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Nature|January 24, 1998
Engineering cyclophilin into a proline-specific endopeptidaseE Quéméneur, M Moutiez, J B Charbonnier, et al.Biochimie|February 28, 1998
Similarities of hydrolytic antibodies revealed by their X-ray structures: a reviewJ B Charbonnier, B Gigant, B Golinelli-Pimpaneau, et al.Proceedings of the National Academy of Sciences of the United States of America|July 22, 1997
X-ray structures of a hydrolytic antibody and of complexes elucidate catalytic pathway from substrate binding and transition state stabilization through water attack and product releaseB Gigant, J B Charbonnier, Z Eshhar, et al.Journal of Biomechanics|February 1, 1995
Aphakia correction by synthetic intracorneal implantation: a new tool for quantitative predetermination of the optical qualityJ B Charbonnier, J C Charmet, D Vallet, et al.Journal of Molecular Biology|November 25, 1998
Crossreactivity, efficiency and catalytic specificity of an esterase-like antibodyB Gigant, J B Charbonnier, Z Eshhar, et al.Protein Science : a Publication of the Protein Society|April 21, 1999
On the role of the cis-proline residue in the active site of DsbAJ B Charbonnier, P Belin, M Moutiez, et al.Journal of Medicinal Chemistry|May 5, 2000
Design of a Gag pentapeptide analogue that binds human cyclophilin A more efficiently than the entire capsid protein: new insights for the development of novel anti-HIV-1 drugsQ Li, M Moutiez, J B Charbonnier, et al.Proceedings of the National Academy of Sciences of the United States of America|December 5, 1995
Crystal structure of the complex of a catalytic antibody Fab fragment with a transition state analog: structural similarities in esterase-like catalytic antibodiesJ B Charbonnier, E Carpenter, B Gigant, et al.European Journal of Biochemistry|June 1, 1997
Mechanism of inactivation of a catalytic antibody by p-nitrophenyl estersB Gigant, J B Charbonnier, B Golinelli-Pimpaneau, et al.Proceedings of the National Academy of Sciences of the United States of America|May 11, 2000
Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: structural basis for recognition of B-cell receptors and superantigen activityM Graille, E A Stura, A L Corper, et al.Pageof 2