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X-WR-CALNAME:Bordeaux Neurocampus
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X-WR-CALDESC:Events for Bordeaux Neurocampus
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DTSTART:20260329T010000
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DTSTART:20261025T010000
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DTSTART;VALUE=DATE:20260922
DTEND;VALUE=DATE:20260924
DTSTAMP:20261006T143425
CREATED:20260403T110641Z
LAST-MODIFIED:20260601T123148Z
UID:196963-1790035200-1790207999@www.bordeaux-neurocampus.fr
SUMMARY:Searching for Principles in Motor Control
DESCRIPTION:Venue: Centre Broca \n\nWorkshop from 22 September 2pm to 23 September 1pm \nSpeakers\nIsabelle Vivodtzev (Institut de Biologie Paris Seine)\nDavid Thura (Lyon Neuroscience Research Centre)\nPauline Maurice (LORIA\, Nancy)\nLuc Estebanez (NeuroPSI\, Saclay)\nOrganizing committee\nGrégory Barrière (CNRS\, Institut de Neurosciences Cognitives et Intégratives d’Aquitaine)\nLaurent Juvin (Univ. Bordeaux\,Institut de Neurosciences Cognitives et Intégratives d’Aquitaine)\nNicolas Mallet (CNRS\, Institut des Maladies Neurodégénératives)\nFabien Wagner(CNRS\, Institut des Maladies Neurodégénératives)\nAymar de Rugy (CNRS\, Institut de Neurosciences Cognitives et Intégratives d’Aquitaine)\nOral presentation selection with the collaboration of  Muriel Thoby-Brisson (Inserm\,Institut de Neurosciences Cognitives et Intégratives d’Aquitaine) \nRegistration\nThe Registration is free but Mandatory through this website\, with a limit of 140 participant : https://motorconf-2026.sciencesconf.org/ \n
URL:https://www.bordeaux-neurocampus.fr/en/event/searching-for-principles-in-motor-control/
CATEGORIES:For scientists,home-event,IMN,Symposium
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BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260923T093000
DTEND;TZID=Europe/Paris:20260923T093000
DTSTAMP:20261006T143425
CREATED:20260827T082334Z
LAST-MODIFIED:20260827T091330Z
UID:205346-1790155800-1790155800@www.bordeaux-neurocampus.fr
SUMMARY:Thesis defense - Tess Bonnard
DESCRIPTION:Venue: BBS \nDefense in french \n\nTess Bonnard\nINCIA \nTitle\nVestibular integration in modified gravity and motion sickness \nAbstract\nMotion sickness arises from conflicts between sensory signals\, particularly those originating from the vestibular system. However\, its underlying mechanisms remain poorly understood\, especially in the case of space motion sickness\, which affects astronauts during exposure to weightlessness. \nThis thesis compares space motion sickness\, reproduced during parabolic flights\, with terrestrial motion sickness induced by virtual reality. It investigates the associated sensory conflicts and physiological responses. \nVestibular perception of rotational movements is impaired in weightlessness\, whereas the perception of translational movements remains accurate. In the presence of sensory conflict\, the sensory input signaling motion appears to be weighted more strongly than the others during the integration and comparison of sensory signals. Sleep quality influences susceptibility to space motion sickness\, and facial colorimetry emerges as an objective indicator of symptom severity. \nThese findings contribute to a better understanding of the mechanisms underlying motion sickness and provide new perspectives for the development of preventive strategies. \nPublications\n\nBonnard\, T.\, Doat\, E.\, Cazalets\, J.\, Guehl\, D.\, & Guillaud\, E. (2025). Visual and vestibular reweighting after cyber‐ and space‐sickness. Experimental Physiology\, 111(1)\, 240‑256. https://doi.org/10.1113/ep092966\nBonnard\, T.\, Morello\, A.\, Doat\, E.\, Cazalets\, J.\, Guehl\, D.\, & Guillaud\, E. (2026). Resilience of otolithic reflex to gravitational changes. Npj Microgravity\, 12(1). https://doi.org/10.1038/s41526-026-00599-9\nBonnard\, T.\, Araka\, L.\, Reina\, A. S.\, Van Berkel\, J.\, Morvan\, C.\, Morgat\, C.\, Guehl\, D.\, Guillaud\, E.\, & Altena\, E. (2026). Sleep’s influence on susceptibility to motion sickness in parabolic flights and virtual reality : An exploratory study. Journal Of Vestibular Research\, 9574271261474571. https://doi.org/10.1177/09574271261474571\nBonnard\, T.\, Doat\, E.\, Cazalets\, J.\, Morgat\, C.\, Guehl\, D.\, & Guillaud\, E. (2026). Turning green in microgravity : facial color changes as best physiological indicator of space sickness. bioRxiv (Cold Spring Harbor Laboratory). https://doi.org/10.64898/2026.03.06.708504\nBonnard\, T.\, Doat\, E.\, Guehl\, D.\, & Guillaud\, E. (2026). Swung and spun in weightlessness : Evidence of immediate canalar underdetection of rotations in parabolic flight. bioRxiv (Cold Spring Harbor Laboratory). https://doi.org/10.64898/2026.06.30.735470\n\nJury\n\nM. Etienne Guillaud – CNRS – Directeur de thèse\nMme Gaelle Quark – Université de Caen – Rapporteure\nM. Lionel Bringoux – Université Aix Marseille – Rapporteur\nMme Guillemette Gauquelin-Koch – Centre national d’études spatiales (CNES) – Examinatrice\nMme Valérie Franco-Vidal – Centre universitaire hospitalier de Bordeaux – Examinatrice\nM. Jordan Navarro – Université Lumière Lyon 2 – Examinateur\n\n
URL:https://www.bordeaux-neurocampus.fr/en/event/thesis-defense-tess-bonnard/
CATEGORIES:Thesis
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BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260923T140000
DTEND;TZID=Europe/Paris:20260923T140000
DTSTAMP:20261006T143425
CREATED:20260604T204645Z
LAST-MODIFIED:20260903T140421Z
UID:201291-1790172000-1790172000@www.bordeaux-neurocampus.fr
SUMMARY:Thesis defense - Ludivine Sabatier
DESCRIPTION:Venue: CARF \nThesis defended in french \n \n\nIMN\nTeam: SynTeam \nThesis directed by Florent Laferrière \nTitle\nAlpha-synuclein cerebral amyloids in synucleinopathies: quantification\, bioactivity and strain properties \nAbstract\nThe presence of proteinaceous inclusions primarily composed of alpha-synuclein (a-syn)\, a protein naturally present in the brain\, is the hallmark of synucleinopathies\, a group of neurodegenerative diseases. These include multiple system atrophy (MSA)\, Parkinson’s disease (PD)\, and dementia with Lewy bodies. Within inclusion bodies\, a-syn is found in the form of amyloid fibrils. By analogy with prion diseases\, it is now generally accepted that synucleinopathies represent distinct a-syn strains. The molecular basis of their divergent phenotypes lies in the structure of the protein’s amyloid assemblies\, which differs across these pathologies. The bioactivity of an amyloid – its ability to recruit normal a-syn\, induce its aggregation and propagate the pathology – constitutes\, alongside structure\, a strain property. However\, the precise links between structure and bioactivity remain to be established. \nNumerous studies have shown that fibrils derived from MSA samples are more bioactive than those from PD samples. Although these studies attempted to normalize or quantify amyloids\, we identified several biases related to their identification and quantification\, such that these bioactivity measurements may reflect differences in dose rather than in specific bioactivity – i.e. relative to the amount of amyloids. Furthermore\, a structural heterogeneity of fibrils exists within MSA itself\, but the functional consequences of this heterogeneity remain to be determined. \nTo this end\, our study first focused on the identification of methodological biases\, before developing procedures enabling unbiased measurement of the amount of amyloid a-syn in biological samples. We established native blotting methods (drop-blot and filter-blot)\, which allow evaluation of the relative amyloid load in samples through immunolabelling with specific antibody pairs that we identified. Moreover\, as some commercial ELISAs do not allow accurate measurement of a-syn amyloids\, due to the use of inappropriate antibodies\, we developed two in-house ELISA assays: one detecting all a-syn species\, and a second specifically and absolutely quantifying amyloid assemblies. \nThanks to the development of these tools\, we were able to accurately quantify amyloid a-syn present in brain samples from synucleinopathy patients\, in order to determine their specific bioactivity. We chose to use a HEK-hSyn-YFP reporter cell line as a model. \nThese in vitro studies showed that fibrils contained in MSA brains are more bioactive than PD fibrils\, both when using crude brain homogenates or amyloid-enriched samples obtained by biochemical fractionation from the same brain tissues. Remarkably\, by extending these measurements to different brain regions across different patients\, we were able to demonstrate that the bioactivity of MSA fibrils was distinct depending on the patient from whom they were derived\, while this property was conserved across brain regions within a given patient. These data document the existence of amyloid sub-strain populations within a single strain. This corroborates studies that revealed structural diversity among MSA filaments from different patients. Our work further indicates the absence of notable structural evolution during the course of cerebral disease progression. \nBiochemical and functional characterization of the in vitro-generated aggregates will determine whether the strain properties of the brain-derived amyloids are conserved upon replication. \nKey words\nAlpha-synuclein\, protein aggregates\, amyloids\, neurodegenerative diseases \nPublications\nBiases in α-synuclein immuno-quantitation: a core problem for basic and ancillary studies of Parkinson’s disease and multiple system atrophy.\nLaferrière F\, Sabatier L\, Claverol S\, De Giorgi F\, Ichas F. Transl Neurodegener. 2024 Mar 25;13(1):15. doi: 10.1186/s40035-024-0040. PMID: 38528639 \nJury\nDr. REZAEI Human\, DR INRAE\, Université Paris-Saclay Rapporteur\nDr. TORRENT Joan\, CRHC INSERM\, Université de Montpellier Rapporteur\nDr. LECOMTE Sophie\, DR CNRS\, Université de Bordeaux Examinatrice\nDr. EL MAMMERI Nadia\, CR CNRS\, Université de Bordeaux Examinatrice \n
URL:https://www.bordeaux-neurocampus.fr/en/event/soutenance-de-these-ludivine-sabatier/
CATEGORIES:IMN,Thesis
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