{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,2]],"date-time":"2026-11-02T23:02:58Z","timestamp":1793660578795,"version":"4.5.1"},"reference-count":58,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,4,1]],"date-time":"2022-04-01T00:00:00Z","timestamp":1648771200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,4,1]],"date-time":"2022-04-01T00:00:00Z","timestamp":1648771200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,3,4]],"date-time":"2023-03-04T00:00:00Z","timestamp":1677888000000},"content-version":"am","delay-in-days":337,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,4,1]],"date-time":"2022-04-01T00:00:00Z","timestamp":1648771200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,4,1]],"date-time":"2022-04-01T00:00:00Z","timestamp":1648771200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,4,1]],"date-time":"2022-04-01T00:00:00Z","timestamp":1648771200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,4,1]],"date-time":"2022-04-01T00:00:00Z","timestamp":1648771200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,4,1]],"date-time":"2022-04-01T00:00:00Z","timestamp":1648771200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["bmn.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Current Opinion in Structural Biology"],"published-print":{"date-parts":[[2022,4]]},"DOI":"10.1016\/j.sbi.2022.102348","type":"journal-article","created":{"date-parts":[[2022,3,4]],"date-time":"2022-03-04T13:24:53Z","timestamp":1646400293000},"page":"102348","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":34,"special_numbering":"C","title":["Glycosylation as a key parameter in the design of nucleic acid vaccines"],"prefix":"10.1016","volume":"73","author":[{"given":"Ahmet","family":"Ozdilek","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1902-7532","authenticated-orcid":false,"given":"Fikri Y.","family":"Avci","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.sbi.2022.102348_bib1","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1002\/emmm.201403876","article-title":"Vaccines for the 21st century","volume":"6","author":"Delany","year":"2014","journal-title":"EMBO Mol Med"},{"key":"10.1016\/j.sbi.2022.102348_bib2","doi-asserted-by":"crossref","first-page":"123","DOI":"10.3389\/fmicb.2018.00123","article-title":"Universal vaccines and vaccine platforms to protect against influenza viruses in humans and agriculture","volume":"9","author":"Rajao","year":"2018","journal-title":"Front Microbiol"},{"key":"10.1016\/j.sbi.2022.102348_bib3","doi-asserted-by":"crossref","first-page":"199","DOI":"10.12688\/f1000research.13588.1","article-title":"Progress and challenges in TB vaccine development","volume":"7","author":"Voss","year":"2018","journal-title":"F1000Res"},{"key":"10.1016\/j.sbi.2022.102348_bib4","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1038\/nrmicro2240","article-title":"Viruses as vaccine vectors for infectious diseases and cancer","volume":"8","author":"Draper","year":"2009","journal-title":"Nat Rev Microbiol"},{"key":"10.1016\/j.sbi.2022.102348_bib5","series-title":"Vaccines","first-page":"1182","article-title":"Technologies for making new vaccines","author":"Ellis","year":"2013"},{"key":"10.1016\/j.sbi.2022.102348_bib6","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.actbio.2018.08.033","article-title":"Engineering DNA vaccines against infectious diseases","volume":"80","author":"Lee","year":"2018","journal-title":"Acta Biomater"},{"key":"10.1016\/j.sbi.2022.102348_bib7","doi-asserted-by":"crossref","first-page":"22","DOI":"10.4236\/wjv.2014.42008","article-title":"DNA vaccines approach: from concepts to applications","volume":"4","author":"Pereira","year":"2014","journal-title":"World J Vaccine"},{"key":"10.1016\/j.sbi.2022.102348_bib8","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1038\/s41434-020-00204-y","article-title":"Self-amplifying RNA vaccines for infectious diseases","volume":"28","author":"Bloom","year":"2021","journal-title":"Gene Ther"},{"key":"10.1016\/j.sbi.2022.102348_bib9","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1038\/nrmicro2240","article-title":"Viruses as vaccine vectors for infectious diseases and cancer","volume":"8","author":"Draper","year":"2010","journal-title":"Nat Rev Microbiol"},{"key":"10.1016\/j.sbi.2022.102348_bib10","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.xphs.2020.11.015","article-title":"The science is there: key considerations for stabilizing viral vector-based covid-19 vaccines","volume":"110","author":"Crommelin","year":"2021","journal-title":"J\u00a0Pharmacol Sci"},{"key":"10.1016\/j.sbi.2022.102348_bib11","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1016\/j.ymthe.2020.01.001","article-title":"Immune responses to viral gene therapy vectors","volume":"28","author":"Shirley","year":"2020","journal-title":"Mol Ther"},{"key":"10.1016\/j.sbi.2022.102348_sref12","doi-asserted-by":"crossref","first-page":"1280","DOI":"10.1073\/pnas.1916131117","article-title":"Host protein glycosylation in nucleic acid vaccines as a potential hurdle in vaccine design for nonviral pathogens","volume":"117","author":"Ozdilek","year":"2020","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.sbi.2022.102348_bib13","doi-asserted-by":"crossref","first-page":"28014","DOI":"10.1073\/pnas.2000260117","article-title":"Visualization of the HIV-1 Env glycan shield across scales","volume":"117","author":"Berndsen","year":"2020","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.sbi.2022.102348_bib14","doi-asserted-by":"crossref","first-page":"7","DOI":"10.3389\/fcimb.2012.00007","article-title":"Campylobacter polysaccharide capsules: virulence and vaccines","volume":"2","author":"Guerry","year":"2012","journal-title":"Front Cell Infect Microbiol"},{"key":"10.1016\/j.sbi.2022.102348_bib15","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1146\/annurev.micro.62.081307.162944","article-title":"Capsules of Streptococcus pneumoniae and other bacteria: paradigms for polysaccharide biosynthesis and regulation","volume":"65","author":"Yother","year":"2011","journal-title":"Annu Rev Microbiol"},{"key":"10.1016\/j.sbi.2022.102348_bib16","doi-asserted-by":"crossref","first-page":"2535","DOI":"10.2174\/15680266113136660180","article-title":"Novel strategies for development of next-generation glycoconjugate vaccines","volume":"13","author":"Avci","year":"2013","journal-title":"Curr Top Med Chem"},{"key":"10.1016\/j.sbi.2022.102348_bib17","doi-asserted-by":"crossref","DOI":"10.1128\/mSphere.00520-19","article-title":"Glycoconjugates: what it would take to master these well-known yet little-understood immunogens for vaccine development","volume":"4","author":"Avci","year":"2019","journal-title":"mSphere"},{"key":"10.1016\/j.sbi.2022.102348_bib18","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1093\/glycob\/cww086","article-title":"Biological roles of glycans","volume":"27","author":"Varki","year":"2017","journal-title":"Glycobiology"},{"key":"10.1016\/j.sbi.2022.102348_bib19","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1002\/pmic.200390052","article-title":"Bacterial glycoproteins: functions, biosynthesis and applications","volume":"3","author":"Upreti","year":"2003","journal-title":"Proteomics"},{"key":"10.1016\/j.sbi.2022.102348_bib20","doi-asserted-by":"crossref","first-page":"e1003705","DOI":"10.1371\/journal.ppat.1003705","article-title":"O-mannosylation of the Mycobacterium tuberculosis adhesin Apa is crucial for T cell antigenicity during infection but is expendable for protection","volume":"9","author":"Nandakumar","year":"2013","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.sbi.2022.102348_bib21","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1016\/S0140-6736(13)60177-4","article-title":"Safety and efficacy of MVA85A, a new tuberculosis vaccine, in infants previously vaccinated with BCG: a randomised, placebo-controlled phase 2b trial","volume":"381","author":"Tameris","year":"2013","journal-title":"Lancet"},{"key":"10.1016\/j.sbi.2022.102348_bib22","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1016\/S2213-2600(15)00037-5","article-title":"Safety, immunogenicity, and efficacy of the candidate tuberculosis vaccine MVA85A in healthy adults infected with HIV-1: a randomised, placebo-controlled, phase 2 trial","volume":"3","author":"Ndiaye","year":"2015","journal-title":"Lancet Respir Med"},{"key":"10.1016\/j.sbi.2022.102348_bib23","doi-asserted-by":"crossref","first-page":"2944","DOI":"10.1016\/j.vaccine.2015.03.070","article-title":"A\u00a0double-blind, randomised, placebo-controlled, dose-finding trial of the novel tuberculosis vaccine AERAS-402, an adenovirus-vectored fusion protein, in healthy, BCG-vaccinated infants","volume":"33","author":"Tameris","year":"2015","journal-title":"Vaccine"},{"key":"10.1016\/j.sbi.2022.102348_bib24","doi-asserted-by":"crossref","first-page":"2754","DOI":"10.3389\/fimmu.2018.02754","article-title":"Glycans as key checkpoints of T cell activity and function","volume":"9","author":"Pereira","year":"2018","journal-title":"Front Immunol"},{"key":"10.1016\/j.sbi.2022.102348_bib25","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1093\/glycob\/cwr087","article-title":"Since there are PAMPs and DAMPs, there must be SAMPs? Glycan \"self-associated molecular patterns\" dampen innate immunity, but pathogens can mimic them","volume":"21","author":"Varki","year":"2011","journal-title":"Glycobiology"},{"key":"10.1016\/j.sbi.2022.102348_bib26","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1111\/j.1749-6632.2011.06362.x","article-title":"Siglecs as sensors of self in innate and adaptive immune responses","volume":"1253","author":"Paulson","year":"2012","journal-title":"Ann N Y Acad Sci"},{"key":"10.1016\/j.sbi.2022.102348_bib27","doi-asserted-by":"crossref","first-page":"818","DOI":"10.1093\/glycob\/cwu067","article-title":"The interplay between Siglecs and sialylated pathogens","volume":"24","author":"Chang","year":"2014","journal-title":"Glycobiology"},{"key":"10.1016\/j.sbi.2022.102348_bib28","doi-asserted-by":"crossref","first-page":"3333","DOI":"10.1182\/blood-2008-11-187302","article-title":"Molecular mimicry of host sialylated glycans allows a bacterial pathogen to engage neutrophil Siglec-9 and dampen the innate immune response","volume":"113","author":"Carlin","year":"2009","journal-title":"Blood"},{"key":"10.1016\/j.sbi.2022.102348_bib29","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1016\/S0966-842X(02)02361-2","article-title":"To sialylate, or not to sialylate: that is the question","volume":"10","author":"Vimr","year":"2002","journal-title":"Trends Microbiol"},{"key":"10.1016\/j.sbi.2022.102348_bib30","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1189\/jlb.0511260","article-title":"Sialoglycoproteins adsorbed by Pseudomonas aeruginosa facilitate their survival by impeding neutrophil extracellular trap through siglec-9","volume":"91","author":"Khatua","year":"2012","journal-title":"J\u00a0Leukoc Biol"},{"key":"10.1016\/j.sbi.2022.102348_bib31","doi-asserted-by":"crossref","first-page":"1142","DOI":"10.1093\/glycob\/cwv057","article-title":"The trans-sialidase, the major Trypanosoma cruzi virulence factor: three decades of studies","volume":"25","author":"Freire-de-Lima","year":"2015","journal-title":"Glycobiology"},{"key":"10.1016\/j.sbi.2022.102348_bib32","first-page":"640","article-title":"Targeting sialic acid-Siglec interactions to reverse immune suppression in cancer","volume":"28","author":"Adams","year":"2018","journal-title":"Glycobiology"},{"key":"10.1016\/j.sbi.2022.102348_bib33","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1038\/nchembio.1388","article-title":"Glycocalyx engineering reveals a Siglec-based mechanism for NK cell immunoevasion","volume":"10","author":"Hudak","year":"2014","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.sbi.2022.102348_bib34","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1159\/000030036","article-title":"Histopathological subtypes and prognosis of gastric cancer are correlated with the expression of mucin-associated sialylated antigens: sialosyl-Lewis(a), Sialosyl-Lewis(x) and sialosyl-Tn","volume":"19","author":"Baldus","year":"1998","journal-title":"Tumour Biol"},{"key":"10.1016\/j.sbi.2022.102348_bib35","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1093\/glycob\/cww062","article-title":"Carbohydrates as T-cell antigens with implications in health and disease","volume":"26","author":"Sun","year":"2016","journal-title":"Glycobiology"},{"key":"10.1016\/j.sbi.2022.102348_bib36","doi-asserted-by":"crossref","first-page":"2550","DOI":"10.1038\/s41467-020-16319-0","article-title":"Glycopeptide epitope facilitates HIV-1 envelope specific humoral immune responses by eliciting T cell help","volume":"11","author":"Sun","year":"2020","journal-title":"Nat Commun"},{"key":"10.1016\/j.sbi.2022.102348_bib37","doi-asserted-by":"crossref","first-page":"15178","DOI":"10.1074\/jbc.RA118.004798","article-title":"Metabolic labeling of HIV-1 envelope glycoprotein gp120 to elucidate the effect of gp120 glycosylation on antigen uptake","volume":"293","author":"Sun","year":"2018","journal-title":"J\u00a0Biol Chem"},{"key":"10.1016\/j.sbi.2022.102348_bib38","doi-asserted-by":"crossref","first-page":"8094","DOI":"10.1128\/JVI.78.15.8094-8101.2004","article-title":"Porcine arterivirus infection of alveolar macrophages is mediated by sialic acid on the virus","volume":"78","author":"Delputte","year":"2004","journal-title":"J\u00a0Virol"},{"key":"10.1016\/j.sbi.2022.102348_sref39","doi-asserted-by":"crossref","first-page":"1480","DOI":"10.1016\/j.bbagen.2019.05.012","article-title":"Exploitation of glycosylation in enveloped virus pathobiology","volume":"1863","author":"Watanabe","year":"2019","journal-title":"Biochim Biophys Acta Gen Subj"},{"key":"10.1016\/j.sbi.2022.102348_bib40","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.sbi.2016.10.003","article-title":"Glycan-protein interactions in viral pathogenesis","volume":"40","author":"Raman","year":"2016","journal-title":"Curr Opin Struct Biol"},{"key":"10.1016\/j.sbi.2022.102348_sref41","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1126\/science.abb9983","article-title":"Site-specific glycan analysis of the SARS-CoV-2 spike","volume":"369","author":"Watanabe","year":"2020","journal-title":"Science"},{"key":"10.1016\/j.sbi.2022.102348_bib42","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1016\/j.chom.2020.08.004","article-title":"Virus-receptor interactions of glycosylated SARS-CoV-2 spike and human ACE2 receptor","volume":"28","author":"Zhao","year":"2020","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.sbi.2022.102348_bib43","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1146\/annurev-biophys-060414-034156","article-title":"Structure and immune recognition of the HIV glycan shield","volume":"47","author":"Crispin","year":"2018","journal-title":"Annu Rev Biophys"},{"key":"10.1016\/j.sbi.2022.102348_bib44","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1038\/s41586-020-2349-y","article-title":"Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody","volume":"583","author":"Pinto","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.sbi.2022.102348_bib45","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1038\/nature10696","article-title":"Structure of HIV-1 gp120 V1\/V2 domain with broadly neutralizing antibody PG9","volume":"480","author":"McLellan","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.sbi.2022.102348_bib46","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1126\/science.1213256","article-title":"A\u00a0potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield","volume":"334","author":"Pejchal","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.sbi.2022.102348_bib47","doi-asserted-by":"crossref","first-page":"13372","DOI":"10.1073\/pnas.0505763102","article-title":"Dissection of the carbohydrate specificity of the broadly neutralizing anti-HIV-1 antibody 2G12","volume":"102","author":"Calarese","year":"2005","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.sbi.2022.102348_sref48","doi-asserted-by":"crossref","first-page":"e1009407","DOI":"10.1371\/journal.ppat.1009407","article-title":"A\u00a0cross-neutralizing antibody between HIV-1 and influenza virus","volume":"17","author":"Lee","year":"2021","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.sbi.2022.102348_bib49","doi-asserted-by":"crossref","first-page":"674","DOI":"10.15585\/mmwr.mm7018e1","article-title":"Effectiveness of pfizer-BioNTech and moderna vaccines against COVID-19 among hospitalized adults aged >\/=65 Years - United States, january-march 2021","volume":"70","author":"Tenforde","year":"2021","journal-title":"MMWR Morb Mortal Wkly Rep"},{"key":"10.1016\/j.sbi.2022.102348_bib50","first-page":"e16197","article-title":"HIV and messenger RNA (mRNA) vaccine","volume":"13","author":"Khalid","year":"2021","journal-title":"Cureus"},{"key":"10.1016\/j.sbi.2022.102348_bib51","article-title":"Current progress in the development of zika virus vaccines","volume":"9","author":"Zhou","year":"2021","journal-title":"Vaccines (Basel)"},{"key":"10.1016\/j.sbi.2022.102348_bib52","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.coph.2021.06.008","article-title":"Recent developments and strategies of Ebola virus vaccines","volume":"60","author":"Sharma","year":"2021","journal-title":"Curr Opin Pharmacol"},{"key":"10.1016\/j.sbi.2022.102348_bib53","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1016\/1043-4666(91)90018-9","article-title":"Marked cell-type-specific differences in glycosylation of human interleukin-6","volume":"3","author":"May","year":"1991","journal-title":"Cytokine"},{"key":"10.1016\/j.sbi.2022.102348_bib54","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1038\/nrm3383","article-title":"Vertebrate protein glycosylation: diversity, synthesis and function","volume":"13","author":"Moremen","year":"2012","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.1016\/j.sbi.2022.102348_bib55","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/bs.apcsb.2019.08.008","article-title":"Glycosylation changes in inflammatory diseases","volume":"119","author":"Groux-Degroote","year":"2020","journal-title":"Adv Protein Chem Struct Biol"},{"key":"10.1016\/j.sbi.2022.102348_bib56","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1155\/2008\/493289","article-title":"Glycosylation of serum proteins in inflammatory diseases","volume":"25","author":"Gornik","year":"2008","journal-title":"Dis Markers"},{"key":"10.1016\/j.sbi.2022.102348_bib57","doi-asserted-by":"crossref","first-page":"102945","DOI":"10.1016\/j.ebiom.2020.102945","article-title":"Interferon-alpha alters host glycosylation machinery during treated HIV infection","volume":"59","author":"Giron","year":"2020","journal-title":"EBioMedicine"},{"key":"10.1016\/j.sbi.2022.102348_sref58","doi-asserted-by":"crossref","first-page":"107991","DOI":"10.1016\/j.celrep.2020.107991","article-title":"Sialyl-Lewis(X) glycoantigen is enriched on cells with persistent HIV transcription during therapy","volume":"32","author":"Colomb","year":"2020","journal-title":"Cell Rep"}],"container-title":["Current Opinion in Structural Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959440X22000276?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959440X22000276?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,17]],"date-time":"2025-10-17T13:25:33Z","timestamp":1760707533000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0959440X22000276"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,4]]},"references-count":58,"alternative-id":["S0959440X22000276"],"URL":"https:\/\/doi.org\/10.1016\/j.sbi.2022.102348","relation":{},"ISSN":["0959-440X"],"issn-type":[{"value":"0959-440X","type":"print"}],"subject":[],"published":{"date-parts":[[2022,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Glycosylation as a key parameter in the design of nucleic acid vaccines","name":"articletitle","label":"Article Title"},{"value":"Current Opinion in Structural Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.sbi.2022.102348","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"102348"}}