT: accelerated for clustering the next-generation sequencing data","volume":"28","author":"Fu","year":"2012","journal-title":"Bioinformatics"},{"key":"2023051609024775400_btab357-B17","doi-asserted-by":"publisher","DOI":"10.1093\/bib\/bbab156","article-title":"EMNUSS: a deep learning framework for secondary structure annotation in cryo-EM maps","author":"He","year":"2021","journal-title":"Brief. Bioinformatics"},{"key":"2023051609024775400_btab357-B18","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1093\/bioinformatics\/btv665","article-title":"Highly accurate sequence-based prediction of half-sphere exposures of amino acid residues in proteins","volume":"32","author":"Heffernan","year":"2016","journal-title":"Bioinformatics"},{"key":"2023051609024775400_btab357-B19","doi-asserted-by":"crossref","first-page":"W500","DOI":"10.1093\/nar\/gkh429","article-title":"STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins","volume":"32","author":"Heinig","year":"2004","journal-title":"Nucleic Acids Res"},{"key":"2023051609024775400_btab357-B20","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1038\/s41592-019-0637-y","article-title":"Bottom-up structural proteomics: cryoEM of protein complexes enriched from the cellular milieu","volume":"17","author":"Ho","year":"2020","journal-title":"Nat. Methods"},{"key":"2023051609024775400_btab357-B21","doi-asserted-by":"crossref","first-page":"3840","DOI":"10.1038\/s41467-018-06298-8","article-title":"Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin","volume":"9","author":"Hu","year":"2018","journal-title":"Nat. Commun"},{"key":"2023051609024775400_btab357-B22","first-page":"2261","author":"Huang","year":"2017"},{"key":"2023051609024775400_btab357-B23","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1021\/acs.jcim.9b01103","article-title":"Comparing cryo-EM reconstructions and validating atomic model fit using difference maps","volume":"60","author":"Joseph","year":"2020","journal-title":"J. Chem. Inf. Model"},{"key":"2023051609024775400_btab357-B24","doi-asserted-by":"crossref","first-page":"2436","DOI":"10.1021\/acs.jcim.0c00090","article-title":"Practical considerations for atomistic structure modeling with cryo-EM maps","volume":"60","author":"Kim","year":"2020","journal-title":"J. Chem. Inf. Model"},{"key":"2023051609024775400_btab357-B25","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1038\/s41592-020-01051-w","article-title":"Cryo-EM model validation recommendations based on outcomes of the 2019 EMDataResource challenge","volume":"18","author":"Lawson","year":"2021","journal-title":"Nat. Methods"},{"key":"2023051609024775400_btab357-B26","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1038\/nmeth.2472","article-title":"Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM","volume":"10","author":"Li","year":"2013","journal-title":"Nat. Methods"},{"key":"2023051609024775400_btab357-B27","doi-asserted-by":"crossref","first-page":"990","DOI":"10.1016\/j.str.2009.06.001","article-title":"EM-fold: de novo folding of alpha-helical proteins guided by intermediate-resolution electron microscopy density maps","volume":"17","author":"Lindert","year":"2009","journal-title":"Structure (London, England: 1993)"},{"key":"2023051609024775400_btab357-B28","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1038\/s41589-020-0477-1","article-title":"Cryo-electron microscopy for the study of virus assembly","volume":"16","author":"Luque","year":"2020","journal-title":"Nat. Chem. Biol"},{"key":"2023051609024775400_btab357-B29","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1038\/s41592-019-0500-1","article-title":"Protein secondary structure detection in intermediate-resolution cryo-EM maps using deep learning","volume":"16","author":"Maddhuri Venkata Subramaniya","year":"2019","journal-title":"Nat. Methods"},{"key":"2023051609024775400_btab357-B30","doi-asserted-by":"crossref","first-page":"14788","DOI":"10.1002\/anie.202000421","article-title":"Haruspex: a neural network for the automatic identification of oligonucleotides and protein secondary structure in cryo-electron microscopy maps","volume":"59","author":"Mostosi","year":"2020","journal-title":"Angew. Chem"},{"key":"2023051609024775400_btab357-B31","doi-asserted-by":"crossref","first-page":"W24","DOI":"10.1093\/nar\/gkr393","article-title":"CLICK\u2014topology-independent comparison of biomolecular 3D structures","volume":"39","author":"Nguyen","year":"2011","journal-title":"Nucleic Acids Res"},{"key":"2023051609024775400_btab357-B32","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1038\/nature16940","article-title":"Cryo-EM structure of the yeast U4\/U6.U5 tri-snRNP at 3.7 \u00c5 resolution","volume":"530","author":"Nguyen","year":"2016","journal-title":"Nature"},{"key":"2023051609024775400_btab357-B33","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1038\/nmeth.3694","article-title":"The development of cryo-EM into a mainstream structural biology technique","volume":"13","author":"Nogales","year":"2016","journal-title":"Nat. Methods"},{"key":"2023051609024775400_btab357-B34","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1107\/S2059798317004181","article-title":"Trends in the Electron Microscopy Data Bank (EMDB)","volume":"73","author":"Patwardhan","year":"2017","journal-title":"Acta Crystallogr. D Struct. Biol"},{"key":"2023051609024775400_btab357-B35","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1002\/prot.10550","article-title":"Using multiple structure alignments, fast model building, and energetic analysis in fold recognition and homology modeling","volume":"53","author":"Petrey","year":"2003","journal-title":"Proteins"},{"key":"2023051609024775400_btab357-B36","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2014a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem"},{"key":"2023051609024775400_btab357-B37","doi-asserted-by":"crossref","first-page":"e2017525118","DOI":"10.1073\/pnas.2017525118","article-title":"DeepTracer for fast de novo cryo-EM protein structure modeling and special studies on CoV-related complexes","volume":"118","author":"Pfab","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2023051609024775400_btab357-B38","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/j.jsb.2010.03.007","article-title":"Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions","volume":"170","author":"Pintilie","year":"2010","journal-title":"J. Struct. Biol"},{"key":"2023051609024775400_btab357-B39","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1038\/s41592-020-0731-1","article-title":"Measurement of atom resolvability in cryo-EM maps with Q-scores","volume":"17","author":"Pintilie","year":"2020","journal-title":"Nat. Methods"},{"key":"2023051609024775400_btab357-B40","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1038\/nmeth.4169","article-title":"cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination","volume":"14","author":"Punjani","year":"2017","journal-title":"Nat. Methods"},{"key":"2023051609024775400_btab357-B41","doi-asserted-by":"crossref","first-page":"16450","DOI":"10.1002\/anie.201710679","article-title":"Cryo-EM revolutionizes the structure determination of biomolecules","volume":"56","author":"Raunser","year":"2017","journal-title":"Angew. Chem"},{"key":"2023051609024775400_btab357-B42","author":"Ruder","year":"2017"},{"key":"2023051609024775400_btab357-B43","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1016\/j.tcb.2018.06.002","article-title":"Illuminating GPCR signaling by cryo-EM","volume":"28","author":"Safdari","year":"2018","journal-title":"Trends Cell Biol"},{"key":"2023051609024775400_btab357-B44","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.jsb.2012.09.006","article-title":"RELION: implementation of a Bayesian approach to cryo-EM structure determination","volume":"180","author":"Scheres","year":"2012","journal-title":"J. Struct. Biol"},{"key":"2023051609024775400_btab357-B45","doi-asserted-by":"crossref","first-page":"4282","DOI":"10.1038\/s41598-020-60598-y","article-title":"Deep learning to predict protein backbone structure from high-resolution cryo-EM density maps","volume":"10","author":"Si","year":"2020","journal-title":"Sci. Rep"},{"key":"2023051609024775400_btab357-B46","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/0022-2836(81)90087-5","article-title":"Identification of common molecular subsequences","volume":"147","author":"Smith","year":"1981","journal-title":"J. Mol. Biol"},{"key":"2023051609024775400_btab357-B47","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.jsb.2006.05.009","article-title":"EMAN2: an extensible image processing suite for electron microscopy","volume":"157","author":"Tang","year":"2007","journal-title":"J. Struct. Biol"},{"key":"2023051609024775400_btab357-B48","doi-asserted-by":"crossref","first-page":"1146","DOI":"10.1038\/s41592-019-0580-y","article-title":"Real-time cryo-electron microscopy data preprocessing with Warp","volume":"16","author":"Tegunov","year":"2019","journal-title":"Nat. Methods"},{"key":"2023051609024775400_btab357-B49","doi-asserted-by":"crossref","first-page":"1618","DOI":"10.1038\/s41467-018-04053-7","article-title":"De novo main-chain modeling for EM maps using MAINMAST","volume":"9","author":"Terashi","year":"2018","journal-title":"Nat. Commun"},{"key":"2023051609024775400_btab357-B50","doi-asserted-by":"crossref","first-page":"2634","DOI":"10.1021\/acs.jcim.9b01110","article-title":"MAINMASTseg: automated map segmentation method for cryo-EM density maps with symmetry","volume":"60","author":"Terashi","year":"2020","journal-title":"J. Chem. Inf. Model"},{"key":"2023051609024775400_btab357-B51","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1038\/s41592-018-0173-1","article-title":"A fully automatic method yielding initial models from high-resolution cryo-electron microscopy maps","volume":"15","author":"Terwilliger","year":"2018","journal-title":"Nat. Methods"},{"key":"2023051609024775400_btab357-B52","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1002\/pro.3740","article-title":"Cryo-EM map interpretation and protein model-building using iterative map segmentation","volume":"29","author":"Terwilliger","year":"2020","journal-title":"Protein Sci"},{"key":"2023051609024775400_btab357-B53","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1038\/nmeth.3287","article-title":"De novo protein structure determination from near-atomic-resolution cryo-EM maps","volume":"12","author":"Wang","year":"2015","journal-title":"Nat. Methods"},{"key":"2023051609024775400_btab357-B54","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1093\/bioinformatics\/btz609","article-title":"Topology-independent and global protein structure alignment through an FFT-based algorithm","volume":"36","author":"Wen","year":"2020","journal-title":"Bioinformatics"},{"key":"2023051609024775400_btab357-B55","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1006\/jmbi.2001.4865","article-title":"Extending the accuracy limits of prediction for side-chain conformations","volume":"311","author":"Xiang","year":"2001","journal-title":"J. Mol. Biol"},{"key":"2023051609024775400_btab357-B56","doi-asserted-by":"crossref","first-page":"2614","DOI":"10.1021\/acs.jcim.9b01099","article-title":"SPREAD: a fully automated toolkit for single-particle cryogenic electron microscopy data 3D reconstruction with image-network-aided orientation assignment","volume":"60","author":"Xie","year":"2020","journal-title":"J. Chem. Inf. Model"},{"key":"2023051609024775400_btab357-B57","doi-asserted-by":"crossref","first-page":"1303","DOI":"10.1021\/acs.jcim.8b00149","article-title":"Resolution measurement from a single reconstructed cryo-EM density map with multiscale spectral analysis","volume":"58","author":"Yang","year":"2018","journal-title":"J. Chem. Inf. Model"},{"key":"2023051609024775400_btab357-B58","doi-asserted-by":"crossref","first-page":"1658","DOI":"10.1021\/acs.jcim.8b00853","article-title":"Clustering enhancement of noisy cryo-electron microscopy single-particle images with a network structural similarity metric","volume":"59","author":"Yin","year":"2019","journal-title":"J. Chem. Inf. Model"},{"key":"2023051609024775400_btab357-B59","doi-asserted-by":"crossref","first-page":"5365","DOI":"10.1016\/j.jmb.2020.07.027","article-title":"A new protocol for atomic-level protein structure modeling and refinement using low-to-medium resolution cryo-EM density maps","volume":"432","author":"Zhang","year":"2020","journal-title":"J. Mol. Biol"},{"key":"2023051609024775400_btab357-B60","doi-asserted-by":"crossref","first-page":"2302","DOI":"10.1093\/nar\/gki524","article-title":"TM-align: a protein structure alignment algorithm based on the TM-score","volume":"33","author":"Zhang","year":"2005","journal-title":"Nucleic Acids Res"}],"container-title":["Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/bioinformatics\/advance-article-pdf\/doi\/10.1093\/bioinformatics\/btab357\/38490208\/btab357.pdf","content-type":"application\/pdf","content-version":"am","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article-pdf\/37\/20\/3480\/50338411\/btab357.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article-pdf\/37\/20\/3480\/50338411\/btab357.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,16]],"date-time":"2023-05-16T05:04:57Z","timestamp":1684213497000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/bioinformatics\/article\/37\/20\/3480\/6274645"}},"subtitle":[],"editor":[{"given":"Lenore","family":"Cowen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2021,5,12]]},"references-count":60,"journal-issue":{"issue":"20","published-print":{"date-parts":[[2021,10,25]]}},"URL":"https:\/\/doi.org\/10.1093\/bioinformatics\/btab357","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2020.08.28.271981","asserted-by":"object"}]},"ISSN":["1367-4803","1367-4811"],"issn-type":[{"value":"1367-4803","type":"print"},{"value":"1367-4811","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2021,10,15]]},"published":{"date-parts":[[2021,5,12]]}}}