{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T02:37:19Z","timestamp":1790995039746,"version":"4.1.0"},"reference-count":75,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2024,6,1]],"date-time":"2024-06-01T00:00:00Z","timestamp":1717200000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,6,1]],"date-time":"2024-06-01T00:00:00Z","timestamp":1717200000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,5,6]],"date-time":"2024-05-06T00:00:00Z","timestamp":1714953600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["1S10OD018518"],"award-info":[{"award-number":["1S10OD018518"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000937","name":"M.J. Murdock Charitable Trust","doi-asserted-by":"publisher","award":["2014162"],"award-info":[{"award-number":["2014162"]}],"id":[{"id":"10.13039\/100000937","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100009612","name":"Oregon State University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100009612","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["MCB 2034446"],"award-info":[{"award-number":["MCB 2034446"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["RM1-GM144227"],"award-info":[{"award-number":["RM1-GM144227"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2024,6]]},"DOI":"10.1016\/j.jbc.2024.107354","type":"journal-article","created":{"date-parts":[[2024,5,7]],"date-time":"2024-05-07T01:29:21Z","timestamp":1715045361000},"page":"107354","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":39,"title":["Phosphorylation in the Ser\/Arg-rich region of the nucleocapsid of SARS-CoV-2 regulates phase separation by inhibiting self-association of a distant helix"],"prefix":"10.1016","volume":"300","author":[{"given":"Hannah","family":"Stuwe","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6858-0086","authenticated-orcid":false,"given":"Patrick N.","family":"Reardon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhen","family":"Yu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sahana","family":"Shah","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kaitlyn","family":"Hughes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elisar J.","family":"Barbar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2024.107354_bib1","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.jbc.2024.107354_bib2","doi-asserted-by":"crossref","first-page":"2991","DOI":"10.3390\/v6082991","article-title":"The coronavirus nucleocapsid is a multifunctional protein","volume":"6","author":"McBride","year":"2014","journal-title":"Viruses"},{"key":"10.1016\/j.jbc.2024.107354_bib3","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1016\/j.cell.2020.09.018","article-title":"Molecular architecture of the SARS-CoV-2 virus","volume":"183","author":"Yao","year":"2020","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2024.107354_bib4","doi-asserted-by":"crossref","first-page":"3917","DOI":"10.1038\/s41467-021-22785-x","article-title":"The architecture of the SARS-CoV-2 RNA genome inside virion","volume":"12","author":"Cao","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2024.107354_bib5","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.100821","article-title":"Arginine methylation of SARS-Cov-2 nucleocapsid protein regulates RNA binding, its ability to suppress stress granule formation, and viral replication","volume":"297","author":"Cai","year":"2021","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107354_bib6","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2021.109482","article-title":"Compartmentalization-aided interaction screening reveals extensive high-order complexes within the SARS-CoV-2 proteome","volume":"36","author":"Xu","year":"2021","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2024.107354_bib7","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","volume":"94","author":"Cong","year":"2020","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.jbc.2024.107354_bib8","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1016\/j.scib.2021.01.013","article-title":"SARS-CoV-2 nucleocapsid protein phase separates with G3BPs to disassemble stress granules and facilitate viral production","volume":"66","author":"Luo","year":"2021","journal-title":"Sci. Bull."},{"key":"10.1016\/j.jbc.2024.107354_bib9","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2024.113965","article-title":"Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replication and pathogenicity","volume":"43","author":"Yang","year":"2024","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2024.107354_bib10","doi-asserted-by":"crossref","first-page":"1143","DOI":"10.1038\/s41422-020-00408-2","article-title":"Liquid-liquid phase separation by SARS-CoV-2 nucleocapsid protein and RNA","volume":"30","author":"Chen","year":"2020","journal-title":"Cell Res."},{"key":"10.1016\/j.jbc.2024.107354_bib11","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1038\/s41467-020-20768-y","article-title":"The SARS-CoV-2 nucleocapsid phosphoprotein forms mutually exclusive condensates with RNA and the membrane-associated M protein","volume":"12","author":"Lu","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2024.107354_bib12","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.3001425","article-title":"SARS-CoV-2 nucleocapsid protein forms condensates with viral genomic RNA","volume":"19","author":"Jack","year":"2021","journal-title":"PLoS Biol."},{"key":"10.1016\/j.jbc.2024.107354_bib13","doi-asserted-by":"crossref","DOI":"10.1002\/pro.4409","article-title":"Contributions of the N-terminal intrinsically disordered region of the severe acute respiratory syndrome coronavirus 2 nucleocapsid protein to RNA-induced phase separation","volume":"31","author":"Zachrdla","year":"2022","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2024.107354_bib14","doi-asserted-by":"crossref","first-page":"8168","DOI":"10.1093\/nar\/gkac596","article-title":"Double-stranded RNA drives SARS-CoV-2 nucleocapsid protein to undergo phase separation at specific temperatures","volume":"50","author":"Roden","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jbc.2024.107354_bib15","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2020106478","article-title":"SARS-CoV-2 nucleocapsid protein phase-separates with RNA and with human hnRNPs","volume":"39","author":"Perdikari","year":"2020","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2024.107354_bib16","doi-asserted-by":"crossref","first-page":"e4826","DOI":"10.1002\/pro.4826","article-title":"Nucleocapsid proteins from human coronaviruses possess phase separation capabilities and promote FUS pathological aggregation","volume":"32","author":"Dong","year":"2023","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2024.107354_bib17","doi-asserted-by":"crossref","first-page":"2379","DOI":"10.1038\/s41467-023-37865-3","article-title":"Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils","volume":"14","author":"Tayeb-Fligelman","year":"2023","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2024.107354_bib18","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.101677","article-title":"Phase separation by the SARS-CoV-2 nucleocapsid protein: consensus and open questions","volume":"298","author":"Cascarina","year":"2022","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107354_bib19","doi-asserted-by":"crossref","first-page":"1092","DOI":"10.1016\/j.molcel.2020.11.025","article-title":"Phosphoregulation of phase separation by the SARS-CoV-2 N protein suggests a biophysical basis for its dual functions","volume":"80","author":"Carlson","year":"2020","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2024.107354_bib20","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2308355120","article-title":"Cellular nucleic acid-binding protein restricts SARS-CoV-2 by regulating interferon and disrupting RNA-protein condensates","volume":"120","author":"Chen","year":"2023","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2024.107354_bib21","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2020105938","article-title":"Structures of the SARS-CoV-2 nucleocapsid and their perspectives for drug design","volume":"39","author":"Peng","year":"2020","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2024.107354_bib22","doi-asserted-by":"crossref","first-page":"2890","DOI":"10.1016\/j.bpj.2021.03.023","article-title":"Multivalent binding of the partially disordered SARS-CoV-2 nucleocapsid phosphoprotein dimer to RNA","volume":"120","author":"Forsythe","year":"2021","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2024.107354_bib23","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1186\/s43556-020-00001-4","article-title":"Structural characterization of the C-terminal domain of SARS-CoV-2 nucleocapsid protein","volume":"1","author":"Zhou","year":"2020","journal-title":"Mol. Biomed."},{"key":"10.1016\/j.jbc.2024.107354_bib24","doi-asserted-by":"crossref","first-page":"pgad333","DOI":"10.1093\/pnasnexus\/pgad333","article-title":"RNA structure and multiple weak interactions balance the interplay between RNA binding and phase separation of SARS-CoV-2 nucleocapsid","volume":"2","author":"Estelle","year":"2023","journal-title":"PNAS Nexus"},{"key":"10.1016\/j.jbc.2024.107354_bib25","doi-asserted-by":"crossref","first-page":"3331","DOI":"10.1038\/s41467-023-38882-y","article-title":"The preference signature of the SARS-CoV-2 Nucleocapsid NTD for its 5'-genomic RNA elements","volume":"14","author":"Korn","year":"2023","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2024.107354_bib26","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1016\/j.ijbiomac.2022.01.121","article-title":"Insights into the specificity for the interaction of the promiscuous SARS-CoV-2 nucleocapsid protein N-terminal domain with deoxyribonucleic acids","volume":"203","author":"Caruso","year":"2022","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.jbc.2024.107354_bib27","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2021.167108","article-title":"The inherent dynamics and interaction sites of the SARS-CoV-2 nucleocapsid N-terminal region","volume":"433","author":"Redzic","year":"2021","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2024.107354_bib28","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1009100","article-title":"Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid phosphoprotein","volume":"16","author":"Dinesh","year":"2020","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2024.107354_bib29","doi-asserted-by":"crossref","first-page":"2609","DOI":"10.1093\/nar\/gkad1215","article-title":"The disordered N-terminal tail of SARS-CoV-2 Nucleocapsid protein forms a dynamic complex with RNA","volume":"52","author":"Cubuk","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jbc.2024.107354_bib30","doi-asserted-by":"crossref","first-page":"929","DOI":"10.3390\/biom12070929","article-title":"NMR reveals specific tracts within the intrinsically disordered regions of the SARS-CoV-2 nucleocapsid protein involved in RNA encountering","volume":"12","author":"Pontoriero","year":"2022","journal-title":"Biomolecules"},{"key":"10.1016\/j.jbc.2024.107354_bib31","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1010121","article-title":"Structural dynamics of SARS-CoV-2 nucleocapsid protein induced by RNA binding","volume":"18","author":"Ribeiro-Filho","year":"2022","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.jbc.2024.107354_bib32","doi-asserted-by":"crossref","first-page":"1890","DOI":"10.1002\/pro.3909","article-title":"Architecture and self-assembly of the SARS-CoV-2 nucleocapsid protein","volume":"29","author":"Ye","year":"2020","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2024.107354_bib33","doi-asserted-by":"crossref","first-page":"pgac049","DOI":"10.1093\/pnasnexus\/pgac049","article-title":"Plasticity in structure and assembly of SARS-CoV-2 nucleocapsid protein","volume":"1","author":"Zhao","year":"2022","journal-title":"PNAS Nexus"},{"key":"10.1016\/j.jbc.2024.107354_bib34","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.adg6473","article-title":"A\u00a0conserved oligomerization domain in the disordered linker of coronavirus nucleocapsid proteins","volume":"9","author":"Zhao","year":"2023","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jbc.2024.107354_bib35","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2021.102523","article-title":"Energetic and structural features of SARS-CoV-2 N-protein co-assemblies with nucleic acids","volume":"24","author":"Zhao","year":"2021","journal-title":"iScience"},{"key":"10.1016\/j.jbc.2024.107354_bib36","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1016\/j.cell.2020.06.034","article-title":"The global phosphorylation landscape of SARS-CoV-2 infection","volume":"182","author":"Bouhaddou","year":"2020","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2024.107354_bib37","article-title":"Protein post-translational modification in SARS-CoV-2 and host interaction","volume":"13","author":"Cheng","year":"2022","journal-title":"Front. Immunol."},{"key":"10.1016\/j.jbc.2024.107354_bib38","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102560","article-title":"Reconstitution of the SARS-CoV-2 ribonucleosome provides insights into genomic RNA packaging and regulation by phosphorylation","volume":"298","author":"Carlson","year":"2022","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107354_bib39","article-title":"Targeting the coronavirus nucleocapsid protein through GSK-3 inhibition","volume":"118","author":"Liu","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2024.107354_bib40","doi-asserted-by":"crossref","first-page":"4152","DOI":"10.1111\/j.1742-4658.2008.06564.x","article-title":"Phosphorylation of the arginine\/serine dipeptide-rich motif of the severe acute respiratory syndrome coronavirus nucleocapsid protein modulates its multimerization, translation inhibitory activity and cellular localization","volume":"275","author":"Peng","year":"2008","journal-title":"FEBS J."},{"key":"10.1016\/j.jbc.2024.107354_bib41","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2023.105362","article-title":"Assembly of SARS-CoV-2 ribonucleosomes by truncated N(\u2217) variant of the nucleocapsid protein","volume":"299","author":"Adly","year":"2023","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107354_bib42","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.abm0808","article-title":"Host protein kinases required for SARS-CoV-2 nucleocapsid phosphorylation and viral replication","volume":"15","author":"Yaron","year":"2022","journal-title":"Sci. Signal."},{"key":"10.1016\/j.jbc.2024.107354_bib43","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1007\/s12104-021-10014-x","article-title":"(1)H, (13)C and (15)N Backbone chemical shift assignments of the n-terminal and central intrinsically disordered domains of SARS-CoV-2 nucleoprotein","volume":"15","author":"Guseva","year":"2021","journal-title":"Biomol. NMR Assign."},{"key":"10.1016\/j.jbc.2024.107354_bib44","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.jbc.2024.107354_bib45","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.101306","article-title":"Phosphorylation regulates arginine-rich RNA-binding protein solubility and oligomerization","volume":"297","author":"Kundinger","year":"2021","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107354_bib46","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102613","article-title":"Accessing isotopically labeled proteins containing genetically encoded phosphoserine for NMR with optimized expression conditions","volume":"298","author":"Vesely","year":"2022","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107354_bib47","series-title":"Revealing sequences and modifications of intact proteins using electron fragmentation","author":"Franklin","year":"2023"},{"key":"10.1016\/j.jbc.2024.107354_bib48","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1007\/s12104-021-10009-8","article-title":"The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1-248 residue construct: sequence-specific resonance assignments through NMR","volume":"15","author":"Schiavina","year":"2021","journal-title":"Biomol. NMR Assign."},{"key":"10.1016\/j.jbc.2024.107354_bib49","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1021\/bi701995m","article-title":"Dynein light chain LC8 is a dimerization hub essential in diverse protein networks","volume":"47","author":"Barbar","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2024.107354_bib50","doi-asserted-by":"crossref","first-page":"6041","DOI":"10.1038\/s41467-020-19843-1","article-title":"Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates","volume":"11","author":"Savastano","year":"2020","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2024.107354_bib51","article-title":"A\u00a0specific phosphorylation-dependent conformational switch of SARS-CoV-2 nucleoprotein inhibits RNA binding","author":"Botova","year":"2024","journal-title":"bioRxiv"},{"key":"10.1016\/j.jbc.2024.107354_bib52","doi-asserted-by":"crossref","first-page":"2599","DOI":"10.1021\/acschemneuro.1c00873","article-title":"Hyperphosphorylation-mimetic TDP-43 drives amyloid formation and possesses neuronal toxicity at the oligomeric stage","volume":"13","author":"Chiang","year":"2022","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.jbc.2024.107354_bib53","doi-asserted-by":"crossref","first-page":"15351","DOI":"10.1021\/bi051122c","article-title":"SR-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization","volume":"44","author":"Luo","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2024.107354_bib54","doi-asserted-by":"crossref","first-page":"219","DOI":"10.3389\/fmolb.2020.00219","article-title":"SR\/RS motifs as critical determinants of coronavirus life cycle","volume":"7","author":"Nikolakaki","year":"2020","journal-title":"Front Mol. Biosci."},{"key":"10.1016\/j.jbc.2024.107354_bib55","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1093\/nar\/gkac1179","article-title":"Structural domains of SARS-CoV-2 nucleocapsid protein coordinate to compact long nucleic acid substrates","volume":"51","author":"Morse","year":"2023","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jbc.2024.107354_bib56","doi-asserted-by":"crossref","first-page":"1936","DOI":"10.1038\/s41467-021-21953-3","article-title":"The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA","volume":"12","author":"Cubuk","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2024.107354_bib57","doi-asserted-by":"crossref","first-page":"25","DOI":"10.3389\/fnmol.2019.00025","article-title":"Molecular mechanisms of TDP-43 misfolding and pathology in amyotrophic lateral sclerosis","volume":"12","author":"Prasad","year":"2019","journal-title":"Front Mol. Neurosci."},{"key":"10.1016\/j.jbc.2024.107354_bib58","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abm4034","article-title":"The intrinsically disordered SARS-CoV-2 nucleoprotein in dynamic complex with its viral partner nsp3a","volume":"8","author":"Bessa","year":"2022","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jbc.2024.107354_bib59","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2021.166875","article-title":"The mechanism of SARS-CoV-2 nucleocapsid protein recognition by the human 14-3-3 proteins","volume":"433","author":"Tugaeva","year":"2021","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2024.107354_bib60","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/j.bpj.2024.01.001","article-title":"Phosphomimetic substitutions in TDP-43\u2019s transiently \u03b1-helical region suppress phase separation","volume":"123","author":"Haider","year":"2024","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2024.107354_bib61","doi-asserted-by":"crossref","first-page":"6090","DOI":"10.1074\/jbc.AC117.001037","article-title":"TAR DNA-binding protein 43 (TDP-43) liquid-liquid phase separation is mediated by just a few aromatic residues","volume":"293","author":"Li","year":"2018","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107354_bib62","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1021\/acscentsci.3c00191","article-title":"Autonomous synthesis of functional, permanently phosphorylated proteins for defining the interactome of monomeric 14-3-3\u03b6","volume":"9","author":"Zhu","year":"2023","journal-title":"ACS Cent. Sci."},{"key":"10.1016\/j.jbc.2024.107354_bib63","doi-asserted-by":"crossref","DOI":"10.26508\/lsa.201900366","article-title":"Systematic identification of recognition motifs for the hub protein LC8","volume":"2","author":"Jespersen","year":"2019","journal-title":"Life Sci. Alliance"},{"key":"10.1016\/j.jbc.2024.107354_bib64","doi-asserted-by":"crossref","first-page":"1564","DOI":"10.1021\/acschembio.9b00307","article-title":"A\u00a0highly versatile expression system for the production of multiply phosphorylated proteins","volume":"14","author":"Zhu","year":"2019","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.jbc.2024.107354_bib65","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.chroma.2014.02.029","article-title":"A\u00a0new set of highly efficient, tag-cleaving proteases for purifying recombinant proteins","volume":"1337","author":"Frey","year":"2014","journal-title":"J.\u00a0Chromatogr. A"},{"key":"10.1016\/j.jbc.2024.107354_bib66","doi-asserted-by":"crossref","first-page":"620","DOI":"10.1002\/biot.201100155","article-title":"Recombinant protein expression and purification: a comprehensive review of affinity tags and microbial applications","volume":"7","author":"Young","year":"2012","journal-title":"Biotechnol. J."},{"key":"10.1016\/j.jbc.2024.107354_bib67","doi-asserted-by":"crossref","first-page":"4959","DOI":"10.1016\/j.jmb.2019.10.011","article-title":"The LC8-RavP ensemble structure evinces A role for LC8 in regulating lyssavirus polymerase functionality","volume":"431","author":"Jespersen","year":"2019","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2024.107354_bib68","doi-asserted-by":"crossref","first-page":"9042","DOI":"10.1021\/ja062025p","article-title":"Speeding up three-dimensional protein NMR experiments to a few minutes","volume":"128","author":"Schanda","year":"2006","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2024.107354_bib69","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: a multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J.\u00a0Biomol. NMR"},{"key":"10.1016\/j.jbc.2024.107354_bib70","first-page":"313","article-title":"Using NMRView to visualize and analyze the NMR spectra of macromolecules","volume":"278","author":"Johnson","year":"2004","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.jbc.2024.107354_bib71","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1007\/s10858-016-0072-7","article-title":"Sparse multidimensional iterative lineshape-enhanced (SMILE) reconstruction of both non-uniformly sampled and conventional NMR data","volume":"68","author":"Ying","year":"2017","journal-title":"J.\u00a0Biomol. NMR"},{"key":"10.1016\/j.jbc.2024.107354_bib72","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1007\/s10858-011-9508-2","article-title":"Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution","volume":"50","author":"Kjaergaard","year":"2011","journal-title":"J.\u00a0Biomol. NMR"},{"key":"10.1016\/j.jbc.2024.107354_bib73","doi-asserted-by":"crossref","first-page":"1606","DOI":"10.1016\/S0006-3495(00)76713-0","article-title":"Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling","volume":"78","author":"Schuck","year":"2000","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2024.107354_bib74","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1007\/s00249-023-01629-0","article-title":"SEDNTERP: a calculation and database utility to aid interpretation of analytical ultracentrifugation and light scattering data","volume":"52","author":"Philo","year":"2023","journal-title":"Eur. Biophys. J."},{"key":"10.1016\/j.jbc.2024.107354_bib75","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/S0076-6879(04)84013-8","article-title":"Analysis of heterogeneous interactions","volume":"384","author":"Cole","year":"2004","journal-title":"Methods Enzymol."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925824018556?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925824018556?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,6,27]],"date-time":"2024-06-27T00:18:10Z","timestamp":1719447490000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925824018556"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,6]]},"references-count":75,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2024,6]]}},"alternative-id":["S0021925824018556"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2024.107354","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2024,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Phosphorylation in the Ser\/Arg-rich region of the nucleocapsid of SARS-CoV-2 regulates phase separation by inhibiting self-association of a distant helix","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2024.107354","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"107354"}}