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DTSTART:20250330T010000
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DTSTART:20251026T010000
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TZNAME:CEST
DTSTART:20260329T010000
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DTSTART:20261025T010000
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BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260618T140000
DTEND;TZID=Europe/Paris:20260618T160000
DTSTAMP:20260617T104436
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:20260618T141500
DTEND;TZID=Europe/Paris:20260618T163000
DTSTAMP:20260617T104436
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:20260619T093000
DTEND;TZID=Europe/Paris:20260619T103000
DTSTAMP:20260617T104436
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:20260619T100000
DTEND;TZID=Europe/Paris:20260619T110000
DTSTAMP:20260617T104436
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:20260622T133000
DTEND;TZID=Europe/Paris:20260622T153000
DTSTAMP:20260617T104436
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:20260623T100000
DTEND;TZID=Europe/Paris:20260623T110000
DTSTAMP:20260617T104436
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:20260625T130000
DTEND;TZID=Europe/Paris:20260625T140000
DTSTAMP:20260617T104436
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:20260617T104436
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:20260617T104436
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
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