Targeting of T/Tn antigens with a plant lectin to kill human leukemia cells by photochemotherapy.

Autor: Guillaume Poiroux, Marguerite Pitié, Raphaël Culerrier, Elodie Lafont, Bruno Ségui, Els J M Van Damme, Willy J Peumans, Jean Bernadou, Thierry Levade, Pierre Rougé, Annick Barre, Hervé Benoist

Publikováno v: PLoS ONE, Vol 6, Iss 8, p e23315 (2011)

Photochemotherapy is used both for solid tumors and in extracorporeal treatment of various hematologic disorders. Nevertheless, its development in oncology remains limited, because of the low selectivity of photosensitizers (PS) towards human tumor c

Externí odkaz: https://doaj.org/article/a8620ab1c7fd4b5fb175c50679e15cb8

Preliminary Investigations of the Effect of Lipophilic Analogues of the Active Metabolite of Isoniazid Toward Bacterial and Plasmodial Strains

Autor: Patricia Constant, Jean Bernadou, Frédéric Coslédan, Bernard Meunier, Tamara Delaine, Annaïk Quémard, Vania Bernardes-Génisson

Publikováno v: Chemical Biology & Drug Design. 79:1001-1006

Five lipophilic analogues 1–5 of the active metabolite of the antitubercular drug isoniazid (INH), selected as inhibitors of Mycobacterium smegmatis and Mycobacterium tuberculosis growth, were evaluated for their activity against Corynebacterium gl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d7cecbf7f3fb803ff2cedc00257bd9fa
https://doi.org/10.1111/j.1747-0285.2012.01374.x

Binding of the tautomeric forms of isoniazid-NAD adducts to the active site of the Mycobacterium tuberculosis enoyl-ACP reductase (InhA): A theoretical approach

Autor: Jean Bernadou, Vania Bernardes-Génisson, Jean-Luc Stigliani, Tamara Delaine, Philippe Arnaud, Bernard Meunier

Publikováno v: Journal of Molecular Graphics and Modelling. 27:536-545

The front-line antituberculosis drug isoniazid (INH) inhibits InhA, the NADH-dependent fatty acid biosynthesis enoyl ACP-reductase from Mycobacterium tuberculosis, via formation of covalent adducts with NAD (INH-NAD adducts). While ring tautomers wer

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f739f76edf24e849ee6034ee3c66237
https://doi.org/10.1016/j.jmgm.2008.09.006

Crystal structure of the enoyl-ACP reductase of Mycobacterium tuberculosis (InhA) in the apo-form and in complex with the active metabolite of isoniazid pre-formed by a biomimetic approach

Autor: Alexandra Delbot, Michel Baltas, Aurélien Chollet, Sylviane Julien, Christian Lherbet, Lionel Mourey, Geneviève Pratviel, Laurent Maveyraud, Vania Bernardes-Génisson, Jean Bernadou

Publikováno v: Journal of Structural Biology
Journal of Structural Biology, Elsevier, 2015, 190, pp.328-337. ⟨10.1016/j.jsb.2015.04.008⟩
Journal of Structural Biology, 2015, 190, pp.328-337. ⟨10.1016/j.jsb.2015.04.008⟩
Journal of Structural Biology, Elsevier, 2015, 190 (3), pp.328-337. ⟨10.1016/j.jsb.2015.04.008⟩

International audience; InhA is an enoyl-ACP reductase of Mycobacterium tuberculosis implicated in the biosynthesis of mycolic acids, essential constituents of the mycobacterial cell wall. To date, this enzyme is considered as a promising target for

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ec7155ebdea6aae0da28680023e2d89
https://hal.archives-ouvertes.fr/hal-03002973/file/chollet-jstructbiol15.pdf

In Vitro Inhibition of the Mycobacterium tuberculosis β-Ketoacyl-Acyl Carrier Protein Reductase MabA by Isoniazid

Autor: Hedia Marrakchi, Annaíik Quémard, Stéphanie Ducasse-Cabanot, Mamadou Daffé, Gilles Labesse, Jean Bernadou, Martin Cohen-Gonsaud, Michel Nguyen, Didier Zerbib

Publikováno v: Antimicrobial Agents and Chemotherapy. 48:242-249

The first-line specific antituberculous drug isoniazid inhibits the fatty acid elongation system (FAS) FAS-II involved in the biosynthesis of mycolic acids, which are major lipids of the mycobacterial envelope. The MabA protein that catalyzes the sec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::487ee6dc78b79a91147e09d1f97d8f9e
https://doi.org/10.1128/aac.48.1.242-249.2004