메뉴 건너뛰기




Volumn 5, Issue 10, 2013, Pages 2424-2446

Transport of the influenza virus genome from nucleus to nucleus

Author keywords

Genome packaging; Influenza virus; Intracellular transport; NEP; Nuclear export; Nuclear import; Rab11; Viral entry

Indexed keywords

CASPASE 3; INFLUENZA VIRUS HEMAGGLUTININ; KARYOPHERIN; NUCLEAR EXPORT PROTEIN; RAB11A PROTEIN; RAB11B PROTEIN; RAN PROTEIN; RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS SIALIDASE;

EID: 84885141603     PISSN: 19994915     EISSN: None     Source Type: Journal    
DOI: 10.3390/v5102424     Document Type: Review
Times cited : (74)

References (167)
  • 1
    • 84974694553 scopus 로고    scopus 로고
    • Orthomyxoviridae
    • In, 6th ed.; Knipe, D.M., Howley, P., Eds.; Lippincott Williams & Wilkins: Philadelphia, PA, USA, Chapter 40
    • Shaw, M.; Palese, P. Orthomyxoviridae. In Fields Virology, 6th ed.; Knipe, D.M., Howley, P., Eds.; Lippincott Williams & Wilkins: Philadelphia, PA, USA, 2013; Chapter 40, Volume 1, pp. 1151-1185.
    • (2013) Fields Virology , vol.1 , pp. 1151-1185
    • Shaw, M.1    Palese, P.2
  • 3
    • 0036720769 scopus 로고    scopus 로고
    • A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs
    • Fodor, E.; Crow, M.; Mingay, L.J.; Deng, T.; Sharps, J.; Fechter, P.; Brownlee, G.G. A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs. J. Virol. 2002, 76, 8989-9001.
    • (2002) J. Virol. , vol.76 , pp. 8989-9001
    • Fodor, E.1    Crow, M.2    Mingay, L.J.3    Deng, T.4    Sharps, J.5    Fechter, P.6    Brownlee, G.G.7
  • 4
    • 9944250866 scopus 로고    scopus 로고
    • Increased amounts of the influenza virus nucleoprotein do not promote higher levels of viral genome replication
    • Mullin, A.E.; Dalton, R.M.; Amorim, M.J.; Elton, D.; Digard, P. Increased amounts of the influenza virus nucleoprotein do not promote higher levels of viral genome replication. J. Gen. Virol. 2004, 85, 3689-3698.
    • (2004) J. Gen. Virol. , vol.85 , pp. 3689-3698
    • Mullin, A.E.1    Dalton, R.M.2    Amorim, M.J.3    Elton, D.4    Digard, P.5
  • 5
    • 0028024644 scopus 로고
    • Nuclear import of microinjected influenza virus ribonucleoproteins
    • Kemler, I.; Whittaker, G.; Helenius, A. Nuclear import of microinjected influenza virus ribonucleoproteins. Virology 1994, 202, 1028-1033.
    • (1994) Virology , vol.202 , pp. 1028-1033
    • Kemler, I.1    Whittaker, G.2    Helenius, A.3
  • 11
    • 33845890539 scopus 로고    scopus 로고
    • The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA
    • Ye, Q.; Krug, R.M.; Tao, Y.J. The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA. Nature 2006, 444, 1078-1082.
    • (2006) Nature , vol.444 , pp. 1078-1082
    • Ye, Q.1    Krug, R.M.2    Tao, Y.J.3
  • 12
    • 0036210827 scopus 로고    scopus 로고
    • The influenza virus nucleoprotein: A multifunctional RNA-binding protein pivotal to virus replication
    • Portela, A.; Digard, P. The influenza virus nucleoprotein: A multifunctional RNA-binding protein pivotal to virus replication. J. Gen. Virol. 2002, 83, 723-734.
    • (2002) J. Gen. Virol. , vol.83 , pp. 723-734
    • Portela, A.1    Digard, P.2
  • 13
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich, D.; Kutay, U. Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell. Dev. Biol. 1999, 15, 607-660.
    • (1999) Annu. Rev. Cell. Dev. Biol. , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 14
    • 0033397980 scopus 로고    scopus 로고
    • Python: A programming language for software integration and development
    • Sanner, M.F. Python: A programming language for software integration and development. J. Mol. Graph. Model. 1999, 17, 57-61.
    • (1999) J. Mol. Graph. Model. , vol.17 , pp. 57-61
    • Sanner, M.F.1
  • 15
    • 0020826340 scopus 로고
    • Does the higher order structure of the influenza virus ribonucleoprotein guide sequence rearrangements in influenza viral RNA?
    • Jennings, P.A.; Finch, J.T.; Winter, G.; Robertson, J.S. Does the higher order structure of the influenza virus ribonucleoprotein guide sequence rearrangements in influenza viral RNA? Cell 1983, 34, 619-627.
    • (1983) Cell , vol.34 , pp. 619-627
    • Jennings, P.A.1    Finch, J.T.2    Winter, G.3    Robertson, J.S.4
  • 16
    • 31444441789 scopus 로고    scopus 로고
    • Architecture of ribonucleoprotein complexes in influenza A virus particles
    • Noda, T.; Sagara, H.; Yen, A.; Takada, A.; Kida, H.; Cheng, R.H.; Kawaoka, Y. Architecture of ribonucleoprotein complexes in influenza A virus particles. Nature 2006, 439, 490-492.
    • (2006) Nature , vol.439 , pp. 490-492
    • Noda, T.1    Sagara, H.2    Yen, A.3    Takada, A.4    Kida, H.5    Cheng, R.H.6    Kawaoka, Y.7
  • 17
    • 80052041082 scopus 로고    scopus 로고
    • RAB11A is essential for transport of the influenza virus genome to the plasma membrane
    • Eisfeld, A.J.; Kawakami, E.; Watanabe, T.; Neumann, G.; Kawaoka, Y. RAB11A is essential for transport of the influenza virus genome to the plasma membrane. J. Virol. 2011, 85, 6117-6126.
    • (2011) J. Virol. , vol.85 , pp. 6117-6126
    • Eisfeld, A.J.1    Kawakami, E.2    Watanabe, T.3    Neumann, G.4    Kawaoka, Y.5
  • 19
    • 17444430403 scopus 로고    scopus 로고
    • Association of the influenza A virus RNA-dependent RNA polymerase with cellular RNA polymerase II
    • Engelhardt, O.G.; Smith, M.; Fodor, E. Association of the influenza A virus RNA-dependent RNA polymerase with cellular RNA polymerase II. J. Virol. 2005, 79, 5812-5818.
    • (2005) J. Virol. , vol.79 , pp. 5812-5818
    • Engelhardt, O.G.1    Smith, M.2    Fodor, E.3
  • 20
    • 33847421368 scopus 로고    scopus 로고
    • Identification of cellular interaction partners of the influenza virus ribonucleoprotein complex and polymerase complex using proteomic-based approaches
    • Mayer, D.; Molawi, K.; Martinez-Sobrido, L.; Ghanem, A.; Thomas, S.; Baginsky, S.; Grossmann, J.; Garcia-Sastre, A.; Schwemmle, M. Identification of cellular interaction partners of the influenza virus ribonucleoprotein complex and polymerase complex using proteomic-based approaches. J. Proteome Res. 2007, 6, 672-682.
    • (2007) J. Proteome Res. , vol.6 , pp. 672-682
    • Mayer, D.1    Molawi, K.2    Martinez-Sobrido, L.3    Ghanem, A.4    Thomas, S.5    Baginsky, S.6    Grossmann, J.7    Garcia-Sastre, A.8    Schwemmle, M.9
  • 21
    • 59749097063 scopus 로고    scopus 로고
    • Avian influenza A virus polymerase association with nucleoprotein, but not polymerase assembly, is impaired in human cells during the course of infection
    • Rameix-Welti, M.A.; Tomoiu, A.; dos Santos Afonso, E.; van der Werf, S.; Naffakh, N. Avian influenza A virus polymerase association with nucleoprotein, but not polymerase assembly, is impaired in human cells during the course of infection. J. Virol. 2009, 83, 1320-1331.
    • (2009) J. Virol. , vol.83 , pp. 1320-1331
    • Rameix-Welti, M.A.1    Tomoiu, A.2    dos Santos Afonso, E.3    van der Werf, S.4    Naffakh, N.5
  • 22
    • 34248397190 scopus 로고    scopus 로고
    • Influenza virus infection causes specific degradation of the largest subunit of cellular RNA polymerase II
    • Rodriguez, A.; Perez-Gonzalez, A.; Nieto, A. Influenza virus infection causes specific degradation of the largest subunit of cellular RNA polymerase II. J. Virol. 2007, 81, 5315-5324.
    • (2007) J. Virol. , vol.81 , pp. 5315-5324
    • Rodriguez, A.1    Perez-Gonzalez, A.2    Nieto, A.3
  • 25
    • 70649087924 scopus 로고    scopus 로고
    • Mechanisms and functional implications of the degradation of host RNA polymerase II in influenza virus infected cells
    • Vreede, F.T.; Chan, A.Y.; Sharps, J.; Fodor, E. Mechanisms and functional implications of the degradation of host RNA polymerase II in influenza virus infected cells. Virology 2010, 396, 125-134.
    • (2010) Virology , vol.396 , pp. 125-134
    • Vreede, F.T.1    Chan, A.Y.2    Sharps, J.3    Fodor, E.4
  • 26
    • 78349236605 scopus 로고    scopus 로고
    • The role of the influenza virus RNA polymerase in host shut-off
    • Vreede, F.T.; Fodor, E. The role of the influenza virus RNA polymerase in host shut-off. Virulence 2010, 1, 436-439.
    • (2010) Virulence , vol.1 , pp. 436-439
    • Vreede, F.T.1    Fodor, E.2
  • 27
    • 84883124285 scopus 로고    scopus 로고
    • Biogenesis, assembly and export of viral messenger ribonucleoproteins in the influenza A virus infected cell
    • York, A.; Fodor, E. Biogenesis, assembly and export of viral messenger ribonucleoproteins in the influenza A virus infected cell. RNA Biol. 2013, 10, 1274-1282.
    • (2013) RNA Biol. , vol.10 , pp. 1274-1282
    • York, A.1    Fodor, E.2
  • 28
    • 0019403963 scopus 로고
    • Identification of a second protein (M2) encoded by RNA segment 7 of influenza virus
    • Lamb, R.A.; Choppin, P.W. Identification of a second protein (M2) encoded by RNA segment 7 of influenza virus. Virology 1981, 112, 729-737.
    • (1981) Virology , vol.112 , pp. 729-737
    • Lamb, R.A.1    Choppin, P.W.2
  • 30
    • 0018715086 scopus 로고
    • Segment 8 of the influenza virus genome is unique in coding for two polypeptides
    • Lamb, R.A.; Choppin, P.W. Segment 8 of the influenza virus genome is unique in coding for two polypeptides. Proc. Natl. Acad. Sci. USA 1979, 76, 4908-4912.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4908-4912
    • Lamb, R.A.1    Choppin, P.W.2
  • 31
    • 84874044936 scopus 로고    scopus 로고
    • Adaptive mutation in influenza A virus non-structural gene is linked to host switching and induces a novel protein by alternative splicing
    • Selman, M.; Dankar, S.; Forbes, N.; JIa, J.-J.; Brown, E. Adaptive mutation in influenza A virus non-structural gene is linked to host switching and induces a novel protein by alternative splicing. Emerg. Microbes Infect. 2012, 1, e42.
    • (2012) Emerg. Microbes Infect. , vol.1
    • Selman, M.1    Dankar, S.2    Forbes, N.3    JIa, J.-J.4    Brown, E.5
  • 33
    • 84870250746 scopus 로고    scopus 로고
    • Nuclear import of the influenza A virus transcriptional machinery
    • Hutchinson, E.C.; Fodor, E. Nuclear import of the influenza A virus transcriptional machinery. Vaccine 2012, 30, 7353-7358.
    • (2012) Vaccine , vol.30 , pp. 7353-7358
    • Hutchinson, E.C.1    Fodor, E.2
  • 34
    • 84871020431 scopus 로고    scopus 로고
    • The nuclear import machinery is a determinant of influenza virus host adaptation
    • Resa-Infante, P.; Gabriel, G. The nuclear import machinery is a determinant of influenza virus host adaptation. Bioessays 2013, 35, 23-27.
    • (2013) Bioessays , vol.35 , pp. 23-27
    • Resa-Infante, P.1    Gabriel, G.2
  • 35
    • 20744460177 scopus 로고    scopus 로고
    • In vitro assembly of PB2 with a PB1-PA dimer supports a new model of assembly of influenza A virus polymerase subunits into a functional trimeric complex
    • Deng, T.; Sharps, J.; Fodor, E.; Brownlee, G.G. In vitro assembly of PB2 with a PB1-PA dimer supports a new model of assembly of influenza A virus polymerase subunits into a functional trimeric complex. J. Virol. 2005, 79, 8669-8674.
    • (2005) J. Virol. , vol.79 , pp. 8669-8674
    • Deng, T.1    Sharps, J.2    Fodor, E.3    Brownlee, G.G.4
  • 36
    • 4143148582 scopus 로고    scopus 로고
    • The PA subunit is required for efficient nuclear accumulation of the PB1 subunit of the influenza A virus RNA polymerase complex
    • Fodor, E.; Smith, M. The PA subunit is required for efficient nuclear accumulation of the PB1 subunit of the influenza A virus RNA polymerase complex. J. Virol. 2004, 78, 9144-9153.
    • (2004) J. Virol. , vol.78 , pp. 9144-9153
    • Fodor, E.1    Smith, M.2
  • 37
    • 73949092407 scopus 로고    scopus 로고
    • Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy
    • Huet, S.; Avilov, S.V.; Ferbitz, L.; Daigle, N.; Cusack, S.; Ellenberg, J. Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy. J. Virol. 2010, 84, 1254-1264.
    • (2010) J. Virol. , vol.84 , pp. 1254-1264
    • Huet, S.1    Avilov, S.V.2    Ferbitz, L.3    Daigle, N.4    Cusack, S.5    Ellenberg, J.6
  • 38
    • 0022780985 scopus 로고
    • Nuclear location of all three influenza polymerase proteins and a nuclear signal in polymerase PB2
    • Jones, I.M.; Reay, P.A.; Philpott, K.L. Nuclear location of all three influenza polymerase proteins and a nuclear signal in polymerase PB2. EMBO J. 1986, 5, 2371-2376.
    • (1986) EMBO J. , vol.5 , pp. 2371-2376
    • Jones, I.M.1    Reay, P.A.2    Philpott, K.L.3
  • 39
    • 70350125974 scopus 로고    scopus 로고
    • Nuclear dynamics of influenza A virus ribonucleoproteins revealed by live-cell imaging studies
    • Loucaides, E.M.; von Kirchbach, J.C.; Foeglein, A.; Sharps, J.; Fodor, E.; Digard, P. Nuclear dynamics of influenza A virus ribonucleoproteins revealed by live-cell imaging studies. Virology 2009, 394, 154-163.
    • (2009) Virology , vol.394 , pp. 154-163
    • Loucaides, E.M.1    von Kirchbach, J.C.2    Foeglein, A.3    Sharps, J.4    Fodor, E.5    Digard, P.6
  • 40
    • 57549086823 scopus 로고    scopus 로고
    • The host-dependent interaction of alpha-importins with influenza PB2 polymerase subunit is required for virus RNA replication
    • Resa-Infante, P.; Jorba, N.; Zamarreno, N.; Fernandez, Y.; Juarez, S.; Ortin, J. The host-dependent interaction of alpha-importins with influenza PB2 polymerase subunit is required for virus RNA replication. PLoS One 2008, 3, e3904.
    • (2008) PLoS One , vol.3
    • Resa-Infante, P.1    Jorba, N.2    Zamarreno, N.3    Fernandez, Y.4    Juarez, S.5    Ortin, J.6
  • 41
    • 77956643301 scopus 로고    scopus 로고
    • Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT
    • Fislova, T.; Thomas, B.; Graef, K.M.; Fodor, E. Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT. J. Virol. 2010, 84, 8691-8699.
    • (2010) J. Virol. , vol.84 , pp. 8691-8699
    • Fislova, T.1    Thomas, B.2    Graef, K.M.3    Fodor, E.4
  • 42
    • 33846491250 scopus 로고    scopus 로고
    • Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits
    • Naito, T.; Momose, F.; Kawaguchi, A.; Nagata, K. Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits. J. Virol. 2007, 81, 1339-1349.
    • (2007) J. Virol. , vol.81 , pp. 1339-1349
    • Naito, T.1    Momose, F.2    Kawaguchi, A.3    Nagata, K.4
  • 43
    • 0346003805 scopus 로고    scopus 로고
    • Identification of Hsp90 as a stimulatory host factor involved in influenza virus RNA synthesis
    • Momose, F.; Naito, T.; Yano, K.; Sugimoto, S.; Morikawa, Y.; Nagata, K. Identification of Hsp90 as a stimulatory host factor involved in influenza virus RNA synthesis. J. Biol. Chem. 2002, 277, 45306-45314.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45306-45314
    • Momose, F.1    Naito, T.2    Yano, K.3    Sugimoto, S.4    Morikawa, Y.5    Nagata, K.6
  • 45
    • 78649446614 scopus 로고    scopus 로고
    • Human importin alpha and RNA do not compete for binding to influenza A virus nucleoprotein
    • Boulo, S.; Akarsu, H.; Lotteau, V.; Muller, C.W.; Ruigrok, R.W.; Baudin, F. Human importin alpha and RNA do not compete for binding to influenza A virus nucleoprotein. Virology 2011, 409, 84-90.
    • (2011) Virology , vol.409 , pp. 84-90
    • Boulo, S.1    Akarsu, H.2    Lotteau, V.3    Muller, C.W.4    Ruigrok, R.W.5    Baudin, F.6
  • 46
    • 79960374214 scopus 로고    scopus 로고
    • Characterization of the interaction between the influenza A virus polymerase subunit PB1 and the host nuclear import factor Ran-binding protein 5
    • Hutchinson, E.C.; Orr, O.E.; Man Liu, S.; Engelhardt, O.G.; Fodor, E. Characterization of the interaction between the influenza A virus polymerase subunit PB1 and the host nuclear import factor Ran-binding protein 5. J. Gen. Virol. 2011, 92 (Pt 8), 1859-1869.
    • (2011) J. Gen. Virol. , Issue.92 PART 8 , pp. 1859-1869
    • Hutchinson, E.C.1    Orr, O.E.2    Man Liu, S.3    Engelhardt, O.G.4    Fodor, E.5
  • 47
    • 84880367286 scopus 로고    scopus 로고
    • The RNA polymerase of influenza a virus: Mechanisms of viral transcription and replication
    • Fodor, E. The RNA polymerase of influenza a virus: Mechanisms of viral transcription and replication. Acta Virol. 2013, 57, 113-122.
    • (2013) Acta Virol. , vol.57 , pp. 113-122
    • Fodor, E.1
  • 48
    • 84874584098 scopus 로고    scopus 로고
    • Biochemical and structural evidence in support of a coherent model for the formation of the double-helical influenza A virus ribonucleoprotein
    • Ye, Q.; Guu, T.S.; Mata, D.A.; Kuo, R.L.; Smith, B.; Krug, R.M.; Tao, Y.J. Biochemical and structural evidence in support of a coherent model for the formation of the double-helical influenza A virus ribonucleoprotein. mBio 2012, 4, e00467-12.
    • (2012) mBio , vol.4
    • Ye, Q.1    Guu, T.S.2    Mata, D.A.3    Kuo, R.L.4    Smith, B.5    Krug, R.M.6    Tao, Y.J.7
  • 49
    • 0023155247 scopus 로고
    • Influenza virus gene expression: Control mechanisms at early and late times of infection and nuclear-cytoplasmic transport of virus-specific RNAs
    • Shapiro, G.I.; Gurney, T., Jr.; Krug, R.M. Influenza virus gene expression: Control mechanisms at early and late times of infection and nuclear-cytoplasmic transport of virus-specific RNAs. J. Virol. 1987, 61, 764-773.
    • (1987) J. Virol. , vol.61 , pp. 764-773
    • Shapiro, G.I.1    Gurney Jr., T.2    Krug, R.M.3
  • 50
    • 67249108203 scopus 로고    scopus 로고
    • Genetic trans-complementation establishes a new model for influenza virus RNA transcription and replication
    • Jorba, N.; Coloma, R.; Ortin, J. Genetic trans-complementation establishes a new model for influenza virus RNA transcription and replication. PLoS Pathog. 2009, 5, e1000462.
    • (2009) PLoS Pathog. , vol.5
    • Jorba, N.1    Coloma, R.2    Ortin, J.3
  • 51
    • 4143153932 scopus 로고    scopus 로고
    • Model suggesting that replication of influenza virus is regulated by stabilization of replicative intermediates
    • Vreede, F.T.; Jung, T.E.; Brownlee, G.G. Model suggesting that replication of influenza virus is regulated by stabilization of replicative intermediates. J. Virol. 2004, 78, 9568-9572.
    • (2004) J. Virol. , vol.78 , pp. 9568-9572
    • Vreede, F.T.1    Jung, T.E.2    Brownlee, G.G.3
  • 52
    • 0024535928 scopus 로고
    • Control of influenza virus gene expression: Quantitative analysis of each viral RNA species in infected cells
    • Hatada, E.; Hasegawa, M.; Mukaigawa, J.; Shimizu, K.; Fukuda, R. Control of influenza virus gene expression: Quantitative analysis of each viral RNA species in infected cells. J. Biochem. 1989, 105, 537-546.
    • (1989) J. Biochem. , vol.105 , pp. 537-546
    • Hatada, E.1    Hasegawa, M.2    Mukaigawa, J.3    Shimizu, K.4    Fukuda, R.5
  • 53
    • 67649227447 scopus 로고    scopus 로고
    • NS2/NEP protein regulates transcription and replication of the influenza virus RNA genome
    • Robb, N.C.; Smith, M.; Vreede, F.T.; Fodor, E. NS2/NEP protein regulates transcription and replication of the influenza virus RNA genome. J. Gen. Virol. 2009, 90, 1398-1407.
    • (2009) J. Gen. Virol. , vol.90 , pp. 1398-1407
    • Robb, N.C.1    Smith, M.2    Vreede, F.T.3    Fodor, E.4
  • 54
    • 0034957221 scopus 로고    scopus 로고
    • The packaging signal of influenza viral RNA molecules
    • Tchatalbachev, S.; Flick, R.; Hobom, G. The packaging signal of influenza viral RNA molecules. Rna 2001, 7, 979-989.
    • (2001) Rna , vol.7 , pp. 979-989
    • Tchatalbachev, S.1    Flick, R.2    Hobom, G.3
  • 55
    • 0028835724 scopus 로고
    • Nucleus-Targeting domain of the matrix protein (M1) of influenza virus
    • Ye, Z.; Robinson, D.; Wagner, R.R. Nucleus-Targeting domain of the matrix protein (M1) of influenza virus. J. Virol. 1995, 69, 1964-1970.
    • (1995) J. Virol. , vol.69 , pp. 1964-1970
    • Ye, Z.1    Robinson, D.2    Wagner, R.R.3
  • 56
    • 0035264603 scopus 로고    scopus 로고
    • In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein
    • Baudin, F.; Petit, I.; Weissenhorn, W.; Ruigrok, R.W. In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein. Virology 2001, 281, 102-108.
    • (2001) Virology , vol.281 , pp. 102-108
    • Baudin, F.1    Petit, I.2    Weissenhorn, W.3    Ruigrok, R.W.4
  • 57
    • 34547584458 scopus 로고    scopus 로고
    • Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions
    • Noton, S.L.; Medcalf, E.; Fisher, D.; Mullin, A.E.; Elton, D.; Digard, P. Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions. J. Gen. Virol. 2007, 88, 2280-2290.
    • (2007) J. Gen. Virol. , vol.88 , pp. 2280-2290
    • Noton, S.L.1    Medcalf, E.2    Fisher, D.3    Mullin, A.E.4    Elton, D.5    Digard, P.6
  • 58
    • 0032865668 scopus 로고    scopus 로고
    • Association of influenza virus matrix protein with ribonucleoproteins
    • Ye, Z.; Liu, T.; Offringa, D.P.; McInnis, J.; Levandowski, R.A. Association of influenza virus matrix protein with ribonucleoproteins. J. Virol. 1999, 73, 7467-7473.
    • (1999) J. Virol. , vol.73 , pp. 7467-7473
    • Ye, Z.1    Liu, T.2    Offringa, D.P.3    McInnis, J.4    Levandowski, R.A.5
  • 59
    • 80052051986 scopus 로고    scopus 로고
    • The SUMOylation of matrix protein M1 modulates the assembly and morphogenesis of influenza A virus
    • Wu, C.Y.; Jeng, K.S.; Lai, M.M. The SUMOylation of matrix protein M1 modulates the assembly and morphogenesis of influenza A virus. J. Virol. 2011, 85, 6618-6628.
    • (2011) J. Virol. , vol.85 , pp. 6618-6628
    • Wu, C.Y.1    Jeng, K.S.2    Lai, M.M.3
  • 60
    • 0024454843 scopus 로고
    • RNA-Binding properties of influenza A virus matrix protein M1
    • Wakefield, L.; Brownlee, G.G. RNA-Binding properties of influenza A virus matrix protein M1. Nucleic Acids Res. 1989, 17, 8569-8580.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8569-8580
    • Wakefield, L.1    Brownlee, G.G.2
  • 61
    • 0141737104 scopus 로고    scopus 로고
    • Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)
    • Akarsu, H.; Burmeister, W.P.; Petosa, C.; Petit, I.; Muller, C.W.; Ruigrok, R.W.; Baudin, F. Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2). EMBO J. 2003, 22, 4646-4655.
    • (2003) EMBO J. , vol.22 , pp. 4646-4655
    • Akarsu, H.1    Burmeister, W.P.2    Petosa, C.3    Petit, I.4    Muller, C.W.5    Ruigrok, R.W.6    Baudin, F.7
  • 62
    • 78650884304 scopus 로고    scopus 로고
    • Crucial role of the influenza virus NS2 (NEP) C-terminal domain in M1 binding and nuclear export of vRNP
    • Shimizu, T.; Takizawa, N.; Watanabe, K.; Nagata, K.; Kobayashi, N. Crucial role of the influenza virus NS2 (NEP) C-terminal domain in M1 binding and nuclear export of vRNP. FEBS Lett. 2011, 585, 41-46.
    • (2011) FEBS Lett. , vol.585 , pp. 41-46
    • Shimizu, T.1    Takizawa, N.2    Watanabe, K.3    Nagata, K.4    Kobayashi, N.5
  • 64
    • 0027236576 scopus 로고
    • Molecular assembly of influenza virus: Association of the NS2 protein with virion matrix
    • Yasuda, J.; Nakada, S.; Kato, A.; Toyoda, T.; Ishihama, A. Molecular assembly of influenza virus: Association of the NS2 protein with virion matrix. Virology 1993, 196, 249-255.
    • (1993) Virology , vol.196 , pp. 249-255
    • Yasuda, J.1    Nakada, S.2    Kato, A.3    Toyoda, T.4    Ishihama, A.5
  • 65
    • 0034671826 scopus 로고    scopus 로고
    • Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1
    • Neumann, G.; Hughes, M.T.; Kawaoka, Y. Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1. EMBO J. 2000, 19, 6751-6758.
    • (2000) EMBO J. , vol.19 , pp. 6751-6758
    • Neumann, G.1    Hughes, M.T.2    Kawaoka, Y.3
  • 66
    • 0032472328 scopus 로고    scopus 로고
    • The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins
    • O'Neill, R.E.; Talon, J.; Palese, P. The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins. EMBO J. 1998, 17, 288-296.
    • (1998) EMBO J. , vol.17 , pp. 288-296
    • O'Neill, R.E.1    Talon, J.2    Palese, P.3
  • 67
    • 84872000172 scopus 로고    scopus 로고
    • A second CRM1-dependent nuclear export signal in the influenza A virus NS2 protein contributes to the nuclear export of viral ribonucleoproteins
    • Huang, S.; Chen, J.; Chen, Q.; Wang, H.; Yao, Y.; Chen, J.; Chen, Z. A second CRM1-dependent nuclear export signal in the influenza A virus NS2 protein contributes to the nuclear export of viral ribonucleoproteins. J. Virol. 2013, 87, 767-778.
    • (2013) J. Virol. , vol.87 , pp. 767-778
    • Huang, S.1    Chen, J.2    Chen, Q.3    Wang, H.4    Yao, Y.5    Chen, J.6    Chen, Z.7
  • 68
    • 84872028152 scopus 로고    scopus 로고
    • Emerging roles for the influenza A virus nuclear export protein (NEP)
    • Paterson, D.; Fodor, E. Emerging roles for the influenza A virus nuclear export protein (NEP). PLoS Pathog. 2012, 8, e1003019.
    • (2012) PLoS Pathog. , vol.8
    • Paterson, D.1    Fodor, E.2
  • 69
    • 0033946767 scopus 로고    scopus 로고
    • Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins
    • Bui, M.; Wills, E.G.; Helenius, A.; Whittaker, G.R. Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins. J. Virol. 2000, 74, 1781-1786.
    • (2000) J. Virol. , vol.74 , pp. 1781-1786
    • Bui, M.1    Wills, E.G.2    Helenius, A.3    Whittaker, G.R.4
  • 70
    • 0034749515 scopus 로고    scopus 로고
    • Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway
    • Elton, D.; Simpson-Holley, M.; Archer, K.; Medcalf, L.; Hallam, R.; McCauley, J.; Digard, P. Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway. J. Virol. 2001, 75, 408-419.
    • (2001) J. Virol. , vol.75 , pp. 408-419
    • Elton, D.1    Simpson-Holley, M.2    Archer, K.3    Medcalf, L.4    Hallam, R.5    McCauley, J.6    Digard, P.7
  • 71
    • 84861325015 scopus 로고    scopus 로고
    • A nuclear export signal in the matrix protein of Influenza A virus is required for efficient virus replication
    • Cao, S.; Liu, X.; Yu, M.; Li, J.; Jia, X.; Bi, Y.; Sun, L.; Gao, G.F.; Liu, W. A nuclear export signal in the matrix protein of Influenza A virus is required for efficient virus replication. J. Virol. 2012, 86, 4883-4891.
    • (2012) J. Virol. , vol.86 , pp. 4883-4891
    • Cao, S.1    Liu, X.2    Yu, M.3    Li, J.4    Jia, X.5    Bi, Y.6    Sun, L.7    Gao, G.F.8    Liu, W.9
  • 72
    • 84861325395 scopus 로고    scopus 로고
    • Identification and characterization of three novel nuclear export signals in the influenza A virus nucleoprotein
    • Yu, M.; Liu, X.; Cao, S.; Zhao, Z.; Zhang, K.; Xie, Q.; Chen, C.; Gao, S.; Bi, Y.; Sun, L.; et al. Identification and characterization of three novel nuclear export signals in the influenza A virus nucleoprotein. J. Virol. 2012, 86, 4970-4980.
    • (2012) J. Virol. , vol.86 , pp. 4970-4980
    • Yu, M.1    Liu, X.2    Cao, S.3    Zhao, Z.4    Zhang, K.5    Xie, Q.6    Chen, C.7    Gao, S.8    Bi, Y.9    Sun, L.10
  • 73
    • 80053436121 scopus 로고    scopus 로고
    • Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting
    • Chase, G.P.; Rameix-Welti, M.A.; Zvirbliene, A.; Zvirblis, G.; Gotz, V.; Wolff, T.; Naffakh, N.; Schwemmle, M. Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting. PLoS Pathog. 2011, 7, e1002187.
    • (2011) PLoS Pathog. , vol.7
    • Chase, G.P.1    Rameix-Welti, M.A.2    Zvirbliene, A.3    Zvirblis, G.4    Gotz, V.5    Wolff, T.6    Naffakh, N.7    Schwemmle, M.8
  • 74
    • 0028278094 scopus 로고
    • Apoptosis: A mechanism of cell killing by influenza A and B viruses
    • Hinshaw, V.S.; Olsen, C.W.; Dybdahl-Sissoko, N.; Evans, D. Apoptosis: A mechanism of cell killing by influenza A and B viruses. J. Virol. 1994, 68, 3667-3673.
    • (1994) J. Virol. , vol.68 , pp. 3667-3673
    • Hinshaw, V.S.1    Olsen, C.W.2    Dybdahl-Sissoko, N.3    Evans, D.4
  • 76
    • 0034722379 scopus 로고    scopus 로고
    • Caspases disrupt the nuclear-cytoplasmic barrier
    • Faleiro, L.; Lazebnik, Y. Caspases disrupt the nuclear-cytoplasmic barrier. J. Cell Biol. 2000, 151, 951-959.
    • (2000) J. Cell Biol. , vol.151 , pp. 951-959
    • Faleiro, L.1    Lazebnik, Y.2
  • 77
    • 33745186230 scopus 로고    scopus 로고
    • Membrane accumulation of influenza A virus hemagglutinin triggers nuclear export of the viral genome via protein kinase Calpha-mediated activation of ERK signaling
    • Marjuki, H.; Alam, M.I.; Ehrhardt, C.; Wagner, R.; Planz, O.; Klenk, H.D.; 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. J. Biol. Chem. 2006, 281, 16707-16715.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16707-16715
    • Marjuki, H.1    Alam, M.I.2    Ehrhardt, C.3    Wagner, R.4    Planz, O.5    Klenk, H.D.6    Ludwig, S.7    Pleschka, S.8
  • 78
    • 0035090589 scopus 로고    scopus 로고
    • Influenza virus propagation is impaired by inhibition of the Raf/MEK/ERK signalling cascade
    • Pleschka, S.; Wolff, T.; Ehrhardt, C.; Hobom, G.; Planz, O.; Rapp, U.R.; Ludwig, S. Influenza virus propagation is impaired by inhibition of the Raf/MEK/ERK signalling cascade. Nat. Cell Biol. 2001, 3, 301-305.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 301-305
    • Pleschka, S.1    Wolff, T.2    Ehrhardt, C.3    Hobom, G.4    Planz, O.5    Rapp, U.R.6    Ludwig, S.7
  • 80
    • 77956292773 scopus 로고    scopus 로고
    • Splicing of influenza A virus NS1 mRNA is independent of the viral NS1 protein
    • Robb, N.C.; Jackson, D.; Vreede, F.T.; Fodor, E. Splicing of influenza A virus NS1 mRNA is independent of the viral NS1 protein. J. Gen. Virol. 2010, 91, 2331-2340.
    • (2010) J. Gen. Virol. , vol.91 , pp. 2331-2340
    • Robb, N.C.1    Jackson, D.2    Vreede, F.T.3    Fodor, E.4
  • 81
    • 84873177126 scopus 로고    scopus 로고
    • Influenza A virus utilizes suboptimal splicing to coordinate the timing of infection
    • Chua, M.A.; Schmid, S.; Perez, J.T.; Langlois, R.A.; Tenoever, B.R. Influenza A virus utilizes suboptimal splicing to coordinate the timing of infection. Cell Rep. 2013, 3, 23-29.
    • (2013) Cell Rep. , vol.3 , pp. 23-29
    • Chua, M.A.1    Schmid, S.2    Perez, J.T.3    Langlois, R.A.4    Tenoever, B.R.5
  • 82
    • 0000747079 scopus 로고
    • Asymmetric budding of viruses in epithelial monlayers: A model system for study of epithelial polarity
    • Rodriguez Boulan, E.; Sabatini, D.D. Asymmetric budding of viruses in epithelial monlayers: A model system for study of epithelial polarity. Proc. Natl. Acad. Sci. USA 1978, 75, 5071-5075.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5071-5075
    • Rodriguez Boulan, E.1    Sabatini, D.D.2
  • 83
    • 25444530020 scopus 로고    scopus 로고
    • 'Genome gating'; polarized intranuclear trafficking of influenza virus RNPs
    • Elton, D.; Amorim, M.J.; Medcalf, L.; Digard, P. 'Genome gating'; polarized intranuclear trafficking of influenza virus RNPs. Biol. Lett. 2005, 1, 113-117.
    • (2005) Biol. Lett. , vol.1 , pp. 113-117
    • Elton, D.1    Amorim, M.J.2    Medcalf, L.3    Digard, P.4
  • 84
    • 77952719625 scopus 로고    scopus 로고
    • The Rab11 pathway is required for influenza A virus budding and filament formation
    • Bruce, E.A.; Digard, P.; Stuart, A.D. The Rab11 pathway is required for influenza A virus budding and filament formation. J. Virol. 2010, 84, 5848-5859.
    • (2010) J. Virol. , vol.84 , pp. 5848-5859
    • Bruce, E.A.1    Digard, P.2    Stuart, A.D.3
  • 85
    • 77958099827 scopus 로고    scopus 로고
    • Involvement of vesicular trafficking system in membrane targeting of the progeny influenza virus genome
    • Jo, S.; Kawaguchi, A.; Takizawa, N.; Morikawa, Y.; Momose, F.; Nagata, K. Involvement of vesicular trafficking system in membrane targeting of the progeny influenza virus genome. Microbes Infect./Inst. Pasteur 2010, 12, 1079-1084.
    • (2010) Microbes Infect./Inst. Pasteur , vol.12 , pp. 1079-1084
    • Jo, S.1    Kawaguchi, A.2    Takizawa, N.3    Morikawa, Y.4    Momose, F.5    Nagata, K.6
  • 86
    • 35548976680 scopus 로고    scopus 로고
    • Visualization of microtubule-mediated transport of influenza viral progeny ribonucleoprotein
    • Momose, F.; Kikuchi, Y.; Komase, K.; Morikawa, Y. Visualization of microtubule-mediated transport of influenza viral progeny ribonucleoprotein. Microbes Infect./Inst. Pasteur 2007, 9, 1422-1433.
    • (2007) Microbes Infect./Inst. Pasteur , vol.9 , pp. 1422-1433
    • Momose, F.1    Kikuchi, Y.2    Komase, K.3    Morikawa, Y.4
  • 87
    • 79955415241 scopus 로고    scopus 로고
    • A Rab11-and microtubule-dependent mechanism for cytoplasmic transport of influenza A virus viral RNA
    • Amorim, M.J.; Bruce, E.A.; Read, E.K.; Foeglein, A.; Mahen, R.; Stuart, A.D.; Digard, P. A Rab11-and microtubule-dependent mechanism for cytoplasmic transport of influenza A virus viral RNA. J. Virol. 2011, 85, 4143-4156.
    • (2011) J. Virol. , vol.85 , pp. 4143-4156
    • Amorim, M.J.1    Bruce, E.A.2    Read, E.K.3    Foeglein, A.4    Mahen, R.5    Stuart, A.D.6    Digard, P.7
  • 88
    • 84869014044 scopus 로고    scopus 로고
    • YB-1 functions as a porter to lead influenza virus ribonucleoprotein complexes to microtubules
    • Kawaguchi, A.; Matsumoto, K.; Nagata, K. YB-1 functions as a porter to lead influenza virus ribonucleoprotein complexes to microtubules. J. Virol. 2012, 86, 11086-11095.
    • (2012) J. Virol. , vol.86 , pp. 11086-11095
    • Kawaguchi, A.1    Matsumoto, K.2    Nagata, K.3
  • 89
    • 80052444493 scopus 로고    scopus 로고
    • Human immunodeficiency virus rev-binding protein is essential for influenza a virus replication and promotes genome trafficking in late-stage infection
    • Eisfeld, A.J.; Neumann, G.; Kawaoka, Y. Human immunodeficiency virus rev-binding protein is essential for influenza a virus replication and promotes genome trafficking in late-stage infection. J. Virol. 2011, 85, 9588-9598.
    • (2011) J. Virol. , vol.85 , pp. 9588-9598
    • Eisfeld, A.J.1    Neumann, G.2    Kawaoka, Y.3
  • 90
    • 79959439722 scopus 로고    scopus 로고
    • Apical transport of influenza A virus ribonucleoprotein requires Rab11-positive recycling endosome
    • Momose, F.; Sekimoto, T.; Ohkura, T.; Jo, S.; Kawaguchi, A.; Nagata, K.; Morikawa, Y. Apical transport of influenza A virus ribonucleoprotein requires Rab11-positive recycling endosome. PLoS One 2011, 6, e21123.
    • (2011) PLoS One , vol.6
    • Momose, F.1    Sekimoto, T.2    Ohkura, T.3    Jo, S.4    Kawaguchi, A.5    Nagata, K.6    Morikawa, Y.7
  • 91
    • 84870242864 scopus 로고    scopus 로고
    • Influenza A virus progeny vRNP trafficking in live infected cells studied with the virus-encoded fluorescently tagged PB2 protein
    • Avilov, S.V.; Moisy, D.; Naffakh, N.; Cusack, S. Influenza A virus progeny vRNP trafficking in live infected cells studied with the virus-encoded fluorescently tagged PB2 protein. Vaccine 2012, 30, 7411-7417.
    • (2012) Vaccine , vol.30 , pp. 7411-7417
    • Avilov, S.V.1    Moisy, D.2    Naffakh, N.3    Cusack, S.4
  • 92
  • 94
    • 12344281478 scopus 로고    scopus 로고
    • Using single-particle tracking to study nuclear trafficking of viral genes
    • Babcock, H.P.; Chen, C.; Zhuang, X. Using single-particle tracking to study nuclear trafficking of viral genes. Biophys. J. 2004, 87, 2749-2758.
    • (2004) Biophys. J. , vol.87 , pp. 2749-2758
    • Babcock, H.P.1    Chen, C.2    Zhuang, X.3
  • 96
    • 84878522822 scopus 로고    scopus 로고
    • Colocalization of different influenza viral RNA segments in the cytoplasm before viral budding as shown by single-molecule sensitivity FISH analysis
    • Chou, Y.Y.; Heaton, N.S.; Gao, Q.; Palese, P.; Singer, R.; Lionnet, T. Colocalization of different influenza viral RNA segments in the cytoplasm before viral budding as shown by single-molecule sensitivity FISH analysis. PLoS Pathog. 2013, 9, e1003358.
    • (2013) PLoS Pathog. , vol.9
    • Chou, Y.Y.1    Heaton, N.S.2    Gao, Q.3    Palese, P.4    Singer, R.5    Lionnet, T.6
  • 99
    • 84875475885 scopus 로고    scopus 로고
    • An in vitro network of intermolecular interactions between viral RNA segments of an avian H5N2 influenza A virus: Comparison with a human H3N2 virus
    • Gavazzi, C.; Isel, C.; Fournier, E.; Moules, V.; Cavalier, A.; Thomas, D.; Lina, B.; Marquet, R. An in vitro network of intermolecular interactions between viral RNA segments of an avian H5N2 influenza A virus: Comparison with a human H3N2 virus. Nucleic Acids Res. 2013, 41, 1241-1254.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 1241-1254
    • Gavazzi, C.1    Isel, C.2    Fournier, E.3    Moules, V.4    Cavalier, A.5    Thomas, D.6    Lina, B.7    Marquet, R.8
  • 102
    • 84885164210 scopus 로고    scopus 로고
    • The genome packaging signal of the influenza A virus genome comprises a genome incorporation signal and a genome bundling signal
    • doi:10.1128/JVI.01301-13
    • Goto, H.; Muramoto, Y.; Noda, T.; Kawaoka, Y. The genome packaging signal of the influenza A virus genome comprises a genome incorporation signal and a genome bundling signal. J. Virol. 2013, doi:10.1128/JVI.01301-13.
    • (2013) J. Virol.
    • Goto, H.1    Muramoto, Y.2    Noda, T.3    Kawaoka, Y.4
  • 103
    • 84864148469 scopus 로고    scopus 로고
    • The influenza A virus PB2, PA, NP, and M segments play a pivotal role during genome packaging
    • Gao, Q.; Chou, Y.Y.; Doganay, S.; Vafabakhsh, R.; Ha, T.; Palese, P. The influenza A virus PB2, PA, NP, and M segments play a pivotal role during genome packaging. J. Virol. 2012, 86, 7043-7051.
    • (2012) J. Virol. , vol.86 , pp. 7043-7051
    • Gao, Q.1    Chou, Y.Y.2    Doganay, S.3    Vafabakhsh, R.4    Ha, T.5    Palese, P.6
  • 104
    • 56449098772 scopus 로고    scopus 로고
    • Mutational analysis of cis-acting RNA signals in segment 7 of influenza A virus
    • Hutchinson, E.C.; Curran, M.D.; Read, E.K.; Gog, J.R.; Digard, P. Mutational analysis of cis-acting RNA signals in segment 7 of influenza A virus. J. Virol. 2008, 82, 11869-11879.
    • (2008) J. Virol. , vol.82 , pp. 11869-11879
    • Hutchinson, E.C.1    Curran, M.D.2    Read, E.K.3    Gog, J.R.4    Digard, P.5
  • 106
    • 70349970792 scopus 로고    scopus 로고
    • Characterisation of influenza A viruses with mutations in segment 5 packaging signals
    • Hutchinson, E.C.; Wise, H.M.; Kudryavtseva, K.; Curran, M.D.; Digard, P. Characterisation of influenza A viruses with mutations in segment 5 packaging signals. Vaccine 2009, 27, 6270-6275.
    • (2009) Vaccine , vol.27 , pp. 6270-6275
    • Hutchinson, E.C.1    Wise, H.M.2    Kudryavtseva, K.3    Curran, M.D.4    Digard, P.5
  • 107
    • 35348814973 scopus 로고    scopus 로고
    • Specific residues of the influenza A virus hemagglutinin viral RNA are important for efficient packaging into budding virions
    • Marsh, G.A.; Hatami, R.; Palese, P. Specific residues of the influenza A virus hemagglutinin viral RNA are important for efficient packaging into budding virions. J. Virol. 2007, 81, 9727-9736.
    • (2007) J. Virol. , vol.81 , pp. 9727-9736
    • Marsh, G.A.1    Hatami, R.2    Palese, P.3
  • 108
    • 39749119294 scopus 로고    scopus 로고
    • Highly conserved regions of influenza a virus polymerase gene segments are critical for efficient viral RNA packaging
    • Marsh, G.A.; Rabadan, R.; Levine, A.J.; Palese, P. Highly conserved regions of influenza a virus polymerase gene segments are critical for efficient viral RNA packaging. J. Virol. 2008, 82, 2295-2304.
    • (2008) J. Virol. , vol.82 , pp. 2295-2304
    • Marsh, G.A.1    Rabadan, R.2    Levine, A.J.3    Palese, P.4
  • 110
    • 77952302527 scopus 로고    scopus 로고
    • Sorting of influenza A virus RNA genome segments after nuclear export
    • Takizawa, N.; Kumakura, M.; Takeuchi, K.; Kobayashi, N.; Nagata, K. Sorting of influenza A virus RNA genome segments after nuclear export. Virology 2010, 401, 248-256.
    • (2010) Virology , vol.401 , pp. 248-256
    • Takizawa, N.1    Kumakura, M.2    Takeuchi, K.3    Kobayashi, N.4    Nagata, K.5
  • 111
    • 84879547713 scopus 로고    scopus 로고
    • Influenza virus reassortment occurs with high frequency in the absence of segment mismatch
    • Marshall, N.; Priyamvada, L.; Ende, Z.; Steel, J.; Lowen, A.C. Influenza virus reassortment occurs with high frequency in the absence of segment mismatch. PLoS Pathog. 2013, 9, e1003421.
    • (2013) PLoS Pathog. , vol.9
    • Marshall, N.1    Priyamvada, L.2    Ende, Z.3    Steel, J.4    Lowen, A.C.5
  • 112
    • 0012568303 scopus 로고
    • The multiplication of influenza virus. II. Multiplicity reactivation of ultraviolet irradiated virus
    • Barry, R.D. The multiplication of influenza virus. II. Multiplicity reactivation of ultraviolet irradiated virus. Virology 1961, 14, 398-405.
    • (1961) Virology , vol.14 , pp. 398-405
    • Barry, R.D.1
  • 113
    • 0015420065 scopus 로고
    • Isolation and preliminary characterization of temperature-sensitive mutants of influenza virus
    • Sugiura, A.; Tobita, K.; Kilbourne, E.D. Isolation and preliminary characterization of temperature-sensitive mutants of influenza virus. J. Virol. 1972, 10, 639-647.
    • (1972) J. Virol. , vol.10 , pp. 639-647
    • Sugiura, A.1    Tobita, K.2    Kilbourne, E.D.3
  • 114
    • 84886050113 scopus 로고    scopus 로고
    • The short stalk length of HPAI H5N1 influenza neuraminidase limits transmission of pandemic H1N1 virus in ferrets
    • doi:10.1128/JVI.00967-13
    • Blumenkrantz, D.; Roberts, K.L.; Shelton, H.; Lycett, S.; Barclay, W.S. The short stalk length of HPAI H5N1 influenza neuraminidase limits transmission of pandemic H1N1 virus in ferrets. J. Virol. 2013, doi:10.1128/JVI.00967-13.
    • (2013) J. Virol.
    • Blumenkrantz, D.1    Roberts, K.L.2    Shelton, H.3    Lycett, S.4    Barclay, W.S.5
  • 117
    • 79952069060 scopus 로고    scopus 로고
    • Influenza virus assembly and budding
    • Rossman, J.S.; Lamb, R.A. Influenza virus assembly and budding. Virology 2011, 411, 229-236.
    • (2011) Virology , vol.411 , pp. 229-236
    • Rossman, J.S.1    Lamb, R.A.2
  • 119
    • 0035950932 scopus 로고    scopus 로고
    • Role of ATP in influenza virus budding
    • Hui, E.K.; Nayak, D.P. Role of ATP in influenza virus budding. Virology 2001, 290, 329-341.
    • (2001) Virology , vol.290 , pp. 329-341
    • Hui, E.K.1    Nayak, D.P.2
  • 120
    • 0036937194 scopus 로고    scopus 로고
    • Role of G protein and protein kinase signalling in influenza virus budding in MDCK cells
    • Hui, E.K.; Nayak, D.P. Role of G protein and protein kinase signalling in influenza virus budding in MDCK cells. J. Gen. Virol. 2002, 83, 3055-3066.
    • (2002) J. Gen. Virol. , vol.83 , pp. 3055-3066
    • Hui, E.K.1    Nayak, D.P.2
  • 121
    • 0027946853 scopus 로고
    • Abortive replication of influenza virus A/WSN/33 in HeLa229 cells: Defective viral entry and budding processes
    • Gujuluva, C.N.; Kundu, A.; Murti, K.G.; Nayak, D.P. Abortive replication of influenza virus A/WSN/33 in HeLa229 cells: Defective viral entry and budding processes. Virology 1994, 204, 491-505.
    • (1994) Virology , vol.204 , pp. 491-505
    • Gujuluva, C.N.1    Kundu, A.2    Murti, K.G.3    Nayak, D.P.4
  • 122
    • 84859924183 scopus 로고    scopus 로고
    • Interaction of influenza A virus matrix protein with RACK1 is required for virus release
    • Demirov, D.; Gabriel, G.; Schneider, C.; Hohenberg, H.; Ludwig, S. Interaction of influenza A virus matrix protein with RACK1 is required for virus release. Cell. Microbiol. 2012, 14, 774-789.
    • (2012) Cell. Microbiol. , vol.14 , pp. 774-789
    • Demirov, D.1    Gabriel, G.2    Schneider, C.3    Hohenberg, H.4    Ludwig, S.5
  • 123
    • 77956637693 scopus 로고    scopus 로고
    • Influenza virus M2 protein mediates ESCRT-independent membrane scission
    • Rossman, J.S.; Jing, X.; Leser, G.P.; Lamb, R.A. Influenza virus M2 protein mediates ESCRT-independent membrane scission. Cell 2010, 142, 902-913.
    • (2010) Cell , vol.142 , pp. 902-913
    • Rossman, J.S.1    Jing, X.2    Leser, G.P.3    Lamb, R.A.4
  • 124
    • 0000443647 scopus 로고
    • Filamentous forms associated with newly isolated influenza virus
    • Chu, C.M.; Dawson, I.M.; Elford, W.J. Filamentous forms associated with newly isolated influenza virus. Lancet 1949, 1, 602.
    • (1949) Lancet , vol.1 , pp. 602
    • Chu, C.M.1    Dawson, I.M.2    Elford, W.J.3
  • 125
    • 0000128765 scopus 로고
    • Genetic studies of influenza viruses. I. Viral morphology and growth capacity as exchangeable genetic traits. Rapid in ovo adaptation of early passage Asian strain isolates by combination with PR8
    • Kilbourne, E.D.; Murphy, J.S. Genetic studies of influenza viruses. I. Viral morphology and growth capacity as exchangeable genetic traits. Rapid in ovo adaptation of early passage Asian strain isolates by combination with PR8. J. Exp. Med. 1960, 111, 387-406.
    • (1960) J. Exp. Med. , vol.111 , pp. 387-406
    • Kilbourne, E.D.1    Murphy, J.S.2
  • 128
    • 77951437276 scopus 로고    scopus 로고
    • Influenza virus m2 ion channel protein is necessary for filamentous virion formation
    • Rossman, J.S.; Jing, X.; Leser, G.P.; Balannik, V.; Pinto, L.H.; Lamb, R.A. Influenza virus m2 ion channel protein is necessary for filamentous virion formation. J. Virol. 2010, 84, 5078-5088.
    • (2010) J. Virol. , vol.84 , pp. 5078-5088
    • Rossman, J.S.1    Jing, X.2    Leser, G.P.3    Balannik, V.4    Pinto, L.H.5    Lamb, R.A.6
  • 129
    • 84879526764 scopus 로고    scopus 로고
    • Cryotomography of budding influenza A virus reveals filaments with diverse morphologies that mostly do not bear a genome at their distal end
    • Vijayakrishnan, S.; Loney, C.; Jackson, D.; Suphamungmee, W.; Rixon, F.J.; Bhella, D. Cryotomography of budding influenza A virus reveals filaments with diverse morphologies that mostly do not bear a genome at their distal end. PLoS Pathog. 2013, 9, e1003413.
    • (2013) PLoS Pathog. , vol.9
    • Vijayakrishnan, S.1    Loney, C.2    Jackson, D.3    Suphamungmee, W.4    Rixon, F.J.5    Bhella, D.6
  • 131
    • 0036401535 scopus 로고    scopus 로고
    • A functional link between the actin cytoskeleton and lipid rafts during budding of filamentous influenza virions
    • Simpson-Holley, M.; Ellis, D.; Fisher, D.; Elton, D.; McCauley, J.; Digard, P. A functional link between the actin cytoskeleton and lipid rafts during budding of filamentous influenza virions. Virology 2002, 301, 212-225.
    • (2002) Virology , vol.301 , pp. 212-225
    • Simpson-Holley, M.1    Ellis, D.2    Fisher, D.3    Elton, D.4    McCauley, J.5    Digard, P.6
  • 132
    • 0000283734 scopus 로고
    • Studies of two kinds of virus particles which comprise influenza A2 virus strains. III. Morphological characteristics: Independence to morphological and functional traits
    • Choppin, P.W.; Murphy, J.S.; Tamm, I. Studies of two kinds of virus particles which comprise influenza A2 virus strains. III. Morphological characteristics: independence to morphological and functional traits. J. Exp. Med. 1960, 112, 945-952.
    • (1960) J. Exp. Med. , vol.112 , pp. 945-952
    • Choppin, P.W.1    Murphy, J.S.2    Tamm, I.3
  • 133
    • 0342514345 scopus 로고
    • Biological and physical properties of the Ryan strain of filamentous influenza virus
    • Ada, G.L.; Perry, B.T.; Abbot, A. Biological and physical properties of the Ryan strain of filamentous influenza virus. J. Gen. Microbiol. 1958, 19, 23-39.
    • (1958) J. Gen. Microbiol. , vol.19 , pp. 23-39
    • Ada, G.L.1    Perry, B.T.2    Abbot, A.3
  • 134
    • 0012395009 scopus 로고
    • Studies on filamentary forms of influenza virus with special reference to the use of dark-ground-microscopy
    • Burnet, F.M.; Lind, P.E. Studies on filamentary forms of influenza virus with special reference to the use of dark-ground-microscopy. Archiv. Fur Die Gesamte Virusforsch. 1957, 7, 413-428.
    • (1957) Archiv. Fur Die Gesamte Virusforsch. , vol.7 , pp. 413-428
    • Burnet, F.M.1    Lind, P.E.2
  • 135
    • 33645340865 scopus 로고
    • Morphological characteristics of type A2 ("A-Asia") influenza virus isolated in Rumania
    • Portocala, R.; Dumitrescu, S.; Rothschild, L.; Ionescu, N.I. Morphological characteristics of type A2 ("A-Asia") influenza virus isolated in Rumania. Acta Virol. 1959, 3, 113-114.
    • (1959) Acta Virol. , vol.3 , pp. 113-114
    • Portocala, R.1    Dumitrescu, S.2    Rothschild, L.3    Ionescu, N.I.4
  • 137
    • 0017286522 scopus 로고
    • Influenza virus recombination. I. Matrix protein markers and segregation during mixed infections
    • Laver, W.G.; Downie, J.C. Influenza virus recombination. I. Matrix protein markers and segregation during mixed infections. Virology 1976, 70, 105-117.
    • (1976) Virology , vol.70 , pp. 105-117
    • Laver, W.G.1    Downie, J.C.2
  • 138
    • 0018412958 scopus 로고
    • Nonrandom association of parental genes in influenza A virus recombinants
    • Lubeck, M.D.; Palese, P.; Schulman, J.L. Nonrandom association of parental genes in influenza A virus recombinants. Virology 1979, 95, 269-274.
    • (1979) Virology , vol.95 , pp. 269-274
    • Lubeck, M.D.1    Palese, P.2    Schulman, J.L.3
  • 139
    • 0017697770 scopus 로고
    • Three-Factor cross of influenza virus
    • Nakajima, K.; Sugiura, A. Three-Factor cross of influenza virus. Virology 1977, 81, 486-489.
    • (1977) Virology , vol.81 , pp. 486-489
    • Nakajima, K.1    Sugiura, A.2
  • 140
    • 44449086287 scopus 로고    scopus 로고
    • Deviation from the random distribution pattern of influenza A virus gene segments in reassortants produced under non-selective conditions
    • Varich, N.L.; Gitelman, A.K.; Shilov, A.A.; Smirnov, Y.A.; Kaverin, N.V. Deviation from the random distribution pattern of influenza A virus gene segments in reassortants produced under non-selective conditions. Arch. Virol. 2008, 153, 1149-1154.
    • (2008) Arch. Virol. , vol.153 , pp. 1149-1154
    • Varich, N.L.1    Gitelman, A.K.2    Shilov, A.A.3    Smirnov, Y.A.4    Kaverin, N.V.5
  • 141
    • 84861908388 scopus 로고    scopus 로고
    • One influenza virus particle packages eight unique viral RNAs as shown by FISH analysis
    • Chou, Y.Y.; Vafabakhsh, R.; Doganay, S.; Gao, Q.; Ha, T.; Palese, P. One influenza virus particle packages eight unique viral RNAs as shown by FISH analysis. Proc. Natl. Acad. Sci. USA 2012, 109, 9101-9106.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 9101-9106
    • Chou, Y.Y.1    Vafabakhsh, R.2    Doganay, S.3    Gao, Q.4    Ha, T.5    Palese, P.6
  • 142
    • 45749112583 scopus 로고    scopus 로고
    • A seven-segmented influenza A virus expressing the influenza C virus glycoprotein HEF
    • Gao, Q.; Brydon, E.W.; Palese, P. A seven-segmented influenza A virus expressing the influenza C virus glycoprotein HEF. J. Virol. 2008, 82, 6419-6426.
    • (2008) J. Virol. , vol.82 , pp. 6419-6426
    • Gao, Q.1    Brydon, E.W.2    Palese, P.3
  • 143
  • 144
    • 84869059389 scopus 로고    scopus 로고
    • Filamentous influenza virus enters cells via macropinocytosis
    • Rossman, J.S.; Leser, G.P.; Lamb, R.A. Filamentous influenza virus enters cells via macropinocytosis. J. Virol. 2012, 86, 10950-10960.
    • (2012) J. Virol. , vol.86 , pp. 10950-10960
    • Rossman, J.S.1    Leser, G.P.2    Lamb, R.A.3
  • 145
    • 23844500631 scopus 로고    scopus 로고
    • Characterization of the host cell entry of filamentous influenza virus
    • Sieczkarski, S.B.; Whittaker, G.R. Characterization of the host cell entry of filamentous influenza virus. Arch. Virol. 2005, 150, 1783-1796.
    • (2005) Arch. Virol. , vol.150 , pp. 1783-1796
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 147
    • 50149096579 scopus 로고    scopus 로고
    • Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus
    • Chen, C.; Zhuang, X. Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus. Proc. Natl. Acad. Sci. USA 2008, 105, 11790-11795.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11790-11795
    • Chen, C.1    Zhuang, X.2
  • 148
    • 33644764063 scopus 로고    scopus 로고
    • Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes
    • Lakadamyali, M.; Rust, M.J.; Zhuang, X. Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes. Cell 2006, 124, 997-1009.
    • (2006) Cell , vol.124 , pp. 997-1009
    • Lakadamyali, M.1    Rust, M.J.2    Zhuang, X.3
  • 149
    • 78149333191 scopus 로고    scopus 로고
    • The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells
    • Eierhoff, T.; Hrincius, E.R.; Rescher, U.; Ludwig, S.; Ehrhardt, C. The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells. PLoS Pathog. 2010, 6, e1001099.
    • (2010) PLoS Pathog. , vol.6
    • Eierhoff, T.1    Hrincius, E.R.2    Rescher, U.3    Ludwig, S.4    Ehrhardt, C.5
  • 150
    • 78650533541 scopus 로고    scopus 로고
    • Differential infectious entry of human influenza A/NWS/33 virus (H1N1) in mammalian kidney cells
    • De Conto, F.; Covan, S.; Arcangeletti, M.C.; Orlandini, G.; Gatti, R.; Dettori, G.; Chezzi, C. Differential infectious entry of human influenza A/NWS/33 virus (H1N1) in mammalian kidney cells. Virus Res. 2011, 155, 221-230.
    • (2011) Virus Res. , vol.155 , pp. 221-230
    • De Conto, F.1    Covan, S.2    Arcangeletti, M.C.3    Orlandini, G.4    Gatti, R.5    Dettori, G.6    Chezzi, C.7
  • 151
    • 0034142287 scopus 로고    scopus 로고
    • Early stages of influenza virus entry into Mv-1 lung cells: Involvement of dynamin
    • Roy, A.M.; Parker, J.S.; Parrish, C.R.; Whittaker, G.R. Early stages of influenza virus entry into Mv-1 lung cells: Involvement of dynamin. Virology 2000, 267, 17-28.
    • (2000) Virology , vol.267 , pp. 17-28
    • Roy, A.M.1    Parker, J.S.2    Parrish, C.R.3    Whittaker, G.R.4
  • 152
    • 0021270365 scopus 로고
    • Uncoating of influenza virus in endosomes
    • Yoshimura, A.; Ohnishi, S. Uncoating of influenza virus in endosomes. J. Virol. 1984, 51, 497-504.
    • (1984) J. Virol. , vol.51 , pp. 497-504
    • Yoshimura, A.1    Ohnishi, S.2
  • 153
    • 33646932780 scopus 로고    scopus 로고
    • The M2 proton channels of influenza A and B viruses
    • Pinto, L.H.; Lamb, R.A. The M2 proton channels of influenza A and B viruses. J. Biol. Chem. 2006, 281, 8997-9000.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8997-9000
    • Pinto, L.H.1    Lamb, R.A.2
  • 154
    • 0029861558 scopus 로고    scopus 로고
    • Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins
    • Bui, M.; Whittaker, G.; Helenius, A. Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins. J. Virol. 1996, 70, 8391-8401.
    • (1996) J. Virol. , vol.70 , pp. 8391-8401
    • Bui, M.1    Whittaker, G.2    Helenius, A.3
  • 155
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J.J.; Wiley, D.C. Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin. Annu. Rev. Biochem. 2000, 69, 531-569.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 156
    • 0026070664 scopus 로고
    • Transport of incoming influenza virus nucleocapsids into the nucleus
    • Martin, K.; Helenius, A. Transport of incoming influenza virus nucleocapsids into the nucleus. J. Virol. 1991, 65, 232-244.
    • (1991) J. Virol. , vol.65 , pp. 232-244
    • Martin, K.1    Helenius, A.2
  • 157
    • 0018742964 scopus 로고
    • Inhibition of influenza virus uncoating by rimantadine hydrochloride
    • Koff, W.C.; Knight, V. Inhibition of influenza virus uncoating by rimantadine hydrochloride. J. Virol. 1979, 31, 261-263.
    • (1979) J. Virol. , vol.31 , pp. 261-263
    • Koff, W.C.1    Knight, V.2
  • 158
    • 77953231673 scopus 로고    scopus 로고
    • Influenza virus infection in multinucleated skeletal myofibers
    • Nevalainen, M.; Nissinen, M.; Kaakinen, M.; Metsikko, K. Influenza virus infection in multinucleated skeletal myofibers. Exp. Cell Res. 2010, 316, 1784-1794.
    • (2010) Exp. Cell Res. , vol.316 , pp. 1784-1794
    • Nevalainen, M.1    Nissinen, M.2    Kaakinen, M.3    Metsikko, K.4
  • 159
    • 0026006258 scopus 로고
    • Nuclear transport of influenza virus ribonucleoproteins: The viral matrix protein (M1) promotes export and inhibits import
    • Martin, K.; Helenius, A. Nuclear transport of influenza virus ribonucleoproteins: The viral matrix protein (M1) promotes export and inhibits import. Cell 1991, 67, 117-130.
    • (1991) Cell , vol.67 , pp. 117-130
    • Martin, K.1    Helenius, A.2
  • 160
    • 0029998889 scopus 로고    scopus 로고
    • Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryons
    • Whittaker, G.; Bui, M.; Helenius, A. Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryons. J. Virol. 1996, 70, 2743-2756.
    • (1996) J. Virol. , vol.70 , pp. 2743-2756
    • Whittaker, G.1    Bui, M.2    Helenius, A.3
  • 161
    • 67649989017 scopus 로고    scopus 로고
    • The directionality of the nuclear transport of the influenza A genome is driven by selective exposure of nuclear localization sequences on nucleoprotein
    • Wu, W.W.; Pante, N. The directionality of the nuclear transport of the influenza A genome is driven by selective exposure of nuclear localization sequences on nucleoprotein. Virol. J. 2009, 6, 68.
    • (2009) Virol. J. , vol.6 , pp. 68
    • Wu, W.W.1    Pante, N.2
  • 162
    • 0029130751 scopus 로고
    • Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import
    • O'Neill, R.E.; 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. J. Biol. Chem. 1995, 270, 22701-22704.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22701-22704
    • O'Neill, R.E.1    Jaskunas, R.2    Blobel, G.3    Palese, P.4    Moroianu, J.5
  • 163
    • 34250363900 scopus 로고    scopus 로고
    • Nuclear import of influenza A viral ribonucleoprotein complexes is mediated by two nuclear localization sequences on viral nucleoprotein
    • Wu, W.W.; Sun, Y.H.; Pante, N. Nuclear import of influenza A viral ribonucleoprotein complexes is mediated by two nuclear localization sequences on viral nucleoprotein. Virol. J. 2007, 4, 49.
    • (2007) Virol. J. , vol.4 , pp. 49
    • Wu, W.W.1    Sun, Y.H.2    Pante, N.3
  • 164
    • 35748958705 scopus 로고    scopus 로고
    • Ultrastructural analysis of the nuclear localization sequences on influenza A ribonucleoprotein complexes
    • Wu, W.W.; Weaver, L.L.; Pante, N. Ultrastructural analysis of the nuclear localization sequences on influenza A ribonucleoprotein complexes. J. Mol. Biol. 2007, 374, 910-916.
    • (2007) J. Mol. Biol. , vol.374 , pp. 910-916
    • Wu, W.W.1    Weaver, L.L.2    Pante, N.3
  • 165
    • 14544270958 scopus 로고    scopus 로고
    • An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein
    • Cros, J.F.; Garcia-Sastre, A.; Palese, P. An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein. Traffic 2005, 6, 205-213.
    • (2005) Traffic , vol.6 , pp. 205-213
    • Cros, J.F.1    Garcia-Sastre, A.2    Palese, P.3
  • 167
    • 84857468667 scopus 로고    scopus 로고
    • Human-like PB2 627K influenza virus polymerase activity is regulated by importin-alpha1 and-alpha7
    • Hudjetz, B.; Gabriel, G. Human-like PB2 627K influenza virus polymerase activity is regulated by importin-alpha1 and-alpha7. PLoS Pathog. 2012, 8, e1002488.
    • (2012) PLoS Pathog. , vol.8
    • Hudjetz, B.1    Gabriel, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.