Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Inger Lauritzen"'
Autor:
Inger Lauritzen, Anaïs Bécot, Alexandre Bourgeois, Raphaëlle Pardossi-Piquard, Maria-Grazia Biferi, Martine Barkats, Fréderic Checler
Publikováno v:
Translational Neurodegeneration, Vol 8, Iss 1, Pp 1-17 (2019)
Abstract Background We recently demonstrated an endolysosomal accumulation of the β-secretase-derived APP C-terminal fragment (CTF) C99 in brains of Alzheimer disease (AD) mouse models. Moreover, we showed that the treatment with the γ-secretase in
Externí odkaz:
https://doaj.org/article/027cf11112fc4c188a93980afe965595
Autor:
Anaïs Bécot, Raphaëlle Pardossi-Piquard, Alexandre Bourgeois, Eric Duplan, Qingli Xiao, Abhinav Diwan, Jin-Moo Lee, Inger Lauritzen, Frédéric Checler
Publikováno v:
Cells, Vol 9, Iss 5, p 1204 (2020)
Brains that are affected by Alzheimer’s disease (AD) are characterized by the overload of extracellular amyloid β (Aβ) peptides, but recent data from cellular and animal models propose that Aβ deposition is preceded by intraneuronal accumulation
Externí odkaz:
https://doaj.org/article/04bb316409824a829defe16053ebd53c
Autor:
Elissa Afram, Inger Lauritzen, Alexandre Bourgeois, Wejdane El Manaa, Eric Duplan, Mounia Chami, Audrey Valverde, Charlotte Bauer, Raphaëlle Pardossi-Piquard, Frederic Checler
Publikováno v:
Cellular and Molecular Life Sciences. 80
The processing of the amyloid precursor protein (APP) is one of the key events contributing to Alzheimer’s disease (AD) etiology. Canonical cleavages by β- and γ-secretases lead to Aβ production which accumulate in amyloid plaques. Recently, the
Autor:
Thomas Goiran, Vanessa Alexandra Morais, Mounia Chami, Umut Ozcan, Loan Vaillant Beuchot, Frédéric Checler, Mario Salazar, Han You, Sandra Lacas-Gervais, Wejdane El Manaa, Cristine Alves da Costa, Eric Duplan, Inger Lauritzen, Ling Qi
Publikováno v:
Autophagy
article-version (VoR) Version of Record
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
article-version (VoR) Version of Record
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
© 2021 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/
Autor:
Julie Cazareth, Raphaëlle Pardossi-Piquard, Arnaud Mary, Inger Lauritzen, Renaud Bussiere, Alexandre Bourgeois, Véronique Paquis-Flucklinger, Sandra Lacas-Gervais, Paula Fernanda Kinoshita, Konstantina Fragaki, Frédéric Checler, Loan Vaillant-Beuchot, Rosanna Mary, Mounia Chami, Valérie Buée-Scherrer, Sophie Pagnotta, Cécile Martin, Fanny Eysert, Charlotte Bauer, Céline Badot, Luc Buée
Publikováno v:
Acta Neuropathologica
Acta Neuropathologica, Springer Verlag, 2020, ⟨10.1007/s00401-020-02234-7⟩
Acta Neuropathologica, Springer Verlag, 2020, ⟨10.1007/s00401-020-02234-7⟩
Several lines of recent evidence indicate that the amyloid precursor protein-derived C-terminal fragments (APP-CTFs) could correspond to an etiological trigger of Alzheimer’s disease (AD) pathology. Altered mitochondrial homeostasis is considered a
Autor:
Inger Lauritzen, Raphaëlle Pardossi-Piquard, Frédéric Checler, Anaïs Bécot, Alexandre Bourgeois
Publikováno v:
Current Alzheimer Research
Current Alzheimer Research, Bentham Science Publishers, 2019, 16 (5), pp.453-457. ⟨10.2174/1567205016666190325092841⟩
Current Alzheimer Research, Bentham Science Publishers, 2019, 16 (5), pp.453-457. ⟨10.2174/1567205016666190325092841⟩
Background: Alzheimer’s disease (AD) is associated with extracellular accumulation and aggregation of amyloid β (Aβ) peptides ultimately seeding in senile plaques. Recent data show that their direct precursor C99 (βCTF) also accumulates in AD-af
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2021, 296, pp.100489. ⟨10.1016/j.jbc.2021.100489⟩
The Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2021, 296, pp.100489. ⟨10.1016/j.jbc.2021.100489⟩
The Journal of Biological Chemistry
Genetic, biochemical, and anatomical grounds led to the proposal of the amyloid cascade hypothesis centered on the accumulation of amyloid beta peptides (Aβ) to explain Alzheimer's disease (AD) etiology. In this context, a bulk of efforts have aimed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7369894a2aa1da28201c7ede1ccfab27
https://hal.archives-ouvertes.fr/hal-03369883/document
https://hal.archives-ouvertes.fr/hal-03369883/document
Autor:
Raphaëlle Pardossi-Piquard, Frédéric Checler, Jin-Moo Lee, Inger Lauritzen, Qingli Xiao, Anaïs Bécot, Eric Duplan, Abhinav Diwan, Alexandre Bourgeois
Publikováno v:
Cells
Cells, Vol 9, Iss 1204, p 1204 (2020)
Cells, MDPI, 2020, 9 (5), ⟨10.3390/cells9051204⟩
Volume 9
Issue 5
Cells, Vol 9, Iss 1204, p 1204 (2020)
Cells, MDPI, 2020, 9 (5), ⟨10.3390/cells9051204⟩
Volume 9
Issue 5
Brains that are affected by Alzheimer&rsquo
s disease (AD) are characterized by the overload of extracellular amyloid &beta
(A&beta
) peptides, but recent data from cellular and animal models propose that A&beta
deposition is prec
s disease (AD) are characterized by the overload of extracellular amyloid &beta
(A&beta
) peptides, but recent data from cellular and animal models propose that A&beta
deposition is prec
Autor:
Alexandre Bourgeois, Martine Barkats, Inger Lauritzen, Raphaëlle Pardossi-Piquard, Maria-Grazia Biferi, Frédéric Checler, Anaïs Bécot
Publikováno v:
Translational Neurodegeneration
Translational Neurodegeneration, [London] : BioMed Central, 2012-, 2019, 8 (1), ⟨10.1186/s40035-019-0176-6⟩
Translational Neurodegeneration, Vol 8, Iss 1, Pp 1-17 (2019)
Translational Neurodegeneration, [London] : BioMed Central, 2012-, 2019, 8, ⟨10.1186/s40035-019-0176-6⟩
Translational Neurodegeneration, [London] : BioMed Central, 2012-, 2019, 8 (1), ⟨10.1186/s40035-019-0176-6⟩
Translational Neurodegeneration, Vol 8, Iss 1, Pp 1-17 (2019)
Translational Neurodegeneration, [London] : BioMed Central, 2012-, 2019, 8, ⟨10.1186/s40035-019-0176-6⟩
BackgroundWe recently demonstrated an endolysosomal accumulation of the β-secretase-derived APP C-terminal fragment (CTF) C99 in brains of Alzheimer disease (AD) mouse models. Moreover, we showed that the treatment with the γ-secretase inhibitor (D
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edfc8b0e8451b44f6d787dd526cb4f11
https://hal.archives-ouvertes.fr/hal-02556329
https://hal.archives-ouvertes.fr/hal-02556329
Autor:
Alain Lacampagne, Andrew R. Marks, Steven Reiken, Clark A. Briggs, Xiaoping Liu, Ottavio Arancio, Andrew F. Teich, Shreaya Chakroborty, Charlotte Bauer, Michael L. Shelanski, Nathalie Saint, Inger Lauritzen, Fabrice Duprat, Grace E. Stutzmann, Mounia Chami, Frédéric Checler, Ran Zalk, Renaud Bussiere, Albano C. Meli
Publikováno v:
Acta Neuropathologica
Acta Neuropathologica, Springer Verlag, 2017, 134 (5), pp.749-767. ⟨10.1007/s00401-017-1733-7⟩
Acta Neuropathologica, Springer Verlag, 2017, 134 (5), pp.749-767. ⟨10.1007/s00401-017-1733-7⟩
The mechanisms underlying ryanodine receptor (RyR) dysfunction associated with Alzheimer disease (AD) are still not well understood. Here, we show that neuronal RyR2 channels undergo post-translational remodeling (PKA phosphorylation, oxidation, and