J Hennecke|D C Wiley - JoVE Visualize

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Cell|February 21, 1992

Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activityL Godley, J Pfeifer, D Steinhauer, et al.

Science (New York, N.Y.)|May 30, 1986

Protein, DNA, and virus crystallography with a focused imaging proportional counterR M Durbin, R Burns, J Moulai, et al.

Journal of Immunology (Baltimore, Md. : 1950)|May 5, 1999

Peptide recognition by two HLA-A2/Tax11-19-specific T cell clones in relationship to their MHC/peptide/TCR crystal structuresS Hausmann, W E Biddison, K J Smith, et al.

Nature|May 26, 1994

Binary and ternary complexes between T-cell receptor, class II MHC and superantigen in vitroA Seth, L J Stern, T H Ottenhoff, et al.

Nature Structural Biology|October 3, 1999

Selection of gp41-mediated HIV-1 cell entry inhibitors from biased combinatorial libraries of non-natural binding elementsM Ferrer, T M Kapoor, T Strassmaier, et al.

Virology|October 15, 1984

Antigenic analyses of influenza virus haemagglutinins with different receptor-binding specificitiesR S Daniels, A R Douglas, J J Skehel, et al.

Proceedings of the National Academy of Sciences of the United States of America|January 1, 1992

Crystallographic detection of a second ligand binding site in influenza virus hemagglutininN K Sauter, G D Glick, R L Crowther, et al.

Proceedings of the National Academy of Sciences of the United States of America|February 1, 1982

Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusionJ J Skehel, P M Bayley, E B Brown, et al.

Cell|July 1, 1988

Evidence that multiple residues on both the alpha-helices of the class I MHC molecule are simultaneously recognized by the T cell receptorP Ajitkumar, S S Geier, K V Kesari, et al.

Biochemistry|October 13, 1992

Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallographyN K Sauter, J E Hanson, G D Glick, et al.

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Showing results (161-170 of 179) with videos related to

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Pageof 18

Cell|February 21, 1992

Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activityL Godley, J Pfeifer, D Steinhauer, et al.

Science (New York, N.Y.)|May 30, 1986

Protein, DNA, and virus crystallography with a focused imaging proportional counterR M Durbin, R Burns, J Moulai, et al.

Journal of Immunology (Baltimore, Md. : 1950)|May 5, 1999

Peptide recognition by two HLA-A2/Tax11-19-specific T cell clones in relationship to their MHC/peptide/TCR crystal structuresS Hausmann, W E Biddison, K J Smith, et al.

Nature|May 26, 1994

Binary and ternary complexes between T-cell receptor, class II MHC and superantigen in vitroA Seth, L J Stern, T H Ottenhoff, et al.

Nature Structural Biology|October 3, 1999

Selection of gp41-mediated HIV-1 cell entry inhibitors from biased combinatorial libraries of non-natural binding elementsM Ferrer, T M Kapoor, T Strassmaier, et al.

Virology|October 15, 1984

Antigenic analyses of influenza virus haemagglutinins with different receptor-binding specificitiesR S Daniels, A R Douglas, J J Skehel, et al.

Proceedings of the National Academy of Sciences of the United States of America|January 1, 1992

Crystallographic detection of a second ligand binding site in influenza virus hemagglutininN K Sauter, G D Glick, R L Crowther, et al.

Proceedings of the National Academy of Sciences of the United States of America|February 1, 1982

Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusionJ J Skehel, P M Bayley, E B Brown, et al.

Cell|July 1, 1988

Evidence that multiple residues on both the alpha-helices of the class I MHC molecule are simultaneously recognized by the T cell receptorP Ajitkumar, S S Geier, K V Kesari, et al.

Biochemistry|October 13, 1992

Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallographyN K Sauter, J E Hanson, G D Glick, et al.

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