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X-WR-CALNAME:Bordeaux Neurocampus
X-ORIGINAL-URL:https://www.bordeaux-neurocampus.fr/en/
X-WR-CALDESC:Events for Bordeaux Neurocampus
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DTSTART:20230326T010000
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DTSTART:20231029T010000
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DTSTART;VALUE=DATE:20231024
DTEND;VALUE=DATE:20231110
DTSTAMP:20260410T160727
CREATED:20221122T113608Z
LAST-MODIFIED:20231109T141649Z
UID:152946-1698105600-1699574399@www.bordeaux-neurocampus.fr
SUMMARY:Cajal lectures: Advanced techniques for synapse biology
DESCRIPTION:Venue: CGFB \nFree access \n\nOctober 24 – 9:00am \nCécile Charrier (Institute of Biology\, École Normale Supérieure\, France)\nMolecular mechanisms of synaptic development: insights from a human-specific gene. \nOctober 24 – 11:00am \nBrian Mac Cabe (EPFL\, Lausanne\, Swiss)\nUnknown knowns of Drosophila synapses. \nOctober 26 – 9:00am\n Noa Lipstein (LeibnizFMP\, Germany)\nSynaptic transmission in health and disease. \nOctober 26 – 11:00am\n Julie Perroy (IGF\, University of Montpellier\, France)\nMolecular dynamics at glutamatergic synapses and beyond. \nOctober 28 – 9:00am \nJosef Kittler (University College London\, UK)\nMolecular mechanism of inhibitory synapse formation and plasticity. \nOctober 30 – 9:00am \nDaniel Choquet (CNRS/University of Bordeaux\, France)\nNanoscale synapse organization and function. \nNovember 2 – 9:00am \nMarina Mikhaylova (Humboldt University \, Germany)\nCalcium and synaptic heterogeneity. \nNovember 3 – 9:00am\nRosa Paolicelli (University of Lausanne\, Swiss)\nMicroglia: key players in synapse remodeling in the healthy and diseased brain. \nNovember 3 – 11:00am \nAlfredo Kirkwood (Johns Hopkins University\, USA)\nPrinciples of Hebbian\, Pavlovian and Homeostatic synaptic plasticity. \nNovember 6 – 9:00am \nJuan Burrone (King’s College London\, UK)\nThe emergence and plasticity of inhibitory synapses: from dendrites to the axon initial segment. \nNovember 6 – 11:00am \nAxion BioSystems : Presentation \nNovember 7 – 9:00am \nNael Nadif Kasri (Radboud University Medical Center\, Netherlands)\nLeveraging spontaneous activity in human neuronal stem cell-derived neurons to model neurodevelopmental disorders. \nNovember 9 – 9:00am \nChristian Lohmann (Netherlands Institute for Neuroscience\, Netherlands)\nImaging synapse development. \nNovember 9 – 11:00am \nJulijana Gjorgjieva (Max Planck Institute for Brain Research\, Germany)\nEmergence of organization and computations at the subcellular and cellular scales. \nCourse directors\nAna Luisa Carvalho – Coimbra University\, Portugal \nMathieu Letellier – Bordeaux University\, France \nHey-Kyoung Lee – John Hopkins University.\, US \nAbout the course\nAdvanced techniques for synapse biology – CAJAL (cajal-training.org) \n
URL:https://www.bordeaux-neurocampus.fr/en/event/advanced-techniques-for-synapse-biology/
CATEGORIES:Cajal Lectures,For scientists
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DTSTART;TZID=Europe/Paris:20231031T140000
DTEND;TZID=Europe/Paris:20231031T140000
DTSTAMP:20260410T160727
CREATED:20231026T141006Z
LAST-MODIFIED:20231026T143033Z
UID:163748-1698760800-1698760800@www.bordeaux-neurocampus.fr
SUMMARY:IECB Seminar - Nadia El Mammeri
DESCRIPTION:Venue:  IECB – 2 Rue Robert Escarpit\, 33600 Pessac \n\nNadia El Mammeri\nMIT\, Department of Chemistry \nInvited by Antoine Loquet\,  IECB\nContact: a.loquet@iecb.u-bordeaux.fr \nTitle\nUnderstanding Tau’s Chemical code: microtubules\, lipid membranes\, anionic co-factors\, and phosphorylation \nAbstract\nThe protein tau associates and stabilizes microtubules (MT) to maintain neuronal health. Post-translational modifications that lead to tau aggregation in brains with neurodegenerative diseases. To understand the mechanism of the early misfolding events in AD\, we are using magic-angle-spinning (MAS) solid-state NMR spectroscopy and cryo-electron microscopy to investigate the structure and dynamics of tau bound to microtubules [1]\, lipid bilayers [2]\, as well as amyloid fibrils formed with anionic cofactors [3] or co-factor-free pseudophosphorylation mutations[4]. \nWhen complexed with MTs\, tau exhibits well-resolved dipolar 2D correlation spectra that can be assigned to a 45-residue segment spanning the R’ and the C-terminal half of the R4 repeat. This result changes the prevailing model that all 5 MT-binding regions are immobilized. Moreover\, the NMR assigned immobilized residues of R’ dock well into cryo-EM densities\, leading to a revised paradigm of MT-binding. \nWhen complexed to lipid membranes\, tau converted from a disordered random coil to an ordered β-sheet. Small unilamellar vesicles (SUVs) and large unilamellar vesicles (LUVs) cause different equilibrium conformations. SUV-bound tau developed amyloid fibrils while LUV-bound tau does not but has a different β-sheet assembly that contains the R’ repeat. Removing cholesterol from the SUV abolished fibril formation. Thus\, high membrane curvature and cholesterol are both required for fibril formation. \nIn the presence of heparin\, P2R tau assembles into amyloid fibrils. We assigned the rigid β-sheet core to the R2 and R3 repeats. Unexpectedly\, the folds differ between 24˚C and 12˚C: R2 forms a β-arch at 24˚C but a continuous β-strand at 12˚C\, which dimerizes with another protofilament. This indicates that R2 has enhanced conformational plasticity than R3\, similarly to in brain-extracted 4R tau aggregates. \nPseudo-phosphorylated mutants of tau can self-assemble in the absence of any co-factors. Using SSNMR and cryo-EM\, we found that specific disease-related phosphorylation patterns induce specific amyloid structures. These results have implications for the functional and pathological state of tau in diseases. They also demonstrate the power of solid-state NMR to reveal both the structure and dynamics of complex biomolecular assemblies in neurodegenerative diseases. \n
URL:https://www.bordeaux-neurocampus.fr/en/event/iecb-seminar-nadia-el-mammeri/
CATEGORIES:For scientists,home-event,Other events
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