Influenza Infection (Homo sapiens)

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The virus particle initially associates with a human host cell by binding to sialic acid-containing receptors on the host cell surface. The bound virus is endocytosed by one of four distinct mechanisms. The low endosomal pH sets in motion a number of steps that lead to viral membrane fusion mediated by the viral hemagglutinin (HA) protein, and the eventual release of the uncoated viral ribonucleoprotein complex into the cytosol of the host cell. The ribonucleoprotein complex is transported through the nuclear pore into the nucleus. Once in the nucleus, the incoming negative-sense viral RNA (vRNA) is transcribed into messenger RNA (mRNA) by a primer-dependent mechanism. Replication occurs via a two step process. A full-length complementary RNA (cRNA), a positive-sense copy of the vRNA, is first made and this in turn is used as a template to produce more vRNA. The viral proteins are expressed and processed and eventually assemble with vRNAs at budding sites within the host cell membrane. The viral protein complexes and ribonucleoproteins are assembled into viral particles and bud from the host cell, enveloped in the host cell's membrane.

This release contains a framework for the further annotation of the viral life-cycle. View original pathway at:Reactome.</div>

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Bibliography

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1. Honda A, Mizumoto K, Ishihama A.; ''Two separate sequences of PB2 subunit constitute the RNA cap-binding site of influenza virus RNA polymerase.''; PubMed Europe PMC Scholia
2. Cros JF, García-Sastre A, Palese P.; ''An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein.''; PubMed Europe PMC Scholia
3. Lamb RA, Choppin PW, Chanock RM, Lai CJ.; ''Mapping of the two overlapping genes for polypeptides NS1 and NS2 on RNA segment 8 of influenza virus genome.''; PubMed Europe PMC Scholia
4. Li Y, Chen ZY, Wang W, Baker CC, Krug RM.; ''The 3'-end-processing factor CPSF is required for the splicing of single-intron pre-mRNAs in vivo.''; PubMed Europe PMC Scholia
5. Lin DH, Stuwe T, Schilbach S, Rundlet EJ, Perriches T, Mobbs G, Fan Y, Thierbach K, Huber FM, Collins LN, Davenport AM, Jeon YE, Hoelz A.; ''Architecture of the symmetric core of the nuclear pore.''; PubMed Europe PMC Scholia
6. Plotch SJ, Krug RM.; ''Influenza virion transcriptase: synthesis in vitro of large, polyadenylic acid-containing complementary RNA.''; PubMed Europe PMC Scholia
7. Robertson JS, Schubert M, Lazzarini RA.; ''Polyadenylation sites for influenza virus mRNA.''; PubMed Europe PMC Scholia
8. Liu C, Eichelberger MC, Compans RW, Air GM.; ''Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding.''; PubMed Europe PMC Scholia
9. Wang C, Takeuchi K, Pinto LH, Lamb RA.; ''Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block.''; PubMed Europe PMC Scholia
10. Rabut G, Doye V, Ellenberg J.; ''Mapping the dynamic organization of the nuclear pore complex inside single living cells.''; PubMed Europe PMC Scholia
11. Neumann G, Castrucci MR, Kawaoka Y.; ''Nuclear import and export of influenza virus nucleoprotein.''; PubMed Europe PMC Scholia
12. Heino S, Lusa S, Somerharju P, Ehnholm C, Olkkonen VM, Ikonen E.; ''Dissecting the role of the golgi complex and lipid rafts in biosynthetic transport of cholesterol to the cell surface.''; PubMed Europe PMC Scholia
13. Scheiffele P, Roth MG, Simons K.; ''Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain.''; PubMed Europe PMC Scholia
14. Fontoura BM, Blobel G, Matunis MJ.; ''A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96.''; PubMed Europe PMC Scholia
15. Ori A, Banterle N, Iskar M, Iskar M, Andrés-Pons A, Escher C, Khanh Bui H, Sparks L, Solis-Mezarino V, Rinner O, Bork P, Lemke EA, Beck M.; ''Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines.''; PubMed Europe PMC Scholia
16. Kabachinski G, Schwartz TU.; ''The nuclear pore complex--structure and function at a glance.''; PubMed Europe PMC Scholia
17. Ma K, Roy AM, Whittaker GR.; ''Nuclear export of influenza virus ribonucleoproteins: identification of an export intermediate at the nuclear periphery.''; PubMed Europe PMC Scholia
18. Poon LL, Pritlove DC, Sharps J, Brownlee GG.; ''The RNA polymerase of influenza virus, bound to the 5' end of virion RNA, acts in cis to polyadenylate mRNA.''; PubMed Europe PMC Scholia
19. Engelhardt OG, Fodor E.; ''Functional association between viral and cellular transcription during influenza virus infection.''; PubMed Europe PMC Scholia
20. Jones IM, Reay PA, Philpott KL.; ''Nuclear location of all three influenza polymerase proteins and a nuclear signal in polymerase PB2.''; PubMed Europe PMC Scholia
21. Area E, Martín-Benito J, Gastaminza P, Torreira E, Valpuesta JM, Carrascosa JL, Ortín J.; ''3D structure of the influenza virus polymerase complex: localization of subunit domains.''; PubMed Europe PMC Scholia
22. Noah DL, Twu KY, Krug RM.; ''Cellular antiviral responses against influenza A virus are countered at the posttranscriptional level by the viral NS1A protein via its binding to a cellular protein required for the 3' end processing of cellular pre-mRNAS.''; PubMed Europe PMC Scholia
23. Westera L, Jennings AM, Maamary J, Schwemmle M, García-Sastre A, Bortz E.; ''Poly-ADP Ribosyl Polymerase 1 (PARP1) Regulates Influenza A Virus Polymerase.''; PubMed Europe PMC Scholia
24. Doms RW, Lamb RA, Rose JK, Helenius A.; ''Folding and assembly of viral membrane proteins.''; PubMed Europe PMC Scholia
25. Chen Z, Li Y, Krug RM.; ''Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machinery.''; PubMed Europe PMC Scholia
26. Molinari M, Helenius A.; ''Chaperone selection during glycoprotein translocation into the endoplasmic reticulum.''; PubMed Europe PMC Scholia
27. Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ.; ''Proteomic analysis of the mammalian nuclear pore complex.''; PubMed Europe PMC Scholia
28. Alonso-Caplen FV, Nemeroff ME, Qiu Y, Krug RM.; ''Nucleocytoplasmic transport: the influenza virus NS1 protein regulates the transport of spliced NS2 mRNA and its precursor NS1 mRNA.''; PubMed Europe PMC Scholia
29. McCown MF, Pekosz A.; ''The influenza A virus M2 cytoplasmic tail is required for infectious virus production and efficient genome packaging.''; PubMed Europe PMC Scholia
30. Luo GX, Luytjes W, Enami M, Palese P.; ''The polyadenylation signal of influenza virus RNA involves a stretch of uridines followed by the RNA duplex of the panhandle structure.''; PubMed Europe PMC Scholia
31. Saito T, Taylor G, Webster RG.; ''Steps in maturation of influenza A virus neuraminidase.''; PubMed Europe PMC Scholia
32. Hagen M, Chung TD, Butcher JA, Krystal M.; ''Recombinant influenza virus polymerase: requirement of both 5' and 3' viral ends for endonuclease activity.''; PubMed Europe PMC Scholia
33. Hausmann J, Kretzschmar E, Garten W, Klenk HD.; ''Biosynthesis, intracellular transport and enzymatic activity of an avian influenza A virus neuraminidase: role of unpaired cysteines and individual oligosaccharides.''; PubMed Europe PMC Scholia
34. Wang P, Palese P, O'Neill RE.; ''The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal.''; PubMed Europe PMC Scholia
35. Ye Q, Krug RM, Tao YJ.; ''The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA.''; PubMed Europe PMC Scholia
36. Stegmann T.; ''Membrane fusion mechanisms: the influenza hemagglutinin paradigm and its implications for intracellular fusion.''; PubMed Europe PMC Scholia
37. Shimizu K, Iguchi A, Gomyou R, Ono Y.; ''Influenza virus inhibits cleavage of the HSP70 pre-mRNAs at the polyadenylation site.''; PubMed Europe PMC Scholia
38. Park CJ, Bae SH, Lee MK, Varani G, Choi BS.; ''Solution structure of the influenza A virus cRNA promoter: implications for differential recognition of viral promoter structures by RNA-dependent RNA polymerase.''; PubMed Europe PMC Scholia
39. Neumann G, Hughes MT, Kawaoka Y.; ''Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1.''; PubMed Europe PMC Scholia
40. Barman S, Ali A, Hui EK, Adhikary L, Nayak DP.; ''Transport of viral proteins to the apical membranes and interaction of matrix protein with glycoproteins in the assembly of influenza viruses.''; PubMed Europe PMC Scholia
41. Elster C, Fourest E, Baudin F, Larsen K, Cusack S, Ruigrok RW.; ''A small percentage of influenza virus M1 protein contains zinc but zinc does not influence in vitro M1-RNA interaction.''; PubMed Europe PMC Scholia
42. O'Neill RE, Jaskunas R, Blobel G, Palese P, Moroianu J.; ''Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import.''; PubMed Europe PMC Scholia
43. Daniels R, Kurowski B, Johnson AE, Hebert DN.; ''N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin.''; PubMed Europe PMC Scholia
44. Askjaer P, Jensen TH, Nilsson J, Englmeier L, Kjems J.; ''The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP.''; PubMed Europe PMC Scholia
45. Nayak DP, Hui EK, Barman S.; ''Assembly and budding of influenza virus.''; PubMed Europe PMC Scholia
46. Cianci C, Tiley L, Krystal M.; ''Differential activation of the influenza virus polymerase via template RNA binding.''; PubMed Europe PMC Scholia
47. Nemergut ME, Lindsay ME, Brownawell AM, Macara IG.; ''Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor.''; PubMed Europe PMC Scholia
48. Detjen BM, St Angelo C, Katze MG, Krug RM.; ''The three influenza virus polymerase (P) proteins not associated with viral nucleocapsids in the infected cell are in the form of a complex.''; PubMed Europe PMC Scholia
49. Li ML, Ramirez BC, Krug RM.; ''RNA-dependent activation of primer RNA production by influenza virus polymerase: different regions of the same protein subunit constitute the two required RNA-binding sites.''; PubMed Europe PMC Scholia
50. Kash JC, Goodman AG, Korth MJ, Katze MG.; ''Hijacking of the host-cell response and translational control during influenza virus infection.''; PubMed Europe PMC Scholia
51. Pleschka S, Wolff T, Ehrhardt C, Hobom G, Planz O, Rapp UR, Ludwig S.; ''Influenza virus propagation is impaired by inhibition of the Raf/MEK/ERK signalling cascade.''; PubMed Europe PMC Scholia
52. Mukaigawa J, Nayak DP.; ''Two signals mediate nuclear localization of influenza virus (A/WSN/33) polymerase basic protein 2.''; PubMed Europe PMC Scholia
53. Honda A, Uéda K, Nagata K, Ishihama A.; ''RNA polymerase of influenza virus: role of NP in RNA chain elongation.''; PubMed Europe PMC Scholia
54. Brownlee GG, Sharps JL.; ''The RNA polymerase of influenza a virus is stabilized by interaction with its viral RNA promoter.''; PubMed Europe PMC Scholia
55. Crow M, Deng T, Addley M, Brownlee GG.; ''Mutational analysis of the influenza virus cRNA promoter and identification of nucleotides critical for replication.''; PubMed Europe PMC Scholia
56. Vreede FT, Jung TE, Brownlee GG.; ''Model suggesting that replication of influenza virus is regulated by stabilization of replicative intermediates.''; PubMed Europe PMC Scholia
57. Krug RM.; ''Priming of influenza viral RNA transcription by capped heterologous RNAs.''; PubMed Europe PMC Scholia
58. Bergmann M, Garcia-Sastre A, Carnero E, Pehamberger H, Wolff K, Palese P, Muster T.; ''Influenza virus NS1 protein counteracts PKR-mediated inhibition of replication.''; PubMed Europe PMC Scholia
59. Yasuda J, Nakada S, Kato A, Toyoda T, Ishihama A.; ''Molecular assembly of influenza virus: association of the NS2 protein with virion matrix.''; PubMed Europe PMC Scholia
60. Sugrue RJ, Belshe RB, Hay AJ.; ''Palmitoylation of the influenza A virus M2 protein.''; PubMed Europe PMC Scholia
61. Chen W, Calvo PA, Malide D, Gibbs J, Schubert U, Bacik I, Basta S, O'Neill R, Schickli J, Palese P, Henklein P, Bennink JR, Yewdell JW.; ''A novel influenza A virus mitochondrial protein that induces cell death.''; PubMed Europe PMC Scholia
62. Luo C, Nobusawa E, Nakajima K.; ''An analysis of the role of neuraminidase in the receptor-binding activity of influenza B virus: the inhibitory effect of Zanamivir on haemadsorption.''; PubMed Europe PMC Scholia
63. Marjuki H, Alam MI, Ehrhardt C, Wagner R, Planz O, Klenk HD, Ludwig S, Pleschka S.; ''Membrane accumulation of influenza A virus hemagglutinin triggers nuclear export of the viral genome via protein kinase Calpha-mediated activation of ERK signaling.''; PubMed Europe PMC Scholia
64. Suntharalingam M, Wente SR.; ''Peering through the pore: nuclear pore complex structure, assembly, and function.''; PubMed Europe PMC Scholia
65. Li ML, Rao P, Krug RM.; ''The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits.''; PubMed Europe PMC Scholia
66. Melén K, Kinnunen L, Fagerlund R, Ikonen N, Twu KY, Krug RM, Julkunen I.; ''Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes.''; PubMed Europe PMC Scholia
67. Palese P, Compans RW.; ''Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): mechanism of action.''; PubMed Europe PMC Scholia
68. Nilsson J, Askjaer P, Kjems J.; ''A role for the basic patch and the C terminus of RanGTP in regulating the dynamic interactions with importin beta, CRM1 and RanBP1.''; PubMed Europe PMC Scholia
69. Li N, Ren A, Wang X, Fan X, Zhao Y, Gao GF, Cleary P, Wang B.; ''Influenza viral neuraminidase primes bacterial coinfection through TGF-β-mediated expression of host cell receptors.''; PubMed Europe PMC Scholia
70. Kosinski J, Mosalaganti S, von Appen A, Teimer R, DiGuilio AL, Wan W, Bui KH, Hagen WJ, Briggs JA, Glavy JS, Hurt E, Beck M.; ''Molecular architecture of the inner ring scaffold of the human nuclear pore complex.''; PubMed Europe PMC Scholia
71. DONALD HB, ISAACS A.; ''Counts of influenza virus particles.''; PubMed Europe PMC Scholia
72. Chanturiya AN, Basañez G, Schubert U, Henklein P, Yewdell JW, Zimmerberg J.; ''PB1-F2, an influenza A virus-encoded proapoptotic mitochondrial protein, creates variably sized pores in planar lipid membranes.''; PubMed Europe PMC Scholia
73. Stegmann T, Morselt HW, Scholma J, Wilschut J.; ''Fusion of influenza virus in an intracellular acidic compartment measured by fluorescence dequenching.''; PubMed Europe PMC Scholia
74. Veit M, Klenk HD, Kendal A, Rott R.; ''The M2 protein of influenza A virus is acylated.''; PubMed Europe PMC Scholia
75. Enami M, Sharma G, Benham C, Palese P.; ''An influenza virus containing nine different RNA segments.''; PubMed Europe PMC Scholia
76. Braam J, Ulmanen I, Krug RM.; ''Molecular model of a eucaryotic transcription complex: functions and movements of influenza P proteins during capped RNA-primed transcription.''; PubMed Europe PMC Scholia
77. Neumann G, Brownlee GG, Fodor E, Kawaoka Y.; ''Orthomyxovirus replication, transcription, and polyadenylation.''; PubMed Europe PMC Scholia
78. Garman E, Laver G.; ''Controlling influenza by inhibiting the virus's neuraminidase.''; PubMed Europe PMC Scholia
79. Ward AC, Castelli LA, Lucantoni AC, White JF, Azad AA, Macreadie IG.; ''Expression and analysis of the NS2 protein of influenza A virus.''; PubMed Europe PMC Scholia
80. Martin K, Helenius A.; ''Transport of incoming influenza virus nucleocapsids into the nucleus.''; PubMed Europe PMC Scholia
81. Perez DR, Donis RO.; ''Functional analysis of PA binding by influenza a virus PB1: effects on polymerase activity and viral infectivity.''; PubMed Europe PMC Scholia
82. Nemeroff ME, Barabino SM, Li Y, Keller W, Krug RM.; ''Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs.''; PubMed Europe PMC Scholia
83. Watanabe K, Takizawa N, Katoh M, Hoshida K, Kobayashi N, Nagata K.; ''Inhibition of nuclear export of ribonucleoprotein complexes of influenza virus by leptomycin B.''; PubMed Europe PMC Scholia
84. Vreede FT, Brownlee GG.; ''Influenza virion-derived viral ribonucleoproteins synthesize both mRNA and cRNA in vitro.''; PubMed Europe PMC Scholia
85. Plotch SJ, Bouloy M, Ulmanen I, Krug RM.; ''A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription.''; PubMed Europe PMC Scholia
86. Amorim MJ, Read EK, Dalton RM, Medcalf L, Digard P.; ''Nuclear export of influenza A virus mRNAs requires ongoing RNA polymerase II activity.''; PubMed Europe PMC Scholia
87. Zhang J, Lamb RA.; ''Characterization of the membrane association of the influenza virus matrix protein in living cells.''; PubMed Europe PMC Scholia
88. González S, Zürcher T, Ortín J.; ''Identification of two separate domains in the influenza virus PB1 protein involved in the interaction with the PB2 and PA subunits: a model for the viral RNA polymerase structure.''; PubMed Europe PMC Scholia
89. Petosa C, Schoehn G, Askjaer P, Bauer U, Moulin M, Steuerwald U, Soler-López M, Baudin F, Mattaj IW, Müller CW.; ''Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex.''; PubMed Europe PMC Scholia
90. Carrasco M, Amorim MJ, Digard P.; ''Lipid raft-dependent targeting of the influenza A virus nucleoprotein to the apical plasma membrane.''; PubMed Europe PMC Scholia
91. Mikulásová A, Varecková E, Fodor E.; ''Transcription and replication of the influenza a virus genome.''; PubMed Europe PMC Scholia
92. Nakagawa Y, Oda K, Nakada S.; ''The PB1 subunit alone can catalyze cRNA synthesis, and the PA subunit in addition to the PB1 subunit is required for viral RNA synthesis in replication of the influenza virus genome.''; PubMed Europe PMC Scholia
93. Veit M, Kretzschmar E, Kuroda K, Garten W, Schmidt MF, Klenk HD, Rott R.; ''Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin.''; PubMed Europe PMC Scholia
94. Palese P, Tobita K, Ueda M, Compans RW.; ''Characterization of temperature sensitive influenza virus mutants defective in neuraminidase.''; PubMed Europe PMC Scholia
95. Pritlove DC, Fodor E, Seong BL, Brownlee GG.; ''In vitro transcription and polymerase binding studies of the termini of influenza A virus cRNA: evidence for a cRNA panhandle.''; PubMed Europe PMC Scholia
96. Schmitt AP, Lamb RA.; ''Escaping from the cell: assembly and budding of negative-strand RNA viruses.''; PubMed Europe PMC Scholia
97. Salom D, Hill BR, Lear JD, DeGrado WF.; ''pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus.''; PubMed Europe PMC Scholia
98. Deng T, Vreede FT, Brownlee GG.; ''Different de novo initiation strategies are used by influenza virus RNA polymerase on its cRNA and viral RNA promoters during viral RNA replication.''; PubMed Europe PMC Scholia
99. Boulo S, Akarsu H, Ruigrok RW, Baudin F.; ''Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes.''; PubMed Europe PMC Scholia
100. De Marcos Lousa C, Trézéguet V, Dianoux AC, Brandolin G, Lauquin GJ.; ''The human mitochondrial ADP/ATP carriers: kinetic properties and biogenesis of wild-type and mutant proteins in the yeast S. cerevisiae.''; PubMed Europe PMC Scholia
101. Lamb RA, Lai CJ, Choppin PW.; ''Sequences of mRNAs derived from genome RNA segment 7 of influenza virus: colinear and interrupted mRNAs code for overlapping proteins.''; PubMed Europe PMC Scholia
102. Tatu U, Hammond C, Helenius A.; ''Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment.''; PubMed Europe PMC Scholia
103. Zheng H, Lee HA, Palese P, García-Sastre A.; ''Influenza A virus RNA polymerase has the ability to stutter at the polyadenylation site of a viral RNA template during RNA replication.''; PubMed Europe PMC Scholia
104. Baudin F, Petit I, Weissenhorn W, Ruigrok RW.; ''In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein.''; PubMed Europe PMC Scholia
105. Fortes P, Beloso A, Ortín J.; ''Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport.''; PubMed Europe PMC Scholia
106. Chen Z, Krug RM.; ''Selective nuclear export of viral mRNAs in influenza-virus-infected cells.''; PubMed Europe PMC Scholia
107. Donelan NR, Basler CF, García-Sastre A.; ''A recombinant influenza A virus expressing an RNA-binding-defective NS1 protein induces high levels of beta interferon and is attenuated in mice.''; PubMed Europe PMC Scholia
108. Mayer D, Molawi K, Martínez-Sobrido L, Ghanem A, Thomas S, Baginsky S, Grossmann J, García-Sastre A, Schwemmle M.; ''Identification of cellular interaction partners of the influenza virus ribonucleoprotein complex and polymerase complex using proteomic-based approaches.''; PubMed Europe PMC Scholia
109. Fodor E, Pritlove DC, Brownlee GG.; ''The influenza virus panhandle is involved in the initiation of transcription.''; PubMed Europe PMC Scholia
110. Bortz E, Westera L, Maamary J, Steel J, Albrecht RA, Manicassamy B, Chase G, Martínez-Sobrido L, Schwemmle M, García-Sastre A.; ''Host- and strain-specific regulation of influenza virus polymerase activity by interacting cellular proteins.''; PubMed Europe PMC Scholia
111. Morris SJ, Price GE, Barnett JM, Hiscox SA, Smith H, Sweet C.; ''Role of neuraminidase in influenza virus-induced apoptosis.''; PubMed Europe PMC Scholia
112. Takeda M, Leser GP, Russell CJ, Lamb RA.; ''Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion.''; PubMed Europe PMC Scholia
113. Veit M, Schmidt MF.; ''Timing of palmitoylation of influenza virus hemagglutinin.''; PubMed Europe PMC Scholia
114. Son KN, Liang Z, Lipton HL.; ''Double-Stranded RNA Is Detected by Immunofluorescence Analysis in RNA and DNA Virus Infections, Including Those by Negative-Stranded RNA Viruses.''; PubMed Europe PMC Scholia
115. Gething MJ, McCammon K, Sambrook J.; ''Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport.''; PubMed Europe PMC Scholia

History

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Compare	Revision	Action	Time	User	Comment
	115105	view	18:57, 25 January 2021	Egonw	Removed an empty reference.
	114625	view	16:08, 25 January 2021	ReactomeTeam	Reactome version 75
	113585	view	08:08, 3 November 2020	Egonw	Removed the empty reference (we now know this is a book that the convertor cannot handle).
	113073	view	11:13, 2 November 2020	ReactomeTeam	Reactome version 74
	112844	view	05:16, 12 October 2020	Egonw	Removed an empty (and unused) reference
	112308	view	15:22, 9 October 2020	ReactomeTeam	Reactome version 73
	101951	view	12:13, 20 November 2018	Egonw	Removed an empty reference.
	101207	view	11:10, 1 November 2018	ReactomeTeam	reactome version 66
	100745	view	20:35, 31 October 2018	ReactomeTeam	reactome version 65
	100289	view	19:12, 31 October 2018	ReactomeTeam	reactome version 64
	99835	view	15:56, 31 October 2018	ReactomeTeam	reactome version 63
	99392	view	14:33, 31 October 2018	ReactomeTeam	reactome version 62 (2nd attempt)
	99088	view	12:39, 31 October 2018	ReactomeTeam	reactome version 62
	94058	view	13:54, 16 August 2017	ReactomeTeam	reactome version 61
	93687	view	11:31, 9 August 2017	ReactomeTeam	reactome version 61
	87172	view	19:26, 18 July 2016	Mkutmon	Ontology Term : 'infectious disease pathway' added !
	86810	view	09:27, 11 July 2016	ReactomeTeam	reactome version 56
	83087	view	09:57, 18 November 2015	ReactomeTeam	Version54
	81411	view	12:56, 21 August 2015	ReactomeTeam	Version53
	76880	view	08:15, 17 July 2014	ReactomeTeam	Fixed remaining interactions
	76585	view	11:56, 16 July 2014	ReactomeTeam	Fixed remaining interactions
	75918	view	09:57, 11 June 2014	ReactomeTeam	Re-fixing comment source
	75618	view	10:48, 10 June 2014	ReactomeTeam	Reactome 48 Update
	74973	view	13:49, 8 May 2014	Anwesha	Fixing comment source for displaying WikiPathways description
	74617	view	08:40, 30 April 2014	ReactomeTeam	New pathway

External references

DataNodes

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Name	Type	Database reference	Comment
18S rRNA	Protein	X03205 (EMBL)
28S rRNA	Protein	M11167 (EMBL)
2xMe-SNRPB	Protein	P14678 (Uniprot-TrEMBL)
2xMe-SNRPD1	Protein	P62314 (Uniprot-TrEMBL)
2xMe-SNRPD3	Protein	P62318 (Uniprot-TrEMBL)
5.8S rRNA	Protein	J01866 (EMBL)
5S rRNA	Protein	V00589 (EMBL)
7-methylguanosine cap	Metabolite	CHEBI:17825 (ChEBI)
80S ribosome	Complex	R-HSA-72500 (Reactome)
AAAS	Protein	Q9NRG9 (Uniprot-TrEMBL)
ALYREF	Protein	Q86V81 (Uniprot-TrEMBL)
ASR2B		R-NUL-72050 (Reactome)
ATP	Metabolite	CHEBI:15422 (ChEBI)
Acidified Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore	Complex	R-HSA-R-FLU-189177 (Reactome)
Ala-tRNA(Ala)		R-HSA-379700 (Reactome)
Aminoacyl-tRNA	Complex	R-HSA-37001 (Reactome)
Arg-tRNA(Arg)		R-HSA-379720 (Reactome)
Asn-tRNA(Asn)		R-HSA-379728 (Reactome)
Asp-tRNA(Asp)		R-HSA-379707 (Reactome)
CALR	Protein	P27797 (Uniprot-TrEMBL)
CANX	Protein	P27824 (Uniprot-TrEMBL)
CC1.3 protein /3 RRM, RS		R-NUL-72051 (Reactome)
CCAR1	Protein	Q8IX12 (Uniprot-TrEMBL)
CD2BP2	Protein	O95400 (Uniprot-TrEMBL)
CLTA	Protein	P09496 (Uniprot-TrEMBL)
CTP	Metabolite	CHEBI:17677 (ChEBI)
Clathrin	Complex	R-HSA-177482 (Reactome)
Cleaved HA Influenza A Viral Particle	Complex	R-HSA-R-FLU-169239 (Reactome)
Crm1:Ran GTPase:GDP	Complex	R-HSA-165538 (Reactome)
Cys-tRNA(Cys)		R-HSA-379719 (Reactome)
DHX9	Protein	Q08211 (Uniprot-TrEMBL)
DNAJC3	Protein	Q13217 (Uniprot-TrEMBL)
DnaJ hom. NP_055602		R-NUL-72055 (Reactome)
Elongated vRNA-mRNA Complex	Complex	R-HSA-R-FLU-192700 (Reactome)	Capped, synthesized RNA strand complementary to vRNA, plus viral polymerase and template vRNA (Plotch, 1977).
FAU	Protein	P62861 (Uniprot-TrEMBL)
FUS	Protein	P35637 (Uniprot-TrEMBL)
GDP	Metabolite	CHEBI:17552 (ChEBI)
GRSF1	Protein	Q12849 (Uniprot-TrEMBL)
GTF2F1	Protein	P35269 (Uniprot-TrEMBL)
GTF2F2	Protein	P13984 (Uniprot-TrEMBL)
GTP	Metabolite	CHEBI:15996 (ChEBI)
Genomic RNA Segment 1	Protein	AF389115 (EMBL)
Genomic RNA Segment 2	Protein	AF389116 (EMBL)
Genomic RNA Segment 3	Protein	AF389117 (EMBL)
Genomic RNA Segment 4	Protein	AF389118 (EMBL)
Genomic RNA Segment 5	Protein	AF389119 (EMBL)
Genomic RNA Segment 6	Protein	AF389120 (EMBL)
Genomic RNA Segment 7	Protein	AF389121 (EMBL)
Genomic RNA Segment 8	Protein	AF389122 (EMBL)
Gln-tRNA(Gln)		R-HSA-379772 (Reactome)
Glu-tRNA(Glu)		R-HSA-379751 (Reactome)
Gly-tRNA(Gly)		R-HSA-379784 (Reactome)
Glycosylated NA Tetramer	Complex	R-HSA-R-FLU-195724 (Reactome)
Glycosylated NA Tetramer	Complex	R-HSA-R-FLU-195775 (Reactome)
Glycosylated NA Tetramer	Complex	R-HSA-R-FLU-195796 (Reactome)
Glycosylated NA	Protein	P03468 (Uniprot-TrEMBL)
Glycosylated NA	Protein	P03468 (Uniprot-TrEMBL)
Glycosylated and folded HA trimer	Complex	R-HSA-R-FLU-195787 (Reactome)
Glycosylated and folded HA trimer	Complex	R-HSA-R-FLU-195803 (Reactome)
Glycosylated and folded HA trimer	Complex	R-HSA-R-FLU-195819 (Reactome)
Glycosylated and folded HA	Protein	P03452 (Uniprot-TrEMBL)
Glycosylated and folded HA	Protein	P03452 (Uniprot-TrEMBL)
Glycosylated, palmitylated and folded HA trimer:Lipid Raft Complex	Complex	R-HSA-R-FLU-195723 (Reactome)
Glycosylated, palmitylated and folded HA trimer:Lipid Raft Complex	Complex	R-HSA-R-FLU-195755 (Reactome)
Glycosylated, palmitylated and folded HA trimer	Complex	R-HSA-R-FLU-195725 (Reactome)
Glycosylated, palmitylated and folded HA trimer	Complex	R-HSA-R-FLU-195738 (Reactome)
Gycosylated NA Tetramer:Lipid Raft	Complex	R-HSA-R-FLU-195735 (Reactome)
Gycosylated NA Tetramer:Lipid Raft	Complex	R-HSA-R-FLU-195736 (Reactome)
Gycosylated NA Tetramer	Complex	R-HSA-R-FLU-195728 (Reactome)
H+	Metabolite	CHEBI:15378 (ChEBI)
H+	Metabolite	CHEBI:15378 (ChEBI)
HA folded and glycosylated	Protein	P03452 (Uniprot-TrEMBL)
HA folded, glycosylated, and palmitylated	Protein	P03452 (Uniprot-TrEMBL)
HA mRNA	Protein	V01088 (EMBL)
HA1	Protein	P03452 (Uniprot-TrEMBL)
HA2	Protein	P03452 (Uniprot-TrEMBL)
HA	Protein	P03452 (Uniprot-TrEMBL)
HNRNPA0	Protein	Q13151 (Uniprot-TrEMBL)
HNRNPA1	Protein	P09651 (Uniprot-TrEMBL)
HNRNPA2B1	Protein	P22626 (Uniprot-TrEMBL)
HNRNPA3	Protein	P51991 (Uniprot-TrEMBL)
HNRNPC	Protein	P07910 (Uniprot-TrEMBL)
HNRNPD	Protein	Q14103 (Uniprot-TrEMBL)
HNRNPF	Protein	P52597 (Uniprot-TrEMBL)
HNRNPH1	Protein	P31943 (Uniprot-TrEMBL)
HNRNPH2	Protein	P55795 (Uniprot-TrEMBL)
HNRNPK	Protein	P61978 (Uniprot-TrEMBL)
HNRNPL	Protein	P14866 (Uniprot-TrEMBL)
HNRNPM	Protein	P52272 (Uniprot-TrEMBL)
HNRNPR	Protein	O43390 (Uniprot-TrEMBL)
HNRNPU	Protein	Q00839 (Uniprot-TrEMBL)
HNRNPUL1	Protein	Q9BUJ2 (Uniprot-TrEMBL)
HSP90AA1	Protein	P07900 (Uniprot-TrEMBL)
HSPA1A	Protein	P0DMV8 (Uniprot-TrEMBL)
His-tRNA(His)		R-HSA-379786 (Reactome)
Host Derived Lipid Bilayer Membrane Rich In Sphingolipids And Cholesterol		R-NUL-169703 (Reactome)
Host Derived Lipid Bilayer Membrane Rich In Sphingolipids And Cholesterol		R-NUL-169703 (Reactome)
Host Derived Lipid Bilayer Membrane Rich In Sphingolipids And Cholesterol		R-NUL-189135 (Reactome)
Host Derived Lipid Bilayer Membrane Rich In Sphingolipids And Cholesterol		R-NUL-189136 (Reactome)
HuR /3 RRM protein		R-NUL-72046 (Reactome)
IPO5	Protein	O00410 (Uniprot-TrEMBL)
Ile-tRNA(Ile)		R-HSA-379787 (Reactome)
Influenza A Viral Envelope Inserted Into The Endocytic Vesicle Membrane	Complex	R-HSA-R-FLU-189157 (Reactome)
Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore	Complex	R-HSA-R-FLU-189181 (Reactome)
Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane	Complex	R-HSA-R-FLU-189138 (Reactome)
Influenza A Viral Particle With A Fusion Competent HA2	Complex	R-HSA-R-FLU-189182 (Reactome)
Influenza A Viral Particle	Complex	R-HSA-R-FLU-189171 (Reactome)
Influenza A Viral Particle	Complex	R-HSA-R-FLU-195941 (Reactome)
Influenza H1N1 cRNA (extending)		R-FLU-193303 (Reactome)
Influenza cRNA (complete)		R-NUL-192638 (Reactome)
Influenza cRNA (complete)		R-NUL-192638 (Reactome)
Initiated cRNA-vRNA Complex	Complex	R-HSA-R-FLU-192650 (Reactome)	cRNA bound by NP and trimeric polymerase, capable of vRNA synthesis from the cRNA template.
Initiated vRNA Transcription Complex	Complex	R-HSA-R-FLU-192756 (Reactome)	Viral RNA bound by polymerase PB1-PB2-PA subunits, primed by a 5' end cap cleaved from a host mRNA, and the second ribonucleotide (a G) complementary to a the vRNA second position (a C, Beaton, 1981; Krug, 1981; Li, 2001).
Initiated vRNA-cRNA Complex	Complex	R-HSA-R-FLU-192901 (Reactome)	vRNA bound by NP and trimeric polymerase, capable of complementary RNA synthesis.
Inter-Membrane Spanning HA2	Protein	P03452 (Uniprot-TrEMBL)
Intracellular assembly complex	Complex	R-HSA-R-FLU-195925 (Reactome)
KPNA1	Protein	P52294 (Uniprot-TrEMBL)
KPNA1	Protein	P52294 (Uniprot-TrEMBL)
KPNB1	Protein	Q14974 (Uniprot-TrEMBL)
KPNB1	Protein	Q14974 (Uniprot-TrEMBL)
Leu-tRNA(Leu)		R-HSA-379757 (Reactome)
Lipid Raft		R-NUL-195731 (Reactome)
Lipid Raft		R-NUL-195764 (Reactome)
Lipid Raft		R-NUL-195764 (Reactome)
Lys-tRNA(Lys)		R-HSA-379736 (Reactome)
M1	Protein	P03485 (Uniprot-TrEMBL)
M1 mRNA	Protein	AF389121 (EMBL)
M1 mRNA	Rna	AF389121 (EMBL)
M1	Protein	P03485 (Uniprot-TrEMBL)
M2	Protein	P06821 (Uniprot-TrEMBL)
M2 Tetramer	Complex	R-HSA-R-FLU-195727 (Reactome)
M2 Tetramer	Complex	R-HSA-R-FLU-195794 (Reactome)
M2 Tetramer	Complex	R-HSA-R-FLU-195797 (Reactome)
M2 mRNA	Protein	AF389121 (EMBL)
M2 mRNA	Rna	AF389121 (EMBL)
M2	Protein	P06821 (Uniprot-TrEMBL)
Mature intronless transcript derived mRNA with m7G cap removed		R-NUL-193039 (Reactome)	A mature mRNA that has been 3' cleaved, subsequently polyadenylated, and a m7G 5' cap. The m7G has been removed or snatched. This product was derived from an intronless transcript.
Mature intronless transcript derived mRNA		R-NUL-158444 (Reactome)	A mature mRNA that has been 3' cleaved, subsequently polyadenylated, and a m7G 5' cap. This product was derived from an intronless transcript.
Mature intronless transcript derived mRNA		R-NUL-158444 (Reactome)	A mature mRNA that has been 3' cleaved, subsequently polyadenylated, and a m7G 5' cap. This product was derived from an intronless transcript.
Met-tRNA(Met)		R-HSA-379794 (Reactome)
NA	Protein	P03468 (Uniprot-TrEMBL)
NA mRNA	Protein	J02146 (EMBL)
NA	Protein	P03468 (Uniprot-TrEMBL)
NCBP1	Protein	Q09161 (Uniprot-TrEMBL)
NCBP2	Protein	P52298 (Uniprot-TrEMBL)
NEP/NS2	Protein	P03508 (Uniprot-TrEMBL)
NEP/NS2	Protein	P03508 (Uniprot-TrEMBL)
NFAR-2 protein		R-NUL-72039 (Reactome)
NFX.1	Protein	O43831 (Uniprot-TrEMBL)
NP	Protein	P03466 (Uniprot-TrEMBL)
NP mRNA	Protein	J02147 (EMBL)
NP:Lipid Raft	Complex	R-HSA-R-FLU-195737 (Reactome)
NP:Lipid Raft	Complex	R-HSA-R-FLU-195766 (Reactome)
NP	Protein	P03466 (Uniprot-TrEMBL)
NS1	Protein	P03496 (Uniprot-TrEMBL)
NS1 mRNA	Protein	J02150 (EMBL)
NS1 mRNA	Rna	J02150 (EMBL)
NS1	Protein	P03496 (Uniprot-TrEMBL)
NS2 mRNA	Protein	J02150 (EMBL)
NS2 mRNA	Rna	J02150 (EMBL)
NTP	Complex	R-HSA-R-ALL-30595 (Reactome)
NUP107	Protein	P57740 (Uniprot-TrEMBL)
NUP133	Protein	Q8WUM0 (Uniprot-TrEMBL)
NUP153	Protein	P49790 (Uniprot-TrEMBL)
NUP155	Protein	O75694 (Uniprot-TrEMBL)
NUP160	Protein	Q12769 (Uniprot-TrEMBL)
NUP188	Protein	Q5SRE5 (Uniprot-TrEMBL)
NUP205	Protein	Q92621 (Uniprot-TrEMBL)
NUP210	Protein	Q8TEM1 (Uniprot-TrEMBL)
NUP214	Protein	P35658 (Uniprot-TrEMBL)
NUP35	Protein	Q8NFH5 (Uniprot-TrEMBL)
NUP37	Protein	Q8NFH4 (Uniprot-TrEMBL)
NUP43	Protein	Q8NFH3 (Uniprot-TrEMBL)
NUP50	Protein	Q9UKX7 (Uniprot-TrEMBL)
NUP54	Protein	Q7Z3B4 (Uniprot-TrEMBL)
NUP62	Protein	P37198 (Uniprot-TrEMBL)
NUP85	Protein	Q9BW27 (Uniprot-TrEMBL)
NUP88	Protein	Q99567 (Uniprot-TrEMBL)
NUP93	Protein	Q8N1F7 (Uniprot-TrEMBL)
NUP98-3	Protein	P52948-3 (Uniprot-TrEMBL)
NUP98-4	Protein	P52948-4 (Uniprot-TrEMBL)
NUP98-5	Protein	P52948-5 (Uniprot-TrEMBL)
NUPL1-2	Protein	Q9BVL2-1 (Uniprot-TrEMBL)
NUPL2	Protein	O15504 (Uniprot-TrEMBL)
Nuclear Pore Complex (NPC)	Complex	R-HSA-157689 (Reactome)
Nup45	Protein	Q9BVL2-2 (Uniprot-TrEMBL)
P1 mRNA	Protein	J02151 (EMBL)
PA	Protein	P03433 (Uniprot-TrEMBL)
PA mRNA	Protein	V01106 (EMBL)
PA	Protein	P03433 (Uniprot-TrEMBL)
PB1	Protein	P03431 (Uniprot-TrEMBL)
PB1 mRNA	Protein	J02151 (EMBL)
PB1 mRNA	Rna	J02151 (EMBL)
PB1-F2	Protein	P0C0U1 (Uniprot-TrEMBL)
PB1	Protein	P03431 (Uniprot-TrEMBL)
PB2	Protein	P03428 (Uniprot-TrEMBL)
PB2 mRNA	Protein	AAM75155.1 (EMBL)
PB2	Protein	P03428 (Uniprot-TrEMBL)
PCBP1	Protein	Q15365 (Uniprot-TrEMBL)
PCBP2	Protein	Q15366 (Uniprot-TrEMBL)
POLR2A	Protein	P24928 (Uniprot-TrEMBL)
POLR2B	Protein	P30876 (Uniprot-TrEMBL)
POLR2C	Protein	P19387 (Uniprot-TrEMBL)
POLR2D	Protein	O15514 (Uniprot-TrEMBL)
POLR2E	Protein	P19388 (Uniprot-TrEMBL)
POLR2F	Protein	P61218 (Uniprot-TrEMBL)
POLR2G	Protein	P62487 (Uniprot-TrEMBL)
POLR2H	Protein	P52434 (Uniprot-TrEMBL)
POLR2I	Protein	P36954 (Uniprot-TrEMBL)
POLR2J	Protein	P52435 (Uniprot-TrEMBL)
POLR2K	Protein	P53803 (Uniprot-TrEMBL)
POLR2L	Protein	P62875 (Uniprot-TrEMBL)
POM121	Protein	Q96HA1 (Uniprot-TrEMBL)
PTBP1	Protein	P26599 (Uniprot-TrEMBL)
Phe-tRNA(Phe)		R-HSA-379792 (Reactome)
Pi	Metabolite	CHEBI:18367 (ChEBI)
Pro-tRNA(Pro)		R-HSA-379746 (Reactome)
RAE1	Protein	P78406 (Uniprot-TrEMBL)
RAN	Protein	P62826 (Uniprot-TrEMBL)
RANBP2	Protein	P49792 (Uniprot-TrEMBL)
RBM5	Protein	P52756 (Uniprot-TrEMBL)
RBMX	Protein	P38159 (Uniprot-TrEMBL)
RNA Polymerase II (phosphorylated):TFIIF:capped pre-mRNA	Complex	R-HSA-113405 (Reactome)
RNP Complex:Karyopherin alpha	Complex	R-HSA-R-FLU-188871 (Reactome)
RNP pre-assembly complex	Complex	R-HSA-R-FLU-196496 (Reactome)
RNP:Karyopherin alpha:Karyopherin beta complex	Complex	R-HSA-R-FLU-188844 (Reactome)
RNP:Karyopherin alpha:Karyopherin beta complex	Complex	R-HSA-R-FLU-188853 (Reactome)
RNPS1	Protein	Q15287 (Uniprot-TrEMBL)
RPL10	Protein	P27635 (Uniprot-TrEMBL)
RPL10A	Protein	P62906 (Uniprot-TrEMBL)
RPL11	Protein	P62913 (Uniprot-TrEMBL)
RPL12	Protein	P30050 (Uniprot-TrEMBL)
RPL13	Protein	P26373 (Uniprot-TrEMBL)
RPL13A	Protein	P40429 (Uniprot-TrEMBL)
RPL14	Protein	P50914 (Uniprot-TrEMBL)
RPL15	Protein	P61313 (Uniprot-TrEMBL)
RPL17	Protein	P18621 (Uniprot-TrEMBL)
RPL18	Protein	Q07020 (Uniprot-TrEMBL)
RPL18A	Protein	Q02543 (Uniprot-TrEMBL)
RPL19	Protein	P84098 (Uniprot-TrEMBL)
RPL21	Protein	P46778 (Uniprot-TrEMBL)
RPL22	Protein	P35268 (Uniprot-TrEMBL)
RPL23	Protein	P62829 (Uniprot-TrEMBL)
RPL23A	Protein	P62750 (Uniprot-TrEMBL)
RPL24	Protein	P83731 (Uniprot-TrEMBL)
RPL26	Protein	P61254 (Uniprot-TrEMBL)
RPL26L1	Protein	Q9UNX3 (Uniprot-TrEMBL)
RPL27	Protein	P61353 (Uniprot-TrEMBL)
RPL27A	Protein	P46776 (Uniprot-TrEMBL)
RPL28	Protein	P46779 (Uniprot-TrEMBL)
RPL29	Protein	P47914 (Uniprot-TrEMBL)
RPL3	Protein	P39023 (Uniprot-TrEMBL)
RPL30	Protein	P62888 (Uniprot-TrEMBL)
RPL31	Protein	P62899 (Uniprot-TrEMBL)
RPL32	Protein	P62910 (Uniprot-TrEMBL)
RPL34	Protein	P49207 (Uniprot-TrEMBL)
RPL35	Protein	P42766 (Uniprot-TrEMBL)
RPL35A	Protein	P18077 (Uniprot-TrEMBL)
RPL36	Protein	Q9Y3U8 (Uniprot-TrEMBL)
RPL36A	Protein	P83881 (Uniprot-TrEMBL)
RPL37	Protein	P61927 (Uniprot-TrEMBL)
RPL37A	Protein	P61513 (Uniprot-TrEMBL)
RPL38	Protein	P63173 (Uniprot-TrEMBL)
RPL39	Protein	P62891 (Uniprot-TrEMBL)
RPL3L	Protein	Q92901 (Uniprot-TrEMBL)
RPL4	Protein	P36578 (Uniprot-TrEMBL)
RPL40	Protein	P62987 (Uniprot-TrEMBL)
RPL41	Protein	P62945 (Uniprot-TrEMBL)
RPL5	Protein	P46777 (Uniprot-TrEMBL)
RPL6	Protein	Q02878 (Uniprot-TrEMBL)
RPL7	Protein	P18124 (Uniprot-TrEMBL)
RPL7A	Protein	P62424 (Uniprot-TrEMBL)
RPL8	Protein	P62917 (Uniprot-TrEMBL)
RPL9	Protein	P32969 (Uniprot-TrEMBL)
RPLP0	Protein	P05388 (Uniprot-TrEMBL)
RPLP1	Protein	P05386 (Uniprot-TrEMBL)
RPLP2	Protein	P05387 (Uniprot-TrEMBL)
RPS10	Protein	P46783 (Uniprot-TrEMBL)
RPS11	Protein	P62280 (Uniprot-TrEMBL)
RPS12	Protein	P25398 (Uniprot-TrEMBL)
RPS13	Protein	P62277 (Uniprot-TrEMBL)
RPS14	Protein	P62263 (Uniprot-TrEMBL)
RPS15	Protein	P62841 (Uniprot-TrEMBL)
RPS15A	Protein	P62244 (Uniprot-TrEMBL)
RPS16	Protein	P62249 (Uniprot-TrEMBL)
RPS17	Protein	P08708 (Uniprot-TrEMBL)
RPS18	Protein	P62269 (Uniprot-TrEMBL)
RPS19	Protein	P39019 (Uniprot-TrEMBL)
RPS2	Protein	P15880 (Uniprot-TrEMBL)
RPS20	Protein	P60866 (Uniprot-TrEMBL)
RPS21	Protein	P63220 (Uniprot-TrEMBL)
RPS23	Protein	P62266 (Uniprot-TrEMBL)
RPS24	Protein	P62847 (Uniprot-TrEMBL)
RPS25	Protein	P62851 (Uniprot-TrEMBL)
RPS26	Protein	P62854 (Uniprot-TrEMBL)
RPS27	Protein	P42677 (Uniprot-TrEMBL)
RPS27A(77-156)	Protein	P62979 (Uniprot-TrEMBL)
RPS28	Protein	P62857 (Uniprot-TrEMBL)
RPS29	Protein	P62273 (Uniprot-TrEMBL)
RPS3	Protein	P23396 (Uniprot-TrEMBL)
RPS3A	Protein	P61247 (Uniprot-TrEMBL)
RPS4X	Protein	P62701 (Uniprot-TrEMBL)
RPS4Y1	Protein	P22090 (Uniprot-TrEMBL)
RPS5	Protein	P46782 (Uniprot-TrEMBL)
RPS6	Protein	P62753 (Uniprot-TrEMBL)
RPS7	Protein	P62081 (Uniprot-TrEMBL)
RPS8	Protein	P62241 (Uniprot-TrEMBL)
RPS9	Protein	P46781 (Uniprot-TrEMBL)
RPSA	Protein	P08865 (Uniprot-TrEMBL)
Ran GTPase:GTP	Complex	R-HSA-165530 (Reactome)
Ribonucleoprotein (RNP) Complex	Complex	R-HSA-R-FLU-188846 (Reactome)
Ribonucleoprotein (RNP) Complex	Complex	R-HSA-R-FLU-188849 (Reactome)
SA	Metabolite	CHEBI:26667 (ChEBI)
SA	Metabolite	CHEBI:26667 (ChEBI)
SEH1L-2	Protein	Q96EE3-2 (Uniprot-TrEMBL)
SMC1A	Protein	Q14683 (Uniprot-TrEMBL)
SMC2 (P-loop, DA-box)		R-NUL-72056 (Reactome)
SNRNP70	Protein	P08621 (Uniprot-TrEMBL)
SNRPA	Protein	P09012 (Uniprot-TrEMBL)
SNRPD2	Protein	P62316 (Uniprot-TrEMBL)
SNRPE	Protein	P62304 (Uniprot-TrEMBL)
SNRPF	Protein	P62306 (Uniprot-TrEMBL)
SNRPG	Protein	P62308 (Uniprot-TrEMBL)
SRRM1	Protein	Q8IYB3 (Uniprot-TrEMBL)
SRSF1	Protein	Q07955 (Uniprot-TrEMBL)
SRSF2	Protein	Q01130 (Uniprot-TrEMBL)
SRSF3	Protein	P84103 (Uniprot-TrEMBL)
SRSF5	Protein	Q13243 (Uniprot-TrEMBL)
SRSF6	Protein	Q13247 (Uniprot-TrEMBL)
SRSF7	Protein	Q16629 (Uniprot-TrEMBL)
SRSF9	Protein	Q13242 (Uniprot-TrEMBL)
SUGP1	Protein	Q8IWZ8 (Uniprot-TrEMBL)
Segment 1 RNP	Complex	R-HSA-R-FLU-195947 (Reactome)
Segment 2 RNP	Complex	R-HSA-R-FLU-195950 (Reactome)
Segment 3 RNP	Complex	R-HSA-R-FLU-195952 (Reactome)
Segment 4 RNP	Complex	R-HSA-R-FLU-195942 (Reactome)
Segment 5 RNP	Complex	R-HSA-R-FLU-195951 (Reactome)
Segment 6 RNP	Complex	R-HSA-R-FLU-195943 (Reactome)
Segment 7 RNP	Complex	R-HSA-R-FLU-195939 (Reactome)
Segment 8 RNP	Complex	R-HSA-R-FLU-195949 (Reactome)
Ser-tRNA(Ser)		R-HSA-379738 (Reactome)
Sialic Acid Bound Influenza A Viral Particle	Complex	R-HSA-R-FLU-188954 (Reactome)
Sialic Acid Bound Influenza A Viral Particle	Complex	R-HSA-R-FLU-195945 (Reactome)
Spliceosomal E Complex	Complex	R-HSA-72057 (Reactome)
TPR	Protein	P12270 (Uniprot-TrEMBL)
Thr-tRNA(Thr)		R-HSA-379783 (Reactome)
Trp-tRNA(Trp)		R-HSA-379765 (Reactome)
Tyr-tRNA(Tyr)		R-HSA-379785 (Reactome)
U1 snRNA	Protein	V00590 (EMBL)
U1snRNP C protein		R-NUL-71916 (Reactome)
U2AF1	Protein	Q01081 (Uniprot-TrEMBL)
U2AF2	Protein	P26368 (Uniprot-TrEMBL)
UBA, Tudor - FLJ21007		R-NUL-72052 (Reactome)
UTP	Metabolite	CHEBI:15713 (ChEBI)
Val-tRNA(Val)		R-HSA-379790 (Reactome)
Viral Polymerase	Complex	R-HSA-R-FLU-192720 (Reactome)	Heterotrimeric influenza viral polymerase complex consisting of PB1, PB2, and PA; although capable of being imported into the nucleus independently, the three subunits of the influenza polymerase assemble in the nucleus to form a mature ternary polymerase complex that binds viral vRNA or cRNA (reviewed in Buolo et al., 2006).
Viral Proteins	Complex	R-HSA-R-FLU-192631 (Reactome)
Viral Proteins	Complex	R-HSA-R-FLU-2168084 (Reactome)
XPO1	Protein	O14980 (Uniprot-TrEMBL)
XPO1	Protein	O14980 (Uniprot-TrEMBL)
YBX1	Protein	P67809 (Uniprot-TrEMBL)
cRNP	Complex	R-HSA-R-FLU-192682 (Reactome)	Extended cRNA complexed with viral NP and trimeric polymerase.
capped pre-mRNA		R-NUL-72085 (Reactome)
capped, methylated pre-mRNA		R-NUL-77507 (Reactome)
p-S5-POLR2A	Protein	P24928 (Uniprot-TrEMBL)
p68 DEAH protein		R-HSA-72038 (Reactome)
palmitylated M2 Tetramer	Complex	R-HSA-R-FLU-195732 (Reactome)
palmitylated M2 Tetramer	Complex	R-HSA-R-FLU-195761 (Reactome)
palmitylated M2	Protein	P06821 (Uniprot-TrEMBL)
vRNA (Genomic):NP Complex	Complex	R-HSA-R-FLU-193302 (Reactome)
vRNA (genomic)	Complex	R-HSA-R-FLU-192849 (Reactome)
vRNA Transcription Complex	Complex	R-HSA-R-FLU-192703 (Reactome)	The 5' and 3' ends of the vRNA bound to the PB1 subunit of the viral RNA polymerase; PB2 bound to the methylated cap on a host pre-mRNA amino acids (Cianci, 1995; Brownlee, 2002; Honda, 1999).
vRNP Export Complex	Complex	R-HSA-192667 (Reactome)
vRNP destined for Export	Complex	R-HSA-R-FLU-192922 (Reactome)
vRNP:M1 for Export	Complex	R-HSA-R-FLU-192906 (Reactome)
vRNP:M1:NEP:NP	Complex	R-HSA-R-FLU-192768 (Reactome)
vRNP:M1:NEP	Complex	R-HSA-R-FLU-192767 (Reactome)
vRNP	Complex	R-HSA-R-FLU-192774 (Reactome)	A three dimensional crystal structure of NP suggests that this molecule forms a trimer that binds viral RNA (Ye et al., 2006). Mutiple NP trimers complex vRNA or cRNA.
viral mRNA	Complex	R-HSA-R-FLU-192803 (Reactome)
viral mRNA	Complex	R-HSA-R-FLU-192988 (Reactome)

Annotated Interactions

View all...

Source	Target	Type	Database reference	Comment
80S ribosome		mim-catalysis	R-HSA-192704 (Reactome)
80S ribosome		mim-catalysis	R-HSA-192841 (Reactome)
	Acidified Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore	Arrow	R-HSA-168313 (Reactome)
Acidified Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore			R-HSA-168299 (Reactome)
Aminoacyl-tRNA			R-HSA-192704 (Reactome)
Aminoacyl-tRNA			R-HSA-192841 (Reactome)
CALR		Arrow	R-HSA-169921 (Reactome)
CANX		Arrow	R-HSA-169921 (Reactome)
Clathrin		Arrow	R-HSA-168285 (Reactome)
Cleaved HA Influenza A Viral Particle			R-HSA-168272 (Reactome)
	Crm1:Ran GTPase:GDP	Arrow	R-HSA-168880 (Reactome)
DNAJC3		Arrow	R-HSA-192841 (Reactome)
	Elongated vRNA-mRNA Complex	Arrow	R-HSA-168334 (Reactome)
Elongated vRNA-mRNA Complex			R-HSA-168301 (Reactome)
GRSF1		Arrow	R-HSA-192841 (Reactome)
	Glycosylated NA Tetramer	Arrow	R-HSA-168869 (Reactome)
	Glycosylated NA Tetramer	Arrow	R-HSA-168871 (Reactome)
	Glycosylated NA Tetramer	Arrow	R-HSA-169847 (Reactome)
Glycosylated NA Tetramer			R-HSA-168869 (Reactome)
Glycosylated NA Tetramer			R-HSA-168871 (Reactome)
Glycosylated NA Tetramer			R-HSA-195726 (Reactome)
	Glycosylated NA	Arrow	R-HSA-169919 (Reactome)
Glycosylated NA			R-HSA-169847 (Reactome)
	Glycosylated and folded HA trimer	Arrow	R-HSA-168869 (Reactome)
	Glycosylated and folded HA trimer	Arrow	R-HSA-168871 (Reactome)
	Glycosylated and folded HA trimer	Arrow	R-HSA-168875 (Reactome)
Glycosylated and folded HA trimer			R-HSA-168858 (Reactome)
Glycosylated and folded HA trimer			R-HSA-168869 (Reactome)
Glycosylated and folded HA trimer			R-HSA-168871 (Reactome)
	Glycosylated and folded HA	Arrow	R-HSA-169921 (Reactome)
Glycosylated and folded HA			R-HSA-168875 (Reactome)
	Glycosylated, palmitylated and folded HA trimer:Lipid Raft Complex	Arrow	R-HSA-168862 (Reactome)
	Glycosylated, palmitylated and folded HA trimer:Lipid Raft Complex	Arrow	R-HSA-195730 (Reactome)
Glycosylated, palmitylated and folded HA trimer:Lipid Raft Complex			R-HSA-195730 (Reactome)
	Glycosylated, palmitylated and folded HA trimer	Arrow	R-HSA-168858 (Reactome)
Glycosylated, palmitylated and folded HA trimer			R-HSA-168862 (Reactome)
Glycosylated, palmitylated and folded HA trimer			R-HSA-195926 (Reactome)
	Gycosylated NA Tetramer:Lipid Raft	Arrow	R-HSA-195726 (Reactome)
	Gycosylated NA Tetramer:Lipid Raft	Arrow	R-HSA-195730 (Reactome)
Gycosylated NA Tetramer:Lipid Raft			R-HSA-195730 (Reactome)
Gycosylated NA Tetramer			R-HSA-195926 (Reactome)
	H+	Arrow	R-HSA-168299 (Reactome)
H+			R-HSA-168313 (Reactome)
	HA	Arrow	R-HSA-168884 (Reactome)
HA			R-HSA-168884 (Reactome)
HA			R-HSA-169921 (Reactome)
HSP90AA1		Arrow	R-HSA-192830 (Reactome)
HSPA1A		TBar	R-HSA-192746 (Reactome)
Host Derived Lipid Bilayer Membrane Rich In Sphingolipids And Cholesterol			R-HSA-168860 (Reactome)
IPO5		Arrow	R-HSA-192830 (Reactome)
	Influenza A Viral Envelope Inserted Into The Endocytic Vesicle Membrane	Arrow	R-HSA-168299 (Reactome)
	Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore	Arrow	R-HSA-168306 (Reactome)
Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore			R-HSA-168313 (Reactome)
Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane With An Open Pore		mim-catalysis	R-HSA-168313 (Reactome)
	Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane	Arrow	R-HSA-168312 (Reactome)
Influenza A Viral Particle Docked At The Endocytic Vesicle Membrane			R-HSA-168306 (Reactome)
	Influenza A Viral Particle With A Fusion Competent HA2	Arrow	R-HSA-168324 (Reactome)
Influenza A Viral Particle With A Fusion Competent HA2			R-HSA-168312 (Reactome)
	Influenza A Viral Particle	Arrow	R-HSA-168285 (Reactome)
	Influenza A Viral Particle	Arrow	R-HSA-168870 (Reactome)
Influenza A Viral Particle			R-HSA-168324 (Reactome)
	Influenza cRNA (complete)	Arrow	R-HSA-192851 (Reactome)
	Initiated cRNA-vRNA Complex	Arrow	R-HSA-192916 (Reactome)
Initiated cRNA-vRNA Complex			R-HSA-192851 (Reactome)
	Initiated vRNA Transcription Complex	Arrow	R-HSA-168280 (Reactome)
Initiated vRNA Transcription Complex			R-HSA-168334 (Reactome)
	Initiated vRNA-cRNA Complex	Arrow	R-HSA-192832 (Reactome)
Initiated vRNA-cRNA Complex			R-HSA-192624 (Reactome)
	Intracellular assembly complex	Arrow	R-HSA-195926 (Reactome)
Intracellular assembly complex			R-HSA-168860 (Reactome)
	KPNA1	Arrow	R-HSA-168310 (Reactome)
KPNA1			R-HSA-168297 (Reactome)
	KPNB1	Arrow	R-HSA-168310 (Reactome)
KPNB1			R-HSA-168317 (Reactome)
Lipid Raft			R-HSA-168862 (Reactome)
Lipid Raft			R-HSA-168882 (Reactome)
Lipid Raft			R-HSA-195726 (Reactome)
M1 mRNA			R-HSA-192781 (Reactome)
	M1	Arrow	R-HSA-168299 (Reactome)
	M1	Arrow	R-HSA-168894 (Reactome)
M1			R-HSA-168894 (Reactome)
M1			R-HSA-192746 (Reactome)
M1			R-HSA-195926 (Reactome)
	M2 Tetramer	Arrow	R-HSA-168869 (Reactome)
	M2 Tetramer	Arrow	R-HSA-168871 (Reactome)
	M2 Tetramer	Arrow	R-HSA-188544 (Reactome)
M2 Tetramer			R-HSA-168869 (Reactome)
M2 Tetramer			R-HSA-168871 (Reactome)
M2 Tetramer			R-HSA-195739 (Reactome)
	M2 mRNA	Arrow	R-HSA-192781 (Reactome)
	M2 mRNA	Arrow	R-HSA-192925 (Reactome)
M2 mRNA			R-HSA-192925 (Reactome)
	M2	Arrow	R-HSA-195733 (Reactome)
M2			R-HSA-188544 (Reactome)
M2			R-HSA-195733 (Reactome)
	Mature intronless transcript derived mRNA with m7G cap removed	Arrow	R-HSA-168280 (Reactome)
Mature intronless transcript derived mRNA			R-HSA-168326 (Reactome)
	NA	Arrow	R-HSA-195734 (Reactome)
NA			R-HSA-169919 (Reactome)
NA			R-HSA-195734 (Reactome)
NA		mim-catalysis	R-HSA-168870 (Reactome)
	NEP/NS2	Arrow	R-HSA-168299 (Reactome)
NEP/NS2			R-HSA-168893 (Reactome)
NEP/NS2			R-HSA-195926 (Reactome)
	NP:Lipid Raft	Arrow	R-HSA-168882 (Reactome)
	NP:Lipid Raft	Arrow	R-HSA-195730 (Reactome)
NP:Lipid Raft			R-HSA-195730 (Reactome)
NP		Arrow	R-HSA-168326 (Reactome)
NP		Arrow	R-HSA-192677 (Reactome)
NP		Arrow	R-HSA-192832 (Reactome)
NP			R-HSA-168882 (Reactome)
NP			R-HSA-192624 (Reactome)
NP			R-HSA-192851 (Reactome)
NP			R-HSA-192912 (Reactome)
NP			R-HSA-195926 (Reactome)
NS1 mRNA			R-HSA-192781 (Reactome)
NS1		Arrow	R-HSA-192841 (Reactome)
	NS2 mRNA	Arrow	R-HSA-192781 (Reactome)
	NS2 mRNA	Arrow	R-HSA-192925 (Reactome)
NS2 mRNA			R-HSA-192925 (Reactome)
NTP			R-HSA-168334 (Reactome)
NTP			R-HSA-192624 (Reactome)
NTP			R-HSA-192832 (Reactome)
NTP			R-HSA-192851 (Reactome)
Nuclear Pore Complex (NPC)		Arrow	R-HSA-168337 (Reactome)
Nuclear Pore Complex (NPC)		Arrow	R-HSA-168880 (Reactome)
Nuclear Pore Complex (NPC)		mim-catalysis	R-HSA-192627 (Reactome)
Nuclear Pore Complex (NPC)		mim-catalysis	R-HSA-192925 (Reactome)
PA			R-HSA-192677 (Reactome)
PA			R-HSA-192830 (Reactome)
PA			R-HSA-195926 (Reactome)
PB1 mRNA			R-HSA-192704 (Reactome)
	PB1-F2	Arrow	R-HSA-192704 (Reactome)
PB1			R-HSA-192677 (Reactome)
PB1			R-HSA-192830 (Reactome)
PB1			R-HSA-195926 (Reactome)
PB2			R-HSA-192677 (Reactome)
PB2			R-HSA-192830 (Reactome)
PB2			R-HSA-195926 (Reactome)
	Pi	Arrow	R-HSA-168880 (Reactome)
			R-HSA-168272 (Reactome)	Influenza viruses bind via their surface HA (hemagglutinin) to sialic acid in alpha 2,3 or alpha 2,6 linkage with galactose on the host cell surface. Sialic acid in 2,6 linkages is characteristic of human cells while 2,3 linkages are characteristic of avian cells. The specificity of influenza HA for sialic acid in alpha 2,6 or alpha 2,3 linkages is a feature restricting the transfer of influenza viruses between avian species and humans. This species barrier can be overcome, however. Notably, passaged viruses adapt to their host through mutation in the receptor binding site of the viral HA gene.
			R-HSA-168280 (Reactome)	The host cell mRNA bound to viral RNA polymerase PB2 subunit is cleaved by the viral RNA polymerase PB1 subunit's endonuclease activity, and the capped 5' end plus 10-13 nucleotides of the host mRNA remains bound to the polymerase complex (Plotch, 1981; Krug, 1981; Hagen, 1994; Cianci, 1995, Li, 1998; Li, 2001). Viral mRNA may be protected against cap-snatching by the polymerase complex itself, which tightly binds capped viral mRNA (Shih, 1996). A guanine residue, complementary to a cytosine in the vRNA, is added to the host-derived cap, catalyzed by the RNA polymerase activity of the PB1 viral RNA polymerase subunit (Beaton, 1981; Toyoda, 1986).
			R-HSA-168285 (Reactome)	Virus particles bound to the cell surface can be internalized by four mechanisms. Most internalization appears to be mediated by clathrin-coated pits.
			R-HSA-168297 (Reactome)	The eight influenza virus genome segments never exist as naked RNA but are associated with four viral proteins to form viral ribonucleoprotein complexes (vRNPs). The major viral protein in the RNP complex is the nucleocapsid protein (NP), which coats the RNA. The remaining proteins PB1, PB2 and PA bind to the partially complementary ends of the viral RNA, creating the distinctive panhandle structure. The influenza viral NP behaves like a nuclear localization sequence (NLS) containing protein. The RNP docks at the nuclear envelope only in the presence of the heterodimeric karyopherin alpha and beta complex. Here karyopherin alpha recognizes the RNP.
			R-HSA-168299 (Reactome)	The influx of H+ ions into the virion disrupts protein-protein interactions, resulting in the release of the viral RNP from the viral matrix (M1) protein. The uncoating process is complete with the appearance of free RNP complexes in the cytosol.
			R-HSA-168301 (Reactome)	A poly-uridine sequence motif, consisting in most cases of 5-7 U residues, abuts the "panhandle" duplex structure in the vRNA; this sequence is approximately 16 nucleotides from the 5' end of this RNA duplex structure within the vRNA promoter. Encountering this signal, the viral RNA polymerase stutters, leading to the synthesis of a poly-A tail on the viral mRNA (Robertson, 1981; Luo, 1991; Li,1994; Poon, 1998; Zheng et al. 1999).
			R-HSA-168306 (Reactome)	The concerted structural change of several hemagglutinin molecules opens a pore through which the viral RNP will be able to pass into the host cell cytosol.
			R-HSA-168310 (Reactome)	Once the viral RNP and heterodimeric karyopherin complex has been transported into the nucleus the RNP dissasociates from the heterodimeric karyopherins.
			R-HSA-168312 (Reactome)	The fusion peptide of its HA2 subunit interacts with the endosome membrane. The transmembrane domain of the HA2 is inserted into the viral membrane and the fusion peptide is inserted into the endosomal membrane. In the acidic pH structure of HA the two ends of the HA complex are in juxtaposition.
			R-HSA-168313 (Reactome)	The uncoating of influenza viruses in endosomes is blocked by changes in pH caused by weak bases (e.g. ammonium chloride and chloroquine) or ionophores (e.g. monensin). Effective uncoating is also dependent on the presence of the viral M2 ion channel protein. Early on it was recognized that amantadine and rimantadine inhibit replication immediately following virus infection. Later it was found that the virus-associated M2 protein allows the influx of H+ ions from the endosome into the virion. This disrupts protein-protein interactions, resulting in the release of viral RNP free of the viral matrix (M1) protein. Amantadine and rimantadine have been shown to block the ion channel activity of the M2 protein and thus uncoating.
			R-HSA-168317 (Reactome)	The eight influenza virus genome segments are associated with four viral proteins to form viral ribonucleoprotein complexes (vRNPs). The major viral protein in the RNP complex is the nucleocapsid protein (NP), which coats the RNA. The remaining proteins PB1, PB2 and PA bind to the partially complementary ends of the viral RNA. The influenza viral NP behaves like a nuclear localization sequence (NLS) containing protein. The RNP docks at the nuclear envelope only in the presence of the heterodimeric karyopherin alpha and beta complex. Once the NLS is recognized by karyopherin alpha the karyopherin beta subunit joins the complex.
			R-HSA-168324 (Reactome)	The low pH of the endosome causes the viral HA (hemagglutinin) to undergo a structural change which frees the fusion peptide of its HA2 subunit.
			R-HSA-168326 (Reactome)	The 5' end of the vRNA associates with a binding site on the PB1 subunit of the viral RNA polymerase, distinct from the 3' vRNA binding site, which is subsequenty bound forming a loop. These binding events set off allosteric conformational changes in the trimeric polymerase complex that induce PB2 binding of the methylated cap on a host pre-mRNA (Plotch, 1981; Cianci, 1995; Li, 1998; Brownlee, 2002; Kolpashchikov, 2004). PB2 amino acids 242-282 and 538-577 are involved in cap binding (Honda, 1999). Direct or indirect interaction with active, transcribing host RNA polymerase II is thought to supply host mRNA for the caps (Bouloy, 1978; Engelhardt, 2005).
			R-HSA-168334 (Reactome)	Catalyzed by the RNA polymerase activity of the viral PB1 subunit, an mRNA complementary to the bound vRNA is synthesized (Plotch, 1977). PA and PB2 move down the growing mRNA in complex with PB1, with PB2 possibly dissociating from the cap (Braam, 1983). However, the 5’ end of the vRNA may remain bound during elongation as the template is threaded through in a 3’ to 5’ direction until a polyadenylation signal is encountered (Poon, 1998; Zheng, 1999).
			R-HSA-168337 (Reactome)	These RNPs (10-20nm wide) are too large to passively diffuse into the nucleus and therefore, once released from an incoming particle they must rely on the active import mechanism of the host cell nuclear pore complex (NPC). Once the RNP heterodimeric karyopherin complex docks at the NPC, it is transported into the nucleus.
			R-HSA-168857 (Reactome)	Virus NEP/NS2 interacts with human CRM1 (hCRM1), possibly dependent on a nuclear export signal (NES) motif in the NEP/NS2 N-terminal region (O'Neill, 1998; Neumann, 2000). The CRM1/exportin-1 pathway is a cellular mechanism for nuclear export, with CRM1 interacting with the Ran small GTPase and a cargo molecule's leucine-rich NES (Fukuda, 1997; Petosa, 2004). Leptomycin B, which specifically inhibits hCRM1, blocks export of viral RNP (Elton, 2001; Ma, 2001; Watanabe, 2001). Thus, NEP/NS2 interaction with cellular nuclear export machinery is essential for nuclear export of vRNP complexes and influenza virus release. A role for NP protein interaction with export machinery has also been proposed (Elton, 2001).
			R-HSA-168858 (Reactome)	The hemagglutinin of influenza virus is palmitoylated with long-chain fatty acids. Palmitoylation of HA is believed to occur in the cis golgi network (Veit 1993), shortly after trimerisation of the molecule, and before cleavage of the HA into HA1 and HA2. HA is palmitoylated through thioester linkages at three cysteine residues located in the cytoplasmic domain and at the carboxy-terminal end of the transmembrane region. Lack of acylation has no obvious influence on the biological activities of HA.
			R-HSA-168860 (Reactome)	The final step in the budding process is the fusion of the lipid membrane surrounding the virion core, producing an extracellular enveloped virus particle (Nayak et al. 2004).
			R-HSA-168862 (Reactome)	Influenza virus buds preferentially from lipid rafts (Scheiffele et al, 1999). NA protein individually accumulates at, and is selectively incorporated into rafts (Kundu et al., 1996). The signals for raft association lie within the transmembranse domain (TMD), (Barman et al., 2001, Barman et al., 2004), and raft association of NA has been shown to be essential for efficient virus replication. This is believed to be due to a requirement for a concentration of NA at specific areas of the plasma membrane to support a level of NA incorporation into budding particles sufficient to allow for efficient virus release (Barman et al., 2004).
			R-HSA-168869 (Reactome)	Viral proteins are packaged into a golgi apparatus bound transport vesicle.
			R-HSA-168870 (Reactome)	The release of influenza virus particles after seperation of the virus and infected cell membrane is an active process. During the budding process, HA on the surface of the newly budding virion binds to cell surface molecules containing sialic acid residues as seen during attachment. The NA glycoproteins neuraminidase activity is essential to cleave the link between the HA and sialic acid on the surface of the host cell from which the budding virus is emeging from. Thus the NA mediated cleavage of sialic acid residues terminally linked to glycoproteins and glycolipids is the final step in releasing the virus particle from the host cell. This essential role of NA in release of virus particle has been demonstrated with the use of NA inhibitors (Palese, 1976; Luo, 1999; Garman, 2004), ts NA mutant viruses (Palese, 1974) and with viruses lacking NA activity (Liu, 1995). In all cases, viruses remain bound to the cell surface in clumps in the absence of NA enzymatic activity, resulting in loss of infectivity. Addition of exogenous sialidase results in virus release and recovery of infectivity. The sialidase activity of the NA is also important for removing sialic acid from the HA on virus particles, if this is not removed, virus particles aggregate.
			R-HSA-168871 (Reactome)	Once the tranport vesicle arrives at the golgi apparatus, it docks and dumps its contents into the golgi lumen.
			R-HSA-168875 (Reactome)	Trimerisation of the fully folded and fully oxidised HA monomer is thought to occur in the endoplasmic reticulum and ERGIC compartment, following dissociation of HA from calnexin. Trimerisation is generally thought to be the final step in HA maturation occurring in the endoplasmic reticulum before transport to the Golgi apparatus, although Yewdell et al (1988) provide data suggesing that trimerisation may occur within the Golgi.
			R-HSA-168880 (Reactome)	Viral RNP, bound by M1 and NEP/NS2 interacting with CRM1, are shuttled through the nuclear pore into the cytoplasm (Martin, 1991; O'Neill, 1998; Buolo, 2006). This mechanism may resemble export of HIV-1 ribonucleoprotein, where the HIV-1 Rev export protein interacts with CRM1 (Askjaer, 1998). A number of cofactors are implicated in CRM1-mediated export, including the small GTPase Ran, Ran-binding proteins 1 and 3, and a guanine nucleotide exchange factor (Nilsson, 2001; Nemergut, 2002; Petosa, 2004). Ternary CRM1-cofactor-cargo complexes likely interact transiently with nuclear pore proteins (nucleoporins) as they traverse the pore (reviewed in Suntharalingam, 2003). RanGTP is hydrolyzed to RanGDP in the cytoplasm, an activity that can be stimulated by NEP/NS2 (Akarsu, 2003). Influenza infection activates Raf/MEK/ERK signaling, which is necessary for NEP/NS2-mediated export of viral RNP (Pleschka, 2001; Marjuki, 2006). Influenza vRNP complexes released into the cytoplasm do not re-enter the nucleus, as they are thought to remain bound by M1, preventing re-import (Martin, 1991). It has been suggested that M1 binding of zinc cations could distinguish M1 bound to the vRNP from polymerized, matrix M1 present in nascent virions (Elster, 1994).
			R-HSA-168882 (Reactome)	There is evidence that NP alone is intrinsically targeted to the apical plasma membrane and associates with lipid rafts in a cholesterol-dependent manner, which suggests that RNPs could reach the assembly site independently of the other viral components.
			R-HSA-168884 (Reactome)	The integral membrane protein HA is synthesized on membrane-bound ribosomes and subsequently transported across the endoplasmic reticulum, where it is folded, glycosylated, and assembled into a trimer.
			R-HSA-168893 (Reactome)	Structural characterization of NEP/NS2 suggests that acidic residues in the C-terminus of NEP/NS2 bind to M1, with Trp78 critical for interaction (Ward, 1995; Yasuda, 1993; Akarsu, 2003).
			R-HSA-168894 (Reactome)	There is evidence for the association of M1 with lipid rafts in influenza infected cells, whereas M1 expressed alone remains soluble (Ali et al., 2000; Zhang and Lamb, 1996), suggesting association of M1 with other viral proteins in targetting to the cell membrane. Coexpression of HA and NA together with M1 has been shown to promote raft association of M1. This association requires the TMD and cytoplasmic tails of HA and NA (Ali et al, 2000; Zhang et al, 2000). This is consistent with M1 becoming associated with HA and NA during their passage through the exocytic pathway to raft domains in the apical membrane. alternatively M1 may use the cytoskeleton to reach the virus assembly site, as M1 interacts with cytoskeletal components (Alvalos et al., 1997). The M1 interaction depends on the presence of RNP and is most likely mediated by direct binding of F-actin by NP (Digard et al., 1999).
			R-HSA-168895 (Reactome)	The random incorporation model as its name suggests proposes that there is no selection at all on which vRNPs are packaged. It is assumed that each vRNP has equal probability of being packaged, and that if enough vRNPS are packaged a particular percentage of budding virions will receive at least one copy of each genome segment. This model is supported by evidence that infectious virions may possess more than eight vRNPs assuring the presence of a full complement of eight vRNPs in a significant percentage of virus particles. Mathematical analysis of packaging suggested that twelve RNA segments would need to be packaged in order to obtain approximately 10% of virus particles that are fully infectious (Enami, 1991), a number that is compatible with experimental data (Donald, 1954). Due to the low amount of RNA per virion (estimated at 1-2% w/w), enumeration of the precise number of RNAs packaged in a virion is difficult.
			R-HSA-169847 (Reactome)	Tetramerisation of the NA occurs in the ER following an initial dimerisation step. Tetramerisation is believed to be dependant on glycosylation of the NA molecules
			R-HSA-169919 (Reactome)	Glycosylation of NA occurs within the endoplasmic reticulum and is believed to be neccessary for proper tetramerization of the NA dimers. Sugar residues become attached to four of the five potential glycosylation sites in the head of N1 neuraminidase (Hausman et al., 1997).
			R-HSA-169921 (Reactome)	The ectodomain of HA is translocated into the ER lumen, where it undergoes a series of folding events mediated by the formation of disulfide bonds and glycosylation reactions. The formation of a discrete intermediate species of highly folded monomeric protein preceeds trimerisation. The folding process is efficient and rapid, with greater than 90% of the protein trafficked to the golgi apparatus; and mature HA0 subunits appearing in a matter of a few minutes. Calnexin and calreticulin have been identified as cellular lectins which interact transiently with newly synthesized HA by attaching to partially trimmed N-linked oligosaccharides (Herbert et al., 1997), facilitating correct folding of the HA molecule.
			R-HSA-188544 (Reactome)	The M2 from influenza A virus is a 97-residue protein with a single transmembrane helix that associates to form a tetramer in the endoplasmic reticulum (Salom et al, 2000). A 15-20-residue segment C-terminal to the membrane-spanning region has been postulated to aid in the stabilization of the tetrameric assembly (Kochendoerfer et al 1999).
			R-HSA-192624 (Reactome)	Virion vRNP is capable of synthesizing cRNA immediately following entry into the cell nucleus (Vreede, 2006). The PB1 subunit principally catalyzes extension (Nakagawa, 1996). However, cRNA does not accumulate until later in the infection process, possiby requiring NP and the trimeric polymerase for stabilization (Vreede, 2004). The vRNA template is released.
			R-HSA-192627 (Reactome)	The viral polymerase complex produces positive-sense viral mRNA with host-cell derived 5' methyl caps. Capped viral mRNAs are selectively exported from the host cell nucleus through a currently unclear mechanism that may rely on components of the host cell mRNA export machinery (Chen, 2000; Engelhardt, 2006). Polyadenylation of viral mRNA appears be required for influenza mRNA export (Poon, 2000). A coupling of viral mRNA export with cellular pre-mRNA processing complexes, recruited by phosphorylation of host RNA polymerase II C-terminal domain which interacts with the viral polymerase (Engelhardt, 2005), has been proposed as controlling the export of a subset (M1, HA, and NS1, but not NP) of viral mRNA from the nucleus (Amorim, 2007).
			R-HSA-192677 (Reactome)	The nascent vRNP complexes, one for each gene segment, contain the negative-sense viral RNA and polymerase proteins (PB1, PB2, PA, and NP). In a model using negative-sense viral RNP reconstituted from transfected cells, there are multiple NP complexes and one polymerase complex arranged along a closed vRNA loop (Area et al., 2004). The three-dimensional structure of NP has revealed that three NP molecules form a stable trimer, interacting through beta-sheets b5, b6, and b7 in the C-terminal domain of the protein (Ye, 2006), with the viral RNA wrapping around the outside of the complex. Viral RNA from purified virions is present in an RNase-sensitive complex with NP and PB1, PB2, and PA, consistent with this structural model (Baudin et al, 1994; Ruigrok et al., 1995; Klumpp et al., 1997). It is not clear what controls the fate of vRNP, whether it is destined to become a template for transcription, for replication, or for export into the cytoplasm for packaging into virions at the plasma membrane, nor how distinct sub-nuclear localization and NP distribution at the nuclear matrix might mark, or polarize, a vRNP for export (Elton, 2005; Takizawa et al., 2006).
			R-HSA-192704 (Reactome)	For most influenza A strains (such as PR8), the PB1 mRNA segment produces a second protein, PB1-F2, from the +1 open reading frame (Chen, 2001). PB1-F2 is a pro-apoptotic, mitochondria-localized protein (Chen, 2001; Gibbs, 2003) that oligomerizes (Bruns, 2007) and sensitizes cells to death in concert with the mitochondrial ANT3 and VDAC proteins (Zamarin, 2005).
			R-HSA-192746 (Reactome)	M1 protein binds to viral RNP through its C-terminal domain (Baudin, 2001). The influenza M1 protein accumulates in the infected cell nucleus through a nuclear localization signal (NLS) RKLKR (residues 101-105) in its N-terminus (Ye, 1999). A host cell protein, HSP70, is thought to inhibit M1 binding at nonpermissive temperatures (Hirayama et al., 2004).
			R-HSA-192781 (Reactome)	The viral polymerase complex produces positive-sense viral mRNA with host-cell derived 5' methyl caps. Alternately spliced mRNA transcribed from M and NS vRNA segments 7 and 8, producing the spliced mRNA for M2 and NEP/NS2, respectively, are thought to be coupled to the cellular splicing and export mechanisms (Lamb, 1980; Lamb, 1981; Chen, 2000; Li, 2001). As segments 7 and 8 each encode two proteins, splicing must be regulated allowing for alternative mRNAs, with the spliced products in the minority (approximately 10%). M1 splicing may be regulated by the viral polymerase and the cellular SR splicing protein SF2/ASF (Shih, 1995; Shih, 1996); while NS1 splicing appears to be regulated by the viral mRNA intrinsically (Alonso-Caplen, 1991; Valcarel, 1991).
			R-HSA-192830 (Reactome)	The mature ternary influenza viral polymerase complex consists of PB1, PB2, and PA. The N-terminus of PB1 (residues 1-48) interacts with PB2, and amino acids 506-659 in PB1 interact with the PA subunit (Gonzalez, 1996; Perez, 2001). Although monomeric PB1, PB2 and PA, as well as PB1-PB2 and PB1-PA dimers are likely to exist in infected cells, it is believed that most of the polymerase proteins are assembled into the trimeric PB1-PB2-PA complex (Detjen, 1987). Newly synthesized subunits of the polymerase are imported into the nucleus through nuclear localization signals (NLS), which interact with cellular importin family proteins (Jones, 1986; Buolo, 2006). Importin beta-3 (Ran binding protein 5) facilitates nuclear import of PB1 and a PB1-PA dimer (Deng, 2006); coexpression of PA with PB1 was shown to enhance the import of PB1 (Fodor, 2004). A PB1-PB2 dimer has been found to interact with the molecular chaperone heat shock protein 90 (HSP90) to facilitate import (Naito, 2007). The three subunits assembled in the nucleus form a mature ternary polymerase complex that binds viral vRNA or cRNA (Jones, 1986; Buolo, 2006).
			R-HSA-192832 (Reactome)	Viral vRNA, complexed with NP protein, is bound by the trimeric viral polymerase complex in a stable secondary structure-dependent manner, referred to as a panhandle, fork or cork-screw (Fodor, 1994; Brownlee, 2002; Park, 2003; Crow, 2004). This RNA structure is made of both the 5’ and 3' ends of the vRNA. The polymerase is thought to first bind the 5' end of the vRNA and then the 3' end. Synthesis of cRNA initiates without a host cell methylated RNA cap as a primer (Beaton, 1986; Galarza, 1996; Deng, 2006; Engehardt, 2006).
			R-HSA-192841 (Reactome)	Spliced and unspliced viral mRNA exported into the cytoplasm are translated by the host cell ribosomal translation machinery (reviewed in Kash, 2006). At least ten viral proteins are synthesized: HA, NA, PB1, PB2, PA, NP, NS1, NEP/NS2 (from spliced NS mRNA), M1, and M2 (from spliced M mRNA). The abundance of each of these proteins is thought to be controlled by differential mRNA abundances and stability (Tekamp, 1980; Hatada, 1989). As the localization of the nascent polypeptides is different between viral proteins with transmembrane domains (HA, NA and M2, which translocate to the ER and are transported through the Golgi to the plasma membrane) and soluble viral proteins (such as NP, the polymerase subunits, and NS1), mechanisms linking the translation of particular viral mRNA with subsequent protein localization rely on signal sequences recognized by the cell.
			R-HSA-192851 (Reactome)	vRNA is synthesized from the complementary cRNA strand by the trimeric polymerase complex, and bound by free NP protein (Honda, 1988; Mikulasova, 2000; Neumann, 2004). The PB1 subunit, with PA, catalyzes extension (Nakagawa, 1996). The cRNA is released.
			R-HSA-192912 (Reactome)	Viral genomic RNA (vRNA) and complementary RNA (cRNA) are likely bound by the influenza nucleoprotein (NP) immediately upon synthesis. Although two nuclear localization signals have been mapped in the NP, an unconventional N-terminal NLS and a bipartite NLS within amino acids 198-216 (Wang, 1997; Neumann, 1997; Ozawa, 2007), the crystal structure of the NP suggests that only the unconventional NLS is exposed and can be used as a functional NLS (Ye, 2006). This unconvenetional NLS interacts with importins alpha-1 and -2 (Cros et al., 2005; Wang et al., 1997; Buolo et al., 2006). The three-dimensional structure of NP has revealed that NP molecules associate as a trimer, interacting through beta-sheets b5, b6, and b7 in the C-terminal domain of the protein; the viral RNA likely wraps around the outside of the complex (Ye, 2006).
			R-HSA-192916 (Reactome)	Initiation of synthesis of the viral genomic RNA (vRNA) is thought to require hairpin (or panhandle/corkscrew) RNA loop structures formed by both the 5' and 3' ends of the cRNA (Pritlove, 1995; Crow, 2004; Park, 2003; Deng, 2006). The cRNA promoter has a similar structure to the vRNA promoter, but slight sequence differences are believed to result in a stronger cRNA promoter. As with the vRNA promoter, the polymerase is thought to first bind to the 5' end of the cRNA, then to the 3' end, and subsequently initiate RNA synthesis.
			R-HSA-192925 (Reactome)	In the cases of spliced, polyadenylated mRNA transcribed from M (segment 7) and NS (segment 8) vRNA templates (producing the spliced mRNA for M2 and NS2/NEP, respectively), export may be coupled to aspects of the cellular splicing and export mechanisms (Chen, 2000; Alonso-Caplan et al, 1992; Amorim, 2006). Simultaneously, the export of cellular mRNA appear to be inhibited by the viral NS1 protein, which binds to the cellular cleavage and polyadenylation specificity factor (CPSF), preventing polyadenylation and completion of pre-mRNA processing (Nemerof et al., 1998; Fortes, 1994; Lu, 1994; Li, 2001).
			R-HSA-195726 (Reactome)	Influenza virus buds preferentially from lipid rafts (Scheiffele et al, 1999). NA protein individually accumulates at, and is selectively incorporated into rafts (Kundu et al., 1996). The signals for raft association lie within the transmembranse domain (TMD), (Barman et al., 2001, Barman et al., 2004), and raft association of NA has been shown to be essential for efficient virus replication. This is believed to be due to a requirement for a concentration of NA at specific areas of the plasma membrane to support a level of NA incorporation into budding particles sufficient to allow for efficient virus release (Barman et al., 2004).
			R-HSA-195730 (Reactome)	Once processed, the viral proteins are transported from the golgi apparatus to the plasma membrane.
			R-HSA-195733 (Reactome)	The integral membrane protein M2 is synthesized on membrane-bound ribosomes and subsequently transported across the ER, where it is folded and assembled into a tetramer.
			R-HSA-195734 (Reactome)	The integral membrane protein NA is synthesized on membrane-bound ribosomes and subsequently transported across the ER where it is folded and glycosylated. Subsequently NA is assembled into a tetramer.
			R-HSA-195739 (Reactome)	Palmitoylation of influenza A M2 occurs in the ER, or cis golgi network, following tetramerisation. The palmitoylation reaction proceeds via a labile thioester type bond at a specific residue of M2 (Sugrue et al., 1990).
			R-HSA-195926 (Reactome)	As influenza viruses bud from the plasma membrane of infected cells, complete virions are not seen inside cells. In polarized epithelial cells, assembly and budding of influenza occurs from the apical plasma membrane (Schmitt, 2004). For efficient assembly, all virion components must accumulate at the budding site, and it is believed that the viral glycoprotein accumulation determines the site of virus assembly and budding (Nayak, 2004). M1 is thought to be the bridge between the envelope glycoproteins and the RNPs for assembly (Schmitt, 2004). M2 is also required, because if it is not present RNPs are not packaged into budding virions (McCown, 2005), however it role is not known.
RNA Polymerase II (phosphorylated):TFIIF:capped pre-mRNA		Arrow	R-HSA-168326 (Reactome)
	RNP Complex:Karyopherin alpha	Arrow	R-HSA-168297 (Reactome)
RNP Complex:Karyopherin alpha			R-HSA-168317 (Reactome)
	RNP pre-assembly complex	Arrow	R-HSA-168895 (Reactome)
RNP pre-assembly complex			R-HSA-195926 (Reactome)
	RNP:Karyopherin alpha:Karyopherin beta complex	Arrow	R-HSA-168317 (Reactome)
	RNP:Karyopherin alpha:Karyopherin beta complex	Arrow	R-HSA-168337 (Reactome)
RNP:Karyopherin alpha:Karyopherin beta complex			R-HSA-168310 (Reactome)
RNP:Karyopherin alpha:Karyopherin beta complex			R-HSA-168337 (Reactome)
Ran GTPase:GTP			R-HSA-168880 (Reactome)
	Ribonucleoprotein (RNP) Complex	Arrow	R-HSA-168299 (Reactome)
	Ribonucleoprotein (RNP) Complex	Arrow	R-HSA-168310 (Reactome)
Ribonucleoprotein (RNP) Complex			R-HSA-168297 (Reactome)
	SA	Arrow	R-HSA-168285 (Reactome)
SA			R-HSA-168272 (Reactome)
SA			R-HSA-168860 (Reactome)
Segment 1 RNP			R-HSA-168895 (Reactome)
Segment 2 RNP			R-HSA-168895 (Reactome)
Segment 3 RNP			R-HSA-168895 (Reactome)
Segment 4 RNP			R-HSA-168895 (Reactome)
Segment 5 RNP			R-HSA-168895 (Reactome)
Segment 6 RNP			R-HSA-168895 (Reactome)
Segment 7 RNP			R-HSA-168895 (Reactome)
Segment 8 RNP			R-HSA-168895 (Reactome)
	Sialic Acid Bound Influenza A Viral Particle	Arrow	R-HSA-168272 (Reactome)
	Sialic Acid Bound Influenza A Viral Particle	Arrow	R-HSA-168860 (Reactome)
Sialic Acid Bound Influenza A Viral Particle			R-HSA-168285 (Reactome)
Sialic Acid Bound Influenza A Viral Particle			R-HSA-168870 (Reactome)
	Viral Polymerase	Arrow	R-HSA-168301 (Reactome)
	Viral Polymerase	Arrow	R-HSA-192624 (Reactome)
	Viral Polymerase	Arrow	R-HSA-192830 (Reactome)
	Viral Polymerase	Arrow	R-HSA-192851 (Reactome)
Viral Polymerase			R-HSA-168326 (Reactome)
Viral Polymerase			R-HSA-192832 (Reactome)
Viral Polymerase			R-HSA-192916 (Reactome)
Viral Polymerase		mim-catalysis	R-HSA-168280 (Reactome)
Viral Polymerase		mim-catalysis	R-HSA-168301 (Reactome)
Viral Polymerase		mim-catalysis	R-HSA-168334 (Reactome)
Viral Polymerase		mim-catalysis	R-HSA-192624 (Reactome)
Viral Polymerase		mim-catalysis	R-HSA-192832 (Reactome)
Viral Polymerase		mim-catalysis	R-HSA-192851 (Reactome)
Viral Polymerase		mim-catalysis	R-HSA-192916 (Reactome)
	Viral Proteins	Arrow	R-HSA-192841 (Reactome)
XPO1			R-HSA-168857 (Reactome)
	cRNP	Arrow	R-HSA-192624 (Reactome)
	cRNP	Arrow	R-HSA-192851 (Reactome)
cRNP			R-HSA-192916 (Reactome)
	palmitylated M2 Tetramer	Arrow	R-HSA-195730 (Reactome)
	palmitylated M2 Tetramer	Arrow	R-HSA-195739 (Reactome)
palmitylated M2 Tetramer			R-HSA-195730 (Reactome)
palmitylated M2 Tetramer			R-HSA-195926 (Reactome)
	vRNA (Genomic):NP Complex	Arrow	R-HSA-168301 (Reactome)
	vRNA (Genomic):NP Complex	Arrow	R-HSA-192624 (Reactome)
	vRNA (Genomic):NP Complex	Arrow	R-HSA-192851 (Reactome)
	vRNA (Genomic):NP Complex	Arrow	R-HSA-192912 (Reactome)
vRNA (Genomic):NP Complex			R-HSA-168326 (Reactome)
vRNA (Genomic):NP Complex			R-HSA-192832 (Reactome)
vRNA (genomic)			R-HSA-192912 (Reactome)
	vRNA Transcription Complex	Arrow	R-HSA-168326 (Reactome)
vRNA Transcription Complex			R-HSA-168280 (Reactome)
	vRNP Export Complex	Arrow	R-HSA-168857 (Reactome)
vRNP Export Complex			R-HSA-168880 (Reactome)
	vRNP destined for Export	Arrow	R-HSA-192677 (Reactome)
vRNP destined for Export			R-HSA-192746 (Reactome)
	vRNP:M1 for Export	Arrow	R-HSA-192746 (Reactome)
vRNP:M1 for Export			R-HSA-168893 (Reactome)
	vRNP:M1:NEP:NP	Arrow	R-HSA-168880 (Reactome)
	vRNP:M1:NEP	Arrow	R-HSA-168893 (Reactome)
vRNP:M1:NEP			R-HSA-168857 (Reactome)
vRNP			R-HSA-192677 (Reactome)
	viral mRNA	Arrow	R-HSA-168301 (Reactome)
	viral mRNA	Arrow	R-HSA-192627 (Reactome)
viral mRNA			R-HSA-192627 (Reactome)
viral mRNA			R-HSA-192841 (Reactome)