{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T17:12:24Z","timestamp":1790529144905,"version":"4.1.0"},"publisher-location":"Cham","reference-count":86,"publisher":"Springer International Publishing","isbn-type":[{"value":"9783030147402","type":"print"},{"value":"9783030147419","type":"electronic"}],"license":[{"start":{"date-parts":[[2019,1,1]],"date-time":"2019-01-01T00:00:00Z","timestamp":1546300800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2019]]},"DOI":"10.1007\/978-3-030-14741-9_6","type":"book-chapter","created":{"date-parts":[[2019,7,17]],"date-time":"2019-07-17T18:02:34Z","timestamp":1563386554000},"page":"111-127","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["Structure and Function of Negri Bodies"],"prefix":"10.1007","author":[{"given":"Jovan","family":"Nikolic","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C\u00e9cile","family":"Lagaudri\u00e8re-Gesbert","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nathalie","family":"Scrima","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danielle","family":"Blondel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yves","family":"Gaudin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2019,7,18]]},"reference":[{"issue":"5","key":"6_CR1","doi-asserted-by":"publisher","first-page":"381","DOI":"10.1016\/j.coviro.2011.09.008","volume":"1","author":"CL Netherton","year":"2011","unstructured":"Netherton CL, Wileman T (2011) Virus factories, double membrane vesicles and viroplasm generated in animal cells. Curr Opin Virol 1(5):381\u2013387. https:\/\/doi.org\/10.1016\/j.coviro.2011.09.008","journal-title":"Curr Opin Virol"},{"issue":"2","key":"6_CR2","doi-asserted-by":"publisher","first-page":"147","DOI":"10.1042\/BC20040058","volume":"97","author":"RR Novoa","year":"2005","unstructured":"Novoa RR, Calderita G, Arranz R, Fontana J, Granzow H, Risco C (2005) Virus factories: associations of cell organelles for viral replication and morphogenesis. Biol Cell 97(2):147\u2013172. https:\/\/doi.org\/10.1042\/BC20040058","journal-title":"Biol Cell"},{"key":"6_CR3","first-page":"123","volume":"328","author":"VG Chinchar","year":"2009","unstructured":"Chinchar VG, Hyatt A, Miyazaki T, Williams T (2009) Family Iridoviridae: poor viral relations no longer. Curr Top Microbiol Immunol 328:123\u2013170","journal-title":"Curr Top Microbiol Immunol"},{"issue":"4","key":"6_CR4","doi-asserted-by":"publisher","first-page":"1839","DOI":"10.1128\/JVI.76.4.1839-1855.2002","volume":"76","author":"C Risco","year":"2002","unstructured":"Risco C, Rodriguez JR, Lopez-Iglesias C, Carrascosa JL, Esteban M, Rodriguez D (2002) Endoplasmic reticulum-Golgi intermediate compartment membranes and vimentin filaments participate in vaccinia virus assembly. J Virol 76(4):1839\u20131855","journal-title":"J Virol"},{"issue":"2","key":"6_CR5","doi-asserted-by":"publisher","first-page":"524","DOI":"10.1006\/viro.1999.9704","volume":"257","author":"G Rojo","year":"1999","unstructured":"Rojo G, Garcia-Beato R, Vinuela E, Salas ML, Salas J (1999) Replication of African swine fever virus DNA in infected cells. Virology 257(2):524\u2013536","journal-title":"Virology"},{"issue":"10","key":"6_CR6","doi-asserted-by":"publisher","first-page":"839","DOI":"10.1111\/j.1600-0854.2005.00324.x","volume":"6","author":"B Schramm","year":"2005","unstructured":"Schramm B, Locker JK (2005) Cytoplasmic organization of POXvirus DNA replication. Traffic 6(10):839\u2013846. https:\/\/doi.org\/10.1111\/j.1600-0854.2005.00324.x","journal-title":"Traffic"},{"key":"6_CR7","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1146\/annurev.micro.57.030502.090836","volume":"61","author":"T Wileman","year":"2007","unstructured":"Wileman T (2007) Aggresomes and pericentriolar sites of virus assembly: cellular defense or viral design? Annu Rev Microbiol 61:149\u2013167. https:\/\/doi.org\/10.1146\/annurev.micro.57.030502.090836","journal-title":"Annu Rev Microbiol"},{"issue":"12","key":"6_CR8","doi-asserted-by":"publisher","first-page":"1691","DOI":"10.1111\/cmi.12620","volume":"18","author":"G Avila-Perez","year":"2016","unstructured":"Avila-Perez G, Rejas MT, Rodriguez D (2016) Ultrastructural characterization of membranous torovirus replication factories. Cell Microbiol 18(12):1691\u20131708. https:\/\/doi.org\/10.1111\/cmi.12620","journal-title":"Cell Microbiol"},{"key":"6_CR9","doi-asserted-by":"publisher","first-page":"418","DOI":"10.1016\/j.virol.2015.02.029","volume":"479-480","author":"C Harak","year":"2015","unstructured":"Harak C, Lohmann V (2015) Ultrastructure of the replication sites of positive-strand RNA viruses. Virology 479-480:418\u2013433. https:\/\/doi.org\/10.1016\/j.virol.2015.02.029","journal-title":"Virology"},{"issue":"9","key":"6_CR10","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.0050220","volume":"5","author":"BG Kopek","year":"2007","unstructured":"Kopek BG, Perkins G, Miller DJ, Ellisman MH, Ahlquist P (2007) Three-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelle. PLoS Biol 5(9):e220. https:\/\/doi.org\/10.1371\/journal.pbio.0050220","journal-title":"PLoS Biol"},{"issue":"6","key":"6_CR11","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1000958","volume":"6","author":"BS Heinrich","year":"2010","unstructured":"Heinrich BS, Cureton DK, Rahmeh AA, Whelan SP (2010) Protein expression redirects vesicular stomatitis virus RNA synthesis to cytoplasmic inclusions. PLoS Pathog 6(6):e1000958. https:\/\/doi.org\/10.1371\/journal.ppat.1000958","journal-title":"PLoS Pathog"},{"issue":"16","key":"6_CR12","doi-asserted-by":"publisher","first-page":"7948","DOI":"10.1128\/JVI.00554-09","volume":"83","author":"X Lahaye","year":"2009","unstructured":"Lahaye X, Vidy A, Pomier C, Obiang L, Harper F, Gaudin Y, Blondel D (2009) Functional characterization of Negri bodies (NBs) in rabies virus-infected cells: Evidence that NBs are sites of viral transcription and replication. J Virol 83(16):7948\u20137958. https:\/\/doi.org\/10.1128\/JVI.00554-09","journal-title":"J Virol"},{"issue":"2","key":"6_CR13","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1000315","volume":"5","author":"P Menager","year":"2009","unstructured":"Menager P, Roux P, Megret F, Bourgeois JP, Le Sourd AM, Danckaert A, Lafage M, Prehaud C, Lafon M (2009) Toll-like receptor 3 (TLR3) plays a major role in the formation of rabies virus Negri Bodies. PLoS Pathog 5(2):e1000315. https:\/\/doi.org\/10.1371\/journal.ppat.1000315","journal-title":"PLoS Pathog"},{"issue":"21","key":"6_CR14","doi-asserted-by":"publisher","first-page":"11779","DOI":"10.1128\/JVI.01525-12","volume":"86","author":"T Hoenen","year":"2012","unstructured":"Hoenen T, Shabman RS, Groseth A, Herwig A, Weber M, Schudt G, Dolnik O, Basler CF, Becker S, Feldmann H (2012) Inclusion bodies are a site of ebolavirus replication. J Virol 86(21):11779\u201311788. https:\/\/doi.org\/10.1128\/JVI.01525-12","journal-title":"J Virol"},{"issue":"1","key":"6_CR15","doi-asserted-by":"publisher","first-page":"563","DOI":"10.1038\/s41467-017-00655-9","volume":"8","author":"V Rincheval","year":"2017","unstructured":"Rincheval V, Lelek M, Gault E, Bouillier C, Sitterlin D, Blouquit-Laye S, Galloux M, Zimmer C, Eleouet JF, Rameix-Welti MA (2017) Functional organization of cytoplasmic inclusion bodies in cells infected by respiratory syncytial virus. Nat Commun 8(1):563. https:\/\/doi.org\/10.1038\/s41467-017-00655-9","journal-title":"Nat Commun"},{"key":"6_CR16","first-page":"88","volume":"2","author":"A Negri","year":"1903","unstructured":"Negri A (1903) Contributo allo studio dell\u2019 eziologia della rabia. Bol Soc Med Chir Pavia 2:88\u2013114","journal-title":"Bol Soc Med Chir Pavia"},{"key":"6_CR17","doi-asserted-by":"publisher","first-page":"158","DOI":"10.1016\/j.virusres.2016.10.010","volume":"227","author":"RG Dietzgen","year":"2017","unstructured":"Dietzgen RG, Kondo H, Goodin MM, Kurath G, Vasilakis N (2017) The family Rhabdoviridae: mono- and bipartite negative-sense RNA viruses with diverse genome organization and common evolutionary origins. Virus Res 227:158\u2013170. https:\/\/doi.org\/10.1016\/j.virusres.2016.10.010","journal-title":"Virus Res"},{"issue":"4","key":"6_CR18","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1000394","volume":"5","author":"DK Cureton","year":"2009","unstructured":"Cureton DK, Massol RH, Saffarian S, Kirchhausen TL, Whelan SP (2009) Vesicular stomatitis virus enters cells through vesicles incompletely coated with clathrin that depend upon actin for internalization. PLoS Pathog 5(4):e1000394","journal-title":"PLoS Pathog"},{"issue":"1","key":"6_CR19","doi-asserted-by":"publisher","first-page":"440","DOI":"10.1128\/JVI.01864-08","volume":"83","author":"HK Johannsdottir","year":"2009","unstructured":"Johannsdottir HK, Mancini R, Kartenbeck J, Amato L, Helenius A (2009) Host cell factors and functions involved in vesicular stomatitis virus entry. J Virol 83(1):440\u2013453","journal-title":"J Virol"},{"issue":"7","key":"6_CR20","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1005753","volume":"12","author":"S Piccinotti","year":"2016","unstructured":"Piccinotti S, Whelan SP (2016) Rabies internalizes into primary peripheral neurons via clathrin coated pits and requires fusion at the cell body. PLoS Pathog 12(7):e1005753. https:\/\/doi.org\/10.1371\/journal.ppat.1005753","journal-title":"PLoS Pathog"},{"issue":"1","key":"6_CR21","doi-asserted-by":"publisher","first-page":"117","DOI":"10.3390\/v4010117","volume":"4","author":"AAV Albertini","year":"2012","unstructured":"Albertini AAV, Baquero E, Ferlin A, Gaudin Y (2012) Molecular and cellular aspects of rhabdovirus entry. Viruses 4(1):117\u2013139","journal-title":"Viruses"},{"key":"6_CR22","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/B978-0-12-387040-7.00001-9","volume":"79","author":"AA Albertini","year":"2011","unstructured":"Albertini AA, Ruigrok RW, Blondel D (2011) Rabies virus transcription and replication. Adv Virus Res 79:1\u201322. https:\/\/doi.org\/10.1016\/B978-0-12-387040-7.00001-9","journal-title":"Adv Virus Res"},{"issue":"3","key":"6_CR23","doi-asserted-by":"publisher","first-page":"837","DOI":"10.1016\/0092-8674(81)90448-7","volume":"23","author":"BM Blumberg","year":"1981","unstructured":"Blumberg BM, Leppert M, Kolakofsky D (1981) Interaction of VSV leader RNA and nucleocapsid protein may control VSV genome replication. Cell 23(3):837\u2013845","journal-title":"Cell"},{"issue":"5785","key":"6_CR24","doi-asserted-by":"publisher","first-page":"360","DOI":"10.1126\/science.1125280","volume":"313","author":"AA Albertini","year":"2006","unstructured":"Albertini AA, Wernimont AK, Muziol T, Ravelli RB, Clapier CR, Schoehn G, Weissenhorn W, Ruigrok RW (2006) Crystal structure of the rabies virus nucleoprotein-RNA complex. Science 313(5785):360\u2013363. https:\/\/doi.org\/10.1126\/science.1125280","journal-title":"Science"},{"issue":"6","key":"6_CR25","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1128\/JVI.12.6.1325-1335.1973","volume":"12","author":"SU Emerson","year":"1973","unstructured":"Emerson SU, Wagner RR (1973) L protein requirement for in vitro RNA synthesis by vesicular stomatitis virus. J Virol 12(6):1325\u20131335","journal-title":"J Virol"},{"issue":"1","key":"6_CR26","doi-asserted-by":"publisher","first-page":"222","DOI":"10.1016\/0042-6822(88)90253-X","volume":"163","author":"N Hercyk","year":"1988","unstructured":"Hercyk N, Horikami SM, Moyer SA (1988) The vesicular stomatitis virus L protein possesses the mRNA methyltransferase activities. Virology 163(1):222\u2013225","journal-title":"Virology"},{"issue":"1","key":"6_CR27","doi-asserted-by":"publisher","first-page":"85","DOI":"10.1016\/j.molcel.2006.11.013","volume":"25","author":"T Ogino","year":"2007","unstructured":"Ogino T, Banerjee AK (2007) Unconventional mechanism of mRNA capping by the RNA-dependent RNA polymerase of vesicular stomatitis virus. Mol Cell 25(1):85\u201397. https:\/\/doi.org\/10.1016\/j.molcel.2006.11.013","journal-title":"Mol Cell"},{"issue":"2","key":"6_CR28","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1128\/JVI.52.2.515-521.1984","volume":"52","author":"DM Hunt","year":"1984","unstructured":"Hunt DM, Smith EF, Buckley DW (1984) Aberrant polyadenylation by a vesicular stomatitis virus mutant is due to an altered L protein. J Virol 52(2):515\u2013521","journal-title":"J Virol"},{"issue":"2","key":"6_CR29","doi-asserted-by":"publisher","first-page":"314","DOI":"10.1016\/j.cell.2015.06.018","volume":"162","author":"B Liang","year":"2015","unstructured":"Liang B, Li Z, Jenni S, Rahmeh AA, Morin BM, Grant T, Grigorieff N, Harrison SC, Whelan SPJ (2015) Structure of the L protein of vesicular stomatitis virus from electron cryomicroscopy. Cell 162(2):314\u2013327. https:\/\/doi.org\/10.1016\/j.cell.2015.06.018","journal-title":"Cell"},{"issue":"5","key":"6_CR30","doi-asserted-by":"publisher","first-page":"978","DOI":"10.1016\/j.jmb.2009.03.061","volume":"388","author":"FC Gerard","year":"2009","unstructured":"Gerard FC, Ribeiro Ede A Jr, Leyrat C, Ivanov I, Blondel D, Longhi S, Ruigrok RW, Jamin M (2009) Modular organization of rabies virus phosphoprotein. J Mol Biol 388(5):978\u2013996. https:\/\/doi.org\/10.1016\/j.jmb.2009.03.061","journal-title":"J Mol Biol"},{"issue":"1","key":"6_CR31","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1128\/JVI.74.1.91-98.2000","volume":"74","author":"AK Gupta","year":"2000","unstructured":"Gupta AK, Blondel D, Choudhary S, Banerjee AK (2000) The phosphoprotein of rabies virus is phosphorylated by a unique cellular protein kinase and specific isomers of protein kinase C. J Virol 74(1):91\u201398","journal-title":"J Virol"},{"key":"6_CR32","doi-asserted-by":"publisher","first-page":"1757","DOI":"10.1099\/0022-1317-81-7-1757","volume":"81","author":"B Gigant","year":"2000","unstructured":"Gigant B, Iseni F, Gaudin Y, Knossow M, Blondel D (2000) Neither phosphorylation nor the amino-terminal part of rabies virus phosphoprotein is required for its oligomerization. J Gen Virol 81. (Pt 7:1757\u20131761. https:\/\/doi.org\/10.1099\/0022-1317-81-7-1757","journal-title":"J Gen Virol"},{"issue":"20","key":"6_CR33","doi-asserted-by":"publisher","first-page":"10808","DOI":"10.1128\/JVI.00977-09","volume":"83","author":"G Castel","year":"2009","unstructured":"Castel G, Chteoui M, Caignard G, Prehaud C, Mehouas S, Real E, Jallet C, Jacob Y, Ruigrok RW, Tordo N (2009) Peptides that mimic the amino-terminal end of the rabies virus phosphoprotein have antiviral activity. J Virol 83(20):10808\u201310820. https:\/\/doi.org\/10.1128\/JVI.00977-09","journal-title":"J Virol"},{"issue":"3","key":"6_CR34","doi-asserted-by":"crossref","first-page":"1925","DOI":"10.1128\/JVI.72.3.1925-1930.1998","volume":"72","author":"M Chenik","year":"1998","unstructured":"Chenik M, Schnell M, Conzelmann KK, Blondel D (1998) Mapping the interacting domains between the rabies virus polymerase and phosphoprotein. J Virol 72(3):1925\u20131930","journal-title":"J Virol"},{"issue":"2","key":"6_CR35","doi-asserted-by":"publisher","first-page":"406","DOI":"10.1006\/viro.2002.1748","volume":"305","author":"M Mavrakis","year":"2003","unstructured":"Mavrakis M, Iseni F, Mazza C, Schoehn G, Ebel C, Gentzel M, Franz T, Ruigrok RW (2003) Isolation and characterisation of the rabies virus N degrees-P complex produced in insect cells. Virology 305(2):406\u2013414","journal-title":"Virology"},{"issue":"9","key":"6_CR36","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1002248","volume":"7","author":"C Leyrat","year":"2011","unstructured":"Leyrat C, Yabukarski F, Tarbouriech N, Ribeiro EA Jr, Jensen MR, Blackledge M, Ruigrok RW, Jamin M (2011) Structure of the vesicular stomatitis virus N(0)-P complex. PLoS Pathog 7(9):e1002248. https:\/\/doi.org\/10.1371\/journal.ppat.1002248","journal-title":"PLoS Pathog"},{"issue":"7","key":"6_CR37","doi-asserted-by":"publisher","first-page":"3707","DOI":"10.1128\/JVI.02557-09","volume":"84","author":"I Ivanov","year":"2010","unstructured":"Ivanov I, Cr\u00e9pin T, Jamin M, Ruigrok RW (2010) Structure of the dimerization domain of the rabies virus phosphoprotein. J Virol 84(7):3707\u20133710. https:\/\/doi.org\/10.1128\/JVI.02557-09","journal-title":"J Virol"},{"issue":"4","key":"6_CR38","doi-asserted-by":"publisher","first-page":"819","DOI":"10.1016\/j.jmb.2004.08.071","volume":"343","author":"M Mavrakis","year":"2004","unstructured":"Mavrakis M, McCarthy AA, Roche S, Blondel D, Ruigrok RW (2004) Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus. J Mol Biol 343(4):819\u2013831. https:\/\/doi.org\/10.1016\/j.jmb.2004.08.071","journal-title":"J Mol Biol"},{"issue":"3","key":"6_CR39","doi-asserted-by":"publisher","first-page":"558","DOI":"10.1016\/j.jmb.2009.09.042","volume":"394","author":"A Ribeiro Ede Jr","year":"2009","unstructured":"Ribeiro Ede A Jr, Leyrat C, Gerard FC, Albertini AA, Falk C, Ruigrok RW, Jamin M (2009) Binding of rabies virus polymerase cofactor to recombinant circular nucleoprotein-RNA complexes. J Mol Biol 394(3):558\u2013575. https:\/\/doi.org\/10.1016\/j.jmb.2009.09.042","journal-title":"J Mol Biol"},{"issue":"20","key":"6_CR40","doi-asserted-by":"publisher","first-page":"9613","DOI":"10.1128\/JVI.75.20.9613-9622.2001","volume":"75","author":"Y Jacob","year":"2001","unstructured":"Jacob Y, Real E, Tordo N (2001) Functional interaction map of lyssavirus phosphoprotein: identification of the minimal transcription domains. J Virol 75(20):9613\u20139622. https:\/\/doi.org\/10.1128\/JVI.75.20.9613-9622.2001","journal-title":"J Virol"},{"issue":"28","key":"6_CR41","doi-asserted-by":"publisher","first-page":"11713","DOI":"10.1073\/pnas.0903228106","volume":"106","author":"TJ Green","year":"2009","unstructured":"Green TJ, Luo M (2009) Structure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, P. Proc Natl Acad Sci U S A 106(28):11713\u201311718. https:\/\/doi.org\/10.1073\/pnas.0903228106","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"5","key":"6_CR42","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1089\/jir.2006.26.271","volume":"26","author":"MK Chelbi-Alix","year":"2006","unstructured":"Chelbi-Alix MK, Vidy A, El Bougrini J, Blondel D (2006) Rabies viral mechanisms to escape the IFN system: the viral protein P interferes with IRF-3, Stat1, and PML nuclear bodies. J Interf Cytokine Res 26(5):271\u2013280. https:\/\/doi.org\/10.1089\/jir.2006.26.271","journal-title":"J Interf Cytokine Res"},{"issue":"22","key":"6_CR43","doi-asserted-by":"publisher","first-page":"14411","DOI":"10.1128\/JVI.79.22.14411-14420.2005","volume":"79","author":"A Vidy","year":"2005","unstructured":"Vidy A, Chelbi-Alix M, Blondel D (2005) Rabies virus P protein interacts with STAT1 and inhibits interferon signal transduction pathways. J Virol 79(22):14411\u201314420. https:\/\/doi.org\/10.1128\/JVI.79.22.14411-14420.2005","journal-title":"J Virol"},{"issue":"8","key":"6_CR44","doi-asserted-by":"publisher","first-page":"4255","DOI":"10.1128\/JVI.01930-06","volume":"81","author":"A Vidy","year":"2007","unstructured":"Vidy A, El Bougrini J, Chelbi-Alix MK, Blondel D (2007) The nucleocytoplasmic rabies virus P protein counteracts interferon signaling by inhibiting both nuclear accumulation and DNA binding of STAT1. J Virol 81(8):4255\u20134263. https:\/\/doi.org\/10.1128\/JVI.01930-06","journal-title":"J Virol"},{"issue":"52","key":"6_CR45","doi-asserted-by":"publisher","first-page":"7957","DOI":"10.1038\/sj.onc.1205931","volume":"21","author":"D Blondel","year":"2002","unstructured":"Blondel D, Regad T, Poisson N, Pavie B, Harper F, Pandolfi PP, De The H, Chelbi-Alix MK (2002) Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies. Oncogene 21(52):7957\u20137970. https:\/\/doi.org\/10.1038\/sj.onc.1205931","journal-title":"Oncogene"},{"issue":"20","key":"6_CR46","doi-asserted-by":"publisher","first-page":"10719","DOI":"10.1128\/JVI.01286-10","volume":"84","author":"D Blondel","year":"2010","unstructured":"Blondel D, Kheddache S, Lahaye X, Dianoux L, Chelbi-Alix MK (2010) Resistance to rabies virus infection conferred by the PMLIV isoform. J Virol 84(20):10719\u201310726. https:\/\/doi.org\/10.1128\/JVI.01286-10","journal-title":"J Virol"},{"issue":"12","key":"6_CR47","doi-asserted-by":"publisher","first-page":"7673","DOI":"10.1128\/JVI.79.12.7673-7681.2005","volume":"79","author":"K Brzozka","year":"2005","unstructured":"Brzozka K, Finke S, Conzelmann KK (2005) Identification of the rabies virus alpha\/beta interferon antagonist: phosphoprotein P interferes with phosphorylation of interferon regulatory factor 3. J Virol 79(12):7673\u20137681. https:\/\/doi.org\/10.1128\/JVI.79.12.7673-7681.2005","journal-title":"J Virol"},{"issue":"21","key":"6_CR48","doi-asserted-by":"publisher","first-page":"10217","DOI":"10.1128\/JVI.74.21.10217-10222.2000","volume":"74","author":"Y Jacob","year":"2000","unstructured":"Jacob Y, Badrane H, Ceccaldi PE, Tordo N (2000) Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein. J Virol 74(21):10217\u201310222","journal-title":"J Virol"},{"key":"6_CR49","doi-asserted-by":"publisher","first-page":"2691","DOI":"10.1099\/0022-1317-82-11-2691","volume":"82","author":"N Poisson","year":"2001","unstructured":"Poisson N, Real E, Gaudin Y, Vaney MC, King S, Jacob Y, Tordo N, Blondel D (2001) Molecular basis for the interaction between rabies virus phosphoprotein P and the dynein light chain LC8: dissociation of dynein-binding properties and transcriptional functionality of P. J Gen Virol 82. (Pt 11:2691\u20132696. https:\/\/doi.org\/10.1099\/0022-1317-82-11-2691","journal-title":"J Gen Virol"},{"issue":"21","key":"6_CR50","doi-asserted-by":"publisher","first-page":"10212","DOI":"10.1128\/JVI.74.21.10212-10216.2000","volume":"74","author":"H Raux","year":"2000","unstructured":"Raux H, Flamand A, Blondel D (2000) Interaction of the rabies virus P protein with the LC8 dynein light chain. J Virol 74(21):10212\u201310216","journal-title":"J Virol"},{"issue":"3","key":"6_CR51","doi-asserted-by":"publisher","first-page":"1640","DOI":"10.1128\/JVI.02602-14","volume":"89","author":"B Fouquet","year":"2015","unstructured":"Fouquet B, Nikolic J, Larrous F, Bourhy H, Wirblich C, Lagaudriere-Gesbert C, Blondel D (2015) Focal adhesion kinase is involved in rabies virus infection through its interaction with viral phosphoprotein P. J Virol 89(3):1640\u20131651. https:\/\/doi.org\/10.1128\/JVI.02602-14","journal-title":"J Virol"},{"issue":"3","key":"6_CR52","doi-asserted-by":"publisher","first-page":"1939","DOI":"10.1128\/JVI.03320-14","volume":"89","author":"S Oksayan","year":"2015","unstructured":"Oksayan S, Nikolic J, David CT, Blondel D, Jans DA, Moseley GW (2015) Identification of a role for nucleolin in rabies virus infection. J Virol 89(3):1939\u20131943. https:\/\/doi.org\/10.1128\/JVI.03320-14","journal-title":"J Virol"},{"issue":"17","key":"6_CR53","doi-asserted-by":"publisher","first-page":"7229","DOI":"10.1073\/pnas.0701397104","volume":"104","author":"GS Tan","year":"2007","unstructured":"Tan GS, Preuss MA, Williams JC, Schnell MJ (2007) The dynein light chain 8 binding motif of rabies virus phosphoprotein promotes efficient viral transcription. Proc Natl Acad Sci U S A 104(17):7229\u20137234. https:\/\/doi.org\/10.1073\/pnas.0701397104","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"3","key":"6_CR54","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1111\/j.1365-2990.1996.tb00893.x","volume":"22","author":"K Kristensson","year":"1996","unstructured":"Kristensson K, Dastur DK, Manghani DK, Tsiang H, Bentivoglio M (1996) Rabies: interactions between neurons and viruses. A review of the history of Negri inclusion bodies. Neuropathol Appl Neurobiol 22(3):179\u2013187","journal-title":"Neuropathol Appl Neurobiol"},{"issue":"1","key":"6_CR55","doi-asserted-by":"publisher","first-page":"58","DOI":"10.1038\/s41467-017-00102-9","volume":"8","author":"J Nikolic","year":"2017","unstructured":"Nikolic J, Le Bars R, Lama Z, Scrima N, Lagaudriere-Gesbert C, Gaudin Y, Blondel D (2017) Negri bodies are viral factories with properties of liquid organelles. Nat Commun 8(1):58. https:\/\/doi.org\/10.1038\/s41467-017-00102-9","journal-title":"Nat Commun"},{"issue":"4","key":"6_CR56","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1128\/JVI.14.4.981-996.1974","volume":"14","author":"S Matsumoto","year":"1974","unstructured":"Matsumoto S, Schneider LG, Kawai A, Yonezawa T (1974) Further studies on the replication of rabies and rabies-like viruses in organized cultures of mammalian neural tissues. J Virol 14(4):981\u2013996","journal-title":"J Virol"},{"issue":"22","key":"6_CR57","doi-asserted-by":"publisher","first-page":"12333","DOI":"10.1128\/JVI.78.22.12333-12343.2004","volume":"78","author":"S Finke","year":"2004","unstructured":"Finke S, Brzozka K, Conzelmann KK (2004) Tracking fluorescence-labeled rabies virus: enhanced green fluorescent protein-tagged phosphoprotein P supports virus gene expression and formation of infectious particles. J Virol 78(22):12333\u201312343. https:\/\/doi.org\/10.1128\/JVI.78.22.12333-12343.2004","journal-title":"J Virol"},{"issue":"9","key":"6_CR58","doi-asserted-by":"publisher","first-page":"4743","DOI":"10.1128\/JVI.06501-11","volume":"86","author":"X Lahaye","year":"2012","unstructured":"Lahaye X, Vidy A, Fouquet B, Blondel D (2012) Hsp70 protein positively regulates rabies virus infection. J Virol 86(9):4743\u20134751. https:\/\/doi.org\/10.1128\/JVI.06501-11","journal-title":"J Virol"},{"issue":"13","key":"6_CR59","doi-asserted-by":"publisher","first-page":"7608","DOI":"10.1128\/JVI.03186-12","volume":"87","author":"J Zhang","year":"2013","unstructured":"Zhang J, Wu X, Zan J, Wu Y, Ye C, Ruan X, Zhou J (2013a) Cellular chaperonin CCTgamma contributes to rabies virus replication during infection. J Virol 87(13):7608\u20137621. https:\/\/doi.org\/10.1128\/JVI.03186-12","journal-title":"J Virol"},{"issue":"10","key":"6_CR60","doi-asserted-by":"publisher","first-page":"590","DOI":"10.1111\/1348-0421.12186","volume":"58","author":"J Zhang","year":"2014","unstructured":"Zhang J, Ye C, Ruan X, Zan J, Xu Y, Liao M, Zhou J (2014) The chaperonin CCTalpha is required for efficient transcription and replication of rabies virus. Microbiol Immunol 58(10):590\u2013599. https:\/\/doi.org\/10.1111\/1348-0421.12186","journal-title":"Microbiol Immunol"},{"issue":"5","key":"6_CR61","doi-asserted-by":"publisher","first-page":"539","DOI":"10.1292\/jvms.66.539","volume":"66","author":"T Shin","year":"2004","unstructured":"Shin T, Weinstock D, Castro MD, Hamir AN, Wampler T, Walter M, Kim HY, Acland H (2004) Immunohistochemical localization of endothelial and inducible nitric oxide synthase within neurons of cattle with rabies. J Vet Med Sci 66(5):539\u2013541","journal-title":"J Vet Med Sci"},{"issue":"2","key":"6_CR62","doi-asserted-by":"publisher","first-page":"200","DOI":"10.1111\/cmi.12037","volume":"15","author":"R Pollin","year":"2013","unstructured":"Pollin R, Granzow H, Kollner B, Conzelmann KK, Finke S (2013) Membrane and inclusion body targeting of lyssavirus matrix proteins. Cell Microbiol 15(2):200\u2013212. https:\/\/doi.org\/10.1111\/cmi.12037","journal-title":"Cell Microbiol"},{"issue":"5","key":"6_CR63","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1038\/nrm.2017.7","volume":"18","author":"SF Banani","year":"2017","unstructured":"Banani SF, Lee HO, Hyman AA, Rosen MK (2017) Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18(5):285\u2013298. https:\/\/doi.org\/10.1038\/nrm.2017.7","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"5935","key":"6_CR64","doi-asserted-by":"publisher","first-page":"1729","DOI":"10.1126\/science.1172046","volume":"324","author":"CP Brangwynne","year":"2009","unstructured":"Brangwynne CP, Eckmann CR, Courson DS, Rybarska A, Hoege C, Gharakhani J, Julicher F, Hyman AA (2009) Germline P granules are liquid droplets that localize by controlled dissolution\/condensation. Science 324(5935):1729\u20131732. https:\/\/doi.org\/10.1126\/science.1172046","journal-title":"Science"},{"issue":"15","key":"6_CR65","doi-asserted-by":"publisher","first-page":"1603","DOI":"10.15252\/embj.201593517","volume":"35","author":"EM Courchaine","year":"2016","unstructured":"Courchaine EM, Lu A, Neugebauer KM (2016) Droplet organelles? EMBO J 35(15):1603\u20131612. https:\/\/doi.org\/10.15252\/embj.201593517","journal-title":"EMBO J"},{"key":"6_CR66","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1016\/j.sbi.2016.10.015","volume":"44","author":"VN Uversky","year":"2017","unstructured":"Uversky VN (2017) Intrinsically disordered proteins in overcrowded milieu: membrane-less organelles, phase separation, and intrinsic disorder. Curr Opin Struct Biol 44:18\u201330. https:\/\/doi.org\/10.1016\/j.sbi.2016.10.015","journal-title":"Curr Opin Struct Biol"},{"issue":"1","key":"6_CR67","doi-asserted-by":"publisher","first-page":"202","DOI":"10.1091\/mbc.E04-08-0742","volume":"16","author":"KE Handwerger","year":"2005","unstructured":"Handwerger KE, Cordero JA, Gall JG (2005) Cajal bodies, nucleoli, and speckles in the Xenopus oocyte nucleus have a low-density, sponge-like structure. Mol Biol Cell 16(1):202\u2013211. https:\/\/doi.org\/10.1091\/mbc.E04-08-0742","journal-title":"Mol Biol Cell"},{"issue":"11","key":"6_CR68","doi-asserted-by":"publisher","first-page":"4334","DOI":"10.1073\/pnas.1017150108","volume":"108","author":"CP Brangwynne","year":"2011","unstructured":"Brangwynne CP, Mitchison TJ, Hyman AA (2011) Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes. Proc Natl Acad Sci U S A 108(11):4334\u20134339. https:\/\/doi.org\/10.1073\/pnas.1017150108","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"7","key":"6_CR69","doi-asserted-by":"publisher","first-page":"1686","DOI":"10.1016\/j.cell.2016.04.047","volume":"165","author":"M Feric","year":"2016","unstructured":"Feric M, Vaidya N, Harmon TS, Mitrea DM, Zhu L, Richardson TM, Kriwacki RW, Pappu RV, Brangwynne CP (2016) Coexisting liquid phases underlie nucleolar subcompartments. Cell 165(7):1686\u20131697. https:\/\/doi.org\/10.1016\/j.cell.2016.04.047","journal-title":"Cell"},{"issue":"12","key":"6_CR70","doi-asserted-by":"publisher","first-page":"1254","DOI":"10.15252\/embj.201593169","volume":"35","author":"MR Marzahn","year":"2016","unstructured":"Marzahn MR, Marada S, Lee J, Nourse A, Kenrick S, Zhao H, Ben-Nissan G, Kolaitis RM, Peters JL, Pounds S, Errington WJ, Prive GG, Taylor JP, Sharon M, Schuck P, Ogden SK, Mittag T (2016) Higher-order oligomerization promotes localization of SPOP to liquid nuclear speckles. EMBO J 35(12):1254\u20131275. https:\/\/doi.org\/10.15252\/embj.201593169","journal-title":"EMBO J"},{"issue":"3","key":"6_CR71","doi-asserted-by":"publisher","first-page":"487","DOI":"10.1016\/j.cell.2015.12.038","volume":"164","author":"S Jain","year":"2016","unstructured":"Jain S, Wheeler JR, Walters RW, Agrawal A, Barsic A, Parker R (2016) ATPase-modulated stress granules contain a diverse proteome and substructure. Cell 164(3):487\u2013498. https:\/\/doi.org\/10.1016\/j.cell.2015.12.038","journal-title":"Cell"},{"issue":"10","key":"6_CR72","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1005942","volume":"12","author":"J Nikolic","year":"2016","unstructured":"Nikolic J, Civas A, Lama Z, Lagaudriere-Gesbert C, Blondel D (2016) Rabies virus infection induces the formation of stress granules closely connected to the viral factories. PLoS Pathog 12(10):e1005942. https:\/\/doi.org\/10.1371\/journal.ppat.1005942","journal-title":"PLoS Pathog"},{"issue":"7","key":"6_CR73","doi-asserted-by":"publisher","first-page":"674","DOI":"10.1002\/bies.201500175","volume":"38","author":"FC Nielsen","year":"2016","unstructured":"Nielsen FC, Hansen HT, Christiansen J (2016) RNA assemblages orchestrate complex cellular processes. BioEssays 38(7):674\u2013681. https:\/\/doi.org\/10.1002\/bies.201500175","journal-title":"BioEssays"},{"issue":"38","key":"6_CR74","doi-asserted-by":"publisher","first-page":"E5237","DOI":"10.1073\/pnas.1509317112","volume":"112","author":"J Berry","year":"2015","unstructured":"Berry J, Weber SC, Vaidya N, Haataja M, Brangwynne CP (2015) RNA transcription modulates phase transition-driven nuclear body assembly. Proc Natl Acad Sci U S A 112(38):E5237\u2013E5245. https:\/\/doi.org\/10.1073\/pnas.1509317112","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"23","key":"6_CR75","doi-asserted-by":"publisher","first-page":"7189","DOI":"10.1073\/pnas.1504822112","volume":"112","author":"S Elbaum-Garfinkle","year":"2015","unstructured":"Elbaum-Garfinkle S, Kim Y, Szczepaniak K, Chen CC, Eckmann CR, Myong S, Brangwynne CP (2015) The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics. Proc Natl Acad Sci U S A 112(23):7189\u20137194. https:\/\/doi.org\/10.1073\/pnas.1504822112","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"5","key":"6_CR76","doi-asserted-by":"publisher","first-page":"936","DOI":"10.1016\/j.molcel.2015.01.013","volume":"57","author":"TJ Nott","year":"2015","unstructured":"Nott TJ, Petsalaki E, Farber P, Jervis D, Fussner E, Plochowietz A, Craggs TD, Bazett-Jones DP, Pawson T, Forman-Kay JD, Baldwin AJ (2015) Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles. Mol Cell 57(5):936\u2013947. https:\/\/doi.org\/10.1016\/j.molcel.2015.01.013","journal-title":"Mol Cell"},{"issue":"1","key":"6_CR77","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1016\/j.tibs.2007.10.003","volume":"33","author":"P Tompa","year":"2008","unstructured":"Tompa P, Fuxreiter M (2008) Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem Sci 33(1):2\u20138. https:\/\/doi.org\/10.1016\/j.tibs.2007.10.003","journal-title":"Trends Biochem Sci"},{"issue":"35","key":"6_CR78","doi-asserted-by":"publisher","first-page":"14402","DOI":"10.1073\/pnas.1307681110","volume":"110","author":"G Schudt","year":"2013","unstructured":"Schudt G, Kolesnikova L, Dolnik O, Sodeik B, Becker S (2013) Live-cell imaging of Marburg virus-infected cells uncovers actin-dependent transport of nucleocapsids over long distances. Proc Natl Acad Sci U S A 110(35):14402\u201314407. https:\/\/doi.org\/10.1073\/pnas.1307681110","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"Pt 11","key":"6_CR79","doi-asserted-by":"publisher","first-page":"2698","DOI":"10.1099\/vir.0.2008\/004051-0","volume":"89","author":"A Derdowski","year":"2008","unstructured":"Derdowski A, Peters TR, Glover N, Qian R, Utley TJ, Burnett A, Williams JV, Spearman P, Crowe JE Jr (2008) Human metapneumovirus nucleoprotein and phosphoprotein interact and provide the minimal requirements for inclusion body formation. J Gen Virol 89(Pt 11):2698\u20132708. https:\/\/doi.org\/10.1099\/vir.0.2008\/004051-0","journal-title":"J Gen Virol"},{"key":"6_CR80","doi-asserted-by":"publisher","first-page":"3525","DOI":"10.1099\/0022-1317-75-12-3525","volume":"75","author":"R Fearns","year":"1994","unstructured":"Fearns R, Young DF, Randall RE (1994) Evidence that the paramyxovirus simian virus 5 can establish quiescent infections by remaining inactive in cytoplasmic inclusion bodies. J Gen Virol 75. (Pt 12:3525\u20133539. https:\/\/doi.org\/10.1099\/0022-1317-75-12-3525","journal-title":"J Gen Virol"},{"issue":"22","key":"6_CR81","doi-asserted-by":"publisher","first-page":"12457","DOI":"10.1128\/JVI.01565-13","volume":"87","author":"S Zhang","year":"2013","unstructured":"Zhang S, Chen L, Zhang G, Yan Q, Yang X, Ding B, Tang Q, Sun S, Hu Z, Chen M (2013b) An amino acid of human parainfluenza virus type 3 nucleoprotein is critical for template function and cytoplasmic inclusion body formation. J Virol 87(22):12457\u201312470. https:\/\/doi.org\/10.1128\/JVI.01565-13","journal-title":"J Virol"},{"issue":"22","key":"6_CR82","doi-asserted-by":"publisher","first-page":"12339","DOI":"10.1128\/JVI.01127-13","volume":"87","author":"CM Charlier","year":"2013","unstructured":"Charlier CM, Wu YJ, Allart S, Malnou CE, Schwemmle M, Gonzalez-Dunia D (2013) Analysis of borna disease virus trafficking in live infected cells by using a virus encoding a tetracysteine-tagged p protein. J Virol 87(22):12339\u201312348. https:\/\/doi.org\/10.1128\/JVI.01127-13","journal-title":"J Virol"},{"issue":"8","key":"6_CR83","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1005800","volume":"12","author":"PJ Wichgers Schreur","year":"2016","unstructured":"Wichgers Schreur PJ, Kortekaas J (2016) Single-molecule FISH reveals non-selective packaging of rift valley fever virus genome segments. PLoS Pathog 12(8):e1005800. https:\/\/doi.org\/10.1371\/journal.ppat.1005800","journal-title":"PLoS Pathog"},{"issue":"6321","key":"6_CR84","doi-asserted-by":"publisher","first-page":"194","DOI":"10.1126\/science.aal2130","volume":"355","author":"V Chaikeeratisak","year":"2017","unstructured":"Chaikeeratisak V, Nguyen K, Khanna K, Brilot AF, Erb ML, Coker JK, Vavilina A, Newton GL, Buschauer R, Pogliano K, Villa E, Agard DA, Pogliano J (2017) Assembly of a nucleus-like structure during viral replication in bacteria. Science 355(6321):194\u2013197. https:\/\/doi.org\/10.1126\/science.aal2130","journal-title":"Science"},{"issue":"2","key":"6_CR85","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1005444","volume":"12","author":"SW Oh","year":"2016","unstructured":"Oh SW, Onomoto K, Wakimoto M, Onoguchi K, Ishidate F, Fujiwara T, Yoneyama M, Kato H, Fujita T (2016) Leader-containing uncapped viral transcript activates RIG-I in antiviral stress granules. PLoS Pathog 12(2):e1005444. https:\/\/doi.org\/10.1371\/journal.ppat.1005444","journal-title":"PLoS Pathog"},{"issue":"1","key":"6_CR86","doi-asserted-by":"publisher","first-page":"372","DOI":"10.1128\/JVI.02305-12","volume":"87","author":"PX Dinh","year":"2013","unstructured":"Dinh PX, Beura LK, Das PB, Panda D, Das A, Pattnaik AK (2013) Induction of stress granule-like structures in vesicular stomatitis virus-infected cells. J Virol 87(1):372\u2013383. https:\/\/doi.org\/10.1128\/JVI.02305-12","journal-title":"J Virol"}],"container-title":["Advances in Experimental Medicine and Biology","Physical Virology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/978-3-030-14741-9_6","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,1,13]],"date-time":"2021-01-13T03:34:23Z","timestamp":1610508863000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/978-3-030-14741-9_6"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019]]},"ISBN":["9783030147402","9783030147419"],"references-count":86,"URL":"https:\/\/doi.org\/10.1007\/978-3-030-14741-9_6","relation":{},"ISSN":["0065-2598","2214-8019"],"issn-type":[{"value":"0065-2598","type":"print"},{"value":"2214-8019","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019]]},"assertion":[{"value":"18 July 2019","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}}]}}