{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,21]],"date-time":"2026-04-21T06:44:28Z","timestamp":1776753868551,"version":"3.51.2"},"reference-count":52,"publisher":"Oxford University Press (OUP)","issue":"5","license":[{"start":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T00:00:00Z","timestamp":1772150400000},"content-version":"vor","delay-in-days":3,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"UW-Madison Center For High Throughput Computing"},{"name":"UW-Madison"},{"name":"Advanced Computing Initiative"},{"DOI":"10.13039\/100001395","name":"Wisconsin Alumni Research Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100001395","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Wisconsin Institutes for Discovery"},{"DOI":"10.13039\/100000001","name":"NSF","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Morgridge Institute for Research"},{"name":"Rowe Center for Research in Virology"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,2,24]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Positive-strand [(+)RNA] viruses replicate their RNA genomes in poorly understood membrane-associated replication organelles (ROs). Cryo-electron microscopy of nodaviral ROs revealed that viral RNA replication protein A, with polymerase and RNA capping domains, forms a \u201ccrown\u201d of two stacked 12-mer rings at the RO\u2019s opening to the cytosol, providing powerful foundations for analyzing RO formation and function. The lower proto-crown is a ring of 12 polymerases with RNA capping domains clustered to form a central floor. The upper crown mirrors the polymerase ring but has RNA capping domains projecting radially outward. Here, we identify a critical protein A \u201celbow\u201d segment of only 17 amino acids that coordinates most interactions between crown floor subunits. Our extensive mutational and genetic complementation analyses reveal that distinct elbow subsegments cooperatively support proto-crown formation and separately activate the neighboring RNA capping and distal polymerase domains. These and other findings establish the elbow as a master regulator whose separable interactions drive proto-crown assembly, license RNA polymerase and capping and, with an adjacent flexible linker, control protein A\u2019s conformational changes. They also further localize RNA capping to the crown floor. This work illuminates (+)RNA viruses\u2019 elegant regulation of genome replication steps and future control strategies.<\/jats:p>","DOI":"10.1093\/nar\/gkag151","type":"journal-article","created":{"date-parts":[[2026,2,14]],"date-time":"2026-02-14T12:39:19Z","timestamp":1771072759000},"source":"Crossref","is-referenced-by-count":1,"title":["Nodavirus protein A\u2019s interdomain elbow controls RNA replication organelle formation and function"],"prefix":"10.1093","volume":"54","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-6346-7078","authenticated-orcid":false,"given":"Helena","family":"Jaramillo-Mesa","sequence":"first","affiliation":[{"name":"John and Jeanne Rowe Center for Research in Virology, Morgridge Institute for Research, Madison, WI53715 ,","place":["United States"]},{"name":"Institute for Molecular Virology, University of Wisconsin-Madison, Madison, WI53706 ,","place":["United States"]},{"name":"McArdle Laboratory for Cancer Research, University of Wisconsin-Madison, Madison, WI53705 ,","place":["United States"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Megan","family":"Bracken","sequence":"additional","affiliation":[{"name":"John and Jeanne Rowe Center for Research in Virology, Morgridge Institute for Research, Madison, WI53715 ,","place":["United States"]},{"name":"Institute for Molecular Virology, University of Wisconsin-Madison, Madison, WI53706 ,","place":["United States"]},{"name":"McArdle Laboratory for Cancer Research, University of Wisconsin-Madison, Madison, WI53705 ,","place":["United States"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hong","family":"Zhan","sequence":"additional","affiliation":[{"name":"John and Jeanne Rowe Center for Research in Virology, Morgridge Institute for Research, Madison, WI53715 ,","place":["United States"]},{"name":"Institute for Molecular Virology, University of Wisconsin-Madison, Madison, WI53706 ,","place":["United States"]},{"name":"McArdle Laboratory for Cancer Research, University of Wisconsin-Madison, Madison, WI53705 ,","place":["United States"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mark","family":"Horswill","sequence":"additional","affiliation":[{"name":"John and Jeanne Rowe Center for Research in Virology, Morgridge Institute for Research, Madison, WI53715 ,","place":["United States"]},{"name":"Institute for Molecular Virology, University of Wisconsin-Madison, Madison, WI53706 ,","place":["United States"]},{"name":"McArdle Laboratory for Cancer Research, University of Wisconsin-Madison, Madison, WI53705 ,","place":["United States"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Timothy","family":"Grant","sequence":"additional","affiliation":[{"name":"John and Jeanne Rowe Center for Research in Virology, Morgridge Institute for Research, Madison, WI53715 ,","place":["United States"]},{"name":"Department of Biochemistry, University of Wisconsin-Madison, Madison, WI53706 ,","place":["United States"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Johan A","family":"den\u00a0Boon","sequence":"additional","affiliation":[{"name":"John and Jeanne Rowe Center for Research in Virology, Morgridge Institute for Research, Madison, WI53715 ,","place":["United States"]},{"name":"Institute for Molecular Virology, University of Wisconsin-Madison, Madison, WI53706 ,","place":["United States"]},{"name":"McArdle Laboratory for Cancer Research, University of Wisconsin-Madison, Madison, WI53705 ,","place":["United States"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paul","family":"Ahlquist","sequence":"additional","affiliation":[{"name":"John and Jeanne Rowe Center for Research in Virology, Morgridge Institute for Research, Madison, WI53715 ,","place":["United States"]},{"name":"Institute for Molecular Virology, University of Wisconsin-Madison, Madison, WI53706 ,","place":["United States"]},{"name":"McArdle Laboratory for Cancer Research, University of Wisconsin-Madison, Madison, WI53705 ,","place":["United States"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2026,2,27]]},"reference":[{"key":"2026022702162603800_B1","doi-asserted-by":"publisher","first-page":"2675","DOI":"10.1007\/s00018-008-8037-y","article-title":"Recent insights into the biology and biomedical applications of flock house virus","volume":"65","author":"Venter","year":"2008","journal-title":"Cell Mol Life Sci"},{"key":"2026022702162603800_B2","doi-asserted-by":"publisher","first-page":"229","DOI":"10.1016\/S0065-3527(08)60350-4","article-title":"Reverse genetics of nodaviruses","volume-title":"Adv Virus Res","author":"Ball","year":"1999"},{"key":"2026022702162603800_B3","doi-asserted-by":"publisher","first-page":"9465","DOI":"10.1073\/pnas.93.18.9465","article-title":"Complete replication of an animal virus and maintenance of expression vectors derived from it in Saccharomyces cerevisiae","volume":"93","author":"Price","year":"1996","journal-title":"Proc Natl Acad Sci USA"},{"key":"2026022702162603800_B4","doi-asserted-by":"publisher","first-page":"1040","DOI":"10.1038\/nature03870","article-title":"Animal virus replication and RNAi-mediated antiviral silencing in Caenorhabditis elegans","volume":"436","author":"Lu","year":"2005","journal-title":"Nature"},{"key":"2026022702162603800_B5","doi-asserted-by":"publisher","first-page":"2113","DOI":"10.1016\/j.celrep.2017.02.014","article-title":"Ultrastructural characterization of Zika virus replication factories","volume":"18","author":"Cortese","year":"2017","journal-title":"Cell Rep"},{"key":"2026022702162603800_B6","doi-asserted-by":"publisher","first-page":"10438","DOI":"10.1128\/JVI.00986-10","article-title":"The endoplasmic reticulum provides the membrane platform for biogenesis of the flavivirus replication complex","volume":"84","author":"Gillespie","year":"2010","journal-title":"J Virol"},{"key":"2026022702162603800_B7","doi-asserted-by":"publisher","first-page":"e220","DOI":"10.1371\/journal.pbio.0050220","article-title":"Three-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelle","volume":"5","author":"Kopek","year":"2007","journal-title":"PLoS Biol"},{"key":"2026022702162603800_B8","doi-asserted-by":"publisher","first-page":"e83042","DOI":"10.7554\/eLife.83042","article-title":"Architecture of the chikungunya virus replication organelle","volume":"11","author":"Laurent","year":"2022","journal-title":"eLife"},{"key":"2026022702162603800_B9","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1016\/j.chom.2009.03.007","article-title":"Composition and three-dimensional architecture of the dengue virus replication and assembly sites","volume":"5","author":"Welsch","year":"2009","journal-title":"Cell Host Microbe"},{"key":"2026022702162603800_B10","doi-asserted-by":"publisher","first-page":"11664","DOI":"10.1128\/JVI.75.23.11664-11676.2001","article-title":"Flock house virus RNA replicates on outer mitochondrial membranes in drosophila cells","volume":"75","author":"Miller","year":"2001","journal-title":"J Virol"},{"key":"2026022702162603800_B11","doi-asserted-by":"publisher","first-page":"e25940","DOI":"10.7554\/eLife.25940","article-title":"Cryo-electron tomography reveals novel features of a viral RNA replication compartment","volume":"6","author":"Ertel","year":"2017","journal-title":"eLife"},{"key":"2026022702162603800_B12","doi-asserted-by":"publisher","first-page":"18680","DOI":"10.1073\/pnas.2006165117","article-title":"Subdomain cryo-EM structure of nodaviral replication protein A crown complex provides mechanistic insights into RNA genome replication","volume":"117","author":"Unchwaniwala","year":"2020","journal-title":"Proc Natl Acad Sci USA"},{"key":"2026022702162603800_B13","doi-asserted-by":"publisher","first-page":"e2217412120","DOI":"10.1073\/pnas.2217412120","article-title":"Nodavirus RNA replication crown architecture reveals proto-crown precursor and viral protein A conformational switching","volume":"120","author":"Zhan","year":"2023","journal-title":"Proc Natl Acad Sci USA"},{"key":"2026022702162603800_B14","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1146\/annurev-biochem-052521-115736","article-title":"A cool look at positive-strand RNA virus replication organelles: new insights from cryo-electron microscopy","volume":"93","author":"de\u00a0Beijer","year":"2024","journal-title":"Annu Rev Biochem"},{"key":"2026022702162603800_B15","doi-asserted-by":"publisher","first-page":"681","DOI":"10.1016\/j.tig.2024.04.003","article-title":"Positive-strand RNA virus genome replication organelles: structure, assembly, control","volume":"40","author":"den\u00a0Boon","year":"2024","journal-title":"Trends Genet"},{"key":"2026022702162603800_B16","doi-asserted-by":"publisher","first-page":"224","DOI":"10.1038\/s41586-024-07817-y","article-title":"Molecular architecture of coronavirus double-membrane vesicle pore complex","volume":"633","author":"Huang","year":"2024","journal-title":"Nature"},{"key":"2026022702162603800_B17","doi-asserted-by":"publisher","first-page":"101475","DOI":"10.1016\/j.coviro.2025.101475","article-title":"Illuminating druggable dark matter in RNA virus replication using in situ cryo-EM","volume":"72","author":"Sharma","year":"2025","journal-title":"Curr Opin Virol"},{"key":"2026022702162603800_B18","doi-asserted-by":"publisher","first-page":"eadd2536","DOI":"10.1126\/sciadv.add2536","article-title":"Molecular architecture of the Chikungunya virus replication complex","volume":"8","author":"Tan","year":"2022","journal-title":"Sci Adv"},{"key":"2026022702162603800_B19","doi-asserted-by":"publisher","first-page":"1395","DOI":"10.1126\/science.abd3629","article-title":"A molecular pore spans the double membrane of the coronavirus replication organelle","volume":"369","author":"Wolff","year":"2020","journal-title":"Science"},{"key":"2026022702162603800_B20","doi-asserted-by":"publisher","first-page":"7894","DOI":"10.1038\/s41467-023-43666-5","article-title":"SARS-CoV-2 nsp3 and nsp4 are minimal constituents of a pore spanning replication organelle","volume":"14","author":"Zimmermann","year":"2023","journal-title":"Nat Commun"},{"key":"2026022702162603800_B21","doi-asserted-by":"publisher","first-page":"8106","DOI":"10.1038\/s41467-024-51952-z","article-title":"Alphavirus nsP3 organizes into tubular scaffolds essential for infection and the cytoplasmic granule architecture","volume":"15","author":"Kril","year":"2024","journal-title":"Nat Commun"},{"key":"2026022702162603800_B22","doi-asserted-by":"publisher","first-page":"10061","DOI":"10.1128\/JVI.73.12.10061-10069.1999","article-title":"Putative RNA capping activities encoded by brome mosaic virus: methylation and covalent binding of guanylate by replicase protein 1a","volume":"73","author":"Ahola","year":"1999","journal-title":"J Virol"},{"key":"2026022702162603800_B23","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1186\/s13062-015-0050-0","article-title":"Sequence analysis reveals a conserved extension in the capping enzyme of the alphavirus supergroup, and a homologous domain in nodaviruses","volume":"10","author":"Ahola","year":"2015","journal-title":"Biol Direct"},{"key":"2026022702162603800_B24","doi-asserted-by":"publisher","first-page":"483","DOI":"10.3390\/v10090483","article-title":"The RNA capping enzyme domain in protein A is essential for flock house virus replication","volume":"10","author":"Quirin","year":"2018","journal-title":"Viruses"},{"key":"2026022702162603800_B25","doi-asserted-by":"publisher","article-title":"Genetic complementation reveals structure\u2013function links in nodavirus RNA replication complex crowns","author":"den\u00a0Boon","DOI":"10.64898\/2025.12.10.693615"},{"key":"2026022702162603800_B26","doi-asserted-by":"publisher","first-page":"2711","DOI":"10.3390\/v14122711","article-title":"Multifunctional protein A is the only viral protein required for nodavirus RNA replication crown formation","volume":"14","author":"den\u00a0Boon","year":"2022","journal-title":"Viruses"},{"key":"2026022702162603800_B27","doi-asserted-by":"publisher","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":"2026022702162603800_B28","doi-asserted-by":"publisher","first-page":"e4792","DOI":"10.1002\/pro.4792","article-title":"UCSF ChimeraX: tools for structure building and analysis","volume":"32","author":"Meng","year":"2023","journal-title":"Protein Sci"},{"key":"2026022702162603800_B29","doi-asserted-by":"publisher","first-page":"720","DOI":"10.1128\/jvi.69.2.720-727.1995","article-title":"Requirements for the self-directed replication of flock house virus RNA 1","volume":"69","author":"Ball","year":"1995","journal-title":"J Virol"},{"key":"2026022702162603800_B30","doi-asserted-by":"publisher","first-page":"3905","DOI":"10.1128\/JVI.76.8.3905-3919.2002","article-title":"Long-distance base pairing in flock house virus RNA1 regulates subgenomic RNA3 synthesis and RNA2 replication","volume":"76","author":"Lindenbach","year":"2002","journal-title":"J Virol"},{"key":"2026022702162603800_B31","doi-asserted-by":"publisher","first-page":"2976","DOI":"10.1128\/JVI.02040-08","article-title":"5\u2032 cis elements direct nodavirus RNA1 recruitment to mitochondrial sites of replication complex formation","volume":"83","author":"van\u00a0Wynsberghe","year":"2009","journal-title":"J Virol"},{"key":"2026022702162603800_B32","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1006\/viro.2002.1377","article-title":"Replication of the RNA segments of a bipartite viral genome is coordinated by a transactivating subgenomic RNA","volume":"296","author":"Eckerle","year":"2002","journal-title":"Virology"},{"key":"2026022702162603800_B33","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1016\/j.virol.2003.08.029","article-title":"Flock house virus subgenomic RNA3 is replicated and its replication correlates with transactivation of RNA2","volume":"317","author":"Eckerle","year":"2003","journal-title":"Virology"},{"key":"2026022702162603800_B34","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1016\/S0042-6822(03)00190-9","article-title":"The cis-acting replication signal at the 3\u2032 end of flock house virus RNA2 is RNA3-dependent","volume":"311","author":"Albari\u00f1o","year":"2003","journal-title":"Virology"},{"key":"2026022702162603800_B35","doi-asserted-by":"publisher","first-page":"12492","DOI":"10.1128\/JVI.01495-10","article-title":"Nodavirus-induced membrane rearrangement in replication complex assembly requires replicase protein A, RNA templates, and polymerase activity","volume":"84","author":"Kopek","year":"2010","journal-title":"J Virol"},{"key":"2026022702162603800_B36","doi-asserted-by":"publisher","first-page":"392","DOI":"10.1128\/jvi.71.1.392-397.1997","article-title":"Critical residues of Semliki Forest virus RNA capping enzyme involved in methyltransferase and guanylyltransferase-like activities","volume":"71","author":"Ahola","year":"1997","journal-title":"J Virol"},{"key":"2026022702162603800_B37","doi-asserted-by":"publisher","first-page":"2326","DOI":"10.1016\/j.febslet.2012.05.024","article-title":"Functional analysis of the conserved histidine residue of Bamboo mosaic virus capping enzyme in the activity for the formation of the covalent enzyme\u2013m7 GMP intermediate","volume":"586","author":"Lin","year":"2012","journal-title":"FEBS Lett"},{"key":"2026022702162603800_B38","doi-asserted-by":"publisher","first-page":"7269","DOI":"10.1093\/nar\/12.18.7269","article-title":"Primary structural comparison of RNA-dependent polymerases from plant, animal and bacterial viruses","volume":"12","author":"Kamer","year":"1984","journal-title":"Nucleic Acids Res"},{"key":"2026022702162603800_B39","doi-asserted-by":"publisher","first-page":"2197","DOI":"10.1099\/0022-1317-72-9-2197","article-title":"The phylogeny of RNA-dependent RNA polymerases of positive-strand RNA viruses","volume":"72","author":"Koonin","year":"1991","journal-title":"J Gen Virol"},{"key":"2026022702162603800_B40","doi-asserted-by":"publisher","first-page":"4633","DOI":"10.1128\/JVI.02267-06","article-title":"Nodavirus RNA replication protein A induces membrane association of genomic RNA","volume":"81","author":"van\u00a0Wynsberghe","year":"2007","journal-title":"J Virol"},{"key":"2026022702162603800_B41","doi-asserted-by":"publisher","first-page":"615","DOI":"10.1038\/s41586-020-3036-8","article-title":"Capping pores of alphavirus nsP1 gate membranous viral replication factories","volume":"589","author":"Jones","year":"2021","journal-title":"Nature"},{"key":"2026022702162603800_B42","doi-asserted-by":"publisher","first-page":"e2213934120","DOI":"10.1073\/pnas.2213934120","article-title":"Structural basis and dynamics of Chikungunya alphavirus RNA capping by nsP1 capping pores","volume":"120","author":"Jones","year":"2023","journal-title":"Proc Natl Acad Sci USA"},{"key":"2026022702162603800_B43","doi-asserted-by":"publisher","first-page":"111133","DOI":"10.1016\/j.celrep.2022.111133","article-title":"Molecular basis of specific viral RNA recognition and 5\u2032-end capping by the Chikungunya virus nsP1","volume":"40","author":"Zhang","year":"2022","journal-title":"Cell Rep"},{"key":"2026022702162603800_B44","doi-asserted-by":"publisher","first-page":"451","DOI":"10.1146\/annurev-phyto-121823-032017","article-title":"Replication organelles of plant positive-strand RNA viruses: a boost in knowledge following new imaging approaches","volume":"63","author":"Zhang","year":"2025","journal-title":"Annu Rev Phytopathol"},{"key":"2026022702162603800_B45","doi-asserted-by":"publisher","first-page":"e1006134","DOI":"10.1371\/journal.ppat.1006134","article-title":"A positive-strand RNA virus uses alternative protein-protein interactions within a viral protease\/cofactor complex to switch between RNA replication and virion morphogenesis","volume":"13","author":"Dubrau","year":"2017","journal-title":"PLOS Pathog"},{"key":"2026022702162603800_B46","doi-asserted-by":"publisher","first-page":"107367","DOI":"10.1016\/j.jbc.2024.107367","article-title":"Kinetic comparison of all eleven viral polyprotein cleavage site processing events by SARS-CoV-2 main protease using a linked protein FRET platform","volume":"300","author":"Kenward","year":"2024","journal-title":"J Biol Chem"},{"key":"2026022702162603800_B47","doi-asserted-by":"publisher","first-page":"2925","DOI":"10.1002\/j.1460-2075.1994.tb06587.x","article-title":"Polypeptide requirements for assembly of functional Sindbis virus replication complexes: a model for the temporal regulation of minus- and plus-strand RNA synthesis","volume":"13","author":"Lemm","year":"1994","journal-title":"EMBO J"},{"key":"2026022702162603800_B48","doi-asserted-by":"publisher","first-page":"e70030","DOI":"10.1002\/rmv.70030","article-title":"Alphavirus nsP2: a multifunctional regulator of viral replication and promising target for anti-alphavirus therapies","volume":"35","author":"Wang","year":"2025","journal-title":"Rev Med Virol"},{"key":"2026022702162603800_B49","doi-asserted-by":"publisher","first-page":"74","DOI":"10.1016\/j.coviro.2014.09.011","article-title":"Regulation of flavivirus RNA synthesis and replication","volume":"9","author":"Selisko","year":"2014","journal-title":"Curr Opin Virol"},{"key":"2026022702162603800_B50","doi-asserted-by":"publisher","first-page":"249","DOI":"10.1128\/JVI.02085-14","article-title":"Perturbation in the conserved methyltransferase-polymerase interface of flavivirus NS5 differentially affects polymerase initiation and elongation","volume":"89","author":"Wu","year":"2015","journal-title":"J Virol"},{"key":"2026022702162603800_B51","doi-asserted-by":"publisher","first-page":"371","DOI":"10.1038\/nrmicro1389","article-title":"Parallels among positive-strand RNA viruses, reverse-transcribing viruses and double-stranded RNA viruses","volume":"4","author":"Ahlquist","year":"2006","journal-title":"Nat Rev Microbiol"},{"key":"2026022702162603800_B52","doi-asserted-by":"publisher","first-page":"e00860","DOI":"10.1128\/jvi.00860-23","article-title":"Rotavirus core shell protein sites that regulate intra-particle polymerase activity","volume":"97","author":"Anderson","year":"2023","journal-title":"J Virol"}],"container-title":["Nucleic Acids Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/nar\/article-pdf\/54\/5\/gkag151\/67146996\/gkag151.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/nar\/article-pdf\/54\/5\/gkag151\/67146996\/gkag151.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T07:16:36Z","timestamp":1772176596000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/nar\/article\/doi\/10.1093\/nar\/gkag151\/8500560"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2,24]]},"references-count":52,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2026,2,24]]}},"URL":"https:\/\/doi.org\/10.1093\/nar\/gkag151","relation":{},"ISSN":["0305-1048","1362-4962"],"issn-type":[{"value":"0305-1048","type":"print"},{"value":"1362-4962","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2026,3,24]]},"published":{"date-parts":[[2026,2,24]]},"article-number":"gkag151"}}