Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Tina Knäpple"'
Autor:
Angélique Igel-Egalon, Mohammed Moudjou, Davy Martin, Alexandra Busley, Tina Knäpple, Laetitia Herzog, Fabienne Reine, Nad'a Lepejova, Charles-Adrien Richard, Vincent Béringue, Human Rezaei
Publikováno v:
PLoS Pathogens, Vol 13, Iss 9, p e1006557 (2017)
Mammalian prions, the pathogens that cause transmissible spongiform encephalopathies, propagate by self-perpetuating the structural information stored in the abnormally folded, aggregated conformer (PrPSc) of the host-encoded prion protein (PrPC). To
Externí odkaz:
https://doaj.org/article/17a6d625b8d94d58ad6b519bcdcc0de7
Autor:
Vincent Béringue, Laetitia Herzog, Fabienne Reine, Jan Bohl, Christelle Jas-Duval, Mohammed Moudjou, Mathieu Mezache, Tina Knäpple, Florent Laferrière, Marie Doumic, Human Rezaei, Angélique Igel-Egalon
Publikováno v:
Communications Biology
Communications Biology, Nature Publishing Group, 2019, 2, ⟨10.1038/s42003-019-0608-y⟩
Communications Biology, Nature Publishing Group, 2019, 2 (1), pp.1-13. ⟨10.1038/s42003-019-0608-y⟩
Communications Biology, Nature Publishing Group, 2019, 2 (1), ⟨10.1038/s42003-019-0608-y⟩
Communications Biology, 2019, 2 (1), pp.1-13. ⟨10.1038/s42003-019-0608-y⟩
Communications Biology, Vol 2, Iss 1, Pp 1-13 (2019)
Communications Biology (2), 1-13. (2019)
Communications Biology, Nature Publishing Group, 2019, 2, ⟨10.1038/s42003-019-0608-y⟩
Communications Biology, Nature Publishing Group, 2019, 2 (1), pp.1-13. ⟨10.1038/s42003-019-0608-y⟩
Communications Biology, Nature Publishing Group, 2019, 2 (1), ⟨10.1038/s42003-019-0608-y⟩
Communications Biology, 2019, 2 (1), pp.1-13. ⟨10.1038/s42003-019-0608-y⟩
Communications Biology, Vol 2, Iss 1, Pp 1-13 (2019)
Communications Biology (2), 1-13. (2019)
The dynamics of aggregation and structural diversification of misfolded, host-encoded proteins in neurodegenerative diseases are poorly understood. In many of these disorders, including Alzheimer’s, Parkinson’s and prion diseases, the misfolded p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a7e971a289e198b553cd7689b31c66d
https://hal.archives-ouvertes.fr/hal-03401986/document
https://hal.archives-ouvertes.fr/hal-03401986/document
Autor:
F. Lafferriere, Marie Doumic, Angélique Igel-Egalon, Laetitia Herzog, Vincent Béringue, Tina Knäpple, Mohammed Moudjou, Fabienne Reine, Human Rezaei, M. Merzach
Aggregation of misfolded forms from host-encoded proteins is key to the pathogenesis of a number of neurodegenerative disorders, including prion diseases, Alzheimer’s disease and Parkinson’s disease. In prion diseases, the cellular prion protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d30501fd6085473679df435b20d1ced9
Autor:
Tina Knäpple, Mohammed Moudjou, Alexandra Busley, Davy Martin, Nad’a Lepejova, Charles-Adrien Richard, Human Rezaei, Laetitia Herzog, Angélique Igel-Egalon, Fabienne Reine, Vincent Béringue
Publikováno v:
PLoS Pathogens
Plos Pathogens 9 (13), . (2017)
PLoS Pathogens, Public Library of Science, 2017, 13 (9), ⟨10.1371/journal.ppat.1006557⟩
PLoS Pathogens, Vol 13, Iss 9, p e1006557 (2017)
Plos Pathogens 9 (13), . (2017)
PLoS Pathogens, Public Library of Science, 2017, 13 (9), ⟨10.1371/journal.ppat.1006557⟩
PLoS Pathogens, Vol 13, Iss 9, p e1006557 (2017)
Mammalian prions, the pathogens that cause transmissible spongiform encephalopathies, propagate by self-perpetuating the structural information stored in the abnormally folded, aggregated conformer (PrPSc) of the host-encoded prion protein (PrPC). To