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TZID:Europe/Paris
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BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260625T130000
DTEND;TZID=Europe/Paris:20260625T140000
DTSTAMP:20260612T075402Z
CREATED:20260507T093855Z
LAST-MODIFIED:20260612T075402Z
UID:10000148-1782392400-1782396000@sfp-alpes.fr
SUMMARY:Elodie LAINE (Sorbone Université)
DESCRIPTION:What evolution tells us about the impact of mutations — and how to scale it up\n_ \nContact : lucie.lamothe@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/elodie-laine-sorbone-universite/
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:20260626T110000
DTEND;TZID=Europe/Paris:20260626T120000
DTSTAMP:20260604T145405Z
CREATED:20260604T145405Z
LAST-MODIFIED:20260604T145405Z
UID:10000191-1782471600-1782475200@sfp-alpes.fr
SUMMARY:Christophe MASSELON (CEA-Irig/BGE) et Vincent AGACHE (CEA-Leti/DTIS)
DESCRIPTION:Sensing Mass at the Nanoscale : Suspended Nanochannel Resonators and NEMS-MS for Biology\nRésumé : \n\nDetermining the mass of biological nanoparticles opens new avenues for characterizing biological systems at their own scale. In this joint seminar\, researchers from LETI and IRIG will present two complementary nanoresonator platforms : Suspended Nanochannel Resonators (SNR)\, which operate in solution\, and Nanoelectromechanical Mass Spectrometry (NEMS-MS)\, which operates in the gas phase. Together\, these technologies cover a range of biological particles\, from lipid nanoparticles and extracellular vesicles to viral particles. Beyond the technical principles underlying each platform\, selected applications will illustrate the potential of these approaches for the characterization of biological samples.​​​​​\n​\n\n\n\nLes séminaires et soutenances sont ouverts à tous\, notez toutefois que l’accès au campus EPN nécessite un avis de rendez-vous. Merci de remplir ce formulaire  et de l’adresser\, plus de 48h à l’avance\, à ce contact.\nPensez à vous munir d’une pièce d’identité le jour de votre visite.
URL:https://sfp-alpes.fr/event/christophe-masselon-cea-irig-bge-et-vincent-agache-cea-leti-dtis/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260626T140000
DTEND;TZID=Europe/Paris:20260626T160000
DTSTAMP:20260529T140307Z
CREATED:20260529T140204Z
LAST-MODIFIED:20260529T140307Z
UID:10000170-1782482400-1782489600@sfp-alpes.fr
SUMMARY:Soutenance de Thèse de Henri GRÖGER (Irig/IBS)
DESCRIPTION:Structural and functional characterisation of the vaccinia virus PLD- fold endonuclease K4\, telomere-binding protein i1 and the DNA polymerase complex E9A20D4\nRésumé : \n\nPoxviruses\, such as the vaccinia virus (VACV) and the monkeypox virus\, are large\, enveloped dsDNA viruses from the orthopoxvirus genus that replicate entirely within the host cytoplasm. The 2022 and 2024 outbreaks of mpox\, caused by clade IIb and Ib\, respectively\, have revealed the lack of efficient antivirals and underlined the urgency of understanding poxvirus biology. The poxvirus genome is flanked by short\, inverted complementary hairpin telomeres that feature mismatched bases and insertions essential for viral replication. ​\n​\nThis thesis presents the structural and functional characterisation of three proteins central to poxvirus DNA metabolism : the E9A20D4 DNA polymerase holoenzyme\, and two telomere-interacting proteins\, the PLD-fold nuclease K4 and I1. The project initially focused on the VACV polymerase holoenzyme\, but was reoriented towards the telomere-interacting proteins following the publication of numerous competing mpox polymerase structures. ​\n​\nHaving established that VACV polymerase activity requires K+ and is inhibited by Na+\, I undertook a structure determination of the E9A20D4 polymerase holoenzyme bound to template DNA\, primer and incoming nucleotide in the presence of K+\, using single-particle cryogenic electron microscopy (cryo-EM). I obtained both the structure of the complex E9exo−A20D4 as well as the structure of E9exo− alone bound to the primer-template DNA. The structures in the presence of K+ appear identical to published structures in the presence of Na+. However\, I identified an ion binding site in the exonuclease domain of E9. The thumb domain is disordered in the DNA-free structure\, partially disordered in DNA-bound E9 and ordered in the holoenzyme-DNA complex. SAXS data indicate conformational flexibility\, with more open conformations of E9A20D4 lacking an E9-D4 interface\, while mass photometry reveals partial dissociation of E9A20D4 at low concentrations\, even in the presence of substrate. ​\n​\nUsing cryo-EM\, I report the first structures of K4 in both apo and DNA-bound states\, revealing that the active site is occluded by an orthopoxvirus-specific C-terminal extension of the PLD fold that is displaced upon DNA binding. Biochemical characterisation demonstrates that K4 functions as a DNA-specific endonuclease with a preference for single-stranded DNA and hairpin loops. ​\n​\nI also report the first cryo-EM structure of I1 bound to DNA. I1 is known to bind to viral telomeres and is essential for virion maturation. Cryo-EM data showed the presence of dimers where the head domains 2 and 3 of I1 interact with the DNA duplex through electrostatic interactions\, while the N-terminal domain predicted to be α-helical remains disordered. In solution\, isolated I1 or I1 bound to DNA forms higher-order assemblies\, predominantly tetramers\, but also octamers. ​\n​\n​ Altogether\, these findings substantially advance the molecular understanding of poxvirus biology\, providing a foundation for future mechanistic studies and the rational development of antiviral strategies against emerging orthopoxvirus infections.\n​​\n\n\nLes séminaires et soutenances sont ouverts à tous\, notez toutefois que l’accès au campus EPN nécessite un avis de rendez-vous. Merci de remplir ce formulaire  et de l’adresser\, plus de 48h à l’avance\, à ibs.seminaires@ibs.fr. Pensez à vous munir d’une pièce d’identité le jour de votre visite.\n\n  \n  \n  \n  \n  \n 
URL:https://sfp-alpes.fr/event/soutenance-de-these-de-henri-groger-irig-ibs/
LOCATION:Salle des séminaires du CIBB\, EPN Campus - 71 avenue des Martyrs\, Grenoble\, 38000\, France
CATEGORIES:Soutenance,Soutenance de Thèse
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260702T113000
DTEND;TZID=Europe/Paris:20260702T123000
DTSTAMP:20260625T134330Z
CREATED:20260625T134330Z
LAST-MODIFIED:20260625T134330Z
UID:10000204-1782991800-1782995400@sfp-alpes.fr
SUMMARY:Soleiman SHOKUR (EPFL\, Lausanne)
DESCRIPTION:Clinical and Functional Benefits of Prosthetics with Multimodal Feedback\nRésumé : \nSomatosensory feedback in prosthetics has advanced considerably\, with invasive and non-invasive approaches now capable of evoking touch and proprioceptive sensations. Yet modalities have largely been studied in isolation\, and thermotactile feedback — the simultaneous combination of touch and temperature — remains unachieved. This is a critical gap : natural touch is inherently multimodal\, and temperature is not merely a tool for object interac4on but a continuous signal through which we monitor our own body. Its absence from prosthetic feedback represents a fundamental impoverishment of the sensory input the brain expects. In this talk\, I will present recent advances in multimodal sensory feedback and discuss its benefits not only for improving prosthetic function and dexterity\, but also for addressing key clinical consequences of amputation — including phantom limb pain and body perception distortion. \n_ \nContact : homaira.nawabi@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/soleiman-shokur-epfl-lausanne/
LOCATION:GIN – Amphi Serge Kampf\, Grenoble Institut des Neurosciences (GIN) Bât. Edmond J. Safra\, Chemin Fortune Ferrini CHU\, La Tronche\, 38700\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260703T093000
DTEND;TZID=Europe/Paris:20260703T113000
DTSTAMP:20260625T141107Z
CREATED:20260625T141107Z
LAST-MODIFIED:20260625T141107Z
UID:10000206-1783071000-1783078200@sfp-alpes.fr
SUMMARY:Soutenance de thèse par Léonard OLIVOTTO (CEA-Irig/LCBM)
DESCRIPTION:Conception de catalyseurs hybrides enzyme/nanomatériaux et de solvants sur mesure pour réduire le CO2 par des procédés photochimiques et électrochimiques en présence d’oxygène\nRésumé : \nDans la recherche de nouvelles voies de valorisation du CO2 respectueuses de l’environnement\, l’utilisation d’enzymes représente une approche prometteuse. Parmi elles\, la monoxyde de carbone déshydrogénase (NiFe-CODH) réduit de manière réversible le CO2 en CO avec une performance et une sélectivité remarquable en conditions douces. Pour ces raisons\, plusieurs études ont exploré les [NiFe]-CODH en vue d’applications dans la réduction électrocatalytique et photocatalytique du CO2.\nCependant\, l’extrême sensibilité à l’oxygène de leur site actif constitué d’un centre multimétallique NiFE4S4\, limite leur intégration dans des dispositifs industriels. Par conséquent\, plusieurs stratégies ont été développées pour améliorer la tolérance à l’O2 des systèmes électrocatalytiques et photocatalytiques à base d’enzymes. Parmi celles-ci\, l’utilisation de solvants eutectiques profonds (DES) s’est avérée être une méthode intéressante pour la production photocatalytique d’hydrogène à base d’enzymes. \nDans cette thèse\, plusieurs méthodes de modification de surface pour la conception d’électrodes à base de nanotubes de carbone visant à optimiser l’interface CODH-électrode et\, par conséquent\, à améliorer les performances électrocatalytiques pour la réduction du CO2 ont été développées. Une fois optimisées en milieu aqueux\, les performances des bioélectrodes ont été étudiées dans des DES\, et l’effet protecteur de ce solvant non conventionnel contre l’exposition à l’O2 a été exploré. Les connaissances acquises jusque-là ont finalement été réutilisées pour développer des photosystèmes hybrides semi-conducteur-enzyme (SEHP). Le nitrure de carbone a été modifié par une méthode de greffage au diazonium\, caractérisé et démontré comme coopérant avec la CODH pour réaliser de la photoproduction de CO.\nLe système était également opérationnel dans un DES\, avec des performances catalytiques améliorées\, ce qui laisse entrevoir un avenir prometteur pour le développement de SEHP à base de CODH sensibles à l’O2. \nDans l’ensemble\, ces travaux constituent une nouvelle étape vers l’intégration de biocatalyseurs sensibles à l’O2 dans les technologies pertinentes d’utilisation du CO2. ​​​​ \n_ \nContact : alain.farchi@cea.fr \n 
URL:https://sfp-alpes.fr/event/soutenance-de-these-par-leonard-olivotto-cea-irig-lcbm/
LOCATION:Bâtiment André Rassat / Chimie E – Salle de conférence RDC​\, 470 rue de la Chimie\, Gières\, 38610\, France
CATEGORIES:Soutenance,Soutenance de Thèse
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260703T110000
DTEND;TZID=Europe/Paris:20260703T120000
DTSTAMP:20260703T084805Z
CREATED:20260626T133757Z
LAST-MODIFIED:20260703T084805Z
UID:10000210-1783076400-1783080000@sfp-alpes.fr
SUMMARY:Catherine ROYER (Rensselaer Polytechnic Institute\, New York)
DESCRIPTION:Pressure-based mapping of protein conformational landscapes\nRésumé : \nProtein function depends upon dynamics\, and while in recent years great progress has been made in predicting protein structure from sequence\, the sequence determinants of functional dynamics have yet to be defined. We have developed an approach using a combination of high-pressure NMR\, SAXS\, fluorescence\, and computation to locally and globally map protein stability and functional dynamics. On a model repeat protein system we find that single amino acid substitutions lead to large changes in local stability and apparent folding cooperativity\, while global stabilities of the variant proteins are similar. In the case of the Arf GTPases\, which undergo massive conformational changes during their nucleotide switch transition\, we demonstrated that the switch mechanism implicates the population of a functional molten globule. Moreover\, we discovered the sequence determinants of back-to-front allosteric control of the switch that differentiates switching probabilities of the Arf family members\, and likely many other small GTPases. \n_ \nCes séminaires\, ainsi que les soutenances et cours sont ouverts à tous\, notez toutefois que l’accès au campus EPN nécessite un avis de rendez-vous. Merci de remplir ce formulaire et de l’adresser\, plus de 48h à l’avance\, à ce contact. Pensez à vous munir d’une pièce d’identité le jour de votre visite.
URL:https://sfp-alpes.fr/event/catherine-royer-rensselaer-polytechnic-institute-new-york/
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:20260706T110000
DTEND;TZID=Europe/Paris:20260706T120000
DTSTAMP:20260702T131525Z
CREATED:20260702T131457Z
LAST-MODIFIED:20260702T131525Z
UID:10000212-1783335600-1783339200@sfp-alpes.fr
SUMMARY:Guillaume MESTDAGH (INRIA Montbonnot)
DESCRIPTION:Coupling osmosis and mechanics in vertex-based models for plant tissue growth\nRésumé : \nUnderstanding plant growth is fundamental to address global challenges such as food security\, biodiversity\, and soil‑erosion control. The development of plants involves many interconnected physical processes\, occurring at various spatial and temporal scales\, making modeling an indispensable complement to experiments. In particular\, discrete vertex-based models have successfully described the coupling between inter-cell water fluxes and mechanical deformations of cell walls\, in response to a prescribed inner water pressure. \nA two-dimensional vertex-based model represents a group of cells as a tiling of polygons\, with the edges between polygons representing cell walls. Existing vertex-based models postulate a fixed water pressure inside cells as the force driving growth. In reality\, this inner pressure itself is the consequence of osmosis\, a chemical process by which water is attracted into cells with a higher concentration of solute. However\, capturing the interplay between mechanics and solute dynamics in plant tissues into one model remains a challenge that requires novel mathematical frameworks. \nIn this talk\, I will present a new approach to couple solute and water fluxes with mechanics and growth in vertex-based models. The proposed approach is based on a variational formalism where the system physics is described in terms of free energy and dissipation function. After building the model and deriving the evolution equations of the system\, I will show that the resulting formulation can be turned into a numerical method. Finally\, I will illustrate the model properties through a few numerical simulations and discuss its interest for the study of plant growth. \nContact : philippe.marmottant@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/uillaume-mestdagh-inria-montbonnot/
LOCATION:LiPhy – Salle de conférence\, LiPhy 140 avenue de la Physique\, St Martin d'Hères\, 38402\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260707T110000
DTEND;TZID=Europe/Paris:20260707T120000
DTSTAMP:20260702T132320Z
CREATED:20260702T132320Z
LAST-MODIFIED:20260702T132320Z
UID:10000213-1783422000-1783425600@sfp-alpes.fr
SUMMARY:Jérémie TOPIN (Department of Chemistry\, Université Côte d'Azur\, Nice)
DESCRIPTION:The molecular language of smell : reading odors through receptors\nRésumé : \nThis morning\, you may have enjoyed a cup of coffee or tea and felt that its aroma had stimulated your sense of smell. The volatile molecules in your favourite beverage are recognized by the olfactory receptors (ORs) expressed in your olfactory epithelium. But among your 400 ORs\, which ones were activated by these molecules ?\nTo answer this question\, and more generally to determine the molecular recognition spectrum of ORs\, we design the Molecule to Olfactory Receptor M2OR database\n(https://m2or.chemsensim.fr/)\, which brings together 75\,050 bioassay experiments for 51\,683 distinct OR-molecule pairs.[1] We further combine protein language[2] with graph neural networks to predict OR activation\, and propose a tailored architecture incorporating inductive biases from the protein-molecule interaction.[3] This model outperforms state-of-the-art drug- target interaction prediction models as well as standard GNN baselines. Notably\, our predictions are in agreement with combinatorial coding theory in olfaction. \nReferences\n[1] Lalis\, M.\, Hladiš\, M.\, Khalil\, S. A.\, Briand\, L.\, Fiorucci\, S.\, & Topin\, J\, 2024. M2OR: a database of olfactory receptor–odorant pairs for understanding the molecular mechanisms of olfaction. Nucleic Acids Research\, 52(D1)\, D1370-D1379.\n[2] Elnaggar\, A.\, Heinzinger\, M.\, Dallago\, C.\, Rehawi\, G.\, Wang\, Y.\, Jones\, L.\, … & Rost\, B. (2021). Prottrans: Toward understanding the language of life through self-supervised learning. IEEE transactions on pattern analysis and machine intelligence 2022\, 44(10)\, 7112-7127.\n[3] Hladiš\, M.\, Lalis\, M.\, Fiorucci\, S.\, & Topin\, J. Matching receptor to odorant with protein language and graph neural networks 2023. In The Eleventh International Conference on Learning Representations. \nContact : lucie.sancey@univ-grenoble-alpes.fr ou emmanuel.brun@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/jeremie-topin-department-of-chemistry-universite-cote-dazur-nice/
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
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