Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Philippe Tixador"'
Autor:
Elodie Bosc, Julie Anastasie, Feryel Soualmia, Pascale Coric, Ju Youn Kim, Lily Q. Wang, Gullen Lacin, Kaitao Zhao, Ronak Patel, Eric Duplus, Philippe Tixador, Andrew A. Sproul, Bernard Brugg, Michelle Reboud-Ravaux, Carol M. Troy, Michael L. Shelanski, Serge Bouaziz, Michael Karin, Chahrazade El Amri, Etienne D. Jacotot
Publikováno v:
Cell Death and Disease, Vol 13, Iss 11, Pp 1-14 (2022)
Abstract Caspase-2 (Casp2) is a promising therapeutic target in several human diseases, including nonalcoholic steatohepatitis (NASH) and Alzheimer’s disease (AD). However, the design of an active-site-directed inhibitor selective to individual cas
Externí odkaz:
https://doaj.org/article/e2ca2ef1c4d34003bb95c448c8eb4433
Autor:
Simona Gribaudo, Philippe Tixador, Luc Bousset, Alexis Fenyi, Patricia Lino, Ronald Melki, Jean-Michel Peyrin, Anselme L. Perrier
Publikováno v:
Stem Cell Reports, Vol 12, Iss 2, Pp 230-244 (2019)
Summary: Reappraisal of neuropathological studies suggests that pathological hallmarks of Alzheimer’s disease and Parkinson’s disease (PD) spread progressively along predictable neuronal pathways in the human brain through unknown mechanisms. Alt
Externí odkaz:
https://doaj.org/article/78075f0f658f496daa415520c4690dc1
Autor:
Vincent Béringue, Philippe Tixador, Olivier Andréoletti, Fabienne Reine, Johan Castille, Thanh-Lan Laï, Annick Le Dur, Aude Laisné, Laetitia Herzog, Bruno Passet, Human Rezaei, Jean-Luc Vilotte, Hubert Laude
Publikováno v:
PLoS Pathogens, Vol 16, Iss 7, p e1008283 (2020)
Prions are pathogens formed from abnormal conformers (PrPSc) of the host-encoded cellular prion protein (PrPC). PrPSc conformation to disease phenotype relationships extensively vary among prion strains. In particular, prions exhibit a strain-depende
Externí odkaz:
https://doaj.org/article/5a6d7bcf05644281979b0d12312a5022
Autor:
Aurélie Alleaume-Butaux, Simon Nicot, Mathéa Pietri, Anne Baudry, Caroline Dakowski, Philippe Tixador, Hector Ardila-Osorio, Anne-Marie Haeberlé, Yannick Bailly, Jean-Michel Peyrin, Jean-Marie Launay, Odile Kellermann, Benoit Schneider
Publikováno v:
PLoS Pathogens, Vol 11, Iss 8, p e1005073 (2015)
In prion diseases, synapse dysfunction, axon retraction and loss of neuronal polarity precede neuronal death. The mechanisms driving such polarization defects, however, remain unclear. Here, we examined the contribution of RhoA-associated coiled-coil
Externí odkaz:
https://doaj.org/article/f1c7ab37f8994140b4f83ce0e621baa2
Autor:
Florent Laferrière, Philippe Tixador, Mohammed Moudjou, Jérôme Chapuis, Pierre Sibille, Laetitia Herzog, Fabienne Reine, Emilie Jaumain, Hubert Laude, Human Rezaei, Vincent Béringue
Publikováno v:
PLoS Pathogens, Vol 9, Iss 10, p e1003702 (2013)
Prions are proteinaceous infectious agents responsible for fatal neurodegenerative diseases in animals and humans. They are essentially composed of PrP(Sc), an aggregated, misfolded conformer of the ubiquitously expressed host-encoded prion protein (
Externí odkaz:
https://doaj.org/article/e8c310abcac44b519a47452d7bd5e961
Autor:
Philippe Tixador, Laëtitia Herzog, Fabienne Reine, Emilie Jaumain, Jérôme Chapuis, Annick Le Dur, Hubert Laude, Vincent Béringue
Publikováno v:
PLoS Pathogens, Vol 6, Iss 4, p e1000859 (2010)
Prions are unconventional infectious agents thought to be primarily composed of PrP(Sc), a multimeric misfolded conformer of the ubiquitously expressed host-encoded prion protein (PrP(C)). They cause fatal neurodegenerative diseases in both animals a
Externí odkaz:
https://doaj.org/article/530c85bcc5e94f2588c40a6bac14eedf
Autor:
Vincent Béringue, Annick Le Dur, Philippe Tixador, Fabienne Reine, Laurence Lepourry, Armand Perret-Liaudet, Stéphane Haïk, Jean-Luc Vilotte, Michel Fontés, Hubert Laude
Publikováno v:
PLoS ONE, Vol 3, Iss 1, p e1419 (2008)
BackgroundThe evolution of the variant Creutzfeldt-Jakob disease (vCJD) epidemic is hazardous to predict due to uncertainty in ascertaining the prevalence of infection and because the disease might remain asymptomatic or produce an alternate, sporadi
Externí odkaz:
https://doaj.org/article/e7f0eade8b06464f8dd4852ff4d632c8
Crossing Species Barriers Relies on Structurally Distinct Prion Assemblies and Their Complementation
Autor:
Juan María Torres, Angélique Igel-Egalon, Mohammed Moudjou, Florent Laferrière, Laetitia Herzog, Philippe Tixador, Hubert Laude, Fabienne Reine, Human Rezaei, Vincent Béringue
Publikováno v:
Molecular Neurobiology
Molecular Neurobiology, 2020, 57 (6), pp.2572-2587. ⟨10.1007/s12035-020-01897-3⟩
Molecular Neurobiology, Humana Press, 2020, 57 (6), pp.2572-2587. ⟨10.1007/s12035-020-01897-3⟩
Molecular Neurobiology, 2020, 57 (6), pp.2572-2587. ⟨10.1007/s12035-020-01897-3⟩
Molecular Neurobiology, Humana Press, 2020, 57 (6), pp.2572-2587. ⟨10.1007/s12035-020-01897-3⟩
International audience; Prion replication results from the autocatalytic templated assisted conversion of the host-encoded prion protein PrPC into misfolded, polydisperse PrPSc conformers. Structurally distinct PrPSc conformers can give rise to multi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::125d51db48eca92161d326a7e414fb46
https://hal.science/hal-03401965/document
https://hal.science/hal-03401965/document
Autor:
Laetitia Herzog, Hubert Laude, Juan María Torres, Vincent Béringue, Mohammed Moudjou, Florent Laferrière, Human Rezaei, Philippe Tixador, Fabienne Reine, Angélique Igel-Egalon
Backgroundprion replication results from the autocatalytic templated assisted conversion of the host-encoded prion protein PrPCinto misfolded, polydisperse PrPSc conformers. Structurally distinct PrPScconformers can give rise to multiple prion strain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bff04283cd3b9944d2fc73527487280
https://doi.org/10.1101/861278
https://doi.org/10.1101/861278
Autor:
Josquin Courte, Alban Bessede, Benjamin Lassus, Chai K. Lim, Vanessa Tan, Philippe Tixador, Jean-Michel Peyrin, Gilles J. Guillemin
Publikováno v:
Neurotoxicity Research. 33:62-75
β-Methylamino-L-alanine (BMAA) is implicated in neurodegeneration and neurotoxicity, particularly in ALS-Parkinson Dementia Complex. Neurotoxic properties of BMAA have been partly elucidated, while its transcellular spreading capacity has not been e