{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,24]],"date-time":"2026-03-24T03:57:54Z","timestamp":1774324674534,"version":"3.50.1"},"reference-count":59,"publisher":"Oxford University Press (OUP)","issue":"D1","license":[{"start":{"date-parts":[[2020,10,29]],"date-time":"2020-10-29T00:00:00Z","timestamp":1603929600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"name":"National Research, Development and Innovation Office","award":["NKFIH 127961"],"award-info":[{"award-number":["NKFIH 127961"]}]},{"name":"Higher Education Institutional Excellence Programme of the Ministry for Innovation and Technology in Hungary"},{"DOI":"10.13039\/501100002332","name":"Semmelweis University","doi-asserted-by":"publisher","award":["EFOP-3.6.3-VEKOP-16-2017-00009"],"award-info":[{"award-number":["EFOP-3.6.3-VEKOP-16-2017-00009"]}],"id":[{"id":"10.13039\/501100002332","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,1,8]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Protein and lipid membrane interactions play fundamental roles in a large number of cellular processes (e.g. signalling, vesicle trafficking, or viral invasion). A growing number of examples indicate that such interactions can also rely on intrinsically disordered protein regions (IDRs), which can form specific reversible interactions not only with proteins but also with lipids. We named IDRs involved in such membrane lipid-induced disorder-to-order transition as MemMoRFs, in an analogy to IDRs exhibiting disorder-to-order transition upon interaction with protein partners termed Molecular Recognition Features (MoRFs). Currently, both the experimental detection and computational characterization of MemMoRFs are challenging, and information about these regions are scattered in the literature. To facilitate the related investigations we generated a comprehensive database of experimentally validated MemMoRFs based on manual curation of literature and structural data. To characterize the dynamics of MemMoRFs, secondary structure propensity and flexibility calculated from nuclear magnetic resonance chemical shifts were incorporated into the database. These data were supplemented by inclusion of sentences from papers, functional data and disease-related information. The MemMoRF database can be accessed via a user-friendly interface at https:\/\/memmorf.hegelab.org, potentially providing a central resource for the characterization of disordered regions in transmembrane and membrane-associated proteins.<\/jats:p>","DOI":"10.1093\/nar\/gkaa954","type":"journal-article","created":{"date-parts":[[2020,10,28]],"date-time":"2020-10-28T12:11:42Z","timestamp":1603887102000},"page":"D355-D360","source":"Crossref","is-referenced-by-count":16,"title":["The MemMoRF database for recognizing disordered protein regions interacting with cellular membranes"],"prefix":"10.1093","volume":"49","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4321-9670","authenticated-orcid":false,"given":"Georgina","family":"Csizmadia","sequence":"first","affiliation":[{"name":"Department of Biophysics and Radiation Biology, Semmelweis University, Budapest\u00a01094, Hungary"}]},{"given":"G\u00e1bor","family":"Erd\u0151s","sequence":"additional","affiliation":[{"name":"MTA-ELTE Lend\u00fclet Bioinformatics Research Group, Department of Biochemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest\u00a01117, Hungary"}]},{"given":"Hedvig","family":"Tordai","sequence":"additional","affiliation":[{"name":"Department of Biophysics and Radiation Biology, Semmelweis University, Budapest\u00a01094, Hungary"}]},{"given":"Rita","family":"Pad\u00e1nyi","sequence":"additional","affiliation":[{"name":"Department of Biophysics and Radiation Biology, Semmelweis University, Budapest\u00a01094, Hungary"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4525-7793","authenticated-orcid":false,"given":"Silvio","family":"Tosatto","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences, University of Padua, Padua\u00a035131, Italy"}]},{"given":"Zsuzsanna","family":"Doszt\u00e1nyi","sequence":"additional","affiliation":[{"name":"MTA-ELTE Lend\u00fclet Bioinformatics Research Group, Department of Biochemistry, E\u00f6tv\u00f6s Lor\u00e1nd University, Budapest\u00a01117, Hungary"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5195-749X","authenticated-orcid":false,"given":"Tam\u00e1s","family":"Heged\u0171s","sequence":"additional","affiliation":[{"name":"Department of Biophysics and Radiation Biology, Semmelweis University, Budapest\u00a01094, Hungary"}]}],"member":"286","published-online":{"date-parts":[[2020,10,29]]},"reference":[{"key":"2021010313133745900_B1","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1038\/nchembio.2331","article-title":"Simultaneous quantification of protein order and disorder","volume":"13","author":"Sormanni","year":"2017","journal-title":"Nat. Chem. Biol."},{"key":"2021010313133745900_B2","doi-asserted-by":"crossref","first-page":"6681","DOI":"10.1074\/jbc.R115.685859","article-title":"Dancing protein clouds: the strange biology and chaotic physics of intrinsically disordered proteins","volume":"291","author":"Uversky","year":"2016","journal-title":"J. Biol. Chem."},{"key":"2021010313133745900_B3","doi-asserted-by":"crossref","first-page":"6573","DOI":"10.1021\/bi012159+","article-title":"Intrinsic disorder and protein function","volume":"41","author":"Dunker","year":"2002","journal-title":"Biochemistry"},{"key":"2021010313133745900_B4","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1038\/nrm1589","article-title":"Intrinsically unstructured proteins and their functions","volume":"6","author":"Dyson","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021010313133745900_B5","doi-asserted-by":"crossref","first-page":"6589","DOI":"10.1021\/cr400525m","article-title":"Classification of intrinsically disordered regions and proteins","volume":"114","author":"van\u00a0der\u00a0Lee","year":"2014","journal-title":"Chem. Rev."},{"key":"2021010313133745900_B6","doi-asserted-by":"crossref","first-page":"12454","DOI":"10.1021\/bi050736e","article-title":"Coupled folding and binding with alpha-helix-forming molecular recognition elements","volume":"44","author":"Oldfield","year":"2005","journal-title":"Biochemistry"},{"key":"2021010313133745900_B7","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1016\/j.jmb.2006.07.087","article-title":"Analysis of molecular recognition features (MoRFs)","volume":"362","author":"Mohan","year":"2006","journal-title":"J. Mol. Biol."},{"key":"2021010313133745900_B8","doi-asserted-by":"crossref","first-page":"1952","DOI":"10.1002\/pro.3718","article-title":"Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding","volume":"28","author":"Yang","year":"2019","journal-title":"Protein Sci."},{"key":"2021010313133745900_B9","doi-asserted-by":"crossref","first-page":"2839","DOI":"10.1016\/j.bbamem.2015.08.002","article-title":"Disordered regions in transmembrane proteins","volume":"1848","author":"Tusn\u00e1dy","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"2021010313133745900_B10","doi-asserted-by":"crossref","first-page":"e1602794","DOI":"10.1126\/sciadv.1602794","article-title":"Structural and biochemical differences between the Notch and the amyloid precursor protein transmembrane domains","volume":"3","author":"Deatherage","year":"2017","journal-title":"Sci. Adv"},{"key":"2021010313133745900_B11","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1038\/nmeth.2033","article-title":"Facile backbone structure determination of human membrane proteins by NMR spectroscopy","volume":"9","author":"Klammt","year":"2012","journal-title":"Nat. Methods"},{"key":"2021010313133745900_B12","doi-asserted-by":"crossref","first-page":"4315","DOI":"10.1529\/biophysj.108.134155","article-title":"Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers","volume":"95","author":"L\u00f6w","year":"2008","journal-title":"Biophys. J."},{"key":"2021010313133745900_B13","doi-asserted-by":"crossref","first-page":"9595","DOI":"10.1074\/jbc.M411805200","article-title":"Structure and dynamics of micelle-bound human alpha-synuclein","volume":"280","author":"Ulmer","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2021010313133745900_B14","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1007\/s00726-015-1998-x","article-title":"The N-terminal cytoplasmic domain of neuregulin 1 type III is intrinsically disordered","volume":"47","author":"Chukhlieb","year":"2015","journal-title":"Amino Acids"},{"key":"2021010313133745900_B15","doi-asserted-by":"crossref","first-page":"4094","DOI":"10.1073\/pnas.0400742101","article-title":"Membrane-mediated structural transitions at the cytoplasmic face during integrin activation","volume":"101","author":"Vinogradova","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021010313133745900_B16","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.ymeth.2014.10.014","article-title":"Membrane association of the PTEN tumor suppressor: neutron scattering and MD simulations reveal the structure of protein-membrane complexes","volume":"77-78","author":"Nanda","year":"2015","journal-title":"Methods"},{"key":"2021010313133745900_B17","doi-asserted-by":"crossref","first-page":"24043","DOI":"10.1074\/jbc.M502698200","article-title":"A structural model for the membrane-bound form of the juxtamembrane domain of the epidermal growth factor receptor","volume":"280","author":"Choowongkomon","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2021010313133745900_B18","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.jmb.2015.11.007","article-title":"HER2 transmembrane domain dimerization coupled with self-association of membrane-embedded cytoplasmic juxtamembrane regions","volume":"428","author":"Bragin","year":"2016","journal-title":"J. Mol. Biol."},{"key":"2021010313133745900_B19","doi-asserted-by":"crossref","first-page":"1295","DOI":"10.1038\/srep01295","article-title":"Lipid binding by the Unique and SH3 domains of c-Src suggests a new regulatory mechanism","volume":"3","author":"P\u00e9rez","year":"2013","journal-title":"Sci. Rep."},{"key":"2021010313133745900_B20","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1038\/nature20416","article-title":"The activities of amyloids from a structural perspective","volume":"539","author":"Riek","year":"2016","journal-title":"Nature"},{"key":"2021010313133745900_B21","doi-asserted-by":"crossref","first-page":"6565","DOI":"10.1074\/jbc.M113.527747","article-title":"Structure and immunogenicity of a peptide vaccine, including the complete HIV-1 gp41 2F5 epitope: implications for antibody recognition mechanism and immunogen design","volume":"289","author":"Serrano","year":"2014","journal-title":"J. Biol. Chem."},{"key":"2021010313133745900_B22","doi-asserted-by":"crossref","first-page":"40835","DOI":"10.1074\/jbc.M404761200","article-title":"Structure and function of the membrane anchor domain of hepatitis C virus nonstructural protein 5A","volume":"279","author":"Penin","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2021010313133745900_B23","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1038\/nature06531","article-title":"Structure and mechanism of the M2 proton channel of influenza A virus","volume":"451","author":"Schnell","year":"2008","journal-title":"Nature"},{"key":"2021010313133745900_B24","doi-asserted-by":"crossref","first-page":"14821","DOI":"10.1021\/acs.jpcb.5b07375","article-title":"Conformational changes and association of Membrane-Interacting peptides in myelin membrane models: a case of the C-Terminal peptide of proteolipid protein and the antimicrobial peptide melittin","volume":"119","author":"Appadu","year":"2015","journal-title":"J. Phys. Chem. B"},{"key":"2021010313133745900_B25","doi-asserted-by":"crossref","first-page":"13188","DOI":"10.1021\/bi010902s","article-title":"Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states","volume":"40","author":"Neidigh","year":"2001","journal-title":"Biochemistry"},{"key":"2021010313133745900_B26","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.bbamem.2011.07.040","article-title":"Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy","volume":"1818","author":"Gustavsson","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"2021010313133745900_B27","doi-asserted-by":"crossref","first-page":"108163","DOI":"10.1016\/j.abb.2019.108163","article-title":"Shaping membranes with disordered proteins","volume":"677","author":"Fakhree","year":"2019","journal-title":"Arch. Biochem. Biophys."},{"key":"2021010313133745900_B28","doi-asserted-by":"crossref","first-page":"4152","DOI":"10.1038\/s41467-018-06532-3","article-title":"Synergy between intrinsically disordered domains and structured proteins amplifies membrane curvature sensing","volume":"9","author":"Zeno","year":"2018","journal-title":"Nat. Commun."},{"key":"2021010313133745900_B29","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1038\/80930","article-title":"Phosphorylation of T cell receptor zeta is regulated by a lipid dependent folding transition","volume":"7","author":"Aivazian","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"2021010313133745900_B30","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1007\/s10863-005-9476-x","article-title":"Function of FXYD proteins, regulators of Na, K-ATPase","volume":"37","author":"Geering","year":"2005","journal-title":"J. Bioenerg. Biomembr."},{"key":"2021010313133745900_B31","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1038\/nrm1151","article-title":"Phospholamban: a crucial regulator of cardiac contractility","volume":"4","author":"MacLennan","year":"2003","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021010313133745900_B32","doi-asserted-by":"crossref","first-page":"30181","DOI":"10.1074\/jbc.M113.501585","article-title":"The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum","volume":"288","author":"Akin","year":"2013","journal-title":"J. Biol. Chem."},{"key":"2021010313133745900_B33","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/s12551-014-0157-z","article-title":"Phospholamban phosphorylation, mutation, and structural dynamics: a biophysical approach to understanding and treating cardiomyopathy","volume":"7","author":"Ablorh","year":"2015","journal-title":"Biophys. Rev."},{"key":"2021010313133745900_B34","first-page":"D269","article-title":"DisProt: intrinsic protein disorder annotation in 2020","volume":"48","author":"Hatos","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"2021010313133745900_B35","doi-asserted-by":"crossref","first-page":"D471","DOI":"10.1093\/nar\/gkx1071","article-title":"MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins","volume":"46","author":"Piovesan","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"2021010313133745900_B36","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1093\/bioinformatics\/btx640","article-title":"DIBS: a repository of disordered binding sites mediating interactions with ordered proteins","volume":"34","author":"Schad","year":"2018","journal-title":"Bioinformatics"},{"key":"2021010313133745900_B37","doi-asserted-by":"crossref","first-page":"3682","DOI":"10.1093\/bioinformatics\/btx486","article-title":"MFIB: a repository of protein complexes with mutual folding induced by binding","volume":"33","author":"Fich\u00f3","year":"2017","journal-title":"Bioinformatics"},{"key":"2021010313133745900_B38","doi-asserted-by":"crossref","first-page":"D228","DOI":"10.1093\/nar\/gkw1019","article-title":"FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies","volume":"45","author":"Miskei","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"2021010313133745900_B39","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":"2021010313133745900_B40","doi-asserted-by":"crossref","first-page":"D506","DOI":"10.1093\/nar\/gky1049","article-title":"UniProt: a worldwide hub of protein knowledge","volume":"47","author":"UniProt Consortium","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"2021010313133745900_B41","doi-asserted-by":"crossref","first-page":"2224","DOI":"10.1021\/bi3001825","article-title":"Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts","volume":"51","author":"Camilloni","year":"2012","journal-title":"Biochemistry"},{"key":"2021010313133745900_B42","doi-asserted-by":"crossref","first-page":"14970","DOI":"10.1021\/ja054842f","article-title":"A simple method to predict protein flexibility using secondary chemical shifts","volume":"127","author":"Berjanskii","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"2021010313133745900_B43","doi-asserted-by":"crossref","first-page":"D427","DOI":"10.1093\/nar\/gky995","article-title":"The Pfam protein families database in 2019","volume":"47","author":"El-Gebali","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"2021010313133745900_B44","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1016\/0092-8674(94)90007-8","article-title":"Integrin alpha v beta 3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels","volume":"79","author":"Brooks","year":"1994","journal-title":"Cell"},{"key":"2021010313133745900_B45","doi-asserted-by":"crossref","first-page":"1815","DOI":"10.1172\/JCI118227","article-title":"Antiintegrin alpha v beta 3 blocks human breast cancer growth and angiogenesis in human skin","volume":"96","author":"Brooks","year":"1995","journal-title":"J. Clin. Invest."},{"key":"2021010313133745900_B46","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1186\/s12964-018-0248-8","article-title":"Peptides derived from the integrin \u03b2 cytoplasmic tails inhibit angiogenesis","volume":"16","author":"Cao","year":"2018","journal-title":"Cell Commun. Signal."},{"key":"2021010313133745900_B47","doi-asserted-by":"crossref","first-page":"17729","DOI":"10.1073\/pnas.0909589106","article-title":"Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation","volume":"106","author":"Yang","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021010313133745900_B48","doi-asserted-by":"crossref","first-page":"22481","DOI":"10.1073\/pnas.1015545107","article-title":"NMR analysis of the alphaIIb beta3 cytoplasmic interaction suggests a mechanism for integrin regulation","volume":"107","author":"Metcalf","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021010313133745900_B49","doi-asserted-by":"crossref","first-page":"40943","DOI":"10.1074\/jbc.M111.231951","article-title":"Tyrosine phosphorylation as a conformational switch: a case study of integrin \u03b23 cytoplasmic tail","volume":"286","author":"Deshmukh","year":"2011","journal-title":"J. Biol. Chem."},{"key":"2021010313133745900_B50","first-page":"D296","article-title":"ELM-the eukaryotic linear motif resource in 2020","volume":"48","author":"Kumar","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"2021010313133745900_B51","doi-asserted-by":"crossref","first-page":"D512","DOI":"10.1093\/nar\/gku1267","article-title":"PhosphoSitePlus, 2014: mutations, PTMs and recalibrations","volume":"43","author":"Hornbeck","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"2021010313133745900_B52","doi-asserted-by":"crossref","first-page":"842","DOI":"10.1038\/nsb1096-842","article-title":"Experimentally determined hydrophobicity scale for proteins at membrane interfaces","volume":"3","author":"Wimley","year":"1996","journal-title":"Nat. Struct. Biol."},{"key":"2021010313133745900_B53","doi-asserted-by":"crossref","first-page":"W329","DOI":"10.1093\/nar\/gky384","article-title":"IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding","volume":"46","author":"M\u00e9sz\u00e1ros","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"2021010313133745900_B54","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1038\/nmeth.4499","article-title":"LiteMol suite: interactive web-based visualization of large-scale macromolecular structure data","volume":"14","author":"Sehnal","year":"2017","journal-title":"Nat. Methods"},{"key":"2021010313133745900_B55","doi-asserted-by":"crossref","first-page":"D514","DOI":"10.1093\/nar\/gki033","article-title":"Online Mendelian Inheritance in Man (OMIM), a knowledgebase of human genes and genetic disorders","volume":"33","author":"Hamosh","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"2021010313133745900_B56","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1093\/nar\/29.1.308","article-title":"dbSNP: the NCBI database of genetic variation","volume":"29","author":"Sherry","year":"2001","journal-title":"Nucleic Acids Res."},{"key":"2021010313133745900_B57","doi-asserted-by":"crossref","first-page":"D1074","DOI":"10.1093\/nar\/gkx1037","article-title":"DrugBank 5.0: a major update to the DrugBank database for 2018","volume":"46","author":"Wishart","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"2021010313133745900_B58","doi-asserted-by":"crossref","first-page":"D358","DOI":"10.1093\/nar\/gkt1115","article-title":"The MIntAct project\u2013IntAct as a common curation platform for 11 molecular interaction databases","volume":"42","author":"Orchard","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"2021010313133745900_B59","doi-asserted-by":"crossref","first-page":"D607","DOI":"10.1093\/nar\/gky1131","article-title":"STRING v11: protein-protein association networks with increased coverage, supporting functional discovery in genome-wide experimental datasets","volume":"47","author":"Szklarczyk","year":"2019","journal-title":"Nucleic Acids Res."}],"container-title":["Nucleic Acids Research"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/nar\/article-pdf\/49\/D1\/D355\/35364659\/gkaa954.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/academic.oup.com\/nar\/article-pdf\/49\/D1\/D355\/35364659\/gkaa954.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,1,3]],"date-time":"2021-01-03T18:19:20Z","timestamp":1609697960000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/nar\/article\/49\/D1\/D355\/5943195"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,10,29]]},"references-count":59,"journal-issue":{"issue":"D1","published-online":{"date-parts":[[2020,10,29]]},"published-print":{"date-parts":[[2021,1,8]]}},"URL":"https:\/\/doi.org\/10.1093\/nar\/gkaa954","relation":{},"ISSN":["0305-1048","1362-4962"],"issn-type":[{"value":"0305-1048","type":"print"},{"value":"1362-4962","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2021,1,8]]},"published":{"date-parts":[[2020,10,29]]}}}