Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Nathan Riguet"'
Autor:
Khalid A. Ibrahim, Kristin S. Grußmayer, Nathan Riguet, Lely Feletti, Hilal A. Lashuel, Aleksandra Radenovic
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-11 (2023)
Abstract Protein misfolding and aggregation play central roles in the pathogenesis of various neurodegenerative diseases (NDDs), including Huntington’s disease, which is caused by a genetic mutation in exon 1 of the Huntingtin protein (Httex1). The
Externí odkaz:
https://doaj.org/article/377d5977bf6544cea4a57377a3f9148c
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 20, Iss , Pp 309-321 (2022)
The pathological growth of amyloid fibrils in neurons underlies the progression of neurodegenerative diseases including Alzheimer’s and Parkinson’s disease. Fibrils form when soluble monomers oligomerise in the cytoplasm. Their subsequent growth
Externí odkaz:
https://doaj.org/article/b0d215c584c74e0e9efd0098b077893b
Autor:
Nathan Riguet, Anne-Laure Mahul-Mellier, Niran Maharjan, Johannes Burtscher, Marie Croisier, Graham Knott, Janna Hastings, Alice Patin, Veronika Reiterer, Hesso Farhan, Sergey Nasarov, Hilal A. Lashuel
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-27 (2021)
The mechanisms underlying Huntingtin protein (Htt) aggregation are not fully understood. Here the authors perform a detailed investigation of the ultrastructural and biochemical properties of huntingtin cytoplasmic and nuclear inclusions, and reveal
Externí odkaz:
https://doaj.org/article/81663cd6def2472ea737c63e01d4fdd8
Autor:
Florence E. Layburn, Adelie Y.S. Tan, Nasim F. Mehrabi, Maurice A. Curtis, Lynette J. Tippett, Clinton P. Turner, Nathan Riguet, Lorène Aeschbach, Hilal A. Lashuel, Mike Dragunow, Richard L.M. Faull, Malvindar K. Singh-Bains
Publikováno v:
Neurobiology of Disease, Vol 174, Iss , Pp 105884- (2022)
Huntington's disease (HD) is caused by a CAG repeat expansion mutation in the gene encoding the huntingtin (Htt) protein, with mutant Htt protein subsequently forming aggregates within the brain. Mutant Htt is a current target for novel therapeutic s
Externí odkaz:
https://doaj.org/article/682f2366ef5b465c8aba8d90bd1270c5
Publikováno v:
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal, Vol 20, Iss, Pp 309-321 (2022)
Computational and Structural Biotechnology Journal, Vol 20, Iss, Pp 309-321 (2022)
Graphical abstract
Highlights • Fluorescent tags modify the surface and interactome of amyloid fibrils. • Thermal fluctuations of GFP tags create a size-dependent sieve around a fibril. • High molecular weight proteins are preferentially e
Highlights • Fluorescent tags modify the surface and interactome of amyloid fibrils. • Thermal fluctuations of GFP tags create a size-dependent sieve around a fibril. • High molecular weight proteins are preferentially e
Autor:
Florence E. Layburn, Adelie Y. S. Tan, Nasim F. Mehrabi, Maurice A. Curtis, Lynette J. Tippett, Nathan Riguet, Lorène Aeschbach, Hilal A. Lashuel, Mike Dragunow, Richard L. M. Faull, Malvindar K. Singh-Bains
Huntington’s disease (HD) is caused by a CAG repeat expansion mutation in the gene encoding the huntingtin (Htt) protein, with mutant Htt protein subsequently forming aggregates within the brain. Mutant Htt is a current target for novel therapeutic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::754ea9bcb712809b61a79184bb834350
https://doi.org/10.1101/2022.05.03.490349
https://doi.org/10.1101/2022.05.03.490349
Autor:
Hilal A. Lashuel, Giovanni Dietler, Urszula Cendrowska, Anass Chiki, Sean M. DeGuire, Nathan Riguet, Francesco S. Ruggeri, Anne-Laure Mahul-Mellier, Sophie Vieweg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9f0613b886a2e99d7ccb78bc654fc96f
https://doi.org/10.15252/rc.2022402060
https://doi.org/10.15252/rc.2022402060
Autor:
Hesso Farhan, Nathan Riguet, Graham Knott, Alice Patin, Veronika Reiterer, Niran Maharjan, Anne-Laure Mahul-Mellier, Sergey Nasarov, Janna Hastings, Marie Croisier, Hilal A. Lashuel, Johannes Burtscher
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-27 (2021)
Nature Communications
Nature Communications
Despite the strong evidence linking the aggregation of the Huntingtin protein (Htt) to the pathogenesis of Huntington’s disease (HD), the mechanisms underlying Htt aggregation and neurodegeneration remain poorly understood. Herein, we investigated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1beb61f696ae4c4981d1f362b39dd69f
https://doi.org/10.1101/2020.07.29.226977
https://doi.org/10.1101/2020.07.29.226977
Autor:
Bryan Frey, Matthew P. Jackson, James A. Duce, Abdelrahman AlOkda, Nathan Riguet, Hilal A. Lashuel
Publikováno v:
Journal of Neurochemistry
Bimolecular fluorescence complementation (BiFC) was introduced a decade ago as a method to monitor alpha‐synuclein (α‐syn) oligomerization in intact cells. Since then, several α‐syn BiFC cellular assays and animal models have been developed b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25d467fb3fc814c02d6deeda6422fcfe
Autor:
Florence E, Layburn, Adelie Y S, Tan, Nasim F, Mehrabi, Maurice A, Curtis, Lynette J, Tippett, Clinton P, Turner, Nathan, Riguet, Lorène, Aeschbach, Hilal A, Lashuel, Mike, Dragunow, Richard L M, Faull, Malvindar K, Singh-Bains
Huntington's disease (HD) is caused by a CAG repeat expansion mutation in the gene encoding the huntingtin (Htt) protein, with mutant Htt protein subsequently forming aggregates within the brain. Mutant Htt is a current target for novel therapeutic s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02ee3c1478760134f05dcd9b78296648
https://infoscience.epfl.ch/record/298677
https://infoscience.epfl.ch/record/298677