Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Françoise M. Gabert"'
Publikováno v:
European Journal of Immunology. 27:2673-2679
Processing and presentation of covalently linked C3b-tetanus toxin (TT) complexes, as compared to unlinked C3b + TT, lead to increased T cell proliferation. The aim of this study was to analyze the effect of coupling C3b to TT on the efficiency of TT
Autor:
Françoise M. Gabert, Christian L. Villiers, Catherine A. Rey-Millet, Marie-Bernadette Villiers, L. Santoro, Maurice G. Colomb
Publikováno v:
Research in Immunology. 147:75-82
Autor:
Patrice N. Marche, Anne-Marie Laharie, Françoise M. Gabert, François Cretin, Marie-Bernadette Villiers, Vincent A. Serra
Publikováno v:
Molecular Immunology
Molecular Immunology, Elsevier, 2007, 44 (11), pp.2893-2899. ⟨10.1016/j.molimm.2007.01.013⟩
Molecular Immunology, 2007, 44 (11), pp.2893-2899. ⟨10.1016/j.molimm.2007.01.013⟩
Molecular Immunology, Elsevier, 2007, 44 (11), pp.2893-2899. ⟨10.1016/j.molimm.2007.01.013⟩
Molecular Immunology, 2007, 44 (11), pp.2893-2899. ⟨10.1016/j.molimm.2007.01.013⟩
International audience; In addition to its well-established role in innate immunity, the complement component C3 is of critical importance in modulating the humoral response. In this study, we examined the effect of C3b linkage to tetanus toxin (TeNT
Autor:
Françoise M. Gabert, Laure Perrin-Cocon, Christian L. Villiers, Patrice N. Marche, Jean Salamero
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 172(6)
The processing of exogenous Ags is an essential step for the generation of immunogenic peptides that will be presented to T cells. This processing relies on the efficient intracellular targeting of Ags, because it depends on the content of the compar
Autor:
Christian L. Villiers, Marie-Bernadette Villiers, Françoise M. Gabert, Muriel R. Jacquier-Sarlin, Maurice G. Colomb, A M Journet
Publikováno v:
Immunology
Immunology, 1996, 89 (3), pp.348-355. ⟨10.1046/j.1365-2567.1996.d01-747.x⟩
Immunology, Wiley, 1996, 89 (3), pp.348-355. ⟨10.1046/j.1365-2567.1996.d01-747.x⟩
Immunology, 1996, 89 (3), pp.348-355. ⟨10.1046/j.1365-2567.1996.d01-747.x⟩
Immunology, Wiley, 1996, 89 (3), pp.348-355. ⟨10.1046/j.1365-2567.1996.d01-747.x⟩
International audience; Antigen opsonization by the C3b fragment of complement is a significant event in the modulation of cellmediated immune response, but its mechanism is still largely unknown. The structural characteristics of C3b allow it to act
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77302dcfd80cec425e879ade13afcb62
https://hal.science/hal-03223006
https://hal.science/hal-03223006
Autor:
Françoise M. Gabert, Christian L. Villiers, Catherine A. Rey-Millet, Maurice G. Colomb, Serge Chesne
Publikováno v:
Molecular immunology. 31(17)
Complement protein C3, like C4 and α2-macroglobulin (α2M), is a potentially bivalent ligand: (1) its proteolytic fragment, C3b, is able to interact covalently with antigens, and (2) this bound fragment is able to interact non-covalently with specif
Autor:
Françoise M. Gabert, Christian L. Villiers, Christian Drouet, Martine Pernollet, Maurice G. Colomb
Publikováno v:
Molecular immunology. 30(18)
At inflammatory sites, before their processing, antigens are exposed to oxygen free radicals released by activated cells. The effect of hydroxyl radicals (OH·) on the structure of a protein antigen, tetanus toxin (TT) was investigated, as well as th
Autor:
Françoise M. Gabert, Marie-Bernadette Villiers, Maurice G. Colomb, Muriel R. Jacquier, Christian L. Villiers
Publikováno v:
Molecular immunology. 30(2)
Tetanus toxin contains a metal-binding site for zinc, located in its light chain. The sequence accounting for Zn fixation is part of a predicted amphipathic helical secondary structure and corresponds to a putative T cell epitope according to Rothbar
Publikováno v:
Immunology Letters. 56:378
Publikováno v:
Immunology Letters. 56:237