Letteratura scientifica selezionata sul tema "Mutation activatrice"
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Articoli di riviste sul tema "Mutation activatrice":
Piroth, Marie, Sébastien Barbarot, Marie Vincent, Bertrand Isidor e Hélène Aubert. "Macrodactylie isolée et mutation en mosaïque activatrice du gène PIK3CA". Annales de Dermatologie et de Vénéréologie - FMC 1, n. 8 (dicembre 2021): A205. http://dx.doi.org/10.1016/j.fander.2021.09.137.
Nezzar, Adlen. "Molecular biology and thyroid cancer". Batna Journal of Medical Sciences (BJMS) 2, n. 1 (30 giugno 2015): 60–65. http://dx.doi.org/10.48087/bjmstf.2015.2114.
Mesnard, C., B. Isidor, S. Guillard e S. Barbarot. "Macrodactylie isolée secondaire à une mutation activatrice en mosaïque du gène PIK3CA". Annales de Dermatologie et de Vénéréologie 146, n. 12 (dicembre 2019): A251—A252. http://dx.doi.org/10.1016/j.annder.2019.09.397.
Muresan, M., L. Trabelsi, C. Tomâgeski, V. Pascal-Vigneron, M. Klein e G. Weryha. "P1-090 - Hypoparathyroïdie par mutation activatrice du récepteur calcique : à propos d’un cas". Annales d'Endocrinologie 67, n. 5 (ottobre 2006): 434. http://dx.doi.org/10.1016/s0003-4266(06)72743-3.
Humbert, L., K. Mention, A. Jannin, D. Dobbelaere, A. S. Guemann, A. F. Dessein, M. Lemaitre, I. Fajardy, M. C. Vantyghem e C. Douillard. "Hyperinsulinisme par mutation activatrice de la glucokinase diagnostiqué à l’âge adulte : description de 9 cas". Annales d'Endocrinologie 84, n. 5 (ottobre 2023): 516–17. http://dx.doi.org/10.1016/j.ando.2023.07.046.
Rouviere, D., J. Mazieres e A. Didier. "Caractéristiques et prise en charge de l’évolutivité cérébroméningée des cancers bronchiques dans un contexte de mutation activatrice". Revue des Maladies Respiratoires 34 (gennaio 2017): A195—A196. http://dx.doi.org/10.1016/j.rmr.2016.10.461.
Leduc, C., e B. Mennecier. "Quelle est la meilleure séquence thérapeutique chez les patients ayant un CBNPC avec mutation activatrice de l’EGFR ?" Revue des Maladies Respiratoires Actualités 3, n. 4 (settembre 2011): 376–79. http://dx.doi.org/10.1016/s1877-1203(11)70126-4.
Soriancogullen, L., V. Mitchell, J. C. Carel, J. P. Barbet, M. Roger e N. Lahlou. "CO33 - Hypersécrétion d’inhibine B chez les garçons porteurs d’une mutation activatrice du gène du récepteur de la LH". Annales d'Endocrinologie 66, n. 5 (ottobre 2005): 402–3. http://dx.doi.org/10.1016/s0003-4266(05)81834-7.
Rouviere, D., R. Veillon, L. Chaltiel, Y. Simonneau, T. Filleron, J. Milia, N. Guibert et al. "Caractéristiques et prise en charge de l’évolutivité cérébro-méningée des cancers bronchiques dans un contexte de mutation activatrice". Revue des Maladies Respiratoires 36, n. 5 (maggio 2019): 583–90. http://dx.doi.org/10.1016/j.rmr.2019.04.003.
Kuentz, Paul, Sylvie Fraitag, Pierre Vabres, Marie Gonzales, Laurence Faivre e Jean-Baptiste Rivière. "Une mutation post-zygotique activatrice de FGFR2 est responsable d’une forme sévère et atypique de nævus sébacé en prénatal". Morphologie 99, n. 327 (dicembre 2015): 158–59. http://dx.doi.org/10.1016/j.morpho.2015.09.022.
Tesi sul tema "Mutation activatrice":
Gakovic, Milica. "Etudes fonctionnelles de Tyk2 dans la voie de signalisation de l’IFNalpha : analyse d’un nouvel interacteur et d’une mutation activatrice". Paris 6, 2007. https://tel.archives-ouvertes.fr/tel-00808013.
Tyk2 is a member of the Jak family of tyrosine kinases (Jak1, Jak2, Jak3 and Tyk2), which are indispensable components of -helical cytokine signaling cascades. Receptors for - helical cytokines are mostly made of two transmembrane subunits that associate with Jaks. Ligand bridging of two receptor chains brings together the associated Jaks, enabling their activation by transphosphorylation. Activated Jaks phosphorylate the STATs (Signal Transducer and Activator of Transcription) which translocate into the nucleus to drive gene expression. The Jaks have an N-terminal FERM (band 4. 1-ezrin-radixin-moesin) domain, followed by an "SH2-like" domain and two kinase domains: a kinase-like (KL) domain and the catalytic tyrosine-kinase domain. The FERM and SH2-like domains are necessary for receptor binding. The KL domain has no catalytic activity, but plays an important regulatory role. The laboratory is particularly interested in the type I interferon (IFN/) receptor, made of two subunits IFNAR1 and IFNAR2, which bind Tyk2 and Jak1, respectively. During the first part of my thesis, I analyzed a new Tyk2 interacting protein, Pot1 (Partner of Tyk2). Pot1 was isolated in a yeast two-hybrid screen using the Tyk2 FERM domain as bait. To assess the role of Pot1 in IFNsignaling, I monitored IFN-induced response in Pot1-depleted cells by measuring STAT phosphorylation and the induction of a reporter gene. These experiments showed that, in this system, Pot1 depletion had no effect on IFN-induced signaling. A two-hybrid screen was performed with Pot1 as bait. Among the 14 proteins found with high interaction confidence, we focused on GIT1 (G protein-coupled receptor kinase interactor 1), an adaptor protein implicated in a number of cellular processes, like cell migration, receptor internalization and EGF and angiotensin II signaling. To analyze the role of GIT1 in IFNsignaling, I monitored IFN-induced receptor internalization, STAT phosphorylation and the induction of a reporter gene in GIT1-depleted cells. The results obtained allow us to exclude a role for GIT1 in type I IFN signaling. During the second part of my thesis, I analyzed the effect of the V678F substitution on Tyk2 function. This mutation, located in the KL domain, corresponds to the V617F mutation of Jak2 found at the origin of Polycythemia vera. To study the effect of the V678F mutation on Tyk2 activity, I reconstituted Tyk2-deficient cells with Tyk2 WT or the V678F mutant and monitored IFN-induced response. Our results show that the V678F mutation augments basal Tyk2 kinase activity measured in vitro. This gain-of-function leads to an increase of the basal STAT3 phosphorylation level, but has no effect on IFN-induced Jak1 and STAT1/2/5 phosphorylation. As opposed to Jak2, Tyk2 has been implicated only in signaling via heterodimeric receptor complexes. Interestingly, it has been shown that Jak2V617F needs the coexpression of a cognate homodimeric receptor to fully exert its transforming activity in the BaF3 cellular model system. Therefore, we analyzed the effect of Tyk2V678F on signaling via an artificial homodimeric receptor. To this end, we used Tyk2-deficient cells that express a chimeric receptor containing the extracellular domain of erythropoietin receptor fused to the intracellular region of IFNAR1. These cells were stably reconstituted with Tyk2WT or the V678F mutant. In this context, Tyk2V678F confers ligand hypersensitivity as seen by STAT1/3/5 phosphorylation. Moreover, the ensemble of these data point to STAT3 as a preferred substrate of Tyk2
Gakovic, Milica. "Etudes fonctionnelles de Tyk2 dans la voie de signalisation de l'IFNα: analyse d'un nouvel interacteur et d'une mutation activatrice". Phd thesis, Université Pierre et Marie Curie - Paris VI, 2007. http://tel.archives-ouvertes.fr/tel-00808013.
Guérin, Célia. "Caractérisation de nouvelles mutations activatrices dépendantes de l'HGF dans le lobe N-terminal du domaine kinase du récepteur MET dans le cancer du rein héréditaire". Electronic Thesis or Diss., Université de Lille (2022-....), 2023. https://pepite-depot.univ-lille.fr/ToutIDP/EDBSL/2023/2023ULILS074.pdf.
Targeted therapies are currently revolutionizing the management of cancer patients, provided they present a targetable molecular alteration responsible for tumor progression. Receptor tyrosine kinases (RTKs) with activating mutations are major targets of targeted therapies, with EGFR as a representative example, whose mutations lead to its constitutive activation, making it independent of stimulation by its ligand.The MET receptor, another RTK in this family, has activating mutations in kidney and lung cancer. Indeed, type I papillary renal cell carcinoma (HPRC), an uncommon hereditary cancer, is unique in that over 80% of cases have MET activating mutations. In contrast, in non-small cell lung cancer (NSCLC), MET mutations lead to skipping of exon 14 encoding the juxtamembrane domain (MET ex14 mutations). This exon skipping leads to the loss of the juxtamembrane domain, a regulatory domain involved in the negative regulation of the receptor. In an original way from other RTK mutations, these mutations always require stimulation by HGF, the ligand of MET, making HGF production a parameter to be considered in the stratification of patients eligible for targeted therapies.Tyrosine kinase inhibitors (TKIs) directed against MET have very recently been approved for clinical use, offering real hope for patients with these mutations.Thanks to the development of high-throughput sequencing for diagnosis and the emergence of new resistance mutations following treatment with targeted therapies, the spectrum of mutations affecting TKIs is expanding considerably. The current challenge is no longer the detection of these mutations, but their functional interpretation, which can demonstrate their activating character or their targeting by TKIs.In this context, my thesis objective was to exploit sequencing data from patients suffering from HPRC or NSCLC to identify new MET activating mutations and characterize their activation mechanisms in order to determine their eligibility for potential treatment by TKIs.Thanks to a collaboration with the Institute Gustave Roussy, which centralizes sequencing data from HPRC patients, we have identified 8 previously undescribed mutations in a cohort of 158 patients, affecting the extracellular domain (V37A and R426P), the juxtamembrane domain (S1018P and G1086E) and the N-terminal lobe of MET kinase (H1086L, I1102T, C1125G and L1130S). In parallel, thanks to our collaboration with the Lille University Hospital, which centralizes data on 2808 NSCLC patients, we have identified 2 undescribed kinase domain mutations.First, we demonstrated in a fibroblast transformation model that the four N-terminal lobe mutations identified in HPRC are potential MET-activating mutations. Interestingly, although localized to the kinase, these mutations retain a dependence on HGF to induce cell transformation. Moreover, all four mutations are sensitive to TKIs directed against MET.In a second step, to better characterize these new activating mutations, we established T47D epithelial cell lines expressing two of the new activating mutations (H1086L and I1102T), which we compared with wild-type MET and MET ex14, known to retain its dependence on HGF. Our results confirm that both mutations require activation by HGF for activation of downstream signaling pathways and induction of responses such as cell motility. Transcriptomic analysis reveals significant similarities between the transcriptional programs of the MET I1102T, H1086L and MET exon14 mutations, highlighting their involvement in extracellular matrix remodeling and invasion. Xenografts of cells expressing these new mutations in mouse models demonstrate their ability to promote tumor growth [...]
Lienhardt-Roussie, Anne. "Mutations activatrices du récepteur sensible au calcium : aspects moléculaires, phénotypiques et implications thérapeutiques à travers une large étude collaborative". Limoges, 2000. http://www.theses.fr/2000LIMO112L.