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C Wiley

Showing results (281-290 of 348) with videos related to

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The Journal of Biological Chemistry|June 25, 1985
Host-mediated selection of influenza virus receptor variants. Sialic acid-alpha 2,6Gal-specific clones of A/duck/Ukraine/1/63 revert to sialic acid-alpha 2,3Gal-specific wild type in ovoG N Rogers, R S Daniels, J J Skehel, et al.
Journal of Immunology (Baltimore, Md. : 1950)|December 21, 2014
Pillars article: three-dimensional structure of the human class II histocompatibility antigen HLA-DR1. Nature. 1993. 364: 33-39Jerry H Brown, Theodore S Jardetzky, Joan C Gorga, et al.
Molecular and Cellular Neurosciences|November 8, 2015
Intracellular LINGO-1 negatively regulates Trk neurotrophin receptor signalingJames S Meabon, Rian de Laat, Katsuaki Ieguchi, et al.
Biochemistry|October 17, 1989
Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: a 500-MHz proton nuclear magnetic resonance studyN K Sauter, M D Bednarski, B A Wurzburg, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 23, 1996
Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptidesT S Jardetzky, J H Brown, J C Gorga, et al.
Acta Crystallographica. Section D, Biological Crystallography|April 27, 1999
X-ray crystallographic determination of the structure of the influenza C virus haemagglutinin-esterase-fusion glycoproteinX Zhang, P B Rosenthal, F Formanowski, et al.
Virology|May 18, 2000
Electron microscopy of the human respiratory syncytial virus fusion protein and complexes that it forms with monoclonal antibodiesL J Calder, L González-Reyes, B García-Barreno, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 1, 1993
Comparison of the P2 specificity pocket in three human histocompatibility antigens: HLA-A*6801, HLA-A*0201, and HLA-B*2705H C Guo, D R Madden, M L Silver, et al.
Science (New York, N.Y.)|February 16, 1973
Aqueous central cavity in aspartate transcarbamylase from Escherichia coliD R Evans, S G Warren, B F Edwards, et al.
Cold Spring Harbor Symposia on Quantitative Biology|January 1, 1972
The 5.5 Angstrom resolution structure of the regulatory enzyme, asparate transcarbamylaseD C Wiley, D R Evans, S G Warren, et al.
Pageof 35

Showing results (281-290 of 348) with videos related to

Sort By:
Pageof 35
The Journal of Biological Chemistry|June 25, 1985
Host-mediated selection of influenza virus receptor variants. Sialic acid-alpha 2,6Gal-specific clones of A/duck/Ukraine/1/63 revert to sialic acid-alpha 2,3Gal-specific wild type in ovoG N Rogers, R S Daniels, J J Skehel, et al.
Journal of Immunology (Baltimore, Md. : 1950)|December 21, 2014
Pillars article: three-dimensional structure of the human class II histocompatibility antigen HLA-DR1. Nature. 1993. 364: 33-39Jerry H Brown, Theodore S Jardetzky, Joan C Gorga, et al.
Molecular and Cellular Neurosciences|November 8, 2015
Intracellular LINGO-1 negatively regulates Trk neurotrophin receptor signalingJames S Meabon, Rian de Laat, Katsuaki Ieguchi, et al.
Biochemistry|October 17, 1989
Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: a 500-MHz proton nuclear magnetic resonance studyN K Sauter, M D Bednarski, B A Wurzburg, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 23, 1996
Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptidesT S Jardetzky, J H Brown, J C Gorga, et al.
Acta Crystallographica. Section D, Biological Crystallography|April 27, 1999
X-ray crystallographic determination of the structure of the influenza C virus haemagglutinin-esterase-fusion glycoproteinX Zhang, P B Rosenthal, F Formanowski, et al.
Virology|May 18, 2000
Electron microscopy of the human respiratory syncytial virus fusion protein and complexes that it forms with monoclonal antibodiesL J Calder, L González-Reyes, B García-Barreno, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 1, 1993
Comparison of the P2 specificity pocket in three human histocompatibility antigens: HLA-A*6801, HLA-A*0201, and HLA-B*2705H C Guo, D R Madden, M L Silver, et al.
Science (New York, N.Y.)|February 16, 1973
Aqueous central cavity in aspartate transcarbamylase from Escherichia coliD R Evans, S G Warren, B F Edwards, et al.
Cold Spring Harbor Symposia on Quantitative Biology|January 1, 1972
The 5.5 Angstrom resolution structure of the regulatory enzyme, asparate transcarbamylaseD C Wiley, D R Evans, S G Warren, et al.
Pageof 35