Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Caroline Ligny-Lemaire"'
Autor:
Julie Bourdais-Jomaron, Caroline Ligny-Lemaire, Julia Chamot-Rooke, Gilles Phan, Frédéric Ducancel, Jean-Pierre Le Caer, Loïc Quinton
Publikováno v:
Analytical Chemistry
Analytical Chemistry, American Chemical Society, 2005, 77 (20), pp.6630-6639. ⟨10.1021/ac050575k⟩
Analytical Chemistry, 2005, 77 (20), pp.6630-6639. ⟨10.1021/ac050575k⟩
Analytical Chemistry, American Chemical Society, 2005, 77 (20), pp.6630-6639. ⟨10.1021/ac050575k⟩
Analytical Chemistry, 2005, 77 (20), pp.6630-6639. ⟨10.1021/ac050575k⟩
International audience; The standard analytical procedure for screening the proteomic profile of a venom often relies on an appropriate combination of sample extraction, electrophoresis, reversed-phase high-performance liquid chromatography, mass spe
Autor:
F. Sampieri, Rym Benkhalifa, Habib Karoui, Balkiss Bouhaouala-Zahar, Ilhem Zenouaki, Najet Srairi, André Ménez, Caroline Ligny-Lemaire, Frédéric Ducancel, Mohamed El Ayeb, Marcel Pelhate, Pascal Drevet
Publikováno v:
European Journal of Biochemistry. 269:2831-2841
BotXIV and LqhαIT are two structurally related long chain scorpion α-toxins that inhibit sodium current inactivation in excitable cells. However, while LqhαIT from Leiurus quinquestriatus hebraeus is classified as a true and strong insect α-toxin
Autor:
Caroline Ligny-Lemaire, Corinne Chanussot, Jean-Claude Boulain, Laurent Bellanger, Patrick Seguin, André Ménez
Publikováno v:
Journal of Immunological Methods. 197:39-49
A synthetic DNA encoding human proinsulin was inserted in frame in the bacterial alkaline phosphatase gene. A homogeneous recombinant human proinsulin-alkaline phosphatase conjugate was obtained directly from the periplasm of Escherichia coli transfo
Autor:
Hung Lamthanh, Bruno H. Muller, Zvi Wollberg, Andrzej Galat, Yvon Doljansky, Michaël Wery, Frédéric Ducancel, Caroline Ligny-Lemaire, Avner Bdolah, Reto Stöcklin, Tomohisa Ogawa, Mirian A. F. Hayashi
Publikováno v:
Peptides. 25(8)
Sarafotoxins (SRTXs) constitute a family of vasoactive peptides that were initially isolated from the venom of Atractaspis engaddensis, and that are structurally and functionally related to endothelins (ETs). Analysis of the venom of Atractaspis micr