J J Skehel|D C Wiley - JoVE Visualize

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Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences|February 25, 1980

Studies on the structure of the haemagglutininJ J Skehel, M D Waterfield, J W McCauley, et al.

Proceedings of the National Academy of Sciences of the United States of America|May 30, 1998

The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coilW Weissenhorn, L J Calder, S A Wharton, et al.

Nature|October 18, 1984

Three-dimensional structure of an antigenic mutant of the influenza virus haemagglutininM Knossow, R S Daniels, A R Douglas, et al.

The Journal of Biological Chemistry|December 15, 1991

Ligand recognition by influenza virus. The binding of bivalent sialosidesG D Glick, P L Toogood, D C Wiley, et al.

Proceedings of the National Academy of Sciences of the United States of America|June 10, 1997

Assembly of a rod-shaped chimera of a trimeric GCN4 zipper and the HIV-1 gp41 ectodomain expressed in Escherichia coliW Weissenhorn, L J Calder, A Dessen, et al.

The Journal of General Virology|August 1, 1988

Membrane fusion by peptide analogues of influenza virus haemagglutininS A Wharton, S R Martin, R W Ruigrok, et al.

Proceedings of the National Academy of Sciences of the United States of America|December 15, 1991

Amantadine selection of a mutant influenza virus containing an acid-stable hemagglutinin glycoprotein: evidence for virus-specific regulation of the pH of glycoprotein transport vesiclesD A Steinhauer, S A Wharton, J J Skehel, et al.

The EMBO Journal|August 14, 2001

Studies on influenza haemagglutinin fusion peptide mutants generated by reverse geneticsK J Cross, S A Wharton, J J Skehel, et al.

Nature|June 2, 1988

Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acidW Weis, J H Brown, S Cusack, et al.

The EMBO Journal|December 20, 1984

Studies on the adaptation of influenza viruses to MDCK cellsR Rott, M Orlich, H D Klenk, et al.

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Showing results (31-40 of 226) with videos related to

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Pageof 23

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences|February 25, 1980

Studies on the structure of the haemagglutininJ J Skehel, M D Waterfield, J W McCauley, et al.

Proceedings of the National Academy of Sciences of the United States of America|May 30, 1998

The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coilW Weissenhorn, L J Calder, S A Wharton, et al.

Nature|October 18, 1984

Three-dimensional structure of an antigenic mutant of the influenza virus haemagglutininM Knossow, R S Daniels, A R Douglas, et al.

The Journal of Biological Chemistry|December 15, 1991

Ligand recognition by influenza virus. The binding of bivalent sialosidesG D Glick, P L Toogood, D C Wiley, et al.

Proceedings of the National Academy of Sciences of the United States of America|June 10, 1997

Assembly of a rod-shaped chimera of a trimeric GCN4 zipper and the HIV-1 gp41 ectodomain expressed in Escherichia coliW Weissenhorn, L J Calder, A Dessen, et al.

The Journal of General Virology|August 1, 1988

Membrane fusion by peptide analogues of influenza virus haemagglutininS A Wharton, S R Martin, R W Ruigrok, et al.

Proceedings of the National Academy of Sciences of the United States of America|December 15, 1991

Amantadine selection of a mutant influenza virus containing an acid-stable hemagglutinin glycoprotein: evidence for virus-specific regulation of the pH of glycoprotein transport vesiclesD A Steinhauer, S A Wharton, J J Skehel, et al.

The EMBO Journal|August 14, 2001

Studies on influenza haemagglutinin fusion peptide mutants generated by reverse geneticsK J Cross, S A Wharton, J J Skehel, et al.

Nature|June 2, 1988

Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acidW Weis, J H Brown, S Cusack, et al.

The EMBO Journal|December 20, 1984

Studies on the adaptation of influenza viruses to MDCK cellsR Rott, M Orlich, H D Klenk, et al.

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