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BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260313T110000
DTEND;TZID=Europe/Paris:20260313T120000
DTSTAMP:20260404T114247
CREATED:20260227T095412Z
LAST-MODIFIED:20260227T095425Z
UID:10000078-1773399600-1773403200@sfp-alpes.fr
SUMMARY:Peter DAHLBERG (Stanford University\, USA)
DESCRIPTION:Fluorescence-guided cryogenic FIB milling and their application to the study of the NLRP3 inflammasome\nRésumé : \nNumerous critical events in cell biology depend on rare ( 1 copy per cell) and small (<500 nm in diameter) structures. Observation of these processes at high resolution using cryogenic electron tomography (CryoET) presents challenges\, as the structures must first be precisely targeted within thin sections through focused ion beam milling. In this presentation\, I will introduce my group’s work on a tri-coincident system that integrates light\, ion\, and electron microscopy at a single focal point. This approach enables real-time monitoring of the milling process and makes two different modes of guidance possible that require no addition of fluorescent fiducials or image registration and whose accuracy far exceeds the optical diffraction limit. I will discuss both guidance modes in detail and then describe their application to the study of the in situ structure of the NLRP3 inflammasome. Despite its central role in innate immunity as a master regulator responsible for proinflammatory cytokine maturation and cell death\, its in situ structure has remained elusive due to challenges in capturing the small singular punctum it forms per cell in thin sections compatible with CryoET — precisely the kind of target the tri-coincident system was developed for. Using our guidance approach\, our cryo-tomograms revealed that the NLRP3 inflammasome forms a dense condensate within and around the microtubule-organizing center. At a later stage after activation\, we saw further growth of the condensate\, and the cells underwent pyroptosis with widespread mitochondrial damage and autophagy. Our study revealed new insights into NLRP3 structure and other organelle alterations during inflammation. \nContact : ibs.seminaires@ibs.fr
URL:https://sfp-alpes.fr/event/peter-dahlberg-stanford-university-usa/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IBS":MAILTO:ibs.seminaires@ibs
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260312T183000
DTEND;TZID=Europe/Paris:20260312T223000
DTSTAMP:20260404T114247
CREATED:20260130T145238Z
LAST-MODIFIED:20260130T153923Z
UID:10000048-1773340200-1773354600@sfp-alpes.fr
SUMMARY:Hugues Nury (Irig / IBS)
DESCRIPTION:« Soirée du vivant » : récepteurs neuronaux : comment les poisons trouvent leur cible\nCette « S​​oirée du vivant »\, d’un format inédit\, proposera présentation interactive\, quiz participatifs\, échanges libres\, le tout autour de tapas végétales\, pour un moment convivial et grand public.\n​\nHugues Nury\, chercheur CNRS à l’Institut de biologie structurale de Grenoble\, nous plongera dans l’univers fascinant des venins de serpents\, alcaloïdes végétaux et autres insecticides modernes\, qui exercent leurs effets en ciblant des récepteurs neuronaux spécifiques. Il apportera d’abord des connaissances générales pour répondre à des questions essentielles telles : pourquoi certaines substances sont-elles mortelles à des doses infimes tandis que d’autres restent inoffensives ? Comment un récepteur neuronal reconnaît-il son « poison » ?​​​​\n​\n​Il présentera ensuite le projet ANR Pesti Penta qu’il coordonne\, et qui vise à comprendre les mécanismes moléculaires d’action des insecticides sur les récepteurs neuronaux d’insectes. Cette recherche combine biologie structurale\, dynamique moléculaire et électrophysiologie afin d’explorer les interactions entre différentes molécules et leurs cibles biologiques.\nÀ terme\, l’objectif de ces travaux fondamentaux est de contribuer au développement d’insecticides plus efficaces et plus ciblés. \nEn savoir plus : https://www.cea.fr/drf/irig/Pages/Animation-scientifique/seminaires/2026_Nury.aspx
URL:https://sfp-alpes.fr/event/hugues-nury-irig-ibs/
LOCATION:La Casemate\, 2 Place Saint-Laurent\, Grenoble\, 38000\, France
CATEGORIES:Conférence
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260312T130000
DTEND;TZID=Europe/Paris:20260312T140000
DTSTAMP:20260404T114247
CREATED:20260213T093616Z
LAST-MODIFIED:20260226T095902Z
UID:10000066-1773320400-1773324000@sfp-alpes.fr
SUMMARY:Stéphane GUINDON (LIRMM - Montpellier)
DESCRIPTION:Recent advances in phylogeography\nContact : lucie.lamothe@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/stephane-guindon-lirmm-montpellier/
LOCATION:IMAG – Salle de Réunion\, 150 place du Torrent\, St Martin d’Hères\, 38400\, France
CATEGORIES:Séminaire
ORGANIZER;CN="TIMC - IMAG":MAILTO:lucie.lamothe@univ-grenoble-alpes.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260306T140000
DTEND;TZID=Europe/Paris:20260306T150000
DTSTAMP:20260404T114247
CREATED:20260305T145615Z
LAST-MODIFIED:20260305T145620Z
UID:10000093-1772805600-1772809200@sfp-alpes.fr
SUMMARY:Carlo PIFFERI (Centre de Biophysique Moléculaire\, Orléans)
DESCRIPTION:Exploiting disulfide-rich peptides as protein epitope mimics : development of a generalizable conjugation approach for immunogen preparation\nRésumé : \nGeneration of specific antibodies against peptides by immunization requires their covalent conjugation to protein carriers to override their inherently weak immunogenicity. The vast majority of bioconjugation approaches to achieve peptide-protein constructs rely on thiol-maleimide chemistry1 and capitalize on a wide array of commercial maleimide-functionalized protein carriers. Disulfide-rich peptides2 (DRPs) possess a rigid\, constrained structure that makes them ideal for designing synthetic mimics of protein regions/domains. For bioconjugation purposes\, the introduction of a single spare thiol moiety into a linear peptide antigen is straightforward\, while DRPs’ disulfide bonds are prone to intramolecular thiophilic attack by the reactive thiolate. This unintended reactivity competes with the desired Michael addition to the maleimide moiety\, ultimately disrupting the native disulfide bridging framework. As a result\, DRP’s tertiary structure will be altered\, affording an immunogen that is a poor mimic of the native target. Although a few studies have explored the late-stage introduction of thiol-containing cross-linkers onto DRP antigens for their conjugation onto protein carriers\,3\,4 the stability of DRP’s disulfide pattern in the presence of an extra thiol has never been examined. To address this\, we systematically evaluated the influence of different spacers in “DRP-spacer-thiol” constructs\, under thiol-maleimide reaction conditions.5 Our results highlight how both linker length and flexibility are key to maintain DRP disulfides unaltered\, providing a general approach to achieve DRP bioconjugation by thiol-maleimide chemistry. We have applied our approach to a small DRP predicted to closely mimic a surface-accessible epitope of the full LINGO-1 protein\, and obtained a very specific antibody response upon immunization: the resulting polyclonal IgG was able to selectively bind the full-length protein in a cellular context\, with stringent selectivity across its four homologs. \nReferences : \n1. M. Góngora-Benítez\, J. Tulla-Puche & F. Albericio\, Chem. Rev. 2014\, 114\, 901–926.\n2. K. Renault\, J. W. Fredy\, P.-Y. Renard & C. Sabot\, Bioconjug. Chem. 2018\, 29\, 2497–2513.\n3. H. Katayama & M. Mita\, Bioorganic Med. Chem. 2016\, 24\, 3596–3602.\n4. H. Katayama\, R. Mizuno & M. Mita\, Biosci. Biotechnol. Biochem. 2019\, 83\, 1791–1799.\n5. L. Azzoug et al.\, ChemRxiv 2025\, DOI:10.26434/chemrxiv-2025-krjcm \n_ \nContact : david.goyard@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/carlo-pifferi-centre-de-biophysique-moleculaire-orleans/
LOCATION:DCM – Salle C209\, DCM - Bât Chimie Recherche 301 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260305T113000
DTEND;TZID=Europe/Paris:20260305T123000
DTSTAMP:20260404T114247
CREATED:20260227T134443Z
LAST-MODIFIED:20260227T134815Z
UID:10000084-1772710200-1772713800@sfp-alpes.fr
SUMMARY:Viviana RICON MONTES & Andreas OFFENHÄUSSER (Forschungszentrum Jülich\, Allemagne)
DESCRIPTION:Devices that interact with the brain: from nanostructured to flexible electrodes\nRésumé : \nNeural electrodes are the core components of neuroelectronic devices\, enabling the recording and simulation of neural activity. Our research focuses on two primary areas : (1) the design and\ncharacterization of the neuron-electrode interface\, and (2) the development of flexible neural interfaces for both in vivo and in vitro applications. Microelectrode arrays (MEAs) are commonly used to bridge the interface between neurons and electronic systems. However\, current MEAs face limita7ons in signal fidelity\, precision of neural modulation\, and long-term biocompatibility. To address these challenges\, we are developing nanomaterial-based MEAs that offer enhanced physical and chemical properties\, leading to improved cell-electrode coupling. Specifically\, we have engineered a hybrid structure combining vertical nanostraws with nanocavities\, enabling stable\, non-invasive\, and long-term recording at sub-threshold resolution. \nImplantable neural prosthetic devices provide direct access to local neural circuits and are critical components of brain-machine interfaces. While current clinical-grade devices—typically based on silicon or noble metals—have driven significant advances\, they oPen fail to sustain reliable neural communication over extended periods. Our goal is to create next-generation neurotechnologies that integrate seamlessly with biological tissue\, supporting multimodal neural interrogation through electrical\, optical\, or chemical means. We are actively exploring novel device architectures\, materials\, and implantation strategies\, alongside rigorous performance evaluation\, with the ultimate aim of enabling both acute and chronic in vivo applications. Our approach combines thin-film technology and surface micromachining processes with additive manufacturing techniques\, including two-photon lithography. These are integrated with self-\naligned\, template-assisted electrodeposition processes\, kirigami-inspired designs with matched-die forming\, novel bonding methods\, and the modular stacking of two-dimensional neural probes with key-lock systems. These technologies support versatile applications\, ranging from investigating seizure-like activity in in vitro epilepsy models to advancing visual prosthesis that enable bidirectional communication along the visual pathway. \nContact : clement.hebert@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/viviana-ricon-montes-andreas-offenhausser-forschungszentrum-julich-allemagne/
LOCATION:GIN – Amphi Serge Kampf\, Grenoble Institut des Neurosciences (GIN) Bât. Edmond J. Safra\, Chemin Fortune Ferrini CHU\, La Tronche\, 38700\, France
CATEGORIES:Séminaire
ORGANIZER;CN="GIN":MAILTO:yves.goldberg@univ-grenoble-alpes.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260303T140000
DTEND;TZID=Europe/Paris:20260303T140000
DTSTAMP:20260404T114247
CREATED:20260227T153207Z
LAST-MODIFIED:20260227T153207Z
UID:10000089-1772546400-1772546400@sfp-alpes.fr
SUMMARY:Marco MACCARINI (chercheur UGA)
DESCRIPTION:Exploring the Nanostructure of Biomimetic Membranes\nRésumé : \nModel lipid membranes are simplified yet powerful systems that mimic key features of biological plasma membranes—the essential envelopes that define and protect living cells. Their controlled simplicity makes them ideal for precise experimental techniques\, enabling us to explore their interactions with novel nanoengineered materials. \nWhen combined with biological components like proteins\, these membranes not only deepen our understanding of fundamental biological processes but also serve as building blocks for advanced nanoengineered materials with tailored technological applications. \nIn this seminar\, I will present examples from my research\, where laboratory techniques\, large-scale facility analyses\, and computational methods converge to provide in-depth characterization and mechanistic insights into membrane behavior. These findings hold significant potential for advancements in health\, biotechnology\, and fundamental biology. \nShort Bio/CV\nAs  a CNRS Chargé de Recherche\, I’ve recently joined the LMGP to continue my research journey in this scientific new environment. My academic path has taken me across borders—starting with a Physics degree in Italy\, followed by a PhD in Polymer Physics in England\, and postdoctoral experiences in Germany and Canada. Along the way\, I’ve had the privilege of working at world-class facilities like the Institut Laue Langevin\, where I deepened my expertise in large-scale scientific infrastructure. I now continue this work at LMGP\, where my research focuses on the intersection of physics\, materials science\, and biomimetic systems. \nContact : deborah.verger@grenoble-inp.fr
URL:https://sfp-alpes.fr/event/marco-maccarini-chercheur-uga/
LOCATION:LMGP – salle des séminaires\, Grenoble INP -Phelma 3 parvis Louis Néel\, Grenoble\, 38054\, France
CATEGORIES:Séminaire
ORGANIZER;CN="LMGP":MAILTO:deborah.verger@grenoble-inp.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260302T110000
DTEND;TZID=Europe/Paris:20260302T120000
DTSTAMP:20260404T114247
CREATED:20260227T094612Z
LAST-MODIFIED:20260227T094814Z
UID:10000077-1772449200-1772452800@sfp-alpes.fr
SUMMARY:Moritz SENGER (Université d’Uppsala\, Département de chimie pour les sciences de la vie\, Suède)
DESCRIPTION:From Catalysis to Sensing : Proton Transfer in [FeFe]-hydrogenases\nRésumé : \nEnzymes are natures catalysts enabling challenging reactions at ambient conditions and at low overpotentials. In particular\, [FeFe]-hydrogenases which catalyse bidirectional H2 turnover (2e- + 2H+ <-> H2) at high turnover numbers raise interest for their application in a green hydrogen economy. In [FeFe]-hydrogenases catalysis takes place at a unique diiron cofactor that is equipped with carbon monoxide (CO) and cyanide (CN) ligands. They serve as intrinsic infrared active probes sensitive to redox changes located directly at the centre of the catalytic reaction. This in isolation inactive di-iron cofactor becomes efficient H2 catalyst when incorporated into the [FeFe]-hydrogenase protein scaffold. More recently H2 sensing [FeFe]-hydrogenases have been characterised using the identical cofactor but for H2 sensing. The fundamental design principles of the protein scaffolds to selectively tune cofactor function either to efficient H2 catalyst or to H2 sensor remain unknown.Here we use organic dyes to artificially activate catalytic [1-2] and sensory [3-5] [FeFe]-hydrogenases photochemically and investigate them via in situ ATR-FTIR spectroscopy. Following changes of the cofactor CO and CN ligands\, single carboxylic acid residues and collective amide I modes\, we show that protein scaffold differences are not limited to the cofactor second coordination sphere but extend through the whole protein via proton transfer pathways\, secondary structure changes and most likely dimerization events. More general\, our results give a first idea how protein scaffolds can tune cofactor functions. \nReferences :[1] M. Senger\, V. Eichmann\, K. Laun\, J. Duan\, F. Wittkamp\, G. Knor\, U. P. Apfel\, T. Happe\, M. Winkler\, J. Heberle and S. T. Stripp*J Am Chem Soc\, 2019\, 141\, 17394-17403.[2] M. Lorenzi\, M. T. Gamache\, H. J. Redman\, H. Land\, M. Senger* and G. Berggren*ACS Sustain Chem Eng\, 2022\, 10\, 10760-10767.[3] I. Voloshyn\, C. Schumann\, P. R. Cabotaje\, A. Zamader\, H. Land and M. Senger*Chem Commun (Camb)\, 2024\, 60\, 10914-10917[4] M. Senger*\, C. Schumann\, P. R. Cabotaje\, A. Zamader\, P. Huang\, H. Land and G. Berggren*Phys Chem Chem Phys\, 2025\, 27 (18)\, 9864-9875 [5] Cabotaje\, P. R. ; Sekretareva\, A. ; Senger\, M. ; Huang\, P. ; Walter\, K. ; Redman\, H. J. ; Croy\, N. ; Stripp\, S. T. ; Land\, H. ; Berggren\, G.J Am Chem Soc 2025\, 147 (5)\, 4654-4666. \nContact : ibs.seminaires@ibs.fr
URL:https://sfp-alpes.fr/event/moritz-senger-universite-duppsala-departement-de-chimie-pour-les-sciences-de-la-vie-suede/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IBS":MAILTO:ibs.seminaires@ibs
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260227T110000
DTEND;TZID=Europe/Paris:20260227T120000
DTSTAMP:20260404T114247
CREATED:20260129T163105Z
LAST-MODIFIED:20260130T142401Z
UID:10000041-1772190000-1772193600@sfp-alpes.fr
SUMMARY:Jean-Francois COLLET (Institut de Duve\, Bruxelles)
DESCRIPTION:How (and Why) do Gram-Negative Bacteria build an Outer Membrane\nRésumé :  \nGram-negative bacteria are defined by a complex cell envelope in which the outer membrane plays a central role in protection\, nutrient exchange\, and antibiotic resistance. This asymmetric lipid bilayer forms a robust permeability barrier\, yet its biogenesis presents a striking challenge : all outer membrane components are synthesized in the cytoplasm or at the inner membrane and must be transported and assembled across the periplasm without direct energy input. In this talk\, I will discuss how Gram-negative bacteria build their outer membrane and why this process is essential for cellular physiology. I will introduce the major pathways responsible for outer membrane assembly and highlight how their activities need to be coordinated to maintain envelope integrity. I will also present recent work showing that the outer membrane is not merely a passive barrier\, but a mechanically active structure that enables the buildup of periplasmic pressure\, a property critical for envelope stability and bacterial survival. Together\, these findings underscore the outer membrane as a dynamic\, multifunctional organelle and a promising target for future antibacterial strategies. \nContact : ibs.seminaires@ibs.fr
URL:https://sfp-alpes.fr/event/jean-francois-collet-institut-de-duve-bruxelles/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IBS":MAILTO:ibs.seminaires@ibs
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260226T140000
DTEND;TZID=Europe/Paris:20260226T150000
DTSTAMP:20260404T114247
CREATED:20260130T095731Z
LAST-MODIFIED:20260130T102010Z
UID:10000043-1772114400-1772118000@sfp-alpes.fr
SUMMARY:Paulo Henrique MACIEL BUZZETTI (Département de Chimie Moléculaire\, équipe I2BM (nouvel entrant))
DESCRIPTION:From Bio-analytics & Bio-energy : A Journey Through Functional Interfaces & Supramolecular Architectures\nContact : quentin.laurent@univ-grenoble-alpes.fr 
URL:https://sfp-alpes.fr/event/paulo-henrique-maciel-buzzetti-departement-de-chimie-moleculaire-equipe-i2bm-nouvel-entrant/
LOCATION:DCM – Salle C209\, DCM - Bât Chimie Recherche 301 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260226T130000
DTEND;TZID=Europe/Paris:20260226T140000
DTSTAMP:20260404T114247
CREATED:20260130T162946Z
LAST-MODIFIED:20260213T084606Z
UID:10000050-1772110800-1772114400@sfp-alpes.fr
SUMMARY:Céline SCORNAVACCA (ISEM – Montpellier)
DESCRIPTION:A New Algorithm for Computing the Likelihood of a Phylogeny\nContact : lucie.lamothe@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/celine-scornavacca-isem-montpellier/
LOCATION:IMAG – Salle de Réunion\, 150 place du Torrent\, St Martin d’Hères\, 38400\, France
CATEGORIES:Séminaire
ORGANIZER;CN="TIMC - IMAG":MAILTO:lucie.lamothe@univ-grenoble-alpes.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260224T183000
DTEND;TZID=Europe/Paris:20260224T183000
DTSTAMP:20260404T114247
CREATED:20260222T085804Z
LAST-MODIFIED:20260222T090042Z
UID:10000072-1771957800-1771957800@sfp-alpes.fr
SUMMARY:Sophie Abby (TIMC\, Grenoble)
DESCRIPTION:Le premier souffle : comment les microbes ont oxygéné la Terre\nRésumé :  \nCette soirée explore la diversité du vivant à travers l’arbre phylogénétique\, en s’appuyant sur les travaux du projet Quinevol qui étudie les quinones\, molécules essentielles présentes dans tous les organismes vivants. Comment les organismes primitifs respiraient-ils avant l’apparition de l’oxygène ? Comment se sont-ils ensuite adaptés à ce qui était alors un véritable poison ? Un voyage scientifique des origines de la vie jusqu’aux frontières de la recherche actuelle. \n 
URL:https://sfp-alpes.fr/event/sophie-abby-timc-grenoble/
LOCATION:Museum de Grenoble\, 1 Rue Dolomieu\, Grenoble\, 38000\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260219T113000
DTEND;TZID=Europe/Paris:20260219T123000
DTSTAMP:20260404T114247
CREATED:20260212T155849Z
LAST-MODIFIED:20260212T155849Z
UID:10000059-1771500600-1771504200@sfp-alpes.fr
SUMMARY:Sharlen MOORE (Johns Hopkins University\, Baltimore\, USA)
DESCRIPTION:Revealing abrupt transitions from goal-directed to habitual behavior\nRésumé : \nA fundamental tenet of animal behavior is that decision-making involves multiple ‘controllers.’ Initially\, behavior is goal-directed\, driven by desired outcomes\, shifting later to habitual control\, where cues trigger actions independent of the motivational state. Clark Hull’s question from 1943 still resonates today: “Is this transition [to habit] abrupt\, or is it gradual and progressive?” Despite a century-long belief in gradual transitions\, this question remains unanswered as current methods cannot disambiguate goal-directed versus habitual control in real time. Here\, we introduce a novel ‘volitional engagement’ approach\, motivating animals by palatability rather than biological need. Providing less palatable water in the home cage reduced motivation to ‘work’ for plain water in an auditory discrimination task compared to water-restricted animals. Using quantitative behavior and computational modeling\, we found that palatability-driven animals learned to discriminate as quickly as water-restricted animals but exhibited state-like fluctuations when responding to the reward-predicting cue-reflecting goal-directed behavior. After thousands of trials\, these fluctuations spontaneously and abruptly ceased\, with animals always responding to the reward-predicting cue. In line with habitual control\, post- transition behavior displayed motor automaticity\, decreased error sensitivity (assessed via pupillary responses)\, and insensitivity to sensory-specific outcome devaluation. Bilateral lesions of the habit-related dorsolateral striatum (DLS) blocked transitions to habitual behavior. Finally\, we used bilateral fiber photometry in the putative controllers of goal-directed (dorsomedial striatum\, DMS) and habitual (DLS) behavior to monitor the evolution of neural activity across learning. Both the DMS and DLS exhibited learning- related signatures in cue\, lick\, and outcome-related signaling at similar timescales in parallel. Immediately after transitioning to habitual behavior\, outcome-related signaling was suppressed in the DLS and\, to a lesser extent\, in the DMS\, while cue-evoked responses further sharpened. This abrupt shift (reduction in outcome signaling and sharpening of cue-evoked responses) suggests that sensory cues rather than outcomes drive habitual responding. Our results demonstrate that both controllers (DMS and DLS) exhibit learning-related plasticity in parallel but that the behavioral manifestation of habits emerges spontaneously and abruptly in a DLS-dependent manner\, suggesting the involvement of a higher-level process that arbitrates between the two. \nContact : robin.magnard@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/sharlen-moore-johns-hopkins-university-baltimore-usa/
LOCATION:GIN – Amphi Serge Kampf\, Grenoble Institut des Neurosciences (GIN) Bât. Edmond J. Safra\, Chemin Fortune Ferrini CHU\, La Tronche\, 38700\, France
CATEGORIES:Séminaire
ORGANIZER;CN="GIN":MAILTO:yves.goldberg@univ-grenoble-alpes.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260212T140000
DTEND;TZID=Europe/Paris:20260212T150000
DTSTAMP:20260404T114247
CREATED:20260130T094628Z
LAST-MODIFIED:20260130T102105Z
UID:10000042-1770904800-1770908400@sfp-alpes.fr
SUMMARY:Youngsuk KIM (Pusan National University\, Busan\, South Korea (visiting scientist @ DCM))
DESCRIPTION:Carbene–CS2 : Redox-active Radical Ligands\nContact : david.martin@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/youngsuk-kim-pusan-national-university-busan-south-korea-visiting-scientist-dcm/
LOCATION:DCM – Salle C209\, DCM - Bât Chimie Recherche 301 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260212T130000
DTEND;TZID=Europe/Paris:20260212T140000
DTSTAMP:20260404T114247
CREATED:20260124T035658Z
LAST-MODIFIED:20260129T135753Z
UID:10000030-1770901200-1770904800@sfp-alpes.fr
SUMMARY:Delphine ROPERS (Inria – Grenoble)
DESCRIPTION:Computational analyses of bacterial mRNA decay\n  \nPlus d’informations : https://bi-gre.github.io/ \nContact : lucie.lamothe@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/delphine-ropers-inria-grenoble/
LOCATION:IMAG – Salle de Réunion\, 150 place du Torrent\, St Martin d’Hères\, 38400\, France
CATEGORIES:Séminaire
ORGANIZER;CN="TIMC - IMAG":MAILTO:lucie.lamothe@univ-grenoble-alpes.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260206T110000
DTEND;TZID=Europe/Paris:20260206T120000
DTSTAMP:20260404T114247
CREATED:20260129T162542Z
LAST-MODIFIED:20260130T141840Z
UID:10000040-1770375600-1770379200@sfp-alpes.fr
SUMMARY:David SKURNIK (Hôpital Necker- Enfants Malades\, Université Paris Cité)
DESCRIPTION:New approaches in vaccine development\nRésumé : \nHigh-throughput sequencing and particularly original applications such as the TnSeq allow a study of host-pathogen interaction at the full genome scale through a systematic analysis off all the virulence factors of a bacteria in a particular setting. For example\, all the genes important or essential for GI tract colonization of the selected pathogenic bacteria. \nThis allows to reveal new targets for vaccine development. Interestingly\, an ongoing adaptation of the TnSeq allows the systematic identification of these antigens of interest. We call this new technology : TnVaccine. \nContact : ibs.seminaires@ibs.fr
URL:https://sfp-alpes.fr/event/david-skurnik-hopital-necker-enfants-malades-universite-paris-cite/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IBS":MAILTO:ibs.seminaires@ibs
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260127T110000
DTEND;TZID=Europe/Paris:20260127T120000
DTSTAMP:20260404T114247
CREATED:20260123T161211Z
LAST-MODIFIED:20260124T031619Z
UID:10000019-1769511600-1769515200@sfp-alpes.fr
SUMMARY:Nidia MALDONADO CARMONA (University of Florence\, Italy)
DESCRIPTION:Bringing light to pathogens : light-driven strategies for disinfection of pathogens\nAbstract : \nThe emergence of antimicrobial resistance has prompted the search for new strategies\, aiming to find more efficient ways to kill microbial pathogens. In this sense\, Photodynamic Antimicrobial ChemoTherapy (PACT) uses a combination of light\, oxygen and a photosensitizer molecule to produce lethal reactive oxygen species\, which have demonstrated to be highly effective against microorganisms and even against multiresistant microorganisms. During this talk\, I will address the different challenges that surround the field\, ranging from an efficient delivery of photosensitizers using natural biopolymers\, while also addressing the delivery of light into a clinical scenario model\, addressing the difficulties of biological experiments with\ntwo-variables to juggle with\, technical challenges that hinder the application of this technique into the clinic. \nContact : appaixfl@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/bringing-light-to-pathogens-light-driven-strategies-for-disinfection-of-pathogens/
LOCATION:IAB – Salle de séminaire\, IAB Site Santé - Allée des Alpes\, La Tronche\, 38700\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IAB":MAILTO:appaixfl@univ-grenoble-alpes.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260127T103000
DTEND;TZID=Europe/Paris:20260127T113000
DTSTAMP:20260404T114247
CREATED:20260123T154556Z
LAST-MODIFIED:20260124T031428Z
UID:10000018-1769509800-1769513400@sfp-alpes.fr
SUMMARY:Juan FONTECILLA-CAMPS (IBS / Groupe Métalloprotéines)
DESCRIPTION:Exaptation : la composante opportuniste de l’évolution et de la sélection naturelle\nRésumé : \nLa variété et la capacité fonctionnelle des êtres vivants ont toujours intrigué les biologistes. Le philosophe grec Aristote était\, il y a plus de 2300 ans\, le premier à classifier les animaux selon la couleur de leur sang. Il croyait aussi que les mêmes animaux avaient existé\, immuables\, depuis une éternité. Il a fallu attendre le XIXe siècle pour que Charles Darwin explique l’évolution des espèces par la sélection naturelle. Cette évolution peut paraître linéaire et\, pour certains\, elle aurait un but (téléologie). Mais pour les évolutionnistes il n’y pas de plan ni de finalité. Un des résultats fondamentaux de la sélection naturelle est l’adaptation ; une fois qu’un organe est devenu utile\, les mutations aléatoires qui améliorent sa fonction seront sélectionnées parce qu’elles sont avantageuses. Mais la sélection naturelle opère aussi de manière opportuniste\, et un organe donné peut se transformer pour remplir une fonction complètement différente de celle d’origine ; c’est l’exaptation. Un cas classique est la transformation d’écailles de dinosaures en plumes d’oiseaux. Pendant mon séminaire je vais illustrer plusieurs cas d’exaptation biologique\, et discuter aussi l’exaptation culturelle. \nContact : ibs.seminaires@ibs.fr \n  \n 
URL:https://sfp-alpes.fr/event/exaptation-la-composante-opportuniste-de-levolution-et-de-la-selection-naturelle/
LOCATION:IBS\, 71 avenue des Martyrs\, Grenoble
CATEGORIES:Séminaire
ORGANIZER;CN="IBS":MAILTO:ibs.seminaires@ibs
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20250505T140000
DTEND;TZID=Europe/Paris:20250505T170000
DTSTAMP:20260404T114247
CREATED:20250418T090623Z
LAST-MODIFIED:20250418T090623Z
UID:10000005-1746453600-1746464400@sfp-alpes.fr
SUMMARY:Développement d’inhibiteurs peptidiques du virus de la grippe
DESCRIPTION:Benoît SEPARI (IRIG / IBS) \n\n\nLa grippe saisonnière cause la mort de centaines de milliers d’individus chaque année\, tandis que les souches zoonotiques provoquent régulièrement de graves pandémies. Le haut taux de mutation du génome viral limite l’utilisation d’antiviraux ciblant directement influenza\, il est donc nécessaire de développer de nouvelles molécules ciblant des mécanismes viraux ou cellulaires différents et ayant un faible potentiel de mutation. Les antiviraux dirigés contre l’hôte ne cible pas le virus mais plutôt des protéines de l’hôte nécessaires à la réplication du virus\, ainsi\, l’apparition de résistance est beaucoup moins probable. Nous avons donc développé des peptides qui bloquent l’assemblage d’un complexe protéique accessoire du spliceosome humain. Ce complexe est essentiel pour le prolifération du virus car il catalyse l’épissage des ARNs pré-messagers du segment NS en ARNm codant pour les protéines NS1 et NEP. Ce complexe protéique comprend les protéines RED et SMU1\, interagissant directement avec la polymérase virale. La rupture de l’interaction entre RED et SMU1 inhibe l’épissage des pré-ARNm de NS\, sans qu’aucun effet sur la viabilité cellulaire ne puisse être détecté. Des bibliothèques de 10^8 peptides différents ont été conçues\, en étudiant la structure du complexe RED-SMU1 sauvage et en imitant un domaine de fixation naturel de RED. Les peptides les plus affins pour SMU1 ont été sélectionnés par phage display. Des peptides supplémentaires ont également été générés par une approche bioinformatique utilisant un neural network. Les peptides les plus prometteurs ont été caractérisés par ELISA et NGS\, puis des méthodes biophysiques\, structurales et cellulaires ont permis d’identifier des peptides ayant une affinité de l’ordre du nanomolaire pour SMU1 tout en présentant des motifs différents.​\n​\n​ \n\n\n\nL’accès au campus EPN nécessite un avis de rendez-vous. Merci d’adresser votre demande à ibs.seminaires@ibs.fr au moins 48h à l’avance.\nN’oubliez pas de vous munir d’une pièce d’identité.
URL:https://sfp-alpes.fr/event/developpement-dinhibiteurs-peptidiques-du-virus-de-la-grippe/
LOCATION:IBS\, 71 avenue des Martyrs\, Grenoble
CATEGORIES:Soutenance de Thèse
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
END:VCALENDAR