메뉴 건너뛰기




Volumn 11, Issue 7, 2015, Pages

A Novel Antiviral Target Structure Involved in the RNA Binding, Dimerization, and Nuclear Export Functions of the Influenza A Virus Nucleoprotein

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; OSELTAMIVIR; RIBONUCLEOPROTEIN; RK424; UNCLASSIFIED DRUG; VIRUS NUCLEOPROTEIN; CORE PROTEIN; NP PROTEIN, INFLUENZA A VIRUS; RNA BINDING PROTEIN; VIRUS RNA;

EID: 84938795420     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1005062     Document Type: Article
Times cited : (39)

References (55)
  • 1
    • 77956499048 scopus 로고    scopus 로고
    • Influenza virus evolution, host adaptation, and pandemic formation
    • Taubenberger JK, Kash JC, (2010) Influenza virus evolution, host adaptation, and pandemic formation. Cell Host Microbe 7: 440–451. doi: 10.1016/j.chom.2010.05.009 20542248
    • (2010) Cell Host Microbe , vol.7 , pp. 440-451
    • Taubenberger, J.K.1    Kash, J.C.2
  • 2
    • 0022157043 scopus 로고
    • The molecular basis of the specific anti-influenza action of Amantadine
    • Hay AJ, Wolstenholme AJ, Skehel JJ, Smith MH, (1985) The molecular basis of the specific anti-influenza action of Amantadine. EMBO J 4: 3021–3024. 4065098
    • (1985) EMBO J , vol.4 , pp. 3021-3024
    • Hay, A.J.1    Wolstenholme, A.J.2    Skehel, J.J.3    Smith, M.H.4
  • 3
    • 39649114107 scopus 로고    scopus 로고
    • Medical management of influenza infection
    • Moscona A, (2008) Medical management of influenza infection. Annu Rev Med 59: 397–413. 17939760
    • (2008) Annu Rev Med , vol.59 , pp. 397-413
    • Moscona, A.1
  • 4
    • 33644536465 scopus 로고    scopus 로고
    • Adamantane resistance among influenza A viruses isolated early during the 2005–2006 influenza season in the United States
    • Bright RA, Shay DK, Shu B, Cox NJ, Klimov AI, (2006) Adamantane resistance among influenza A viruses isolated early during the 2005–2006 influenza season in the United States. JAMA 295: 891–894. 16456087
    • (2006) JAMA , vol.295 , pp. 891-894
    • Bright, R.A.1    Shay, D.K.2    Shu, B.3    Cox, N.J.4    Klimov, A.I.5
  • 5
    • 67349139846 scopus 로고    scopus 로고
    • Emergence and spread of oseltamivir-resistant A(H1N1) influenza viruses in Oceania, South East Asia and South Africa
    • Hurt AC, Ernest J, Deng YM, Iannello P, Besselaar TG, et al. (2009) Emergence and spread of oseltamivir-resistant A(H1N1) influenza viruses in Oceania, South East Asia and South Africa. Antiviral Res 83: 90–93. doi: 10.1016/j.antiviral.2009.03.003 19501261
    • (2009) Antiviral Res , vol.83 , pp. 90-93
    • Hurt, A.C.1    Ernest, J.2    Deng, Y.M.3    Iannello, P.4    Besselaar, T.G.5
  • 6
    • 62149120632 scopus 로고    scopus 로고
    • Infections with oseltamivir resistant influenza A(H1N1) virus in the United States
    • Dharan NJ, Gubareva LV, Meyer JJ, Okomo-Adhiambo M, McClinton RC, et al. (2009) Infections with oseltamivir resistant influenza A(H1N1) virus in the United States. JAMA 301: 1034–1041. doi: 10.1001/jama.2009.294 19255110
    • (2009) JAMA , vol.301 , pp. 1034-1041
    • Dharan, N.J.1    Gubareva, L.V.2    Meyer, J.J.3    Okomo-Adhiambo, M.4    McClinton, R.C.5
  • 8
    • 33747797031 scopus 로고    scopus 로고
    • Treating viral hepatitis C: efficacy, side effects, and complications
    • Manns MP, Wedemeyer H, Cornberg M, (2006) Treating viral hepatitis C: efficacy, side effects, and complications. Gut 55: 1350–1359. 16905701
    • (2006) Gut , vol.55 , pp. 1350-1359
    • Manns, M.P.1    Wedemeyer, H.2    Cornberg, M.3
  • 9
    • 0031003878 scopus 로고    scopus 로고
    • Roles of the influenza virus polymerase and nucleoprotein in forming a functional RNP structure
    • Klumpp K, Ruigrok RW, Baudin F, (1997) Roles of the influenza virus polymerase and nucleoprotein in forming a functional RNP structure. EMBO J 16: 1248–1257. 9135141
    • (1997) EMBO J , vol.16 , pp. 1248-1257
    • Klumpp, K.1    Ruigrok, R.W.2    Baudin, F.3
  • 10
    • 84871460710 scopus 로고    scopus 로고
    • The structure of native influenza virion ribonucleoproteins
    • Arranz R, Coloma R, Chichon FJ, Conesa JJ, Carrascosa JL, et al. (2012) The structure of native influenza virion ribonucleoproteins. Science 338: 1634–1637. doi: 10.1126/science.1228172 23180776
    • (2012) Science , vol.338 , pp. 1634-1637
    • Arranz, R.1    Coloma, R.2    Chichon, F.J.3    Conesa, J.J.4    Carrascosa, J.L.5
  • 11
    • 33845890539 scopus 로고    scopus 로고
    • The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA
    • Ye Q, Krug RM, Tao YJ, (2006) The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA. Nature 444: 1078–1082. 17151603
    • (2006) Nature , vol.444 , pp. 1078-1082
    • Ye, Q.1    Krug, R.M.2    Tao, Y.J.3
  • 12
    • 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 TS, Mata DA, Kuo RL, Smith B, et al. (2012) Biochemical and structural evidence in support of a coherent model for the formation of the double-helical influenza A virus ribonucleoprotein. MBio 4: e00467–00412. doi: 10.1128/mBio.00467-12 23269829
    • (2012) MBio , vol.4
    • Ye, Q.1    Guu, T.S.2    Mata, D.A.3    Kuo, R.L.4    Smith, B.5
  • 13
    • 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, (1993) Molecular assembly of influenza virus: association of the NS2 protein with virion matrix. Virology 196: 249–255. 8356796
    • (1993) Virology , vol.196 , pp. 249-255
    • Yasuda, J.1    Nakada, S.2    Kato, A.3    Toyoda, T.4    Ishihama, A.5
  • 14
    • 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 WP, Petosa C, Petit I, Müller CW, et al. (2003) Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2). EMBO J 22: 4646–4655. 12970177
    • (2003) EMBO J , vol.22 , pp. 4646-4655
    • Akarsu, H.1    Burmeister, W.P.2    Petosa, C.3    Petit, I.4    Müller, C.W.5
  • 15
    • 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, (2011) Crucial role of the influenza virus NS2 (NEP) C-terminal domain in M1 binding and nuclear export of vRNP. FEBS Lett 585: 41–46. doi: 10.1016/j.febslet.2010.11.017 21081124
    • (2011) FEBS Lett , vol.585 , pp. 41-46
    • Shimizu, T.1    Takizawa, N.2    Watanabe, K.3    Nagata, K.4    Kobayashi, N.5
  • 16
    • 0032865668 scopus 로고    scopus 로고
    • Association of influenza virus matrix protein with ribonucleoproteins
    • Ye Z, Liu T, Offringa DP, McInnis J, Levandowski RA, (1999) Association of influenza virus matrix protein with ribonucleoproteins. J Virol 73: 7467–7473. 10438836
    • (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
  • 17
    • 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 SL, Medcalf E, Fisher D, Mullin AE, Elton D, et al. (2007) Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions. J Gen Virol 88: 2280–2290. 17622633
    • (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
  • 18
    • 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, et al. (2012) Identification and characterization of three novel nuclear export signals in the influenza A virus nucleoprotein. J Virol 86: 4970–4980. doi: 10.1128/JVI.06159-11 22345439
    • (2012) J Virol , vol.86 , pp. 4970-4980
    • Yu, M.1    Liu, X.2    Cao, S.3    Zhao, Z.4    Zhang, K.5
  • 19
    • 84905964758 scopus 로고    scopus 로고
    • Comparative Analysis of Seven Viral Nuclear Export Signals (NESs) Reveals the Crucial Role of Nuclear Export Mediated by the Third NES Consensus Sequence of Nucleoprotein (NP) in Influenza A Virus Replication
    • Chutiwitoonchai N, Kakisaka M, Yamada K, Aida Y, (2014) Comparative Analysis of Seven Viral Nuclear Export Signals (NESs) Reveals the Crucial Role of Nuclear Export Mediated by the Third NES Consensus Sequence of Nucleoprotein (NP) in Influenza A Virus Replication. PLoS One 9: e105081. doi: 10.1371/journal.pone.0105081 25119991
    • (2014) PLoS One , vol.9 , pp. e105081
    • Chutiwitoonchai, N.1    Kakisaka, M.2    Yamada, K.3    Aida, Y.4
  • 20
    • 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, et al. (2001) Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway. J Virol 75: 408–419. 11119609
    • (2001) J Virol , vol.75 , pp. 408-419
    • Elton, D.1    Simpson-Holley, M.2    Archer, K.3    Medcalf, L.4    Hallam, R.5
  • 22
    • 77950516005 scopus 로고    scopus 로고
    • Discovery of novel antiviral agents directed against the influenza A virus nucleoprotein using photo-cross-linked chemical arrays
    • Hagiwara K, Kondoh Y, Ueda A, Yamada K, Goto H, et al. (2010) Discovery of novel antiviral agents directed against the influenza A virus nucleoprotein using photo-cross-linked chemical arrays. Biochem Biophys Res Commun 394: 721–727. doi: 10.1016/j.bbrc.2010.03.058 20230782
    • (2010) Biochem Biophys Res Commun , vol.394 , pp. 721-727
    • Hagiwara, K.1    Kondoh, Y.2    Ueda, A.3    Yamada, K.4    Goto, H.5
  • 23
    • 80053650056 scopus 로고    scopus 로고
    • E339…R416 salt bridge of nucleoprotein as a feasible target for influenza virus inhibitors
    • Shen YF, Chen YH, Chu SY, Lin MI, Hsu HT, et al. (2011) E339…R416 salt bridge of nucleoprotein as a feasible target for influenza virus inhibitors. Proc Natl Acad Sci U S A 108: 16515–16520. doi: 10.1073/pnas.1113107108 21930946
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 16515-16520
    • Shen, Y.F.1    Chen, Y.H.2    Chu, S.Y.3    Lin, M.I.4    Hsu, H.T.5
  • 24
    • 77953259427 scopus 로고    scopus 로고
    • Identification of influenza A nucleoprotein as an antiviral target
    • Kao RY, Yang D, Lau LS, Tsui WH, Hu L, et al. (2010) Identification of influenza A nucleoprotein as an antiviral target. Nat Biotechnol 28: 600–605. doi: 10.1038/nbt.1638 20512121
    • (2010) Nat Biotechnol , vol.28 , pp. 600-605
    • Kao, R.Y.1    Yang, D.2    Lau, L.S.3    Tsui, W.H.4    Hu, L.5
  • 25
    • 80053089237 scopus 로고    scopus 로고
    • Inhibition of influenza virus replication via small molecules that induce the formation of higher-order nucleoprotein oligomers
    • Gerritz SW, Cianci C, Kim S, Pearce BC, Deminie C, et al. (2011) Inhibition of influenza virus replication via small molecules that induce the formation of higher-order nucleoprotein oligomers. Proc Natl Acad Sci U S A 108: 15366–15371. doi: 10.1073/pnas.1107906108 21896751
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 15366-15371
    • Gerritz, S.W.1    Cianci, C.2    Kim, S.3    Pearce, B.C.4    Deminie, C.5
  • 26
    • 84904733675 scopus 로고    scopus 로고
    • Identification of a novel multiple kinase inhibitor with potent antiviral activity against influenza virus by reducing viral polymerase activity
    • Sasaki Y, Kakisaka M, Chutiwitoonchai N, Tajima S, Hikono H, et al. (2014) Identification of a novel multiple kinase inhibitor with potent antiviral activity against influenza virus by reducing viral polymerase activity. Biochem Biophys Res Commun 450: 49–54. doi: 10.1016/j.bbrc.2014.05.058 24858693
    • (2014) Biochem Biophys Res Commun , vol.450 , pp. 49-54
    • Sasaki, Y.1    Kakisaka, M.2    Chutiwitoonchai, N.3    Tajima, S.4    Hikono, H.5
  • 27
    • 0027275566 scopus 로고
    • Physiological parameters in laboratory animals and humans
    • Davies B, Morris T, (1993) Physiological parameters in laboratory animals and humans. Pharm Res 10: 1093–1095. 8378254
    • (1993) Pharm Res , vol.10 , pp. 1093-1095
    • Davies, B.1    Morris, T.2
  • 28
    • 77951214216 scopus 로고    scopus 로고
    • Detection of E119V and E119I mutations in influenza A (H3N2) viruses isolated from an immunocompromised patient: challenges in diagnosis of oseltamivir resistance
    • Okomo-Adhiambo M, Demmler-Harrison GJ, Deyde VM, Sheu TG, Xu X, et al. (2010) Detection of E119V and E119I mutations in influenza A (H3N2) viruses isolated from an immunocompromised patient: challenges in diagnosis of oseltamivir resistance. Antimicrob Agents Chemother 54: 1834–1841. doi: 10.1128/AAC.01608-09 20194700
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 1834-1841
    • Okomo-Adhiambo, M.1    Demmler-Harrison, G.J.2    Deyde, V.M.3    Sheu, T.G.4    Xu, X.5
  • 29
    • 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 YY, Heaton NS, Gao Q, Palese P, Singer RH, et al. (2013) Colocalization of different influenza viral RNA segments in the cytoplasm before viral budding as shown by single-molecule sensitivity FISH analysis. PLoS Pathog 9: e1003358. doi: 10.1371/journal.ppat.1003358 23671419
    • (2013) PLoS Pathog , vol.9 , pp. e1003358
    • Chou, Y.Y.1    Heaton, N.S.2    Gao, Q.3    Palese, P.4    Singer, R.H.5
  • 30
    • 80053436121 scopus 로고    scopus 로고
    • Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting
    • Chase GP, Rameix-Welti MA, Zvirbliene A, Zvirblis G, Gotz V, et al. (2011) Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting. PLoS Pathog 7: e1002187. doi: 10.1371/journal.ppat.1002187 21909257
    • (2011) PLoS Pathog , vol.7 , pp. e1002187
    • Chase, G.P.1    Rameix-Welti, M.A.2    Zvirbliene, A.3    Zvirblis, G.4    Gotz, V.5
  • 31
    • 70349932423 scopus 로고    scopus 로고
    • AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility
    • Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK, et al. (2009) AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. J Comput Chem 30: 2785–2791. doi: 10.1002/jcc.21256 19399780
    • (2009) J Comput Chem , vol.30 , pp. 2785-2791
    • Morris, G.M.1    Huey, R.2    Lindstrom, W.3    Sanner, M.F.4    Belew, R.K.5
  • 32
    • 43949127099 scopus 로고    scopus 로고
    • Application of bioinformatics-coupled experimental analysis reveals a new transport-competent nuclear localization signal in the nucleoprotein of influenza A virus strain
    • Ketha KM, Atreya CD, Kanoh N, Honda K, Simizu S, Muroi M, Osada H (2005) Photo-cross-linked small-molecule affinity matrix for facilitating forward and reverse chemical genetics. 17. (2008) Application of bioinformatics-coupled experimental analysis reveals a new transport-competent nuclear localization signal in the nucleoprotein of influenza A virus strain. BMC Cell Biol 9: 22. doi: 10.1186/1471-2121-9-22 18442378
    • (2008) BMC Cell Biol , vol.9 , pp. 22
    • Ketha, K.M.1    Atreya, C.D.2
  • 33
    • 84857037520 scopus 로고    scopus 로고
    • Oligomerization paths of the nucleoprotein of influenza A virus
    • Tarus B, Bakowiez O, Chenavas S, Duchemin L, Estrozi LF, et al. (2012) Oligomerization paths of the nucleoprotein of influenza A virus. Biochimie 94: 776–785. doi: 10.1016/j.biochi.2011.11.009 22155087
    • (2012) Biochimie , vol.94 , pp. 776-785
    • Tarus, B.1    Bakowiez, O.2    Chenavas, S.3    Duchemin, L.4    Estrozi, L.F.5
  • 34
    • 54049146687 scopus 로고    scopus 로고
    • Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine design
    • Ng AK, Zhang H, Tan K, Li Z, Liu JH, et al. (2008) Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine design. FASEB J 22: 3638–3647. doi: 10.1096/fj.08-112110 18614582
    • (2008) FASEB J , vol.22 , pp. 3638-3647
    • Ng, A.K.1    Zhang, H.2    Tan, K.3    Li, Z.4    Liu, J.H.5
  • 35
    • 0015414910 scopus 로고
    • Structure of the ribonucleoprotein of influenza virus
    • Compans RW, Content J, Duesberg PH, (1972) Structure of the ribonucleoprotein of influenza virus. J Virol 10: 795–800. 4117350
    • (1972) J Virol , vol.10 , pp. 795-800
    • Compans, R.W.1    Content, J.2    Duesberg, P.H.3
  • 36
    • 17644443084 scopus 로고    scopus 로고
    • Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification
    • Ortega J, Martin-Benito J, Zurcher T, Valpuesta JM, Carrascosa JL, et al. (2000) Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification. J Virol 74: 156–163. 10590102
    • (2000) J Virol , vol.74 , pp. 156-163
    • Ortega, J.1    Martin-Benito, J.2    Zurcher, T.3    Valpuesta, J.M.4    Carrascosa, J.L.5
  • 37
    • 77953794395 scopus 로고    scopus 로고
    • Functional analysis of the influenza virus H5N1 nucleoprotein tail loop reveals amino acids that are crucial for oligomerization and ribonucleoprotein activities
    • Chan WH, Ng AK, Robb NC, Lam MK, Chan PK, et al. (2010) Functional analysis of the influenza virus H5N1 nucleoprotein tail loop reveals amino acids that are crucial for oligomerization and ribonucleoprotein activities. J Virol 84: 7337–7345. doi: 10.1128/JVI.02474-09 20463064
    • (2010) J Virol , vol.84 , pp. 7337-7345
    • Chan, W.H.1    Ng, A.K.2    Robb, N.C.3    Lam, M.K.4    Chan, P.K.5
  • 38
    • 84862181488 scopus 로고    scopus 로고
    • PoSSuM: a database of similar protein-ligand binding and putative pockets
    • Ito J, Tabei Y, Shimizu K, Tsuda K, Tomii K, (2012) PoSSuM: a database of similar protein-ligand binding and putative pockets. Nucleic Acids Res 40: D541–548. doi: 10.1093/nar/gkr1130 22135290
    • (2012) Nucleic Acids Res , vol.40 , pp. D541-548
    • Ito, J.1    Tabei, Y.2    Shimizu, K.3    Tsuda, K.4    Tomii, K.5
  • 39
    • 84864485292 scopus 로고    scopus 로고
    • ProBiS-2012: web server and web services for detection of structurally similar binding sites in proteins
    • Konc J, Janezic D, (2012) ProBiS-2012: web server and web services for detection of structurally similar binding sites in proteins. Nucleic Acids Res 40: W214–221. doi: 10.1093/nar/gks435 22600737
    • (2012) Nucleic Acids Res , vol.40 , pp. W214-221
    • Konc, J.1    Janezic, D.2
  • 40
    • 67249130012 scopus 로고    scopus 로고
    • The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit
    • Dias A, Bouvier D, Crepin T, McCarthy AA, Hart DJ, et al. (2009) The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit. Nature 458: 914–918. doi: 10.1038/nature07745 19194459
    • (2009) Nature , vol.458 , pp. 914-918
    • Dias, A.1    Bouvier, D.2    Crepin, T.3    McCarthy, A.A.4    Hart, D.J.5
  • 41
    • 67249100913 scopus 로고    scopus 로고
    • Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site
    • Yuan P, Bartlam M, Lou Z, Chen S, Zhou J, et al. (2009) Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site. Nature 458: 909–913. doi: 10.1038/nature07720 19194458
    • (2009) Nature , vol.458 , pp. 909-913
    • Yuan, P.1    Bartlam, M.2    Lou, Z.3    Chen, S.4    Zhou, J.5
  • 42
    • 84866146827 scopus 로고    scopus 로고
    • Structural and biochemical basis for development of influenza virus inhibitors targeting the PA endonuclease
    • DuBois RM, Slavish PJ, Baughman BM, Yun MK, Bao J, et al. (2012) Structural and biochemical basis for development of influenza virus inhibitors targeting the PA endonuclease. PLoS Pathog 8: e1002830. doi: 10.1371/journal.ppat.1002830 22876176
    • (2012) PLoS Pathog , vol.8 , pp. e1002830
    • DuBois, R.M.1    Slavish, P.J.2    Baughman, B.M.3    Yun, M.K.4    Bao, J.5
  • 44
    • 66149125568 scopus 로고    scopus 로고
    • Mutational analysis of conserved amino acids in the influenza A virus nucleoprotein
    • Li Z, Watanabe T, Hatta M, Watanabe S, Nanbo A, et al. (2009) Mutational analysis of conserved amino acids in the influenza A virus nucleoprotein. J Virol 83: 4153–4162. doi: 10.1128/JVI.02642-08 19225007
    • (2009) J Virol , vol.83 , pp. 4153-4162
    • Li, Z.1    Watanabe, T.2    Hatta, M.3    Watanabe, S.4    Nanbo, A.5
  • 45
    • 84870795662 scopus 로고    scopus 로고
    • Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry
    • Hutchinson EC, Denham EM, Thomas B, Trudgian DC, Hester SS, et al. (2012) Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry. PLoS Pathog 8: e1002993. doi: 10.1371/journal.ppat.1002993 23144613
    • (2012) PLoS Pathog , vol.8 , pp. e1002993
    • Hutchinson, E.C.1    Denham, E.M.2    Thomas, B.3    Trudgian, D.C.4    Hester, S.S.5
  • 46
    • 84872854571 scopus 로고    scopus 로고
    • Nuclear export inhibition through covalent conjugation and hydrolysis of Leptomycin B by CRM1
    • Sun Q, Carrasco YP, Hu Y, Guo X, Mirzaei H, et al. (2013) Nuclear export inhibition through covalent conjugation and hydrolysis of Leptomycin B by CRM1. Proc Natl Acad Sci U S A 110: 1303–1308. doi: 10.1073/pnas.1217203110 23297231
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 1303-1308
    • Sun, Q.1    Carrasco, Y.P.2    Hu, Y.3    Guo, X.4    Mirzaei, H.5
  • 47
    • 0030246992 scopus 로고    scopus 로고
    • Intracellular oligomerization of influenza virus nucleoprotein
    • Prokudina-Kantorovich EN, Semenova NP, (1996) Intracellular oligomerization of influenza virus nucleoprotein. Virology 223: 51–56. 8806539
    • (1996) Virology , vol.223 , pp. 51-56
    • Prokudina-Kantorovich, E.N.1    Semenova, N.P.2
  • 48
    • 0033587599 scopus 로고    scopus 로고
    • Oligomerization of the influenza virus nucleoprotein: identification of positive and negative sequence elements
    • Elton D, Medcalf E, Bishop K, Digard P, (1999) Oligomerization of the influenza virus nucleoprotein: identification of positive and negative sequence elements. Virology 260: 190–200. 10405371
    • (1999) Virology , vol.260 , pp. 190-200
    • Elton, D.1    Medcalf, E.2    Bishop, K.3    Digard, P.4
  • 49
    • 84896717365 scopus 로고    scopus 로고
    • Identification of distant drug off-targets by direct superposition of binding pocket surfaces
    • Schumann M, Armen RS, (2013) Identification of distant drug off-targets by direct superposition of binding pocket surfaces. PLoS One 8: e83533. doi: 10.1371/journal.pone.0083533 24391782
    • (2013) PLoS One , vol.8 , pp. e83533
    • Schumann, M.1    Armen, R.S.2
  • 52
    • 84866879823 scopus 로고    scopus 로고
    • The influence of lipophilicity in drug discovery and design
    • Arnott JA, Planey SL, (2012) The influence of lipophilicity in drug discovery and design. Expert Opin Drug Discov 7: 863–875. 22992175
    • (2012) Expert Opin Drug Discov , vol.7 , pp. 863-875
    • Arnott, J.A.1    Planey, S.L.2
  • 53
    • 37849052232 scopus 로고    scopus 로고
    • The influenza virus resource at the National Center for Biotechnology Information
    • Bao Y, Bolotov P, Dernovoy D, Kiryutin B, Zaslavsky L, et al. (2008) The influenza virus resource at the National Center for Biotechnology Information. J Virol 82: 596–601. 17942553
    • (2008) J Virol , vol.82 , pp. 596-601
    • Bao, Y.1    Bolotov, P.2    Dernovoy, D.3    Kiryutin, B.4    Zaslavsky, L.5
  • 54
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform
    • Katoh K, Misawa K, Kuma K, Miyata T, (2002) MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res 30: 3059–3066. 12136088
    • (2002) Nucleic Acids Res , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4
  • 55
    • 84938804740 scopus 로고    scopus 로고
    • Sherbooke St. West, Suite #910, Montreal, QC, Canada
    • Molecular Operating Environment (MOE), 2013.08; Chemical Computing Group Inc., 1010 Sherbooke St. West, Suite #910, Montreal, QC, Canada, H3A 2R7, 2014.
    • H3A 2R7 , pp. 2014


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.