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BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260623T100000
DTEND;TZID=Europe/Paris:20260623T110000
DTSTAMP:20260529T152039Z
CREATED:20260529T151847Z
LAST-MODIFIED:20260529T152039Z
UID:10000179-1782208800-1782212400@sfp-alpes.fr
SUMMARY:Cyril BRESSY (Aix-Marseille Université - Institut des Sciences Moléculaires de Marseille (iSm2))
DESCRIPTION:Compartmentalized MultiCatalysis : Chirality as Probe\, Separation of Enantiomers & Catalytic Active Transport\nRésumé : \nLife solves the problem of different reaction conditions by the compartmentalization of the catalytic systems. This solution opens new opportunities for the chemists using synthetic membranes to isolate the catalytic systems. \nWe were interested to study the diffusion of molecules through a semi-permeable membrane when no gradient of concentration does exist. Chirality was found to be helpful to be used as probe to study such systems (1). A scale of diffusion energy depending on the structure of the solute was established providing fruitful lessons. \nBased on these results\, compartmentalized multicatalytic systems were set up for different goals : \n– A system where two catalysts of opposite configurations are working in each compartment leading to the physical separation of enantiomeric products starting from a racemic substrate. This is describing a case of compartmentalized parallel kinetic resolution (CPKR)(2).\n– A system to promote the active transport of a molecule able to cross a membrane. The active transport means a transfer against the gradient of concentration (3). \nReferences \n1 .  J. Hou\, S. Chevallier-Michaud\, L. Favre\, D. Hérault & C. Bressy\, J. Membrane Sci. 2026\, in revision.\n2  . a) J. Hou\, S. Chevallier-Michaud\, M. Jean\, L. Favre\, D. Hérault & C. Bressy\, J. Am. Chem. Soc. 2023\, 145\, 27236-27241; b) J. Hou\, D. Hérault\, C. Bressy\, “Method for simultaneous preparation of separated enantiomeric products from racemic substrates”\, Extension internationale PCTEP2022085983 (2022) WO2023126186A1.\n3 . Manuscript in preparation \n_ \nContact : adrien.quintard@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/cyril-bressy-aix-marseille-universite-institut-des-sciences-moleculaires-de-marseille-ism2/
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:20260622T133000
DTEND;TZID=Europe/Paris:20260622T153000
DTSTAMP:20260604T143528Z
CREATED:20260604T143528Z
LAST-MODIFIED:20260604T143528Z
UID:10000188-1782135000-1782142200@sfp-alpes.fr
SUMMARY:Soutenance de Thèse de Khadeeja MUBASHIRA (CEA-Irig/IBS)
DESCRIPTION:Étude de la séparation de phase de la phosphoprotéine du virus de la rage et de sa régulation par LC8\nRésumé : \nRabies virus (RABV) replication occurs in cytoplasmic\, membrane-less compartments known as Negri bodies (NBs)\, formed through liquid-liquid phase separation (LLPS) of viral components. The phosphoprotein (RABV P) is a central\, intrinsically disordered scaf fold of the viral replication machinery. This thesis investigates the structural\, biophysical\, and dynamic properties of RABV P\, with emphasis on its phase separation behavior and interactions with molecular partners. To enable this\, recombinant expression and purification protocols were optimized to produce stable\, high-quality protein samples for reproducible analyses. \nWe first characterized the intrinsic phase behavior of RABV P in vitro. The protein undergoes thermoresponsive LLPS with a lower critical solution temperature (LCST)\, forming reversible condensates within a narrow range of protein and salt concentrations. This process is driven by multivalent interactions within a heterogeneous ensemble of conformations\, where dimers assemble into higher-order oligomers prior to phase separation. The resulting phase diagram reveals a complex\, reentrant system governed by a balance between electrostatic repulsion and attractive dipole-dipole interactions. \nThe role of ionic conditions was further examined. While NaCl induced reentrant phase separation\, LLPS strongly depended on ion identity rather than ionic strength alone. Chloride salts promoted condensate formation\, whereas bromide salts did not\, indicating ion-specific (Hofmeister-type) effects. Systematic trends showed that fluoride enhances phase separation\, while cation effects are weaker. Divalent ions also promoted LLPS\, highlighting valency contributions. Chemical perturbations confirmed that condensates are stabilized by weak interactions: 1\,6-hexanediol partially disrupted droplets\, whereas ATP fully dissolved them. Notably\, RABV P intrinsically phase separates even in water\, modulated by pH\, protein concentration\, and ionic conditions. \nTime-resolved small-angle X-ray scattering (SAXS) revealed the structural evolution underlying LLPS. Following a temperature jump\, RABV P undergoes a hierarchical assembly process\, transitioning from dispersed species to larger structures. Early conformational rearrangements precede the formation of intermediate clusters\, followed by growth into larger assemblies. These structures remain disordered and liquid-like\, supporting a multistep nucleation-and-growth mechanism. \nThe host protein LC8 was investigated as a regulator of RABV P condensation. LC8 binds a conserved motif in RABV P with high affinity\, forming a defined complex and partitioning into condensates. Functionally\, LC8 enhances phase separation by increasing condensate size\, enriching RABV P in the dense phase\, and broadening the phase-separation window. It shifts phase boundaries toward lower concentrations and temperatures while preserving liquid-like properties. These results indicate that LC8 actively promotes condensation by stabilizing interaction-competent conformations and enhancing intermolecular connectivity. \nTo assess whether LC8 can compensate for intrinsic multivalency\, a truncated RABV P lacking the dimerization domain was analyzed. Although LC8 bound this construct\, the interaction was weaker and failed to restore robust phase separation. Only weak condensation was observed under crowding conditions\, demonstrating that LC8 cannot substitute for the native dimerization-driven multivalency.\nOverall\, this work establishes RABV P as a finely tuned multivalent scaffold whose phase behavior arises from the interplay of intrinsic disorder\, ion-specific effects\, and hierarchical assembly. LLPS emerges as a multistep\, non-ideal process rather than a simple binary transition. LC8 acts as a key host regulator that enhances phase separation without altering condensate dynamics\, while intrinsic multivalency remains essential. These findings provide a mechanistic framework for understanding viral condensate formation and highlight potential avenues for antiviral intervention. \n_ \nContact : alain.farchi@cea.fr
URL:https://sfp-alpes.fr/event/soutenance-de-these-de-khadeeja-mubashira-cea-irig-ibs/
LOCATION:Amphi A de Biologie\, Rue de la Piscine\, Saint-Martin-d'Hères\, 38400\, France
CATEGORIES:Soutenance,Soutenance de Thèse
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260619T100000
DTEND;TZID=Europe/Paris:20260619T110000
DTSTAMP:20260529T130829Z
CREATED:20260529T130829Z
LAST-MODIFIED:20260529T130829Z
UID:10000169-1781863200-1781866800@sfp-alpes.fr
SUMMARY:Soutenance HDR de Julien PERARD (Irig/LCBM)
DESCRIPTION:From iron to biohydrogen: how bacteria are inspiring the biotechnologies of tomorrow\nRésumé : \nMicroorganisms play a crucial role in biotechnologies\, enabling the transformation of matter into high-value gases and biomass. At a time when the climate emergency demands a rethinking of our energy models\, my work is part of a responsible research approach\, aiming to reconcile scientific excellence\, environmental sustainability\, and economic viability.​\nOver the past twelve years\, I have dedicated my career to understanding the molecular mechanisms of the Fur and SUF systems (Fe-S cluster biogenesis\, bacterial virulence) and to studying nickel insertion into CO dehydrogenase\, using integrated structural approaches (SAXS\, MALLS\, crystallography). Since 2021\, I have refocused my research on energy biotechnologies. After a brief overview of my scientific journey\, I will detail my projects on developing solutions for BioH₂ production and CO₂ valorization\, particularly through the « Bioraffinery » project (combining photofermentation and methanogenesis)\, inspired by my participation in the 2022 EIC Horizon Prize. I have optimized photobioreactors (PBRs)\, improving their light efficiency and achieving up to 5 mol H₂/mol of substrate from PLA waste.​\nToday\, I am working on optimizing microbial strains and culture conditions\, as well as integrating circular processes for the joint production of BioH₂/BioCH₄. In collaboration with Génoscope\, CEA Tech\, and industrial partners\, I have developed advanced biorafineries to convert by-products into biofuels.​\nMy work\, at the interface of biophysics\, enzymology\, and engineering\, is part of a decarbonized bioeconomy approach.​ \n_ \nContact : alain.farchi@cea.fr
URL:https://sfp-alpes.fr/event/soutenance-hdr-de-julien-perard-irig-lcbm/
LOCATION:DCM – Bât Nanobio\, DCM 570 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Soutenance,Soutenance HDR
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260619T093000
DTEND;TZID=Europe/Paris:20260619T103000
DTSTAMP:20260529T151254Z
CREATED:20260529T151254Z
LAST-MODIFIED:20260529T151254Z
UID:10000178-1781861400-1781865000@sfp-alpes.fr
SUMMARY:Alain WALCARIUS (Laboratoire de Chimie Physique et Microbiologie pour les Matériaux et l’Environnement (LCPME)\, UMR Université de Lorraine-CNRS 7564\, Equipe Chimie et Electrochimie Analytiques\, Nancy)
DESCRIPTION:Intérêt des membranes de silice à porosité orientée en électrochimie analytique et au delà\n_ \nContact : andrew.gross@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/alain-walcarius-laboratoire-de-chimie-physique-et-microbiologie-pour-les-materiaux-et-lenvironnement-lcpme-umr-universite-de-lorraine-cnrs-7564-equipe-chimie-et-electrochimie-analytiques/
LOCATION:DCM – Bât Nanobio\, DCM 570 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260618T141500
DTEND;TZID=Europe/Paris:20260618T163000
DTSTAMP:20260529T150945Z
CREATED:20260529T150859Z
LAST-MODIFIED:20260529T150945Z
UID:10000177-1781792100-1781800200@sfp-alpes.fr
SUMMARY:Soutenance de HDR de Andrew GROSS (DCM (équipe BIOCEN))
DESCRIPTION:Nanostructured porous frameworks to control and drive bioelectrocatalysis for sensing and energy generation\n_ \n Contact : Nathalie.Camerino@univ-grenoble-alpes.fr \n 
URL:https://sfp-alpes.fr/event/soutenance-de-hdr-de-andrew-gross-dcm-equipe-biocen/
LOCATION:DCM – Bât Nanobio\, DCM 570 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Soutenance,Soutenance HDR
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260618T140000
DTEND;TZID=Europe/Paris:20260618T160000
DTSTAMP:20260529T145529Z
CREATED:20260529T144049Z
LAST-MODIFIED:20260529T145529Z
UID:10000174-1781791200-1781798400@sfp-alpes.fr
SUMMARY:Soutenance HDR de Rebekka WILD (IRIG / IBS)
DESCRIPTION:Molecular insight into the wonderful complex world of protein glycosylation\nRésumé : \nThis research habilitation focuses on the characterization of a class of enzymes – glycosyltransferases – that are involved in the biosynthesis of glycoproteins. It emphasizes the use of cryo-electron microscopy (cryo-EM) to study these enzymes\, for which obtaining mechanistic insights remains a challenging task to this day. The presentation will provide an overview of the different types of glycosylation found in humans\, along with a detailed description of the biosynthetic pathways of N-linked glycans and glycosaminoglycans. Subsequently\, I describe my work over the past ten years\, which is divided into two parts : my postdoctoral studies on a central enzyme complex of the N-linked glycosylation machinery and the work of my research team at the Institut de Biologie Structurale focusing on heparan sulfate and chondroitin sulfate biosynthesis. It closes with an overview on ongoing and future projects.​ \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. \n\nN’oubliez pas de vous munir d’une pièce d’identité.​
URL:https://sfp-alpes.fr/event/rebekka-wild-irig-ibs/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Soutenance,Soutenance HDR
ORGANIZER;CN="IBS":MAILTO:ibs.seminaires@ibs
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260615T110000
DTEND;TZID=Europe/Paris:20260615T120000
DTSTAMP:20260529T122925Z
CREATED:20260529T122925Z
LAST-MODIFIED:20260529T122925Z
UID:10000168-1781521200-1781524800@sfp-alpes.fr
SUMMARY:Richard HOLZ (School of Mines\, Golden\, Colorado\, USA)
DESCRIPTION:Targeting Iron-Sulfur Cluster Biosynthesis in Staphylococcus aureus : Mechanistic Insights into the SUF Pathway\n_ \nL’accès au CEA Grenoble nécessite un avis de rendez-vous. Merci d’envoyer la copie de votre pièce d’identité à sandrine.ollagnier@cea.fr\, avant le 08 juin 2026.\nPensez à vous munir de cette pièce d’identité le jour de votre visite. \n  \n 
URL:https://sfp-alpes.fr/event/richard-holz-school-of-mines-golden-colorado-usa/
LOCATION:CEA – Salle de séminaire IRIG (104 – bâtiment C3)\, 17\, avenue des Martyrs\, Grenoble\, 38000\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260612T110000
DTEND;TZID=Europe/Paris:20260612T120000
DTSTAMP:20260604T142423Z
CREATED:20260604T142423Z
LAST-MODIFIED:20260604T142423Z
UID:10000187-1781262000-1781265600@sfp-alpes.fr
SUMMARY:Alexandra COLIN (CEA-Irig/LPCV)
DESCRIPTION:Dynamics and Scaling of Competitive Actin Architectures\nRésumé : \n\nCells constantly experience environmental changes requiring a fast adaptation of their different actin structures. However\, the mechanisms governing the size and dynamics of these multiple actin structures remain unknown. Decoupling the various parameters that would provide a complete understanding of these mechanisms is very complicated in a cellular context. This is why we have developed a bottom-up approach to identify the key molecular mechanisms that determine the size and coexistence of multiple competing actin architectures. We used a reconstituted system consisting of purified proteins and substrates to localize actin polymerization in microwells\, enabling us to work with a limited number of components. With this system\, we reconstituted several dynamic actin architectures\, competing for a limited pool of protein\, over a period of multiple hours. This allowed us to gain key insights into physiological functions related to actin turnover. I will show how we used this system to study the limits of scaling in dynamic structures\, as well as the limits of coexistence in actin networks under resource-limited conditions. Finally\, I will show how we can recapitulate these results in a complementary cellular system\, in which we have demonstrated that an increase in spreading area leads to a decrease in overall turnover\, due to a predominance of structures with low turnover.​​​​​\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/alexandra-colin-cea-irig-lpcv/
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:20260611T130000
DTEND;TZID=Europe/Paris:20260611T140000
DTSTAMP:20260604T104156Z
CREATED:20260507T093550Z
LAST-MODIFIED:20260604T104156Z
UID:10000147-1781182800-1781186400@sfp-alpes.fr
SUMMARY:Anne LOPES (I2BC - Gif sur Yvette)
DESCRIPTION:Emergence of microproteins and de novo genes from noncoding DNA\n_ \nContact : lucie.lamothe@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/anne-lopes-i2bc-gif-sur-yvette/
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:20260611T113000
DTEND;TZID=Europe/Paris:20260611T123000
DTSTAMP:20260605T140154Z
CREATED:20260605T140154Z
LAST-MODIFIED:20260605T140154Z
UID:10000192-1781177400-1781181000@sfp-alpes.fr
SUMMARY:Kirill NOURSKI (University of Iowa\, USA)
DESCRIPTION:What the insula hears and does : Insights from human intracranial electrophysiology\nRésumé : \nThe human insula is known to be involved in auditory processing\, though its detailed response properties remain elusive. Intracranial recordings in human neurosurgical patients provide a unique opportunity to characterize the functional properties of the human insula with high spatiotemporal resolution. Local field potential recordings reveal that posterior insula (InsP) is characterized by larger broadband gamma (30-150 Hz) responses to monosyllabic words compared to anterior insula (InsA). Both subdivisions of the insula generate evoked responses to novel sounds. Single neurons within InsP and\, to a lesser extent\, InsA\, respond to simple sounds in the absence of a behavioral context. InsP and InsA share similar res9ng state functional connectivity profiles with limbic structures. InsP is more closely linked to activity propagated from early auditory cortex\, while InsA is more tightly coupled with prefrontal\, anterior temporal regions and the amygdala. Clinical case studies identify language and music perception deficiencies associated with insula lesions. Finally\, single unit recordings during emergence from general anesthesia reveal a temporal dissociation between reactivation of limbic structures and the insula\, the laPer marking the transition to connected consciousness and the capacity to act on commands. Together\, these results begin to characterize the insula’s place in the auditory hierarchy\, with implications ranging from sensory processing to conscious awareness of our surroundings. \n_ \nContact : julien.bastin@univ-grenoble-alpes.fr \n  \n 
URL:https://sfp-alpes.fr/event/kirill-nourski-university-of-iowa-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
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260609T140000
DTEND;TZID=Europe/Paris:20260609T150000
DTSTAMP:20260529T145613Z
CREATED:20260529T143536Z
LAST-MODIFIED:20260529T145613Z
UID:10000173-1781013600-1781017200@sfp-alpes.fr
SUMMARY:Soutenance HDR de Tristan WAGNER (IRIG / IBS)
DESCRIPTION:Characterization of native enzymes to understand how anaerobic microbes impact biogeochemical cycles\nRésumé : \nMicrobes are actors of the biogeochemical cycles\, transforming gases\, minerals\, and biological matter through enzymatic reaction chains. Among them\, anaerobic archaea\, namely methanogens and methanotrophs\, play a key role in converting planetary carbon\, nitrogen\, and sulfur\, impacting the biosphere and providing green sustainable solutions for our modern society. The last fourteen years of my career were devoted to understanding the molecular basis of these microbial transformations\, such as methane production or degradation\, CO2 and carbon monoxide conversion to biofuels\, N2 fixation\, and sulfur cycling. Since these enzymes harbor O2-sensitive complicated metallocofactors\, most of my work relies on native protein purification from the microbes themselves under strict O2 exclusion. After a brief presentation of my career and PhD project\, the presented work summarizes my most renowned breakthrough regarding the elucidation of molecular tricks in carbon\, nitrogen\, and sulfur metabolisms in methane-generating microbes\, including their regulatory networks. Then\, the latest research led by my group is introduced with : (i) how methanogens munch on methylated substrates such as methanol and lignin-degradation products\, (ii) how an industrial bacterium turns waste gases into biofuels\, (iii) the study of a microbial consortia “that burn” methane and ethane without oxygen via a native approach. Finally\, I will present the features of my past group and my future laboratory. ​​ \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/tristan-wagner-irig-ibs/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Soutenance,Soutenance HDR
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260608T140000
DTEND;TZID=Europe/Paris:20260608T160000
DTSTAMP:20260529T142409Z
CREATED:20260529T142409Z
LAST-MODIFIED:20260529T142409Z
UID:10000171-1780927200-1780934400@sfp-alpes.fr
SUMMARY:Soutenance de Thèse de Antoine CURÉ (IRIG / Symmes)
DESCRIPTION:Vers des copolymères à blocs donneur-accepteur π-conjugués à structure et composition précisément définies : caractérisation avancée et stratégies de synthèse\nRésumé : \nDans un contexte mondial de crise énergétique et de raréfaction des ressources fossiles\, la transition vers les énergies renouvelables constitue un enjeu majeur. Parmi elles\, l’énergie photovoltaïque occupe une place importante. Cependant\, alors que les panneaux solaires au silicium approchent de leurs limites en rendement et en coûts de production\, l’émergence de solutions complémentaires devient nécessaire. Les cellules solaires organiques constituent une alternative intéressante\, avec des rendements atteignant 21 % dans des conditions standard en laboratoire en 2026. Elles présentent également de bonnes performances en lumière diffuse et offrent un potentiel de production à faible coût de dispositifs flexibles et recyclables. Toutefois\, leur stabilité à long terme reste un obstacle à leur industrialisation. La couche active\, composée d’un donneur (polymère) et d’un accepteur (petite molécule)\, subit au cours du temps une séparation de phase qui dégrade les performances. Malgré les progrès réalisés avec les accepteurs polymères\, la viabilité à long terme de ces dispositifs reste à démontrer. ​​​​\n​ Depuis le début des années 2020\, les matériaux monocomposants sont sérieusement envisagés comme une solution à ces problèmes d’instabilité. Contrairement aux mélanges tout-polymères\, ils reposent sur des copolymères à blocs reliant de manière covalente les segments donneurs et accepteurs\, limitant leur mobilité relative et la ségrégation de phase. Si les premières études rapportent des résultats encourageants\, leur structure et leurs propriétés thermiques restent encore mal comprises. La synthèse et l’étude approfondie de ces systèmes constituent l’objectif de cette thèse. ​​​​\nAprès un premier chapitre introductif\, le deuxième chapitre est consacré à l’étude de deux matériaux modèles : le PTQ10\, polymère donneur parmi les plus performants de la littérature\, et le PIDTe\, un polymère accepteur de structure proche de systèmes connus mais dont la synthèse est simplifiée. Ce travail valide leur pertinence comme système modèle et permet de mettre en place les méthodes de caractérisation utilisées dans la suite de la thèse. Le troisième chapitre explore l’analyse structurale des monocomposants par résonance magnétique nucléaire (RMN). L’utilisation de molécules modèles permet d’identifier les signaux caractéristiques des liaisons entre blocs donneurs et accepteurs et d’estimer le nombre moyen de jonctions dans les chaînes de copolymères. Une approche complémentaire par RMN à diffusion ordonnée (DOSY) est également évaluée afin d’estimer la composition des matériaux. Le quatrième chapitre s’intéresse aux propriétés thermiques des monocomposants. Une méthode basée sur la spectroscopie UV-visible est développée pour suivre les évolutions morphologiques à l’échelle nanométrique à l’état solide. Associée à la diffraction des rayons X en incidence rasante (GIWAXS)\, à la microscopie à force atomique (AFM) et à la calorimétrie différentielle à balayage rapide (flash DSC)\, elle permet de comparer la stabilité thermique des monocomposants à celle des mélanges tout-polymères. ​​​​\nEnfin\, le cinquième chapitre vise à synthétiser des monocomposants de structure mieux définie. La modification du monomère du PTQ10 permet d’obtenir un polymère possédant une fonction réactive terminale unique et une structure régiorégulière. Cette régiorégularité améliore l’organisation des chaînes latérales mais semble perturber celle du cœur π-conjugué\, affectant les propriétés optoélectroniques. Différentes stratégies de synthèse de copolymères di- et tri-blocs sont ensuite développées\, ouvrant de nouvelles perspectives. ​​​​\nEn conclusion\, cette thèse contribue à une meilleure compréhension des matériaux monocomposants pour les cellules solaires organiques et propose de nouvelles approches d’analyse et de synthèse pour des dispositifs plus stables et performants. ​​​​ \n_ \nContact : odile.rossignol@cea.fr
URL:https://sfp-alpes.fr/event/soutenance-de-these-de-antoine-cure-irig-symmes/
LOCATION:GreEN-ER – Amphi 2A003\, 21 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:20260604T140000
DTEND;TZID=Europe/Paris:20260604T150000
DTSTAMP:20260529T150404Z
CREATED:20260529T150404Z
LAST-MODIFIED:20260529T150404Z
UID:10000176-1780581600-1780585200@sfp-alpes.fr
SUMMARY:Aurélien DE LA TORRE (ICMMO\, CNRS/Université Paris-Saclay)
DESCRIPTION:Designing cycloadditions to enable total synthesis\nRésumé : \nAsymmetric catalysis is a key topic in organic synthesis\, as it allows the formation of new bonds while controlling stereogenic centers\, which are inherent to natural products and biologically active substances. On the other hand\, dual catalysis is an efficient approach to operate multiple chemical operations through a one-pot process. In this presentation\, we will discuss our recent developments in asymmetric catalysis and dual catalysis\, as well as their application to a concrete total synthesis\nproblem. \n_ \nContact : adrien.quintard@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/aurelien-de-la-torre-icmmo-cnrs-universite-paris-saclay/
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:20260604T113000
DTEND;TZID=Europe/Paris:20260604T123000
DTSTAMP:20260528T151721Z
CREATED:20260528T151721Z
LAST-MODIFIED:20260528T151721Z
UID:10000161-1780572600-1780576200@sfp-alpes.fr
SUMMARY:Timothée PROIX (ETH Zurich)
DESCRIPTION:Neural manifolds for speech processing\nRésumé : \nSpeech comprehension requires the brain to represent and combine phonetic\, lexical\, and semantic information across a linguistic hierarchy. Yet how neuronal populations implement these representations and compositions remains unclear. In this talk\, I will show how the framework of neural manifolds offers a powerful lens for this question\, combining intracranial recordings in the human cortex with population-level analyses and computational modeling.\nI will show that linguistic features are encoded as distinct trajectories on low-dimensional manifolds\, which can be resolved analytically by fitting recurrent neural networks directly to the neural data. I will then discuss how these trajectory-based representations are combined across levels\, from the composition of phonetic features into syllables\, to the interactions between phonetic and semantic representations. Together\, these perspectives point toward a population-level mechanism for the representation and composition of speech processing. \nContact : michael.pereira@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/timothee-proix-eth-zurich/
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:20260602T110000
DTEND;TZID=Europe/Paris:20260602T120000
DTSTAMP:20260528T153318Z
CREATED:20260528T153318Z
LAST-MODIFIED:20260528T153318Z
UID:10000163-1780398000-1780401600@sfp-alpes.fr
SUMMARY:Damien GREGOIRE (IGMM\, Montpellier\, France)
DESCRIPTION:In vivo modeling of tumor heterogeneity in hepatocellular carcinoma\nRésumé : \nOur research aims at a better understanding of how various combinations of oncogenic events drive tumorigenesis. We address two major questions in cancer biology\, within the context of inter-tumoral heterogeneity: (1) what mechanisms underlie oncogenic cooperation in shaping of the tumor cell fate\, and (2)\, how does the genetic identity of a tumor influence its interactions with the microenvironment ? \nWe explore these questions in the context of hepatocellular carcinoma (HCC)\, the most common primary liver cancer. Our approach combines functional studies with advanced preclinical mouse models\, particularly in vivo hepatocyte transfection via hydrodynamic gene transfer. We focus our investigations on tumors driven by either FGF19 overexpression or a spectrum of p53 mutations. \nIn this talk at IAB\, I will present recent findings on these two distinct families of hepatic tumors. Our ultimate goal is to elucidate how the genetic profile of HCC shapes the tumor cell phenotype\, its interactions with the tumor microenvironment—especially immune cells—and its response to treatments. \n_ \nContact : thomas.decaens@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/damien-gregoire-igmm-montpellier-france/
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:20260528T140000
DTEND;TZID=Europe/Paris:20260528T150000
DTSTAMP:20260430T130828Z
CREATED:20260430T130321Z
LAST-MODIFIED:20260430T130828Z
UID:10000143-1779976800-1779980400@sfp-alpes.fr
SUMMARY:Charles McCRORY (Chemistry and Macromolecular Science and Engineering - University of Michigan\, USA)
DESCRIPTION:Breaking Scaling Relationships in Molecular Electrocatalysts for the CO2 Reduction Reaction\nProfesseur invité UGA du 15/05 au 15/06/2026 \nRésumé : \nFor molecular electrocatalysts\, beneficial decreases in effective overpotential are typically correlated with detrimental decrease in catalytic activity. This scaling relationship arises when both effective overpotential and kinetic reactivity scale with metal site nucleophilicity. Our research strategy is to break typical molecular scaling  relationships by designing molecular electrocatalysts with redox-active ligands where the catalytic reaction is initiated by redox activation of the ligand. These systems decouple metal site nucleophilicity from effective overpotential\, thus allowing us to break the correlation between catalyst reactivity and effective overpotential. \nIn this talk\, we will discuss how incorporating electronic substituents onto the redox-active ligand structure of Co(pyridyldiimine) complexes facilitates ligand reduction and leads to an inverse molecular scaling relationship for electrocatalytic CO2 reduction. We will explore the strategy of incorporating cationic charges into the complex as a means of breaking and inverting scaling relationships both through the incorporation of charged substituents into the ligand scaffold and through construction of homo- and heterobimetallic Co-Co and Co-Zn complexes. We will also discuss whether the activity enhancement from these cationic substituents is best described as\nthrough-space electrostatic stabilization of reactive intermediates\, or through-bond inductive effects related to the stabilization of the catalytic intermediates. Finally\, we will explore how these complexes operate for CO2 reduction and other electrocatalytic reductions when incorporated into larger coordination polymers and macromolecular scaffolds. \n_ \nContact : cyrille.costentin@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/charles-mccrory-chemistry-and-macromolecular-science-and-engineering-university-of-michigan-usa/
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:20260528T130000
DTEND;TZID=Europe/Paris:20260528T140000
DTSTAMP:20260521T094049Z
CREATED:20260507T093329Z
LAST-MODIFIED:20260521T094049Z
UID:10000146-1779973200-1779976800@sfp-alpes.fr
SUMMARY:Vincent LACROIX  (LBBE - Lyon)
DESCRIPTION:Repeats : the dark side of transcriptome assembly\n_ \nContact : lucie.lamothe@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/vincent-lacroix-lbbe-lyon/
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:20260526T110000
DTEND;TZID=Europe/Paris:20260526T120000
DTSTAMP:20260424T075655Z
CREATED:20260424T075655Z
LAST-MODIFIED:20260424T075655Z
UID:10000126-1779793200-1779796800@sfp-alpes.fr
SUMMARY:Mark GLOVER (Department of Biochemistry\, University of Alberta\, Edmonton\, Canada)
DESCRIPTION:Mechanism of sRNA recognition and regulation by FinO RNA chaperones\nRésumé : \nThe FinO family of RNA chaperones regulate sRNA function throughout gram negative bacteria. Many of the best characterized family members bind to rho-independent transcription termination structures at the 3’ ends of sRNAs and mediate pairing of the sRNA with their mRNA targets. The crystal structure of the FinO domain of the Legionella pneumophila chaperone RocC bound to its sRNA target reveals a novel interaction that recognizes both the stem and the 3’ end of the terminator structure. The structure suggests a mechanism by which different FinO proteins can selectively bind RNAs with different 3’ tail lengths\, which is likely conserved throughout the FinO family. Biochemical and in vivo studies indicate that intrinsically disordered regions adjacent to the FinO domain are also essential for sRNA regulation\, by remodeling RNA structure to facilitate RNA-RNA association. \n__ \nHôte : Dr Nicolas Coquelle (IBS/Groupe Dynamique et Cinétique des processus moléculaires) \nRappel : L’accès au campus EPN nécessite un avis de rendez-vous. A cet effet merci d’adresser votre demande à ibs.seminaires@ibs.fr (au moins 48h à l’avance).
URL:https://sfp-alpes.fr/event/mark-glover-department-of-biochemistry-university-of-alberta-edmonton-canada/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260521T133000
DTEND;TZID=Europe/Paris:20260521T163000
DTSTAMP:20260430T124956Z
CREATED:20260430T124859Z
LAST-MODIFIED:20260430T124956Z
UID:10000142-1779370200-1779381000@sfp-alpes.fr
SUMMARY:Soutenance de Thèse de Furhan ABDUL-REZAK (DCM (équipe I2BM) - IAB)
DESCRIPTION:Selective Conjugation of Gold Nanoclusters with Macromolecules: From Functionalization to Assembly\nRésumé : à venir \n_ \nContact : nathalie.camerino@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/soutenance-de-these-de-furhan-abdul-rezak-dcm-equipe-i2bm-iab/
LOCATION:IAB – Salle de séminaire\, IAB Site Santé - Allée des Alpes\, La Tronche\, 38700\, France
CATEGORIES:Soutenance,Soutenance de Thèse
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260521T113000
DTEND;TZID=Europe/Paris:20260521T123000
DTSTAMP:20260521T085300Z
CREATED:20260521T085300Z
LAST-MODIFIED:20260521T085300Z
UID:10000152-1779363000-1779366600@sfp-alpes.fr
SUMMARY:Claudie LEMERCIER (Responsable "Associations de patients\, Société et Recherche »\, Délégation Inserm AURA)
DESCRIPTION:Les Associations de Patients et la Recherche\nRésumé : \nLes associations de patients sont un maillon indispensable de notre systèm de santé. Si le financement de projets ou de bourses sont bien connus des chercheurs\, les associations de patients agissent à bien d’autres niveaux qui restent largement méconnus des scientifiques. \nVenez découvrir les actions menées depuis dix ans à la délégation Inserm AuRA pour rapprocher les chercheurs des associations de patients mais également de grand public\, et donner davantage de visibilité aux travaux réalisés dans les laboratoires. La recherche participative en santé sera également abordée. \n_ \nContact : emmanuel.barbier@univ-grenoble-alpes.fr \n  \n  \n 
URL:https://sfp-alpes.fr/event/claudie-lemercier-responsable-associations-de-patients-societe-et-recherche-delegation-inserm-aura/
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:20260521T100000
DTEND;TZID=Europe/Paris:20260521T110000
DTSTAMP:20260430T123713Z
CREATED:20260430T123218Z
LAST-MODIFIED:20260430T123713Z
UID:10000141-1779357600-1779361200@sfp-alpes.fr
SUMMARY:Chloé GRAZON (Laboratoire de Chimie des Polymères Organiques (LCPO)\, Université de Bordeaux / CNRS / Bordeaux INP\, Pessac)
DESCRIPTION:Luminescent nanoparticles as bright nanotools for biosensing & bioimaging\nRésumé : à venir \n_ \nContact : galina.dubacheva@univ-grenoble-alpes.fr \n 
URL:https://sfp-alpes.fr/event/chloe-grazon-laboratoire-de-chimie-des-polymeres-organiques-lcpo-universite-de-bordeaux-cnrs-bordeaux-inp-pessac/
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:20260507T140000
DTEND;TZID=Europe/Paris:20260507T150000
DTSTAMP:20260430T122840Z
CREATED:20260430T122734Z
LAST-MODIFIED:20260430T122840Z
UID:10000140-1778162400-1778166000@sfp-alpes.fr
SUMMARY:Amaury PATIN (Expert in Organic Chemistry\, Nestlé Institute of Food Safety & Analytical Sciences (NIFSAS)\, Lausanne\, Suisse)
DESCRIPTION:The Journey of an Organic Chemist : What Organic Chemistry trains you for— From Drug Discovery toFood (Safety)\nRésumé : \nOrganic chemistry plays a central but often under-recognized role in addressing complex industrial challenges that extend well beyond molecule synthesis. In this seminar\, I will describe how training in organic chemistry can be leveraged across multiple industrial domains\, based on my career spanning academia\, biotech\, and industrial research within a multinational food company. \nThe talk presents a personal career journey illustrating the diversity of opportunities available to organic chemists. Starting from doctoral and postdoctoral research in organic chemistry\, I moved into medicinal chemistry within a biotech startup before joining Nestlé Research\, where organic chemistry became a central tool for addressing challenges in ingredient innovation and food safety. \nThrough selected case studies\, I will show how the same fundamental chemical concepts — reactivity\, molecular structure\, metabolism — can be applied in very different contexts\, from drug discovery to food safety. The seminar will also address the evolution from hands-on scientist to project manager and group leader\, highlighting the importance of soft skills such as communication\, interdisciplinarity\, and leadership. \n_ \nContact : sandrine.py@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/amaury-patin-expert-in-organic-chemistry-nestle-institute-of-food-safety-analytical-sciences-nifsas-lausanne-suisse/
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:20260507T130000
DTEND;TZID=Europe/Paris:20260507T140000
DTSTAMP:20260424T125214Z
CREATED:20260424T125214Z
LAST-MODIFIED:20260424T125214Z
UID:10000133-1778158800-1778162400@sfp-alpes.fr
SUMMARY:Pierre GARCIA (LCB\, Marseille)
DESCRIPTION:When life plays LEGOs : Ancient evolution and extreme diversity of homologous oxidoreductases involved in energy production\n_ \nContact : lucie.lamothe@univ-grenoble-alpes.fr \n 
URL:https://sfp-alpes.fr/event/pierre-garcia-lcb-marseille/
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:20260506T113000
DTEND;TZID=Europe/Paris:20260506T123000
DTSTAMP:20260430T120458Z
CREATED:20260430T115832Z
LAST-MODIFIED:20260430T120458Z
UID:10000138-1778067000-1778070600@sfp-alpes.fr
SUMMARY:Adeline LACROIX (Centre for Addiction and Mental Health\, Toronto\, Canada)
DESCRIPTION:Towards an Understanding of Sex Differences in Socio-Emotional Processing in Autism\nRésumé : \nAutism is characterized by persistent difficulties in social interaction and social cognition. These difficulties are partly related to atypical processing of socio-emotional signals\, including emotional facial expressions. Although core autistic characteristics are observed in both males and females\, increasing evidence suggests that autistic females often show a more subtle socio-emotional profile\, marked by greater attention to social stimuli and more typical-appearing social behavior. However\, this profile remains insufficiently characterized\, and the underlying neurobiological mechanisms are still poorly understood.\n\nGiven the central role of face processing in social cognition\, we conducted a series of behavioral and EEG studies to investigate sex differences in autism during face processing at different stages of attentional processing. Our results reveal sex-related differences in autism from early stages of face processing\, with autistic females showing an intermediate profile between autistic males and non-autistic females. Together\, these findings indicate that aggregating males and females may obscure meaningful neurocognitive differences in socio-emotional processing and highlight the need for sex-informed experimental designs and theoretical frameworks in autism research. They further suggest that early differences in socio-emotional processing may contribute to the subtler phenotypic presentation of autism in females.\n_\nContact : michael.pereira@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/adeline-lacroix-centre-for-addiction-and-mental-health-toronto-canada/
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:20260506T110000
DTEND;TZID=Europe/Paris:20260506T120000
DTSTAMP:20260430T140721Z
CREATED:20260430T140156Z
LAST-MODIFIED:20260430T140721Z
UID:10000144-1778065200-1778068800@sfp-alpes.fr
SUMMARY:Tiffany HO (Lab of Prof Brian Wilson at the Princess Margaret Cancer Center\, Toronto\, Canada)
DESCRIPTION:Redefining photodynamic therapy beyond local : Nanoparticle-enabled photodynamic-immune stimulation for treatment of hot and cold cancers\nRésumé : \nPhotodynamic therapy (PDT) is a cancer-treatment modality that\, under the appropriate treatment parameters\, can induce immunogenic tumor cell death and stimulate anti-tumor immunity (photodynamic immune stimulation\, PDIS). This has the potential to prime adaptive immune responses capable of targeting distant\, untreated lesions\, as well as eradicating primary treated tumor. The clinical impact of PDT has been limited by conventional photosensitizers\, which often exhibit poor tumor selectivity and insufficient immune activation. Nanomedicine-based photosensitizer platforms offer a promising strategy to overcome such limitations. Porphysomes (PS)\, a class of all-organic\, multifunctional porphyrin-lipid nanoparticles currently in Phase I clinical trials for positron emission tomography (PET) imaging of metastatic gynecological cancers\, represent one such platform. \nThis seminar will focus on our work investigating PS-PDIS to drive systemic anti-tumor immunity across tumor models of different immunogenicity\, including immunologically “hot” colorectal (CT26) tumors and “cold” melanoma (B16F10) and ovarian (ID8) tumors. The findings establish a strategy to expand PDT beyond localized tumor ablation toward systemic disease control\, including prevention of recurrence and metastasis in cold tumors typically resistant to conventional immunotherapies. The seminar will also highlight ongoing efforts to develop gold nanocluster-based platforms for both light- and radiation-mediated immune stimulation in pancreatic cancer\, further expanding the scope of nanomaterial-enabled photodynamic and radiodynamic immune stimulation. \nThis work was supported by the Terry Fox Research Institute (PPG 1137) and the Government of Canada’s New Frontiers in Research Fund (NFRF) (#NFRFT-2020-00573). » \n_ \nContact : anne-laure.bulin@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/tiffany-ho-lab-of-prof-brian-wilson-at-the-princess-margaret-cancer-center-toronto-canada/
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:20260504T110000
DTEND;TZID=Europe/Paris:20260504T120000
DTSTAMP:20260430T115259Z
CREATED:20260430T115259Z
LAST-MODIFIED:20260430T115259Z
UID:10000137-1777892400-1777896000@sfp-alpes.fr
SUMMARY:Giulio FACCHINI (Laboratoire Matière et Systèmes Complexes\, Paris)
DESCRIPTION:Deciphering the origin of saddle-shape geometry in the microstructure of echinoderms skeleton\nRésumé : \nThe microstructure of echinoderms skeleton\, like sea stars and sea urchins\, is an impressive example of self-organization and complexity. This structure called stereom is a porous meshwork\, made of calcite\, whose surface is saddle-shaped\, and remind of minimal surfaces. Minimal surfaces have intrigued scientists for centuries\, as they can spontaneously emerge from minimizing interfacial energy like surface tension. Several studies have addressed the morphogenesis of the stereom\, in sea urchins and other echinoderms\, showing that it forms via the addition of tiny mineral bids at the tip of small skeletal elements that successively branch and bridge to form a complex network. Yet\, a global\, mechanistic\, comprehension of how biomineralizing cells control preferential deposition is still lacking. \nDuring the seminar I will present a recent work1 on the morphogenesis of the particular stereom geometry observed in the sea star P. nodosus. Here\, the stereom can take the form of a diamond Triply Periodic Minimal Surface (TPMS) which confer it specific mechanical properties. Using different marking protocols\, we provide the first experimental insight in the formation of the diamond TPMS stereom\, and show that the formation of such a highly ordered structure relies on a precise and timely coordination of the branching and bridging episodes. Moreover\, we provide experimental evidences of an organic precursor made of F – actin fibers exhibiting saddle-shape geometry. We hypothesise that such a fibers template may self-organise under mechanical tension\, thus explaining the peculiar curvature signature of the final structure. Finally\, I will present some ongoing experimental work performed on sea urchins\, showing that the same morphogenetic mechanism could be shared across very different species. \nContact : emmanuel.siefert@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/giulio-facchini-laboratoire-matiere-et-systemes-complexes-paris/
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:20260424T110000
DTEND;TZID=Europe/Paris:20260424T120000
DTSTAMP:20260402T150513Z
CREATED:20260402T150508Z
LAST-MODIFIED:20260402T150513Z
UID:10000116-1777028400-1777032000@sfp-alpes.fr
SUMMARY:Mikhail ELTSOV (Institut de Génétique et de Biologie Moléculaire et Cellulaire\, Illkirch)
DESCRIPTION:Seeing chromatin in situ : advances and challenges of human and machine vision\nRésumé : \nUsing cryo-electron tomography of vitreous sections\, we directly visualized nucleosomes and linker DNA trajectories in situ within flash frozen Drosophila embryos. Measurements of linker length and curvature revealed an irregular zigzag pattern of chromatin folding characterized by relatively limited linker bending. In favorable orientations\, individual nucleosome particles and their structural variants could be identified without the need for structural averaging. Moreover\, we detected particles containing a variable number of DNA gyres\, ranging from fewer than one to up to three\, resembling previously proposed non-octameric nucleosome-like particles. \nTo place these structural observations in the context of functional chromatin organization\, we are developing computational approaches for nucleosome identification in cellular tomograms. We believe that our approach\, Template Learning\, based on training deep-learning networks on synthetic tomographic data\, can provide a general framework for detecting small macromolecular complexes in crowded cellular environments. \n— \nHôte : Irina Gutsche (IBS/MICA)
URL:https://sfp-alpes.fr/event/mikhail-eltsov-institut-de-genetique-et-de-biologie-moleculaire-et-cellulaire-illkirch/
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:20260423T140000
DTEND;TZID=Europe/Paris:20260423T160000
DTSTAMP:20260402T155920Z
CREATED:20260402T155914Z
LAST-MODIFIED:20260402T155920Z
UID:10000119-1776952800-1776960000@sfp-alpes.fr
SUMMARY:Soutenance de Thèse de Moritz KIRCHNER (IRIG / IBS)
DESCRIPTION:Molecular bases of a multiprotein assembly linking membrane biology to stress adaptation in enterobacteria\nRésumé : \n\nEnteric bacteria encounter a variety of stress factors when infecting their host. This includes but is not limited to acid stress\, oxygen limitation and antibiotic stress. Bacteria counteract such stressors using various stress response systems. A central factor in the stress adaptation of enterobacteria is their cell envelope\, in particular their cell membrane. A system of proteins which has been demonstrated to be involved in multiple stress adaptation pathways is the RavA-ViaA-LdcI triad in Escherichia coli. RavA and ViaA are two proteins with as of yet unknown function that have been shown to sensitise E. coli to aminoglycoside antibiotics under anaerobic conditions. RavA forms a large complex with LdcI\, an inducible lysine decarboxylase which is one of the central enzymes involved in acid stress response of E. coli. Both RavA and ViaA have been shown to bind specific anionic lipids and their lipid binding capacity is strongly linked to their sensitising effect to aminoglycosides.\n​This thesis presents the exploration of the connections these three proteins have to each other and their other binding partners by optical and electron microscopy in order to elucidate how their action leads to antibiotic sensitisation and what role their connection to the cell membrane and acid stress might play in this regard. It is shown that LdcI prefers to localise to the cell periphery to efficiently counteract acid stress and that mutations of its active site lead to large domain movements which might play a crucial role in its enzymatic activity. Furthermore\, an investigation of liposome decoration by RavA and ViaA is presented\, demonstrating the effect they have on membrane shape. In addition\, the first cryo-EM structure of ViaA is presented using helical repeat proteins to stabilise the protein. Finally\, predictions of RavA and ViaA protein-protein interactions in the inner E. coli membrane reveal possible functional targets of the proteins and the implications of these new possible avenues for action are discussed with regard of the microscopy investigations.\n\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. Pensez à vous munir d’une pièce d’identité le jour de votre visite.
URL:https://sfp-alpes.fr/event/soutenance-de-these-de-moritz-kirchner-irig-ibs/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Soutenance,Soutenance de Thèse
ORGANIZER;CN="IBS":MAILTO:ibs.seminaires@ibs
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260423T130000
DTEND;TZID=Europe/Paris:20260423T140000
DTSTAMP:20260410T081351Z
CREATED:20260327T093519Z
LAST-MODIFIED:20260410T081351Z
UID:10000114-1776949200-1776952800@sfp-alpes.fr
SUMMARY:Anamaria NESCULEA (LBBE - Lyon)
DESCRIPTION:Genomic correlates of convergent phenotypic evolution in birds\nContact : lucie.lamothe@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/anamaria-nesculea-lbbe-lyon/
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:20260421T140000
DTEND;TZID=Europe/Paris:20260421T160000
DTSTAMP:20260402T154831Z
CREATED:20260402T154628Z
LAST-MODIFIED:20260402T154831Z
UID:10000118-1776780000-1776787200@sfp-alpes.fr
SUMMARY:Soutenance de Thèse de Eymeline PAGEOT (IRIG / IBS)
DESCRIPTION:Decoding chaos : a cryo-em walk through physarum polycephalum heterogeneous cell extracts\nRésumé : \n\nCryo-electron microscopy (cryo-EM) has become a central method in structural biology for determining high-resolution structures of macromolecular assemblies. However\, most cryo-EM studies still rely on highly purified samples\, which limits the range of biological systems that can be investigated. In recent years\, the analysis of cell extracts by single particle cryo-EM has emerged as an alternative strategy to explore the structural diversity of cellular proteins directly from complex mixtures. Despite its potential\, this approach remains technically challenging due to the high level of heterogeneity present in such samples and the difficulty of identifying proteins without complementary techniques such as mass spectrometry.\n\n​ The work presented in this thesis investigates the feasibility of using cryo-EM as a primary discovery tool to determine and identify protein structures directly from fractionated cell extracts. The study focuses on the plasmodial slime mould Physarum polycephalum\, a non-model eukaryotic organism whose structural proteome is largely unexplored. In contrast to most previous studies in the field\, protein identification relied solely on structural information derived from cryo-EM reconstructions.\n\nCell extracts from P. polycephalum were fractionated using biochemical separation methods and analysed by cryo-EM. Because such samples contain a wide range of proteins with different sizes\, shapes\, and abundances\, dedicated image processing strategies were developed to address the challenges posed by particle heterogeneity and flexibility. Particular attention was given to 2D classification\, particle sorting\, and iterative particle picking strategies to improve the recovery of multiple particle orientations and increase the number of particles contributing to 3D reconstructions.\n\nUsing these approaches\, fourteen macromolecular assemblies were identified and solved directly from the heterogeneous samples. In cases where the cryo-EM maps reached sufficient resolution\, atomic models could be built ab initio. For lower-resolution structures\, identification relied on structural comparison with known protein folds and structures predicted by generative tools. This work demonstrates that protein identity and putative function can be inferred directly from the structural information\, opening the possibility of structure-based genome annotation in poorly characterised organisms.\n\nBeyond the individual structures determined in this study\, this work also outlines the methodological challenges associated with large-scale structural exploration of complex biological mixtures. The largely manual nature of several steps in the workflow currently limits the throughput of the approach. Strategies to automate key stages of the pipeline\, including particle classification\, initial model generation\, and structural identification\, are therefore discussed as important directions for future development.​\n\nFinally\, this work highlights the importance of community-driven analysis and open data sharing for the continued development of large-scale structural exploration approaches. Making both the raw cryo-EM data and the solved structures publicly available enables other researchers to further investigate the dataset\, potentially identifying additional structures and improving the analysis using new computational methods\, as well as enabling the development of the methods themselves. In the longer term\, combining such « shotgun » cryo-EM approaches with advances in computational modelling and high-throughput data analysis may contribute to the systematic structural characterisation of cellular proteomes.\n\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. Pensez à vous munir d’une pièce d’identité le jour de votre visite.
URL:https://sfp-alpes.fr/event/soutenance-de-these-de-eymeline-pageot-irig-ibs/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Soutenance,Soutenance de Thèse
ORGANIZER;CN="IBS":MAILTO:ibs.seminaires@ibs
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