Диссертация (1150004), страница 19
Текст из файла (страница 19)
Soc. – 2011. – Vol. 133. – № 35. – P. 13844–13847.133. Portela, A.; Digard, P. The influenza virus nucleoprotein: a multifunctionalRNA-binding protein pivotal to virus replication // J. Gen. Virol. – 2002. – Vol. 83. –Part. 4. – P. 723–734.134. Ye, Q.; Krug, R.
M.; Tao, Y. J. The mechanism by which influenza A virusnucleoprotein forms oligomers and binds RNA // Nature. – 2006. – Vol. 444. – №7122. – P. 1078–1082.135. Ng, A. K.-L.; Zhang, H.; Tan, K.; Li, Z.; Liu, J.-h.; / Chan, P. K.-S.; Li, S.-M.;Shaw, P.-C. et al. Structure of the influenza virus A H5N1 nucleoprotein:implications for RNA binding, oligomerization, and vaccine design // FASEB. –2008.
– Vol. 22. – № 10. – P. 3638–3647.120136. Boulo, S.; Akarsu, H.; Ruigrok, R. W. H.; Baudin, F. Nuclear traffic of influenzavirus proteins and ribonucleoprotein complexes // Virus Res. – 2007. – Vol. 124. – №1–2. – P. 12–21.137. Kao, R. Y.; Yang, D.; Lau, L. S.; Tsui, W. H. W.; Hu, L.; Dai, J.; Chan, M. P.;Yuen, K. Y. et al. Identification of influenza A nucleoprotein as an antiviral target //Nat.
Biotechnol. – 2010. – Vol. 28. – № 6. – P. 600–605.138. Chan, W.-H.; Ng, A. K.-L.; Robb, N. C.; Lam, M. K.-H.; Chan, P. K.-S.; Au, S.W.-N.; Wang, J.-H.; Shaw, P.-C. et al. Functional analysis of the influenza virusH5N1 nucleoprotein tail loop reveals amino acids that are crucial for oligomerizationand ribonucleoprotein activities // J. Virol.
– 2010. – Vol. 84. – № 14. – P. 7337–7345.139. Shen, Y.-F.; Chen, Y.-H.; Chu, S.-Y.; Lin, M.-I.; Hsu, H.-T.; Wu, P.-Y.; Wu, C.J.; Tsai, M.-D. et al. E339. . .R416 salt bridge of nucleoprotein as a feasible target forinfluenza virus inhibitors // Proc. Natl Acad. Sci. U. S. A. – 2011. – Vol. 108. – №40.
– P. 16515–16520.140. Fedichev, P.; Timakhov, R.; Pyrkov, T.; Getmantsev, E.; Vinnik, A. Structurebased drug design of a new chemical class of small molecules active againstinfluenza A nucleoprotein in vitro and in vivo // PLoS Curr. – 2011. – Vol. 3. – P.RRN1253.141. Martin, K.; Helenius, A. Nuclear transport of influenza virus ribonucleoproteins:the viral matrix protein (M1) promotes export and inhibits import // Cell. – 1991.
–Vol. 67. – № 1. – P. 117–130.142. Gómez-Puertas, P.; Albo, C.; Pérez-Pastrana, E.; Vivo, A.; Portela, A. Influenzavirus matrix protein is the major driving force in virus budding // J. Virol. – 2000. –Vol. 74. – № 24. – P. 11538–11547.143. Sha, B.; Luo, M. Structure of a bifunctional membrane-RNA binding protein,influenza virus matrix protein M1 // Nat. Struct. Biol. – 1997. – Vol. 4. – № 3. – P.239–244.144.
Arzt, S.; Baudin, F.; Barge, A.; Timmins, P.; Burmeister, W. P.; Ruigrok, R. W.Combined results from solution studies on intact influenza virus M1 protein and from121a new crystal form of its N-terminal domain show that M1 is an elongated monomer// Virology. – 2001. – Vol. 279. – № 2. – P. 439–446.145. Liu, T.; Ye, Z. Restriction of viral replication by mutation of the influenza virusmatrix protein // J. Virol. – 2002. – Vol. 76. – № 24.
– P. 13055–13061.146. Akarsu, H.; Burmeister, W. P.; Petosa, C.; Petit, I.; Müller, C. W.; Ruigrok, R.W. H.; Baudin, F. Crystal structure of the M1 protein-binding domain of theinfluenza A virus nuclear export protein (NEP/NS2) // EMBO J. – 2003. – Vol. 22. –№ 18. – P. 4646–4655.147. Hale, B. G.; Randall, R. E.; Ortín, J.; Jackson, D. The multifunctional NS1protein of influenza A viruses // J.
Gen. Virol. – 2008. – Vol. 89. – Part. 10. – P.2359–2376.148. Cheng, A.; Wong, S. M.; Yuan, Y. A. Structural basis for dsRNA recognition byNS1 protein of influenza A virus // Cell Res. – 2009. – Vol. 19. – № 2. – P. 187–195.149. Das, K.; Ma, L.-C.; Xiao, R.; Radvansky, B.; Aramini, J.; Zhao, L.; Marklund,J.; Montelione, G. T. et al. Structural basis for suppression of a host antiviral responseby influenza A virus // Proc. Natl Acad.
Sci. U. S. A. – 2008. – Vol. 105. – № 35. –P. 13093–13098.150. Basu, D.; Walkiewicz, M. P.; Frieman, M.; Baric, R. S.; Auble, D. T.; Engel, D.A. Novel influenza virus NS1 antagonists block replication and restore innateimmune function // J. Virol. – 2009. – Vol. 83. – № 4. – P. 1881–1891.151. Lamb, R.
A.; Lai, C. J. Sequence of interrupted and uninterrupted mRNAs andcloned DNA coding for the two overlapping nonstructural proteins of influenza virus// Cell. – 1980. – Vol. 21. – № 2. – P. 475–485.152. Robb, N. C.; Jackson, D.; Vreede, F. T.; Fodor, E. Splicing of influenza A virusNS1 mRNA is independent of the viral NS1 protein // Journal of General Virology. –2010. – Vol.
91. – Part. 9. – P. 2331–2340.153. Kolpashchikov, D. M.; Honda, A.; Ishihama, A. Structure-Function Relationshipof the Influenza Virus RNA Polymerase: Primer-Binding Site on the PB1 Subunit //Biochemistry. – 2004. – Vol. 43. – № 19. – P. 5882–5887.154. Toyoda, T.; Adyshev, D. M.; Kobayashi, M.; Iwata, A.; Ishihama, A. Molecular122assembly of the influenza virus RNA polymerase: determination of the subunitsubunit contact sites // Journal of General Virology. – 1996.
– Vol. 77. – Part. 9. – P.2149–2157.155. Li, M.L.; Rao. P.; Krug. R. M. The active sites of the influenza cap-dependentendonuclease are on different polymerase subunits // EMBO Journal. – 2001. – Vol.20. – № 8. – P. 2078–2086.156. Biswas, S. K.; Nayak, D. P. Mutational analysis of the conserved motifs ofinfluenza A virus polymerase basic protein 1 // Journal of Virology. – 1994. – Vol.68. – № 3. – P.
1819–1826.157. Fechter, P.; Mingay, L.; Sharps, J.; Chambers, A.; Fodor, E.; Brownlee, G. G.Two aromatic residues in the PB2 subunit of influenza A RNA polymerase arecrucial for cap binding // Journal of Biological Chemistry. – 2003. – Vol. 278. – №22. – P.
20381–20388.158. Guilligay, D.; Tarendeau, F.; Resa-Infante, P.; Coloma, R.; Crepin, T.; Sehr, P.;Lewis, J.; Cusack, S. et al. The structural basis for cap binding by influenza viruspolymerase subunit PB2 // Nature Structural and Molecular Biology. – 2008. – Vol.15. – № 5. – P. 500–506.159. Hooker, L.; Sully, R.; Handa, B.; Ono, N.; Koyano, H.; Klumpp, K. QuantitativeAnalysis of Influenza Virus RNP Interaction with RNA Cap Structures andComparison to Human Cap Binding Protein eIF4E // Biochemistry. – 2003. – Vol.42. – № 20.
– P. 6234–6240.160. Furuta, Y.; Takahashi, K.; Fukuda, Y.; Kuno, M.; Kamiyama, T.; Kozaki, K.;Nomura, N.; Egawa, H.; Minami, S.; Watanabe, Y.; Narita, H.; Shiraki, K. In Vitroand In Vivo Activities of Anti-Influenza Virus Compound T-705 // AntimicrobAgents Chemother. – 2002. – Vol. 46. – № 4. – P. 977–981.161. Kawaguchi, A.; Naito, T.; Nagata, K. Involvement of influenza virus PA subunitin assembly of functional RNA polymerase complexes // Journal of Virology.
– 2005.– Vol. 79. – № 2. – P. 732–744.162. Jung, T. E.; Brownlee, G. G. A new promoter-binding site in the PB1 subunit ofthe influenza A virus polymerase // Journal of General Virology. – 2006. – Vol. 87. –123Pt. 3. – P. 679–688.163. Iwai, Y.; Murakami, K.; Gomi, Y.; Hashimoto, T.; Asakawa, Y.; Okuno, Y.;Ishikawa, T. Anti-influenza activity of marchantins, macrocyclic bisbibenzylscontained in liverworts // PLoS One. – 2011. – Vol. 6. – P.
e19825.164. Rodriguez, A.; Pérez-González, A.; Nieto, A. Influenza virus infection causesspecific degradation of the largest subunit of cellular RNA polymerase II // Journal ofVirology. – 2007. – Vol. 81. – № 10. – P. 5315–5324.165. Regan, J. F.; Liang, Y.; Parslow, T. G. Defective assembly of influenza A virusdue to a mutation in the polymerase subunit PA // Journal of Virology.
– 2006. – Vol.80. – № 1. – P. 252–261.166. Nakagawa, Y.; Oda, K.; Nakada, S. The PB1 subunit alone can catalyze cRNAsynthesis, and the PA subunit in addition to the PB1 subunit is required for viral RNAsynthesis in replication of the influenza virus genome // Journal of Virology. – 1996.– Vol. 70. – № 9. – P. 6390–6394.167. Honda, A.; Mizumoto, K.; Ishihama, A.
Minimum molecular architectures fortranscription and replication of the influenza virus // Proceedings of the NationalAcademy of Sciences of the USA. – 2002. – Vol. 99. – № 20. – P. 13166–13171.168. Deng, T.; Sharps, J. L.; Brownlee, G. G. Role of the influenza virusheterotrimeric RNA polymerase complex in the initiation of replication // Journal ofGeneral Virology. – 2006. – Vol. 87. – Pt.
11. – P. 3373–3377.169. Deng, T.; Sharps, J.; Fodor, E.; Brownlee, G. G. In vitro assembly of PB2 with aPB1-PA dimer supports a new model of assembly of influenza A virus polymerasesubunits into a functional trimeric complex // Journal of Virology. – 2005. – Vol. 79.– № 13. – P. 8669–8674.170. Lee, M. T. M.; Bishop, K.; Medcalf, L.; Elton, D.; Digard, P.; Tiley, L.Definition of the minimal viral components required for the initiation of unprimedRNA synthesis by influenza virus RNA polymerase // Nucleic Acids Research. –2002. – Vol.