Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Charlotte Druon"'
Autor:
Gilles Pagès, Frédéric Checler, Peter Heutink, Jie Shen, Sabine Scarzello, Matthew S. Goldberg, Charlotte Druon, Guillaume Robert, Patrick Auberger, Sébastien Grosso, Emilie Giaime, Jacques Pouysségur, C. Alves da Costa, Claire Sunyach
Publikováno v:
Cell Death and Differentiation
Cell Death and Differentiation, Nature Publishing Group, 2009, epub ahead of print. ⟨10.1038/cdd.2009.116⟩
Cell Death and Differentiation, 17(1), 158-169. Nature Publishing Group
Giaime, E, Sunyach, C, Druon, C, Scarzello, S, Robert, G, Grosso, S, Auberger, P, Goldberg, M S, Shen, J, Heutink, P, Pouyssegur, J, Pages, G, Checler, F & da Costa, C A 2010, ' Loss of function of DJ-1 triggered by Parkinson's disease-associated mutation is due to proteolytic resistance to caspase-6 ', Cell Death and Differentiation, vol. 17, no. 1, pp. 158-169 . https://doi.org/10.1038/cdd.2009.116
Cell Death and Differentiation, Nature Publishing Group, 2009, epub ahead of print. ⟨10.1038/cdd.2009.116⟩
Cell Death and Differentiation, 17(1), 158-169. Nature Publishing Group
Giaime, E, Sunyach, C, Druon, C, Scarzello, S, Robert, G, Grosso, S, Auberger, P, Goldberg, M S, Shen, J, Heutink, P, Pouyssegur, J, Pages, G, Checler, F & da Costa, C A 2010, ' Loss of function of DJ-1 triggered by Parkinson's disease-associated mutation is due to proteolytic resistance to caspase-6 ', Cell Death and Differentiation, vol. 17, no. 1, pp. 158-169 . https://doi.org/10.1038/cdd.2009.116
International audience; DJ-1 was recently identified as a gene product responsible for a subset of familial Parkinson's disease (PD). The mechanisms by which mutations in DJ-1 alter its function and account for PD-related pathology remained largely u
Autor:
Sabine Scarzello, Charlotte Druon, Claire Sunyach, Frédéric Checler, Marie-Victoire Guillot-Sestier
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (51), pp.35973-86. ⟨10.1074/jbc.M109.051086⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (51), pp.35973-86. ⟨10.1074/jbc.M109.051086⟩
International audience; Cellular prion protein (PrP(c)) undergoes a disintegrin-mediated physiological cleavage, generating a soluble amino-terminal fragment (N1), the function of which remained unknown. Recombinant N1 inhibits staurosporine-induced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d094d9b28dec1225a1c8cbc32d97b7ed
https://hal.archives-ouvertes.fr/hal-00497181
https://hal.archives-ouvertes.fr/hal-00497181
Autor:
Sabine Scarzello, Charlotte Druon, M. Ettaiche, C. Sunyach, Frédéric Checler, M.-V. Guillot-Sestier
Publikováno v:
Revue Neurologique. 165:58
La proteine prion cellulaire (PrPc) est impliquee dans le developpement des Encephalopathies Spongiformes Transmissibles (EST). Sa maturation physiologique produit un fragment N-terminal soluble, N1 et sa contrepartie C-terminale C1, ancree a la memb