Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Martine, Chartier"'
Autor:
Daniel Baty, Jean-Luc Teillaud, Patrick Chames, André Pèlegrin, Bruno Robert, Brigitte Kerfelec, Charlotte Boix, Ghislaine Behar, Martine Chartier, Corinne Pétiard, Amélie Cornillon, Caroline Rozan
PDF file - 60K, Lack of competition between bsFab and human IgG for FcγRIIIa binding.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cca666b6c70b795ecbb7f15043ac786
https://doi.org/10.1158/1535-7163.22499808
https://doi.org/10.1158/1535-7163.22499808
Autor:
Daniel Baty, Jean-Luc Teillaud, Patrick Chames, André Pèlegrin, Bruno Robert, Brigitte Kerfelec, Charlotte Boix, Ghislaine Behar, Martine Chartier, Corinne Pétiard, Amélie Cornillon, Caroline Rozan
PDF file - 70K
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6118553ab49972b705e04f2af9747754
https://doi.org/10.1158/1535-7163.22499805.v1
https://doi.org/10.1158/1535-7163.22499805.v1
Autor:
Daniel Baty, Jean-Luc Teillaud, Patrick Chames, André Pèlegrin, Bruno Robert, Brigitte Kerfelec, Charlotte Boix, Ghislaine Behar, Martine Chartier, Corinne Pétiard, Amélie Cornillon, Caroline Rozan
PDF file - 120K
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e31fd8289949aaa23fd897d10a8b32a
https://doi.org/10.1158/1535-7163.22499802
https://doi.org/10.1158/1535-7163.22499802
Autor:
Daniel Baty, Jean-Luc Teillaud, Patrick Chames, André Pèlegrin, Bruno Robert, Brigitte Kerfelec, Charlotte Boix, Ghislaine Behar, Martine Chartier, Corinne Pétiard, Amélie Cornillon, Caroline Rozan
Antibody-dependent cell-mediated cytotoxicity, one of the most prominent modes of action of antitumor antibodies, suffers from important limitations due to the need for optimal interactions with Fcγ receptors. In this work, we report the design of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::514928c9d620c9b206d351fa3c5bcf1b
https://doi.org/10.1158/1535-7163.c.6536262
https://doi.org/10.1158/1535-7163.c.6536262
Publikováno v:
Journal of Peptide Science. 10:648-658
A 10-mer random peptide library displayed on filamentous bacteriophage was used to determine the molecular basis of the interaction between the monoclonal anti-colicin A antibody 1C11 and its cognate epitope. Previous studies established that the put
Autor:
Daniel Baty, Elisabeth Mappus, Shu-wen W. Chen, Stéphane Coulon, Jean-Luc Pellequer, Claude Yves Cuilleron, Martine Chartier, Blachère T
Publikováno v:
Journal of Molecular Recognition. 15:6-18
The high-affinity monoclonal anti-estradiol antibody 9D3 presents a specificity defect towards estradiol-3-sulphate and 3-glucuronide conjugates incompatible with use in direct immunoassays. The corresponding single-chain variable fragment (scFv), cl
Autor:
Daniel Baty, Jean Ruf, Stéphanie Blanchin, Christine Duthoit, Valérie Estienne, Pierre Carayon, Josée-Martine Durand-Gorde, Martine Chartier, Roland Montserret
Publikováno v:
International immunology. 14(4)
Thyroid peroxidase (TPO) is involved in autoimmune thyroid diseases and high titers of TPO autoantibodies directed to various conformational B cell epitopes are frequently present in patients' sera. Deciphering these epitopes is a difficult task, but
Autor:
Stéphane, Coulon, Jean-Luc, Pellequer, Thierry, Blachère, Martine, Chartier, Elisabeth, Mappus, Shu-wen W, Chen Sw, Claude Yves, Cuilleron, Daniel, Baty
Publikováno v:
Journal of molecular recognition : JMR. 15(1)
The high-affinity monoclonal anti-estradiol antibody 9D3 presents a specificity defect towards estradiol-3-sulphate and 3-glucuronide conjugates incompatible with use in direct immunoassays. The corresponding single-chain variable fragment (scFv), cl
Autor:
Martine Chartier, Jacques Izard, Juan Manuel González-Mañas, Daniel Baty, Marcel Crest, Michael W. Parker, Denis Duché
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, 1996, 271 (26), pp.15401-15406. ⟨10.1074/jbc.271.26.15401⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1996, 271 (26), pp.15401-15406. ⟨10.1074/jbc.271.26.15401⟩
Journal of Biological Chemistry, 1996, 271 (26), pp.15401-15406. ⟨10.1074/jbc.271.26.15401⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1996, 271 (26), pp.15401-15406. ⟨10.1074/jbc.271.26.15401⟩
International audience; Four colicin A double-cysteine mutants possessing a disulfide bond in their pore-forming domain were constructed to study the translocation and the pore formation of colicin A. The disulfide bonds connected alpha-helices 1 and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2a077c17e74eef92ce821b1a69a0966
https://hal.science/hal-02440976
https://hal.science/hal-02440976
Autor:
Daniel Baty, Christophe Camilla, Patricia Niccoli, Martine Chartier, Jacques Fieschi, Patrick Chames
Publikováno v:
Analytical biochemistry. 234(2)
Thyroglobulin double mutants with various substitutions were obtained with a new polymerase chain reaction-based mutagenesis technique. Maximum length of megaprimer and efficiency of mutagenesis were improved by purification of single-stranded DNA, u