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| Chennoufi, Rahima; Bougherara, Houcine; Gagey-eilstein, Nathalie; Dumat, Blaise; Henry, Etienne; Subra, Frederic; Bury-mone, Stephanie; Mahuteau-betzer, Florence; Tauc, Patrick; Teulade-fichou, Marie-paule; Deprez, Eric. |
| Photodynamic therapy (PDT) leads to cell death by using a combination of a photosensitizer and an external light source for the production of lethal doses of reactive oxygen species (ROS). Since a major limitation of PDT is the poor penetration of UV-visible light in tissues, there is a strong need for organic compounds whose activation is compatible with near-infrared excitation. Triphenylamines (TPAs) are fluorescent compounds, recently shown to efficiently trigger cell death upon visible light irradiation (458 nm), however outside the so-called optical/therapeutic window. Here, we report that TPAs target cytosolic organelles of living cells, mainly mitochondria, triggering a fast apoptosis upon two-photon excitation, thanks to their large two-photon... |
| Tipo: Text |
Palavras-chave: Apoptosis; Small molecules. |
| Ano: 2016 |
URL: http://archimer.ifremer.fr/doc/00320/43168/42726.pdf |
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| Li, Jiayao; Henry, Etienne; Wang, Lanmei; Delelis, Olivier; Wang, Huan; Simon, Francoise; Tauc, Patrick; Brochon, Jean-claude; Zhao, Yunlong; Deprez, Eric. |
| Fatty acid-binding proteins (FABPs) are small cytosolic proteins, largely distributed in invertebrates and vertebrates, which accomplish uptake and intracellular transport of hydrophobic ligands such as fatty acids. Although long chain fatty acids play multiple crucial roles in cellular functions (structural, energy metabolism, regulation of gene expression), the precise functions of FABPs, especially those of invertebrate species, remain elusive. Here, we have identified and characterized a novel FABP family member, Cq-FABP, from the hepatopancreas of red claw crayfish Cherax quadricarinatus. We report the characterization of fatty acid-binding affinity of Cq-FABP by four different competitive fluorescence-based assays. In the two first approaches, the... |
| Tipo: Text |
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| Ano: 2012 |
URL: http://archimer.ifremer.fr/doc/00206/31770/30186.pdf |
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| Carayon, Kevin; Leh, Herve; Henry, Etienne; Simon, Francoise; Mouscadet, Jean-francois; Deprez, Eric. |
| HIV-1 integrase catalyzes the insertion of the viral genome into chromosomal DNA. We characterized the structural determinants of the 3'-processing reaction specificity-the first reaction of the integration process-at the DNA-binding level. We found that the integrase N-terminal domain, containing a pseudo zinc-finger motif, plays a key role, at least indirectly, in the formation of specific integrase-DNA contacts. This motif mediates a cooperative DNA binding of integrase that occurs only with the cognate/viral DNA sequence and the physiologically relevant Mg(2+) cofactor. The DNA-binding was essentially non-cooperative with Mn(2+) or using non-specific/random sequences, regardless of the metallic cofactor. 2,2'-Dithiobisbenzamide-1 induced zinc ejection... |
| Tipo: Text |
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| Ano: 2010 |
URL: http://archimer.ifremer.fr/doc/00206/31773/30183.pdf |
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| Qin, Wei; Bazeille, Nicolas; Henry, Etienne; Zhang, Bo; Deprez, Eric; Xi, Xu-guang. |
| Cadmium is a toxic metal that inactivates DNA-repair proteins via multiple mechanisms, including zinc substitution. In this study, we investigated the effect of Cd2+ on the Bloom protein (BLM), a DNA-repair helicase carrying a zinc-binding domain (ZBD) and playing a critical role to ensure genomic stability. One characteristics of BLM-deficient cells is the elevated rate of sister chromatid exchanges, a phenomenon that is also induced by Cd2+. Here, we show that Cd2+ strongly inhibits both ATPase and helicase activities of BLM. Cd2+ primarily prevents BLM-DNA interaction via its binding to sulfhydryl groups of solvent-exposed cysteine residues and, concomitantly, promotes the formation of large BLM multimers/aggregates. In contrast to previously described... |
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| Ano: 2016 |
URL: https://archimer.ifremer.fr/doc/00341/45196/44599.pdf |
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