Reversible unfolding of infectious prion assemblies reveals the existence of an oligomeric elementary brick.

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

High-Pressure Response of Amyloid Folds

Autor: Joan Torrent, Davy Martin, Angélique Igel-Egalon, Vincent Béringue, Human Rezaei

Publikováno v: Viruses, Vol 11, Iss 3, p 202 (2019)

The abnormal protein aggregates in progressive neurodegenerative disorders, such as Alzheimer’s, Parkinson’s and prion diseases, adopt a generic structural form called amyloid fibrils. The precise amyloid fold can differ between patients and thes

Externí odkaz: https://doaj.org/article/03e551de4805462cbe1f9674c04748f1

An alternative model to prion fragmentation based on the detailed balance between PrPSc and suPrP

Autor: Christopher Eblen, Human Rezaei, Monique Chyba, Yuliia Kravchenko, Vincent Béringue, Angélique Igel-Egalon, Jakob Kotas

SummaryPrion assemblies responsible for transmissible spongiform encephalopathies grow in the form of linear amyloid fibrils. Traditional models for prion growth and tissue-spreading have relied upon the assumption that propagation is based on the pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd640d1c318b4af61cebd8044f63177f
https://doi.org/10.1101/2020.04.24.058917

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⟩

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

Early stage prion assembly involves two subpopulations with different quaternary structures and a secondary templating pathway

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)

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