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Ha, Y., Stevens, D. J., Skehel, J. J., Wiley, D. C. (2001) X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proceedings of the National Academy of Sciences, 98 (20) 11181-11186 doi:10.1073/pnas.201401198

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Reference TypeJournal (article/letter/editorial)
TitleX-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs
JournalProceedings of the National Academy of Sciences
AuthorsHa, Y.Author
Stevens, D. J.Author
Skehel, J. J.Author
Wiley, D. C.Author
Year2001 (September 25)Volume98
Issue20
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.201401198Search in ResearchGate
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Mindat Ref. ID1662235Long-form Identifiermindat:1:5:1662235:7
GUID0
Full ReferenceHa, Y., Stevens, D. J., Skehel, J. J., Wiley, D. C. (2001) X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proceedings of the National Academy of Sciences, 98 (20) 11181-11186 doi:10.1073/pnas.201401198
Plain TextHa, Y., Stevens, D. J., Skehel, J. J., Wiley, D. C. (2001) X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proceedings of the National Academy of Sciences, 98 (20) 11181-11186 doi:10.1073/pnas.201401198
In(2001, September) Proceedings of the National Academy of Sciences Vol. 98 (20) Proceedings of the National Academy of Sciences

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Krystal, M., Young, J. F., Palese, P., Wilson, I. A., Skehel, J. J., Wiley, D. C. (1983) Sequential mutations in hemagglutinins of influenza B virus isolates: definition of antigenic domains. Proceedings of the National Academy of Sciences, 80 (14) 4527-4531 doi:10.1073/pnas.80.14.4527
Skehel, J. J., Stevens, D. J., Daniels, R. S., Douglas, A. R., Knossow, M., Wilson, I. A., Wiley, D. C. (1984) A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody. Proceedings of the National Academy of Sciences, 81 (6) 1779-1783 doi:10.1073/pnas.81.6.1779
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Vazquez, G., Lievremont, J.-P., St. J. Bird, G., Putney, J. W. (2001) Human Trp3 forms both inositol trisphosphate receptor-dependent and receptor-independent store-operated cation channels in DT40 avian B lymphocytes. Proceedings of the National Academy of Sciences, 98 (20) 11777-11782 doi:10.1073/pnas.201238198
(2020) Correction to Supporting Information for Sun et al., Prevalent Eurasian avian-like H1N1 swine influenza virus with 2009 pandemic viral genes facilitating human infection. Proceedings of the National Academy of Sciences, 117 (37) 23194 doi:10.1073/pnas.2017619117
Skehel, J. J., Waterfield, M. D. (1975) Studies on the primary structure of the influenza virus hemagglutinin. Proceedings of the National Academy of Sciences, 72 (1) 93-97 doi:10.1073/pnas.72.1.93
Veits, J., Wiesner, D., Fuchs, W., Hoffmann, B., Granzow, H., Starick, E., Mundt, E., Schirrmeier, H., Mebatsion, T., Mettenleiter, T. C., Romer-Oberdorfer, A. (2006) Newcastle disease virus expressing H5 hemagglutinin gene protects chickens against Newcastle disease and avian influenza. Proceedings of the National Academy of Sciences, 103 (21) 8197-8202 doi:10.1073/pnas.0602461103
Gabriel, G., Dauber, B., Wolff, T., Planz, O., Klenk, H.-D., Stech, J. (2005) The viral polymerase mediates adaptation of an avian influenza virus to a mammalian host. Proceedings of the National Academy of Sciences, 102 (51) 18590-18595 doi:10.1073/pnas.0507415102
Van Hoeven, N., Pappas, C., Belser, J. A., Maines, T. R., Zeng, H., Garcia-Sastre, A., Sasisekharan, R., Katz, J. M., Tumpey, T. M. (2009) Human HA and polymerase subunit PB2 proteins confer transmission of an avian influenza virus through the air. Proceedings of the National Academy of Sciences, 106 (9) 3366-3371 doi:10.1073/pnas.0813172106
Skehel, J. J., Bayley, P. M., Brown, E. B., Martin, S. R., Waterfield, M. D., White, J. M., Wilson, I. A., Wiley, D. C. (1982) Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion. Proceedings of the National Academy of Sciences, 79 (4) 968-972 doi:10.1073/pnas.79.4.968
 
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