{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T14:37:13Z","timestamp":1792852633444,"version":"4.5.0"},"reference-count":52,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2027,1,1]],"date-time":"2027-01-01T00:00:00Z","timestamp":1798761600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2027,1,1]],"date-time":"2027-01-01T00:00:00Z","timestamp":1798761600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T00:00:00Z","timestamp":1791504000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01 GM028301"],"award-info":[{"award-number":["R01 GM028301"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100008530","name":"European Regional Development Fund","doi-asserted-by":"publisher","award":["PID2022-136564NB-I00"],"award-info":[{"award-number":["PID2022-136564NB-I00"]}],"id":[{"id":"10.13039\/501100008530","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100023581","name":"National Science Foundation Graduate Research Fellowship Program","doi-asserted-by":"publisher","award":["DGE2631988"],"award-info":[{"award-number":["DGE2631988"]}],"id":[{"id":"10.13039\/100023581","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100023581","name":"National Science Foundation Graduate Research Fellowship Program","doi-asserted-by":"publisher","award":["DGE2140739"],"award-info":[{"award-number":["DGE2140739"]}],"id":[{"id":"10.13039\/100023581","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100014440","name":"Ministerio de Ciencia, Innovaci\u00f3n y Universidades","doi-asserted-by":"publisher","award":["FORT23\/00008"],"award-info":[{"award-number":["FORT23\/00008"]}],"id":[{"id":"10.13039\/100014440","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011033","name":"State Agency of Research","doi-asserted-by":"publisher","award":["PID2022-136564NB-I00"],"award-info":[{"award-number":["PID2022-136564NB-I00"]}],"id":[{"id":"10.13039\/501100011033","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2027,1]]},"DOI":"10.1016\/j.jmb.2026.170065","type":"journal-article","created":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T23:42:20Z","timestamp":1791848540000},"page":"170065","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Ribosomal Protein eL22 Contributes to the Assembly of 60S Ribosomal Subunits in Saccharomyces cerevisiae"],"prefix":"10.1016","volume":"439","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6631-5089","authenticated-orcid":false,"given":"Jos\u00e9","family":"Fern\u00e1ndez-Fern\u00e1ndez","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9334-0538","authenticated-orcid":false,"given":"Sara","family":"Mart\u00edn-Villanueva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0680-0773","authenticated-orcid":false,"given":"Taylor N.","family":"Ayers","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1415-6757","authenticated-orcid":false,"given":"Carla V.","family":"Galmozzi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John L.","family":"Woolford","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jes\u00fas","family":"de la Cruz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2026.170065_b0005","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a011536","article-title":"The structure and function of the eukaryotic ribosome","volume":"4","author":"Wilson","year":"2012","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.jmb.2026.170065_b0010","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1038\/nsmb.2313","article-title":"One core, two shells: bacterial and eukaryotic ribosomes","volume":"19","author":"Melnikov","year":"2012","journal-title":"Nature Struct. Mol. Biol."},{"key":"10.1016\/j.jmb.2026.170065_b0015","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1146\/annurev-biochem-013118-110817","article-title":"Eukaryotic ribosome assembly","volume":"88","author":"Bassler","year":"2019","journal-title":"Annu. Rev. Biochem"},{"key":"10.1016\/j.jmb.2026.170065_b0020","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1534\/genetics.113.153197","article-title":"Ribosome biogenesis in the yeast Saccharomyces cerevisiae","volume":"195","author":"Woolford","year":"2013","journal-title":"Genetics"},{"key":"10.1016\/j.jmb.2026.170065_b0025","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1038\/35080045","article-title":"The function and synthesis of ribosomes","volume":"2","author":"Lafontaine","year":"2001","journal-title":"Nature Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2026.170065_b0030","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1146\/annurev-biochem-030222-113611","article-title":"Eukaryotic ribosome assembly","volume":"93","author":"Vanden Broeck","year":"2024","journal-title":"Annu. Rev. Biochem"},{"key":"10.1016\/j.jmb.2026.170065_b0035","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1038\/s41580-018-0078-y","article-title":"Ribosome assembly coming into focus","volume":"20","author":"Klinge","year":"2019","journal-title":"Nature Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2026.170065_b0040","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1146\/annurev-biochem-060713-035445","article-title":"High-resolution structure of the eukaryotic 80S ribosome","volume":"83","author":"Yusupova","year":"2014","journal-title":"Annu. Rev. Biochem"},{"key":"10.1016\/j.jmb.2026.170065_b0045","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/S0968-0004(99)01460-7","article-title":"The economics of ribosome biosynthesis in yeast","volume":"24","author":"Warner","year":"1999","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.jmb.2026.170065_b0050","doi-asserted-by":"crossref","DOI":"10.3390\/biom14080975","article-title":"Putting it all together: the roles of ribosomal proteins in nucleolar stages of 60S ribosomal assembly in the yeast Saccharomyces cerevisiae","volume":"14","author":"Ayers","year":"2024","journal-title":"Biomolecules"},{"key":"10.1016\/j.jmb.2026.170065_b0055","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1146\/annurev-biochem-060614-033917","article-title":"Functions of ribosomal proteins in assembly of eukaryotic ribosomes in vivo","volume":"84","author":"de la Cruz","year":"2015","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jmb.2026.170065_b0060","article-title":"Paradigms of ribosome synthesis: Lessons learned from ribosomal proteins","volume":"3","author":"Gamalinda","year":"2015","journal-title":"Translation (Austin)"},{"key":"10.1016\/j.jmb.2026.170065_b0065","doi-asserted-by":"crossref","DOI":"10.3390\/cancers17101597","article-title":"The central role of ribosomal proteins in p53 regulation","volume":"17","author":"Lindstrom","year":"2025","journal-title":"Cancers (Basel)"},{"key":"10.1016\/j.jmb.2026.170065_b0070","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1093\/nar\/gkz637","article-title":"Hallmarks of ribosomopathies","volume":"48","author":"Kampen","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2026.170065_b0075","doi-asserted-by":"crossref","first-page":"1954","DOI":"10.1093\/nar\/gkz1183","article-title":"Differential expression of duplicated ribosomal protein genes modifies ribosome composition in response to stress","volume":"48","author":"Ghulam","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2026.170065_b0080","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0068412","article-title":"Studies on the assembly characteristics of large subunit ribosomal proteins in S. cerevisae","volume":"8","author":"Ohmayer","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jmb.2026.170065_b0085","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0143768","article-title":"Studies on the coordination of ribosomal protein assembly events involved in processing and stabilization of yeast early large ribosomal subunit precursors","volume":"10","author":"Ohmayer","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.jmb.2026.170065_b0090","doi-asserted-by":"crossref","first-page":"1599","DOI":"10.1016\/j.cell.2017.11.039","article-title":"Visualizing the assembly pathway of nucleolar pre-60S ribosomes","volume":"171","author":"Kater","year":"2017","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2026.170065_b0095","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1083\/jcb.151.5.1057","article-title":"Nmd3p is a Crm1p-dependent adapter protein for nuclear export of the large ribosomal subunit","volume":"151","author":"Ho","year":"2000","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jmb.2026.170065_b0100","doi-asserted-by":"crossref","first-page":"D168","DOI":"10.1093\/nar\/gkh004","article-title":"RPG: the Ribosomal Protein Gene database","volume":"32","author":"Nakao","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2026.170065_b0105","doi-asserted-by":"crossref","first-page":"5382","DOI":"10.1093\/nar\/gkf693","article-title":"Comparative analysis of ribosomal proteins in complete genomes: an example of reductive evolution at the domain scale","volume":"30","author":"Lecompte","year":"2002","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2026.170065_b0110","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1038\/nature01644","article-title":"Sequencing and comparison of yeast species to identify genes and regulatory elements","volume":"423","author":"Kellis","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2026.170065_b0115","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1534\/genetics.111.136549","article-title":"Ribosome deficiency protects against ER stress in Saccharomyces cerevisiae","volume":"191","author":"Steffen","year":"2012","journal-title":"Genetics"},{"key":"10.1016\/j.jmb.2026.170065_b0120","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1186\/s13008-016-0024-3","article-title":"Rpl22 is required for IME1 mRNA translation and meiotic induction in S. cerevisiae","volume":"11","author":"Kim","year":"2016","journal-title":"Cell Div"},{"key":"10.1016\/j.jmb.2026.170065_b0125","first-page":"51","article-title":"Characterization of a 40S ribosomal subunit complex in polyribosomes of Saccharomyces cerevisiae treated with cycloheximide","volume":"1","author":"Helser","year":"1981","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2026.170065_b0130","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1101\/gad.2.2.160","article-title":"Depletion of Saccharomyces cerevisiae ribosomal protein L16 causes a decrease in 60S ribosomal subunits and formation of half-mer polysomes","volume":"2","author":"Rotenberg","year":"1988","journal-title":"Genes Dev."},{"key":"10.1016\/j.jmb.2026.170065_b0135","doi-asserted-by":"crossref","first-page":"4715","DOI":"10.1093\/nar\/gky123","article-title":"Ribosomal protein L14 contributes to the early assembly of 60S ribosomal subunits in Saccharomyces cerevisiae","volume":"46","author":"Espinar-Marchena","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2026.170065_b0140","doi-asserted-by":"crossref","first-page":"7519","DOI":"10.1093\/nar\/gkp806","article-title":"Role and dynamics of the ribosomal protein P0 and its related trans-acting factor Mrt4 during ribosome assembly in Saccharomyces cerevisiae","volume":"37","author":"Rodr\u00edguez-Mateos","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2026.170065_b0145","doi-asserted-by":"crossref","first-page":"1561","DOI":"10.1261\/rna.072116.119","article-title":"Pol5 is an essential ribosome biogenesis factor required for 60S ribosomal subunit maturation in Saccharomyces cerevisiae","volume":"25","author":"Ramos-S\u00e1enz","year":"2019","journal-title":"RNA"},{"key":"10.1016\/j.jmb.2026.170065_b0150","doi-asserted-by":"crossref","first-page":"4696","DOI":"10.1038\/s41467-021-24964-2","article-title":"Puf6 primes 60S pre-ribosome nuclear export at low temperature","volume":"12","author":"Gerhardy","year":"2021","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2026.170065_b0155","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1038\/nsmb.3454","article-title":"Eukaryotic ribosome assembly, transport and quality control","volume":"24","author":"Pe\u00f1a","year":"2017","journal-title":"Nature Struct. Mol. Biol."},{"key":"10.1016\/j.jmb.2026.170065_b0160","doi-asserted-by":"crossref","DOI":"10.1093\/molbev\/msac054","article-title":"Looking through the lens of the ribosome biogenesis evolutionary history: possible implications for archaeal phylogeny and eukaryogenesis","volume":"39","author":"Juttner","year":"2022","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.jmb.2026.170065_b0165","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1261\/rna.2720205","article-title":"Nop53p is required for late 60S ribosome subunit maturation and nuclear export in yeast","volume":"11","author":"Thomson","year":"2005","journal-title":"RNA"},{"key":"10.1016\/j.jmb.2026.170065_b0170","doi-asserted-by":"crossref","first-page":"2203","DOI":"10.1016\/j.jmb.2016.03.023","article-title":"The functional role of eL19 and eB12 intersubunit bridge in the eukaryotic ribosome","volume":"428","author":"Kisly","year":"2016","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2026.170065_b0175","doi-asserted-by":"crossref","first-page":"5001","DOI":"10.1093\/nar\/29.24.5001","article-title":"All three functional domains of the large ribosomal subunit protein L25 are required for both early and late pre-rRNA processing steps in Saccharomyces cerevisiae","volume":"29","author":"van Beekvelt","year":"2001","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2026.170065_b0180","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0008249","article-title":"rRNA maturation in yeast cells depleted of large ribosomal subunit proteins","volume":"4","author":"P\u00f6ll","year":"2009","journal-title":"PLoS One"},{"key":"10.1016\/j.jmb.2026.170065_b0185","doi-asserted-by":"crossref","first-page":"2503","DOI":"10.1083\/jcb.201711037","article-title":"Hierarchical recruitment of ribosomal proteins and assembly factors remodels nucleolar pre-60S ribosomes","volume":"217","author":"Biedka","year":"2018","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jmb.2026.170065_b0190","doi-asserted-by":"crossref","first-page":"4449","DOI":"10.1128\/MCB.23.13.4449-4460.2003","article-title":"Sequential protein association with nascent 60S ribosomal particles","volume":"23","author":"Saveanu","year":"2003","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2026.170065_b0195","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1038\/nature17942","article-title":"Diverse roles of assembly factors revealed by structures of late nuclear pre-60S ribosomes","volume":"534","author":"Wu","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2026.170065_b0200","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.52474","article-title":"The GTPase Nog1 co-ordinates the assembly, maturation and quality control of distant ribosomal functional centers","volume":"9","author":"Klingauf-Nerurkar","year":"2020","journal-title":"eLife"},{"key":"10.1016\/j.jmb.2026.170065_b0205","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1016\/j.cell.2007.08.037","article-title":"Functional specificity among ribosomal proteins regulates gene expression","volume":"131","author":"Komili","year":"2007","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2026.170065_b0210","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1038\/ng1994","article-title":"The Shwachman-Bodian-Diamond syndrome protein mediates translational activation of ribosomes in yeast","volume":"39","author":"Menne","year":"2007","journal-title":"Nature Genet."},{"key":"10.1016\/j.jmb.2026.170065_b0215","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1261\/rna.7340404","article-title":"Npa1p is an essential trans-acting factor required for an early step in the assembly of 60S ribosomal subunits in Saccharomyces cerevisiae","volume":"10","author":"Rosado","year":"2004","journal-title":"RNA"},{"key":"10.1016\/j.jmb.2026.170065_b0220","series-title":"Methods in Yeast Genetics: A Cold Spring Harbor Laboratory Course Manual","author":"Kaiser","year":"1994"},{"key":"10.1016\/j.jmb.2026.170065_b0225","doi-asserted-by":"crossref","first-page":"1425","DOI":"10.1093\/nar\/20.6.1425","article-title":"Improved method for high efficiency transformation of intact yeast cells","volume":"20","author":"Gietz","year":"1992","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2026.170065_b0230","series-title":"Molecular Cloning: A Laboratory Manual","author":"Sambrook","year":"1989"},{"key":"10.1016\/j.jmb.2026.170065_b0235","doi-asserted-by":"crossref","first-page":"7283","DOI":"10.1128\/MCB.17.12.7283","article-title":"Fal1p is an essential DEAD-box protein involved in 40S-ribosomal-subunit biogenesis in Saccharomyces cerevisiae","volume":"17","author":"Kressler","year":"1997","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2026.170065_b0240","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1017\/S1355838299990027","article-title":"Overexpression of truncated Nmd3p inhibits protein synthesis in yeast","volume":"5","author":"Belk","year":"1999","journal-title":"RNA"},{"key":"10.1016\/j.jmb.2026.170065_b0245","series-title":"Current Protocols in Molecular Biology","article-title":"Saccharomyces cerevisiae","author":"Ausubel","year":"1994"},{"key":"10.1016\/j.jmb.2026.170065_b0250","series-title":"Protein Synthesis: Methods and Protocols","first-page":"257","article-title":"In vivo mutational analysis of ribosomal RNA in Saccharomyces cerevisiae","author":"Venema","year":"1998"},{"key":"10.1016\/j.jmb.2026.170065_b0255","doi-asserted-by":"crossref","first-page":"1855","DOI":"10.1128\/MCB.18.4.1855","article-title":"Dbp6p is an essential putative ATP-dependent RNA helicase required for 60S-ribosomal-subunit assembly in Saccharomyces cerevisiae","volume":"18","author":"Kressler","year":"1998","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2026.170065_b0260","doi-asserted-by":"crossref","first-page":"5177","DOI":"10.1093\/nar\/gkq260","article-title":"Ribosomal protein L35 is required for 27SB pre-rRNA processing in Saccharomyces cerevisiae","volume":"38","author":"Babiano","year":"2010","journal-title":"Nucleic Acids Res."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283626004389?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283626004389?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T14:09:19Z","timestamp":1792850959000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283626004389"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2027,1]]},"references-count":52,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2027,1]]}},"alternative-id":["S0022283626004389"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2026.170065","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2027,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Ribosomal Protein eL22 Contributes to the Assembly of 60S Ribosomal Subunits in Saccharomyces cerevisiae","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2026.170065","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Author(s). Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}],"article-number":"170065"}}