{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,17]],"date-time":"2026-04-17T21:11:30Z","timestamp":1776460290098,"version":"3.51.2"},"reference-count":72,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2020,10,1]],"date-time":"2020-10-01T00:00:00Z","timestamp":1601510400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,10,1]],"date-time":"2020-10-01T00:00:00Z","timestamp":1601510400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2020,10,1]],"date-time":"2020-10-01T00:00:00Z","timestamp":1601510400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2020,10,1]],"date-time":"2020-10-01T00:00:00Z","timestamp":1601510400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2020,10,1]],"date-time":"2020-10-01T00:00:00Z","timestamp":1601510400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2020,10,1]],"date-time":"2020-10-01T00:00:00Z","timestamp":1601510400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2020,10,1]],"date-time":"2020-10-01T00:00:00Z","timestamp":1601510400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"name":"Nacbraht Biomedical Research Institute Fund"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2020,10]]},"DOI":"10.1016\/j.bbrc.2020.08.024","type":"journal-article","created":{"date-parts":[[2020,8,15]],"date-time":"2020-08-15T07:48:24Z","timestamp":1597477704000},"page":"134-138","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":39,"title":["Mutations in the phosphorylation sites of SARS-CoV-2 encoded nucleocapsid protein and structure model of sequestration by protein 14-3-3"],"prefix":"10.1016","volume":"532","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7112-7477","authenticated-orcid":false,"given":"H.Y. Lim","family":"Tung","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pierre","family":"Limtung","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrc.2020.08.024_bib1","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1056\/NEJMoa2001017","article-title":"A\u00a0novel coronavirus from patients with pneumonia in China","volume":"382","author":"Zhu","year":"2019","journal-title":"N.\u00a0Engl. J. Med."},{"key":"10.1016\/j.bbrc.2020.08.024_bib2","unstructured":"R. Lu, X. Zhao, J. Li, et\u00a0al. Genomic characterization and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding. Lancet 395 (2020), 565-574."},{"key":"10.1016\/j.bbrc.2020.08.024_bib3","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1038\/s41586-020-2012-7","article-title":"A\u00a0pneumonia outbreak associated with a new coronavirus of probable bat origin","volume":"579","author":"Zhou","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2020.08.024_bib4","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1038\/s41586-020-2008-3","article-title":"A\u00a0new coronavirus associated with human respiratory disease in China","volume":"579","author":"Wu","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2020.08.024_bib5","article-title":"SARS-COV-2 infection and virulence: reverse correlations with temperature, humidity and far infrared radiation. Elevated temperature, humidity and far infrared irradiation will significantly lower the viability, infectivity and virulence of SARS-COV-2","author":"Tung","year":"2020","journal-title":"ResearchGate"},{"key":"10.1016\/j.bbrc.2020.08.024_bib6","article-title":"SARS-COV-2 infection and virulence: comparison between United Kingdom and Germany, and other European countries","author":"Tung","year":"2020","journal-title":"Researchgate"},{"key":"10.1016\/j.bbrc.2020.08.024_bib7","article-title":"RBD mutations from circulating SARS-CoV-2 strains enhance the structure stability and infectivity of the spike proteins","author":"Ou","year":"2020","journal-title":"bioRxiv"},{"key":"10.1016\/j.bbrc.2020.08.024_bib8","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1038\/nature02145","article-title":"Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus","volume":"426","author":"Li","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2020.08.024_bib9","first-page":"875","article-title":"A\u00a0crucial role of angiotensin converting enzyme 2 (ACE2) in SARS coronavirus-induced lung injury","volume":"11","author":"Kuba","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2020.08.024_bib10","article-title":"Emerging SARS-CoV-2 mutation hot spots include a novel RNA-dependent-RNA polymerase variant","author":"Panchetti","year":"2020","journal-title":"J.\u00a0Transl. Med."},{"key":"10.1016\/j.bbrc.2020.08.024_bib11","doi-asserted-by":"crossref","DOI":"10.1016\/j.meegid.2020.104260","article-title":"Genetic diversity and evolution of SARS-CoV-2","author":"Phan","year":"2020","journal-title":"Infect. Genet. Evol."},{"key":"10.1016\/j.bbrc.2020.08.024_bib12","doi-asserted-by":"crossref","DOI":"10.1016\/j.nmni.2020.100673","article-title":"Mutated COVID-19 may foretell a great risk for mankind in the future","author":"Dawood","year":"2020","journal-title":"New Microbes New Infect."},{"key":"10.1016\/j.bbrc.2020.08.024_bib13","doi-asserted-by":"crossref","DOI":"10.1016\/j.ygeno.2020.04.016","article-title":"Genotyping coronavirus SARS-CoV-2: methods and implications","author":"Yin","year":"2020","journal-title":"Genomics"},{"key":"10.1016\/j.bbrc.2020.08.024_bib14","series-title":"Evidence for Mutations in SARS-CoV-2 Italian Isolates Potentially Affecting Virus Transmission","author":"Benvenuoto","year":"2020"},{"key":"10.1016\/j.bbrc.2020.08.024_bib15","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01925-19","article-title":"Nucleocapsid protein recruitment to replication-transcription complexes plays a crucial role in coronaviral life cycle","author":"Cong","year":"2020","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.bbrc.2020.08.024_bib16","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.antiviral.2013.12.009","article-title":"The SARS coronavirus nucleocapsid protein--forms and functions","volume":"103","author":"Chang","year":"2014","journal-title":"Antivir. Res."},{"key":"10.1016\/j.bbrc.2020.08.024_bib17","doi-asserted-by":"crossref","first-page":"3100","DOI":"10.1016\/j.vaccine.2006.01.058","article-title":"Immunological characterization of the nucleocapsid protein based SARS vaccine","volume":"24","author":"Liu","year":"2006","journal-title":"Vaccine"},{"key":"10.1016\/j.bbrc.2020.08.024_bib18","doi-asserted-by":"crossref","DOI":"10.2217\/fvl-2020-0020","article-title":"Prediction and analysis of key protein structures of 2029-nCoV","author":"Li","year":"2020","journal-title":"Future Virol."},{"key":"10.1016\/j.bbrc.2020.08.024_bib19","doi-asserted-by":"crossref","first-page":"10669","DOI":"10.1074\/jbc.M509233200","article-title":"The nucleocapsid protein of severe acute respiratory syndrome-coronavirus inhibits the activity of cyclin-cyclindependent kinase complex and blocks S phase progression in mammalian cells","volume":"281","author":"Surjit","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bbrc.2020.08.024_bib20","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1111\/j.1574-695X.2005.00028.x","article-title":"Inhibition of cell proliferation by SARS-CoV infection in Vero E6 cells","volume":"46","author":"Mizutani","year":"2006","journal-title":"FEMS Immunol"},{"key":"10.1016\/j.bbrc.2020.08.024_bib21","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1038\/374131a0","article-title":"Principles of CDK regulations","volume":"374","author":"Morgan","year":"1995","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2020.08.024_bib22","volume":"vol. 1","author":"Meijer","year":"1995"},{"key":"10.1016\/j.bbrc.2020.08.024_bib23","doi-asserted-by":"crossref","first-page":"2461","DOI":"10.1242\/jcs.115.12.2461","article-title":"From cdc 2 to Cdk1: when did the cell cycle kinase join its cyclin partner","volume":"115","author":"Doree","year":"2002","journal-title":"J.\u00a0Cell Sci."},{"key":"10.1016\/j.bbrc.2020.08.024_bib24","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1002\/1439-7633(20020703)3:7<596::AID-CBIC596>3.0.CO;2-U","article-title":"Cyclin dependent kinases and cell cycle control","volume":"3","author":"Nurse","year":"2002","journal-title":"Chembiochem"},{"key":"10.1016\/j.bbrc.2020.08.024_bib25","first-page":"97","article-title":"Role of protein phosphatase-2A (PP-2A) in the control of mitosis and meiosis New Biomed","volume":"1","author":"Tung","year":"2020","journal-title":"Sci. Asia"},{"key":"10.1016\/j.bbrc.2020.08.024_bib26","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1038\/44188","article-title":"14-3-3Sigma is required to prevent mitotic catastrophe after DNA damage","volume":"401","author":"Chan","year":"1999","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2020.08.024_bib27","doi-asserted-by":"crossref","first-page":"1501","DOI":"10.1126\/science.277.5331.1501","article-title":"Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216","volume":"277","author":"Peng","year":"1998","journal-title":"Science"},{"issue":"2004","key":"10.1016\/j.bbrc.2020.08.024_bib28","first-page":"672","article-title":"14-3-3 family members act coordinately to regulate mitotic progression","volume":"3","author":"Dalal","year":"2004","journal-title":"Cell Cycle"},{"key":"10.1016\/j.bbrc.2020.08.024_bib29","doi-asserted-by":"crossref","first-page":"45193","DOI":"10.1074\/jbc.M105971200","article-title":"14-3-3 proteins mediate an essential anti-apoptotic signal","volume":"276","author":"Masters","year":"2001","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bbrc.2020.08.024_bib30","doi-asserted-by":"crossref","first-page":"19347","DOI":"10.1074\/jbc.M213098200","article-title":"Cleavage of 14-3-3 protein by caspase-3 facilitates bad interaction with bcl-x(L) during apoptosis","volume":"278","author":"Won","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bbrc.2020.08.024_bib33","doi-asserted-by":"crossref","first-page":"1715","DOI":"10.1002\/prot.24065","article-title":"Ab initio protein structure assembly using continuous structure fragments and optimized knowledge-based force field","volume":"80","author":"Xu","year":"2012","journal-title":"Proteins"},{"key":"10.1016\/j.bbrc.2020.08.024_bib34","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1002\/prot.24179","article-title":"Toward optimal fragment generations for ab initio protein structure assembly","volume":"81","author":"Xu","year":"2013","journal-title":"Proteins"},{"key":"10.1016\/j.bbrc.2020.08.024_bib35","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1038\/sj.cr.7290290","article-title":"The crystal structure of the nonliganded 14-3-3sigma protein: insights into determinants of isoform specific ligand binding and dimerization","volume":"15","author":"Benzinger","year":"2005","journal-title":"Cell Res."},{"key":"10.1016\/j.bbrc.2020.08.024_bib36","first-page":"386","article-title":"Presenting your structures: the CCP4mg molecular-graphics software","volume":"D67","author":"McNicholas","year":"2011","journal-title":"Acta Crystallogr."},{"key":"10.1016\/j.bbrc.2020.08.024_bib37","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1007\/s10822-009-9317-9","article-title":"Docking flexible ligands in proteins with a solvent exposure- and distance-dependent dielectric function","volume":"25","author":"Garden","year":"2010","journal-title":"J.\u00a0Comput. Aided Mol. Des."},{"key":"10.1016\/j.bbrc.2020.08.024_bib38","doi-asserted-by":"crossref","DOI":"10.1093\/nar\/gki387","article-title":"The FoldX web server: an online force field","author":"Schymkowitz","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbrc.2020.08.024_bib39","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.1093\/bioinformatics\/btu097","article-title":"ZDOCK server: interactive docking prediction of protein-protein complexes and symmetric multimers","volume":"30","author":"Pierce","year":"2014","journal-title":"Bioinformatics"},{"key":"10.1016\/j.bbrc.2020.08.024_bib40","doi-asserted-by":"crossref","first-page":"9454","DOI":"10.1073\/pnas.89.20.9454","article-title":"Cell cycle-dependent localization of casein kinase I to mitotic spindles","volume":"89","author":"Brockman","year":"1992","journal-title":"Proc. Natl. Acad. Sci. Unit. States Am."},{"key":"10.1016\/j.bbrc.2020.08.024_bib41","doi-asserted-by":"crossref","first-page":"6509","DOI":"10.1128\/MCB.25.15.6509-6520.2005","article-title":"Regulation of p53-MDMX interaction by casein kinase 1 alpha","volume":"25","author":"Chen","year":"2005","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.bbrc.2020.08.024_bib42","article-title":"The Yck2 yeast casein kinase 1 isoform shows cell cycle-specific localization to sites of polarized growth and is required for proper septin organization","author":"Bradley","year":"2017","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bbrc.2020.08.024_bib43","first-page":"4731","article-title":"Type 1 protein phosphatase acts in opposition to IpL1 protein kinase in regulating yeast chromosome segregation","volume":"14","author":"Francisco","year":"1994","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.bbrc.2020.08.024_bib44","doi-asserted-by":"crossref","first-page":"6064","DOI":"10.1128\/MCB.15.11.6064","article-title":"Regulation of chromosome segregation by Glc8p, a structural homolog of mammalian inhibitor 2 that functions as both an activator and an inhibitor of yeast protein phosphatase 1","volume":"15","author":"Tung","year":"1995","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.bbrc.2020.08.024_bib45","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1158\/1541-7786.MCR-06-0208","article-title":"Roles of Aurora kinases in mitosis and tumorigenesis","volume":"5","author":"Fu","year":"2007","journal-title":"Mol. Canc. Res."},{"key":"10.1016\/j.bbrc.2020.08.024_bib46","doi-asserted-by":"crossref","first-page":"pp1682","DOI":"10.1126\/science.1172867","article-title":"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution","volume":"325","author":"Holt","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.bbrc.2020.08.024_bib47","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1016\/S0960-9822(00)00221-9","article-title":"Use of an oriented peptide library to determine the optimal substrates of protein kinases","volume":"4","author":"Songyang","year":"1994","journal-title":"Curr. Biol."},{"key":"10.1016\/j.bbrc.2020.08.024_bib48","doi-asserted-by":"crossref","first-page":"14042","DOI":"10.1016\/S0021-9258(18)47901-X","article-title":"Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3","volume":"262","author":"Fiol","year":"1987","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bbrc.2020.08.024_bib49","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj3590001","article-title":"GSK-3 takes centre stage more than 20 years after its discovery","volume":"359","author":"Frame","year":"2001","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbrc.2020.08.024_bib50","author":"Kaidanovich-Beilin"},{"key":"10.1016\/j.bbrc.2020.08.024_bib51","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-018-32435-w","article-title":"Analysis of the role of GSK3 in the mitotic checkpoint","author":"Rashid","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbrc.2020.08.024_bib52","doi-asserted-by":"crossref","first-page":"4888","DOI":"10.1016\/S0021-9258(17)40137-2","article-title":"Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase","volume":"252","author":"Kemp","year":"1977","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bbrc.2020.08.024_bib53","doi-asserted-by":"crossref","first-page":"1555","DOI":"10.1016\/S0021-9258(18)98436-X","article-title":"Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases","volume":"266","author":"Kennelly","year":"1991","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bbrc.2020.08.024_bib54","doi-asserted-by":"crossref","first-page":"30461","DOI":"10.1016\/S0021-9258(18)43836-7","article-title":"Purification of a serine kinase that associates with and phosphorylates human Cdc25C on serine 216","volume":"269","author":"Ogg","year":"1994","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bbrc.2020.08.024_bib55","doi-asserted-by":"crossref","first-page":"4431","DOI":"10.1093\/emboj\/cdg426","article-title":"Functional analysis of CTAK1 substrate binding and identification of PKP2 as a new C-TAK1 substrate","volume":"22","author":"Muller","year":"2003","journal-title":"EMBO J."},{"key":"10.1016\/j.bbrc.2020.08.024_bib56","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.antiviral.2013.12.009","article-title":"The SARS coronavirus nucleocapsid protein--forms and functions","volume":"103","author":"Chang","year":"2014","journal-title":"Antivir. Res."},{"key":"10.1016\/j.bbrc.2020.08.024_bib57","doi-asserted-by":"crossref","first-page":"1647","DOI":"10.1016\/S0021-9258(18)97483-1","article-title":"Chromatographic and electrophoretic fractionation of soluble proteins of brain and liver","volume":"240","author":"Moore","year":"1965","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bbrc.2020.08.024_bib58","doi-asserted-by":"crossref","first-page":"5404","DOI":"10.1016\/S0021-9258(19)69215-X","article-title":"A\u00a0new activator protein that activates tryptophan 5-monooxygenase and tyrosine 3-monooxygenase in the presence of Ca2+-, calmodulin-dependent protein kinase. Purification and characterization","volume":"256","author":"Yamauchi","year":"1981","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bbrc.2020.08.024_bib59","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/0014-5793(87)81194-8","article-title":"Brain 14-3-3 protein is an activator protein that activates tryptophan 5-monooxygenase and tyrosine 3 monooxygenase in the presence of Ca2+, calmodulin-dependent protein kinase II","volume":"219","author":"Ichimura","year":"1987","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbrc.2020.08.024_bib60","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.semcancer.2006.03.005","article-title":"14-3-3 proteins: a historic overview","volume":"16","author":"Aitken","year":"2006","journal-title":"Semin. Canc. Biol."},{"key":"10.1016\/j.bbrc.2020.08.024_bib61","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1006\/bbrc.1993.1796","article-title":"Demonstration of the phosphorylation dependent interaction of tryptophan hydroxylase with the 14-3-3 protein","volume":"194","author":"Furukawa","year":"1993","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbrc.2020.08.024_bib62","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1016\/S0092-8674(00)81067-3","article-title":"Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine","volume":"84","author":"Muslin","year":"1996","journal-title":"Cell"},{"key":"10.1016\/j.bbrc.2020.08.024_bib63","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1016\/S0092-8674(00)80487-0","article-title":"The structural basis for 14-3- 3:phosphopeptide binding specificity","volume":"91","author":"Yaffe","year":"1997","journal-title":"Cell"},{"key":"10.1016\/j.bbrc.2020.08.024_bib64","doi-asserted-by":"crossref","first-page":"6612","DOI":"10.1128\/JVI.00157-06","article-title":"X-ray structures of the N- and CTerminal domains of a coronavirus nucleocapsid protein: implications for nucleocapsid formation","volume":"80","author":"Jayaram","year":"2006","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.bbrc.2020.08.024_bib65","article-title":"Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites","author":"Kang","year":"2020","journal-title":"bioRxiv"},{"key":"10.1016\/j.bbrc.2020.08.024_bib66","series-title":"Crystal Structure of the C-Terminal Domain of SARSCoV- 2 Nucleocapsid Protein","author":"Zhou","year":"2020"},{"key":"10.1016\/j.bbrc.2020.08.024_bib67","series-title":"Structure of SARS-CoV-2 Nucleocapsid Dimerization Domain","author":"Ye","year":"2020"},{"key":"10.1016\/j.bbrc.2020.08.024_bib68","author":"Minasov"},{"key":"10.1016\/j.bbrc.2020.08.024_bib69","series-title":"1.45 Angstrom Resolution Crystal Structure of C-Terminal Dimerization Domain of Nucleocapsid Phosphoprotein from SARS-CoV-2","author":"Zinzula","year":"2020"},{"key":"10.1016\/j.bbrc.2020.08.024_bib70","doi-asserted-by":"crossref","first-page":"188-","DOI":"10.1038\/376188a0","article-title":"Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways","volume":"376","author":"Xiao","year":"1995","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2020.08.024_bib71","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1038\/376191a0","article-title":"Crystal structure of the zeta isoform of the 14-3-3 protein","volume":"376","author":"Liu","year":"1995","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2020.08.024_bib72","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1016\/j.chom.2014.09.009","article-title":"Nucleocapsid phosphorylation and RNA helicase DDX1 recruitment enables Coronavirus transition from discontinuous transcription","volume":"16","author":"Wu","year":"2014","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.bbrc.2020.08.024_bib73","doi-asserted-by":"crossref","first-page":"5229","DOI":"10.1074\/jbc.M805747200","article-title":"Glycogen synthase kinase-3 regulates the phosphorylation of severe acute respiratory syndrome coronavirus nucleocapsid protein and viral replication","volume":"284","author":"Wu","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bbrc.2020.08.024_bib74","doi-asserted-by":"crossref","first-page":"11476","DOI":"10.1128\/JVI.79.17.11476-11486.2005","article-title":"The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation","volume":"79","author":"Surijit","year":"2005","journal-title":"J.\u00a0Virol."}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X20315758?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X20315758?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,17]],"date-time":"2026-04-17T20:35:37Z","timestamp":1776458137000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X20315758"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,10]]},"references-count":72,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2020,10]]}},"alternative-id":["S0006291X20315758"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrc.2020.08.024","relation":{},"ISSN":["0006-291X"],"issn-type":[{"value":"0006-291X","type":"print"}],"subject":[],"published":{"date-parts":[[2020,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Mutations in the phosphorylation sites of SARS-CoV-2 encoded nucleocapsid protein and structure model of sequestration by protein 14-3-3","name":"articletitle","label":"Article Title"},{"value":"Biochemical and Biophysical Research Communications","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbrc.2020.08.024","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}