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X-WR-CALDESC:Évènements pour SFP Alpes
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DTSTART;TZID=Europe/Paris:20261210T140000
DTEND;TZID=Europe/Paris:20261210T160000
DTSTAMP:20261101T223012Z
CREATED:20261101T223012Z
LAST-MODIFIED:20261101T223012Z
UID:10000327-1796911200-1796918400@sfp-alpes.fr
SUMMARY:Soutenance de thèse par Lucie BASTIEN ​ (CEA-Irig/SyMMES)
DESCRIPTION:Développement de peptides comme sondes moléculaires et inhibiteurs de croissance bactérienne\nRésumé : \nL’ampleur des décès associés aux infections bactériennes et la progression de l’antibiorésistance soulignent l’importance de développer des approches de diagnostic rapide et de nouvelles stratégies thérapeutiques. Les peptides antimicrobiens (PAM) sont des biomolécules de défense contre les pathogènes produites par l’ensemble des êtres vivants. Leur intégration à un biocapteur de type micropuce a permis l’identification rapide de faibles charges bactériennes\, démontrant leur potentiel en tant que sondes de reconnaissance. Parmi le panel de PAM utilisé pour cette application des peptides conçus de novo ont présenté une activité antimicrobienne remarquable. L’optimisation de leur séquence a permis d’améliorer leur solubilité et de réduire leur toxicité envers les cellules eucaryotes\, tout en maintenant leur activité antibiotique. Ils présentent ainsi un fort potentiel pour le développement de solutions thérapeutiques et le diagnostic des bactériémies.​​​​​ \n_ \nContact : irig.communication@cea.fr
URL:https://sfp-alpes.fr/event/soutenance-de-these-par-lucie-bastien-cea-irig-symmes/
LOCATION:DCM – Bât Nanobio\, DCM 570 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Soutenance,Soutenance de Thèse
ORGANIZER;CN="IRIG - CEA":MAILTO:irig.communication@cea.fr
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BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20261215T140000
DTEND;TZID=Europe/Paris:20261215T160000
DTSTAMP:20261104T205131Z
CREATED:20261104T205131Z
LAST-MODIFIED:20261104T205131Z
UID:10000349-1797343200-1797350400@sfp-alpes.fr
SUMMARY:Jean-Maxime SCHLACHTER (IRIG / PHELIQS)
DESCRIPTION:Local electronic properties of few-layer NbSe2 and 30°-twisted bilayer graphene\nRésumé : à venir… \n_ \nContact : jean-maxime.schlachter2@cea.fr
URL:https://sfp-alpes.fr/event/jean-maxime-schlachter-irig-pheliqs/
LOCATION:CEA – Grenoble (bâtiment C5 – salle 421A)\, 17\, avenue des Martyrs\, Grenoble\, 38000\, France
CATEGORIES:Soutenance,Soutenance de Thèse
ORGANIZER;CN="IRIG - CEA":MAILTO:irig.communication@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20261215T140000
DTEND;TZID=Europe/Paris:20261215T160000
DTSTAMP:20261106T154824Z
CREATED:20261106T154824Z
LAST-MODIFIED:20261106T154824Z
UID:10000353-1797343200-1797350400@sfp-alpes.fr
SUMMARY:Soutenance de Thèse par Zeinab EL DOR​ (CEA-Irig/BGE)
DESCRIPTION:Modelling Pigmentary Dysregulation in Xeroderma Pigmentosum C via XPC-deficient Skin Cells and Pigmented Reconstructed Skin Models\nRésumé : \nXeroderma pigmentosum group C (XP-C) is a rare autosomal recessive genodermatosis stemming from mutations in XPC\, the damage-recognition factor of global genome nucleotide excision repair. Patients exhibit extreme photosensitivity and a drastically increased susceptibility to skin malignancies. Pigmentary abnormalities\, such as lentigines and hyperpigmentation of sun-exposed skin\, remain largely underexplained\, although they are the earliest clinical signs of the disease. Existing XP-C models have focused on DNA repair and carcinogenesis\, while the pigmentary aspect of the disease has received little attention. This project was designed to characterize that aspect\, from the melanocyte itself to its epidermal microenvironment. \nOur work examined the molecular consequences of XPC loss in melanocytes through quantitative proteomics (LC-MS/MS) of wild-type and previously established XPC-knockout (XPC-KO) human melanocytes\, in the presence and the absence of UVB exposure. Unsupervised clustering\, functional enrichment and protein interaction network analyses converged on a constitutive type I interferon signal in XPC-KO melanocytes and confirmed by immunoblotting. While wild-type melanocytes reached comparable levels only after UVB exposure\, XPC-deficient melanocytes carry\, in the absence of any stress\, an interferon response that normal cells mount only under genotoxic stress. Pharmacological JAK inhibition modified neither the UVB sensitivity nor the photoproduct repair defect of XPC-KO melanocytes\, suggesting that this inflammatory phenotype accompanies rather than causes the DNA repair phenotype. To study pigmentation in a physiologically relevant context\, we then developed a pigmented full-thickness reconstructed human skin model in which melanocytes synthesize melanin and transfer it to the epidermal layers without UV. We then implemented the pigmented epidermal model to explore the impact of XPC-deficient microenvironment on the overall pigmentary phenotype. Combining XPC-KO or wild-type keratinocytes with the same pigmented melanocytes made it possible to detect the contribution of the XP-C epidermal microenvironment. XP-C keratinocytes were sufficient to induce a marked hyperpigmentation of wild-type melanocytes\, with increased melanin content and tyrosinase activity. This suggests that the distinct pigmentary feature of XP-C is not exclusively melanocyte-autonomous but is driven\, at least in part\, by the keratinocyte microenvironment. Treatment of the epidermal equivalents with JAK inhibitors or with N-acetylcysteine partially attenuated this hyperpigmentation\, pointing to an inflammatory component that contributes to\, without fully accounting for\, the phenotype. \nTogether\, these results identify a constitutive type I interferon signature as a hallmark of XPC deficiency in melanocytes and reveal the XP-C keratinocyte microenvironment as a trigger of hyperpigmentation with an inflammatory arm. Beyond XP-C\, the naturally pigmented skin model developed during this work provides a platform for studying keratinocyte–melanocyte crosstalk in pigmentary disorders. This work extends the understanding of XP-C beyond DNA repair and identifies the epidermal microenvironment as a potential target to modulate the pigmentary manifestations of the disease. \n_ \nATTENTION ! L’entrée d​u site CEA-Grenoble nécessite une autorisation préalable et sur présentation de votre pièce d’identité le jour de votre venue (CI ou passeport\, car le permis de conduire n’est pas recevable). Veuillez nous contacter par mail​​ \n​Note : Entry to the CEA-Grenoble site requires prior authorization and the presentation of your ID on the day of your visit (ID card or passport; driver’s licenses are not accepted). Please request this authorization by​ e-mail​ \n\n\n\n\n\n  \n\n\n\n\n​
URL:https://sfp-alpes.fr/event/soutenance-de-these-par-zeinab-el-dor-cea-irig-bge/
LOCATION:CEA – Salle de Séminaire IRIG (1005 – 445)\, 17\, avenue des Martyrs\, Grenoble\, France
CATEGORIES:Soutenance,Soutenance de Thèse
ORGANIZER;CN="IRIG - CEA":MAILTO:irig.communication@cea.fr
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BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20261218T090000
DTEND;TZID=Europe/Paris:20261218T110000
DTSTAMP:20261002T135937Z
CREATED:20261002T135937Z
LAST-MODIFIED:20261002T135937Z
UID:10000292-1797584400-1797591600@sfp-alpes.fr
SUMMARY:Soutenance de thèse par Francesca MOSCA (CEA-Irig/IBS)
DESCRIPTION:Targeting L\,D-Transpeptidases in Lpp-Peptidoglycan Crosslinking in E.coli\nRésumé : \nThis thesis investigated the structure and function of L\,D-transpeptidases (LDTs) responsible for covalently attaching Braun’s lipoprotein (Lpp) to the peptidoglycan layer in Gram-negative bacteria. Because Lpp constitutes the principal covalent connection between the peptidoglycan and the outer membrane\, disruption of this linkage destabilises the bacterial cell envelope. Understanding the molecular mechanisms underlying LDT-mediated Lpp attachment therefore provides a foundation for developing novel inhibitors capable of compromising outer-membrane integrity and enhancing the activity of existing antibiotics against antibiotic-resistant Gram-negative bacteria. The work focused on mainly two aspects of LDT function : the interactions of these enzymes with existing and novel antibiotics\, and with their physiological substrates Lpp and peptidoglycan. Particular emphasis was placed on LdtB\, the most essential LDT in E. coli. Structural and functional characterization was performed using NMR spectroscopy\, biophysical methods\, and biochemical techniques\, complemented by in silico approaches\, including molecular dynamics simulations.This integrative approach was used to decipher the molecular determinants of Lpp-peptidoglycan transpeptidation mechanism and to propose a possible stuctural model for the reaction\, which remains poorly understood despite its biological relevance. In this context\, E. coli served as a model system\, whose study may provide insights into mechanisms that could be conserved across other Gram-negative bacteria. This work was carried out within the framework of the BREAKthrough consortium\, which enabled part of the research to be conducted in collaboration with partner laboratories across Europe​. ​​​​ \n_ \n\n\n​Les 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. \n\n\n\n\nPensez à vous munir d’une pièce d’identité le jour de votre visite.
URL:https://sfp-alpes.fr/event/soutenance-de-these-par-francesca-mosca-cea-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.fr
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