{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T20:28:53Z","timestamp":1787603333510,"version":"build-2736575974"},"reference-count":63,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2021,10,29]],"date-time":"2021-10-29T00:00:00Z","timestamp":1635465600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["1617019"],"award-info":[{"award-number":["1617019"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>The human parainfluenza virus 3 (HPIV3) poses a risk for pneumonia development in young children and immunocompromised patients. To investigate mechanisms of HPIV3 pathogenesis, we characterized the association state and host protein interactions of HPIV3 phosphoprotein (HPIV3 P), an indispensable viral polymerase cofactor. Sequence analysis and homology modeling predict that HPIV3 P possesses a long, disordered N-terminal tail (PTAIL) a coiled-coil multimerization domain (PMD), similar to the well-characterized paramyxovirus phosphoproteins from measles and Sendai viruses. Using a recombinantly expressed and purified construct of PMD and PTAIL, we show that HPIV3 P in solution is primarily an alpha-helical tetramer that is stable up to 60 \u00b0C. Pulldown and isothermal titration calorimetry experiments revealed that HPIV3 P binds the host hub protein LC8, and turbidity experiments demonstrated a new role for LC8 in increasing the solubility of HPIV3 P in the presence of crowding agents such as RNA. For comparison, we show that the multimerization domain of the Zaire Ebola virus phosphoprotein VP35 is also a tetramer and binds LC8 but with significantly higher affinity. Comparative analysis of the domain architecture of various virus phosphoproteins in the order Mononegavirales show multiple predicted and verified LC8 binding motifs, suggesting its prevalence and importance in regulating viral phosphoprotein structures. Our work provides evidence for LC8 binding to phosphoproteins with multiple association states, either tetrameric, as in the HPIV3 and Ebola phosphoproteins shown here, or dimeric as in rabies virus phosphoprotein. Taken together the data suggest that the association states of a virus-specific phosphoprotein and the complex formed by binding of the phosphoprotein to host LC8 are important regulators of viral function.<\/jats:p>","DOI":"10.3390\/biom11111603","type":"journal-article","created":{"date-parts":[[2021,11,1]],"date-time":"2021-11-01T11:47:38Z","timestamp":1635767258000},"page":"1603","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Human Parainfluenza Virus 3 Phosphoprotein Is a Tetramer and Shares Structural and Interaction Features with Ebola Phosphoprotein VP35"],"prefix":"10.3390","volume":"11","author":[{"given":"Joaquin","family":"Rodriguez Galvan","sequence":"first","affiliation":[{"name":"Department of Biochemistry & Biophysics, College of Science, Corvallis, OR 97331, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brianna","family":"Donner","sequence":"additional","affiliation":[{"name":"Department of Biochemistry & Biophysics, College of Science, Corvallis, OR 97331, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cat Hoang","family":"Veseley","sequence":"additional","affiliation":[{"name":"Department of Biochemistry & Biophysics, College of Science, Corvallis, OR 97331, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6858-0086","authenticated-orcid":false,"given":"Patrick","family":"Reardon","sequence":"additional","affiliation":[{"name":"NMR Facility, Oregon State University, Corvallis, OR 97331, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heather M.","family":"Forsythe","sequence":"additional","affiliation":[{"name":"Department of Biochemistry & Biophysics, College of Science, Corvallis, OR 97331, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jesse","family":"Howe","sequence":"additional","affiliation":[{"name":"Department of Biochemistry & Biophysics, College of Science, Corvallis, OR 97331, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gretchen","family":"Fujimura","sequence":"additional","affiliation":[{"name":"Department of Biochemistry & Biophysics, College of Science, Corvallis, OR 97331, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elisar","family":"Barbar","sequence":"additional","affiliation":[{"name":"Department of Biochemistry & Biophysics, College of Science, Corvallis, OR 97331, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,10,29]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1967","DOI":"10.1007\/s00705-019-04247-4","article-title":"Taxonomy of the order Mononegavirales: Update 2019","volume":"164","author":"Amarasinghe","year":"2019","journal-title":"Arch. Virol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1542\/pir.35.6.217","article-title":"Influenza and parainfluenza viral infections in children","volume":"35","author":"Fox","year":"2014","journal-title":"Pediatr. Rev."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1111\/irv.12597","article-title":"Seasonality and clinical impact of human parainfluenza viruses","volume":"12","author":"Maykowski","year":"2018","journal-title":"Influenza Other Respir. Viruses"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1086\/322041","article-title":"Outbreak of human parainfluenza virus 3 infections in a hematopoietic stem cell transplant population","volume":"184","author":"Cortez","year":"2001","journal-title":"J. Infect. Dis."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Liang, B. (2020). Structures of the Mononegavirales Polymerases. J. Virol., 94.","DOI":"10.1128\/JVI.00175-20"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1128\/CMR.16.2.242-264.2003","article-title":"Parainfluenza viruses","volume":"16","author":"Henrickson","year":"2003","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"15688","DOI":"10.3390\/ijms160715688","article-title":"Structural Disorder within Paramyxoviral Nucleoproteins and Phosphoproteins in Their Free and Bound Forms: From Predictions to Experimental Assessment","volume":"16","author":"Habchi","year":"2015","journal-title":"Int. J. Mol. Sci."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1006\/viro.2002.1668","article-title":"Characterization of the oligomerization domain of the phosphoprotein of human parainfluenza virus type 3","volume":"302","author":"Choudhary","year":"2002","journal-title":"Virology"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"5204","DOI":"10.1073\/pnas.92.11.5204","article-title":"Cellular protein kinase C isoform zeta regulates human parainfluenza virus type 3 replication","volume":"92","author":"De","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1006\/viro.1995.1438","article-title":"Human parainfluenza virus type 3 phosphoprotein: Identification of serine 333 as the major site for PKC zeta phosphorylation","volume":"211","author":"Huntley","year":"1995","journal-title":"Virology"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"3900","DOI":"10.1016\/j.febslet.2012.09.021","article-title":"Phosphorylation of measles virus phosphoprotein at S86 and\/or S151 downregulates viral transcriptional activity","volume":"586","author":"Sugai","year":"2012","journal-title":"FEBS Lett."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"4274","DOI":"10.1128\/JVI.72.5.4274-4280.1998","article-title":"A role for the Sendai virus P protein trimer in RNA synthesis","volume":"72","author":"Curran","year":"1998","journal-title":"J. Virol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1006\/viro.1995.9946","article-title":"Paramyxovirus phosphoproteins form homotrimers as determined by an epitope dilution assay, via predicted coiled coils","volume":"214","author":"Curran","year":"1995","journal-title":"Virology"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"eaaw3702","DOI":"10.1126\/sciadv.aaw3702","article-title":"Regulation of measles virus gene expression by P protein coiled-coil properties","volume":"5","author":"Bloyet","year":"2019","journal-title":"Sci. Adv."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"11002","DOI":"10.1128\/JVI.01719-15","article-title":"Oligomerization of Mumps Virus Phosphoprotein","volume":"89","author":"Pickar","year":"2015","journal-title":"J. Virol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"2808","DOI":"10.1128\/JVI.80.6.2808-2814.2006","article-title":"Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus","volume":"80","author":"Ding","year":"2006","journal-title":"J. Virol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.str.2018.09.009","article-title":"Structures of Ebola and Reston Virus VP35 Oligomerization Domains and Comparative Biophysical Characterization in All Ebolavirus Species","volume":"27","author":"Zinzula","year":"2019","journal-title":"Structure"},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Aggarwal, M., Leser, G.P., Kors, C.A., and Lamb, R.A. (2018). Structure of the Paramyxovirus Parainfluenza Virus 5 Nucleoprotein in Complex with an Amino-Terminal Peptide of the Phosphoprotein. J. Virol., 92.","DOI":"10.1128\/JVI.01304-17"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1016\/j.virol.2008.10.019","article-title":"Phosphoprotein, P of human parainfluenza virus type 3 prevents self- association of RNA-dependent RNA polymerase, L","volume":"383","author":"Chattopadhyay","year":"2009","journal-title":"Virology"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"2658","DOI":"10.1128\/jvi.62.8.2658-2664.1988","article-title":"Complex formation with vesicular stomatitis virus phosphoprotein NS prevents binding of nucleocapsid protein N to nonspecific RNA","volume":"62","author":"Masters","year":"1988","journal-title":"J. Virol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1007\/s001140050562","article-title":"Characteristics of Filoviridae: Marburg and Ebola viruses","volume":"86","author":"Beer","year":"1999","journal-title":"Naturwissenschaften"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"96","DOI":"10.4103\/ajm.AJM_150_16","article-title":"Ebola virus disease: Essential clinical knowledge","volume":"7","author":"Khalafallah","year":"2017","journal-title":"Avicenna J. Med."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1038\/nrmicro3524","article-title":"Filovirus pathogenesis and immune evasion: Insights from Ebola virus and Marburg virus","volume":"13","author":"Messaoudi","year":"2015","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"5148","DOI":"10.1128\/JVI.03652-14","article-title":"Ebola virus VP35 interaction with dynein LC8 regulates viral RNA synthesis","volume":"89","author":"Luthra","year":"2015","journal-title":"J. Virol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.virol.2005.06.044","article-title":"Homo-oligomerization facilitates the interferon-antagonist activity of the ebolavirus VP35 protein","volume":"341","author":"Reid","year":"2005","journal-title":"Virology"},{"key":"ref_26","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. Mol. Biol."},{"key":"ref_27","first-page":"2040206619889220","article-title":"Relevance of Ebola virus VP35 homo-dimerization on the type I interferon cascade inhibition","volume":"27","author":"Daino","year":"2019","journal-title":"Antivir. Chem. Chemother."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"10028","DOI":"10.1073\/pnas.0703614104","article-title":"Structural and thermodynamic characterization of a cytoplasmic dynein light chain-intermediate chain complex","volume":"104","author":"Williams","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1110\/ps.03462204","article-title":"The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila","volume":"13","author":"Makokha","year":"2004","journal-title":"Protein Sci."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1966","DOI":"10.1128\/MCB.16.5.1966","article-title":"Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster","volume":"16","author":"Dick","year":"1996","journal-title":"Mol. Cell. Biol."},{"key":"ref_31","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":"ref_32","doi-asserted-by":"crossref","first-page":"2980","DOI":"10.1111\/j.1742-4658.2011.08254.x","article-title":"DYNLL\/LC8: A light chain subunit of the dynein motor complex and beyond","volume":"278","author":"Rapali","year":"2011","journal-title":"FEBS J."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Jespersen, N., Estelle, A., Waugh, N., Davey, N.E., Blikstad, C., Ammon, Y.C., Akhmanova, A., Ivarsson, Y., Hendrix, D.A., and Barbar, E. (2019). Systematic identification of recognition motifs for the hub protein LC8. Life Sci. Alliance, 2.","DOI":"10.26508\/lsa.201900366"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1021\/acs.biochem.5b01099","article-title":"The Anchored Flexibility Model in LC8 Motif Recognition: Insights from the Chica Complex","volume":"55","author":"Clark","year":"2016","journal-title":"Biochemistry"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"2997","DOI":"10.1111\/j.1742-4658.2011.08252.x","article-title":"The association of viral proteins with host cell dynein components during virus infection","volume":"278","year":"2011","journal-title":"FEBS J."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"10217","DOI":"10.1128\/JVI.74.21.10217-10222.2000","article-title":"Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein","volume":"74","author":"Jacob","year":"2000","journal-title":"J. Virol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"10212","DOI":"10.1128\/JVI.74.21.10212-10216.2000","article-title":"Interaction of the rabies virus P protein with the LC8 dynein light chain","volume":"74","author":"Raux","year":"2000","journal-title":"J. Virol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/j.virusres.2006.11.006","article-title":"Herpes simplex virus-type 2 infectivity and agents that block gap junctional intercellular communication","volume":"124","author":"Knabb","year":"2007","journal-title":"Virus Res."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"11496","DOI":"10.1128\/JVI.75.23.11496-11502.2001","article-title":"Extensive attenuation of rabies virus by simultaneously modifying the dynein light chain binding site in the P protein and replacing Arg333 in the G protein","volume":"75","author":"Mebatsion","year":"2001","journal-title":"J. Virol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1021\/mp060086o","article-title":"Evaluation of an LC8-binding peptide for the attachment of artificial cargo to dynein","volume":"4","author":"Bergen","year":"2007","journal-title":"Mol. Pharm."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1765","DOI":"10.1093\/bioinformatics\/btz828","article-title":"QMEANDisCo-distance constraints applied on model quality estimation","volume":"36","author":"Studer","year":"2020","journal-title":"Bioinformatics"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"W296","DOI":"10.1093\/nar\/gky427","article-title":"SWISS-MODEL: Homology modelling of protein structures and complexes","volume":"46","author":"Waterhouse","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"10480","DOI":"10.1038\/s41598-017-09654-8","article-title":"Modeling protein quaternary structure of homo- and hetero-oligomers beyond binary interactions by homology","volume":"7","author":"Bertoni","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1589","DOI":"10.1107\/S139900471400234X","article-title":"Coiled-coil deformations in crystal structures: The measles virus phosphoprotein multimerization domain as an illustrative example","volume":"70","author":"Blocquel","year":"2014","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1038\/79013","article-title":"Tetrameric coiled coil domain of Sendai virus phosphoprotein","volume":"7","author":"Tarbouriech","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"ref_46","unstructured":"Harding, S., Rowe, A.J., and Horton, J.C. (1992). Computer-aided Interpretation of Sedimentation Data for Proteins. Analytical Ultracentrifugation in Biochemistry and Polymer Science, Royal Society of Chemistry."},{"key":"ref_47","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":"ref_48","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1111\/acel.12587","article-title":"Rapamycin inhibits the secretory phenotype of senescent cells by a Nrf2-independent mechanism","volume":"16","author":"Wang","year":"2017","journal-title":"Aging Cell"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"2392","DOI":"10.1093\/bioinformatics\/btx155","article-title":"IcyTree: Rapid browser-based visualization for phylogenetic trees and networks","volume":"33","author":"Vaughan","year":"2017","journal-title":"Bioinformatics"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"D313","DOI":"10.1093\/nar\/gkw1132","article-title":"The SWISS-MODEL Repository-new features and functionality","volume":"45","author":"Bienert","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"S162","DOI":"10.1002\/elps.200900140","article-title":"Automated comparative protein structure modeling with SWISS-MODEL and Swiss-PdbViewer: A historical perspective","volume":"30","author":"Guex","year":"2009","journal-title":"Electrophoresis"},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Studer, G., Tauriello, G., Bienert, S., Biasini, M., Johner, N., and Schwede, T. (2021). ProMod3-A versatile homology modelling toolbox. PLoS Comput. Biol., 17.","DOI":"10.1371\/journal.pcbi.1008667"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1093\/bioinformatics\/btq662","article-title":"Toward the estimation of the absolute quality of individual protein structure models","volume":"27","author":"Benkert","year":"2011","journal-title":"Bioinformatics"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"2722","DOI":"10.1093\/bioinformatics\/btt473","article-title":"lDDT: A local superposition-free score for comparing protein structures and models using distance difference tests","volume":"29","author":"Mariani","year":"2013","journal-title":"Bioinformatics"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"4603","DOI":"10.1016\/j.jmb.2018.09.006","article-title":"Phase Separation in Biology and Disease","volume":"430","author":"Kriwacki","year":"2018","journal-title":"J. Mol. Biol."},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Hu, Z., Wang, Y., Tang, Q., Yang, X., Qin, Y., and Chen, M. (2018). Inclusion bodies of human parainfluenza virus type 3 inhibit antiviral stress granule formation by shielding viral RNAs. PLoS Pathog., 14.","DOI":"10.1371\/journal.ppat.1006948"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/j.virol.2018.02.008","article-title":"An alanine residue in human parainfluenza virus type 3 phosphoprotein is critical for restricting excessive N(0)-P interaction and maintaining N solubility","volume":"518","author":"Zhang","year":"2018","journal-title":"Virology"},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Xie, J., Wang, L., Zhai, G., Wu, D., Lin, Z., Wang, M., Yan, X., Gao, L., Huang, X., and Fearns, R. (2021). Structural architecture of a dimeric paramyxovirus polymerase complex. bioRxiv.","DOI":"10.1101\/2021.09.13.460081"},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Zhang, S., Jiang, Y., Cheng, Q., Zhong, Y., Qin, Y., and Chen, M. (2017). Inclusion Body Fusion of Human Parainfluenza Virus Type 3 Regulated by Acetylated alpha-Tubulin Enhances Viral Replication. J. Virol., 91.","DOI":"10.1128\/JVI.01802-16"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/j.virol.2015.01.029","article-title":"Reverse genetics of Mononegavirales: How they work, new vaccines, and new cancer therapeutics","volume":"479-480","author":"Pfaller","year":"2015","journal-title":"Virology"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1099\/0022-1317-80-5-1199","article-title":"Human parainfluenza virus type 1 phosphoprotein is constitutively phosphorylated at Ser-120 and Ser-184","volume":"80","author":"Byrappa","year":"1999","journal-title":"J. Gen. Virol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"3268","DOI":"10.1128\/jvi.65.6.3268-3275.1991","article-title":"Human parainfluenza virus type 3 transcription in vitro: Role of cellular actin in mRNA synthesis","volume":"65","author":"De","year":"1991","journal-title":"J. Virol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"459","DOI":"10.3389\/fmicb.2015.00459","article-title":"The paramyxovirus polymerase complex as a target for next-generation anti-paramyxovirus therapeutics","volume":"6","author":"Cox","year":"2015","journal-title":"Front. Microbiol."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/11\/11\/1603\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T07:22:40Z","timestamp":1760167360000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/11\/11\/1603"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,10,29]]},"references-count":63,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2021,11]]}},"alternative-id":["biom11111603"],"URL":"https:\/\/doi.org\/10.3390\/biom11111603","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,10,29]]}}}