Academic literature on the topic 'Surexpression protéique'
Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles
Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Surexpression protéique.'
Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.
You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.
Journal articles on the topic "Surexpression protéique":
Couderc, E., F. Morel, G. Guillet, F. X. Bernard, and J. C. Lecron. "Surexpression kératinocytaire de la protéine SAA et activité dans le psoriasis." Annales de Dermatologie et de Vénéréologie 142, no. 6-7 (June 2015): S291. http://dx.doi.org/10.1016/j.annder.2015.04.045.
Verhoest, G., F. Dugay, N. Rioux-Leclercq, X. Le Goff, F. Chesnel, F. Jouan, C. Vigneau, Y. Arlot-Bonnemains, and M. Belaud-Rotureau. "Surexpression de la protéine PAR-3 : facteur de mauvais pronostic dans le carcinome rénal à cellules claires (ccRCC)." Progrès en Urologie 23, no. 13 (November 2013): 1017–18. http://dx.doi.org/10.1016/j.purol.2013.08.003.
Trahan, S., B. Têtu, and P. É. Raymond. "Le carcinome séreux papillaire développé dans un polype de l’endomètre : comportement clinico-pathologique et la surexpression de la protéine p53." Annales de Pathologie 24, no. 1 (February 2004): 97–98. http://dx.doi.org/10.1016/s0242-6498(04)93930-2.
SEYER, P., S. GRANDEMANGE, L. PESSEMESSE, F. CASAS, G. CABELLO, and C. WRUTNIAK-CABELLO. "L’activité mitochondriale est un régulateur majeur de la différenciation des myoblastes et de l’expression des isoformes de myosine." INRAE Productions Animales 19, no. 4 (September 13, 2006): 279–86. http://dx.doi.org/10.20870/productions-animales.2006.19.4.3495.
Fritsch, S., V. Gigoux, P. Clerc, C. Da Costa De Jesus, N. Dusetti, and M. Dufresne. "R20: La surexpression de la protéine E3UL dès les étapes précoces de la carcinogenèse pancréatique induit la dégradation du facteur de transcription Ptf1a par le protéasome." Bulletin du Cancer 97, no. 4 (October 2010): S23—S24. http://dx.doi.org/10.1016/s0007-4551(15)30937-1.
Dissertations / Theses on the topic "Surexpression protéique":
Bardot, Boris. "Etude biochimique et fonctionnelle de la protéine Drm/Gremlin : un nouveau modulateur potentiel de la voie de signalisation Notch." Paris 11, 2001. http://www.theses.fr/2001PA11T032.
Fix, Anne. "Caractérisation des amplifications génomiques et des mécanismes de surexpression de la protéine MYCN dans le neuroblastome." Paris 11, 2008. http://www.theses.fr/2008PA11T005.
Loubeau, Gaëlle. "Impact de la surexpression de la protéine nucléophosmine (NPM1) sur la progression des cancers de la prostate." Phd thesis, Université Blaise Pascal - Clermont-Ferrand II, 2012. http://tel.archives-ouvertes.fr/tel-00870415.
Couplan, Elodie. "Invalidation du gène Ucp2 et surexpression du gène Ucp1 dans le muscle : études de bioénergétique mitochondriale." Paris 6, 2003. http://www.theses.fr/2003PA066073.
Abdelfettah, Souhila. "Conséquences fonctionnelles de la surexpression de l’isoforme courte de la protéine Polycomb-like hPCL3, hPCL3S dans les tumeurs prostatiques." Thesis, Lille 1, 2019. http://www.theses.fr/2019LIL1S112.
The Polycomb PRC2 complex allows the deposition of the repressive epigenetic mark H3K27me3 by its catalytic subunit, EZH2. According to the type of cancers, EZH2 either is overexpressed (prostate) or is subject to loss or gain of function mutations, which lead to aberrant levels of H3K27me3. In vitro, a tetramer consisting of the "core" PRC2 subunits, EZH2, SUZ12, EED and RBBP4 is sufficient to catalyze the trimethylation of H3K27. In vivo, several factors modulating the enzymatic activity of the PRC2 complex or participating in its recruitment and/or its stabilization at the promoters of target genes have been identified. Among them, the three human orthologs of the unique Polycomb-like protein (PCL) of Drosophila, PHF1, PCL2 and PCL3/PHF19 have recently gained much attention. These proteins share a structured N-terminal domain consisting of a TUDOR domain and two PHD domains (Plant Homeo Domain) followed by a "Winged-helix" domain involved in DNA binding. In addition, PHF1 and PHF19 bind H3K36me3 via their TUDOR domain through an "aromatic cage" and thus allow the intrusion of PRC2 into euchromatin, the activation of EZH2 and H3K27me3 deposition. Owing to different polyadenylation sites and alternative splicing events, the human hPCL3/PHF19 locus encodes two isoforms: a full-length protein, hPCL3L/PHF19L and a shorter isoform, hPCL3S/PHF19S, which contains only the domain TUDOR, PHD1-the first of two PHD- domains and a small specific C-terminal region. The PHD1 domain, which is very divergent between the three orthologues, could be associated with specific functions of each orthologue. For example, PHF1 is the only one capable of inducing cell quiescence by interacting with and stabilizing P53 through its PHD1 domain and independently of its TUDOR domain. Our RT-qPCR experiments on a cohort of 25 prostate tumors revealed that hPCL3S is overexpressed in 75% of the cases. In addition, hPCL3S is overexpressed in the DU145 and PC3 hormone-insensitive cell lines, but not in the hormone-sensitive LNCaP cell line. In Wound-healing and proliferation assays, we have shown that the specific siRNA inactivation of hPCL3S decreases the proliferation and migration of DU145 cells that over-express it. Conversely, the stable transfection of hPCL3S into LNCaP increases these properties. These effects partially relied on the up-regulation of genes known to be important for the proliferation and/or migration of prostate cancer cells such as S100A16, PlexinA2 and Spondin1. Stable transfection of a punctual mutant of hPCL3S, W50A, is unable to bind H3K36me3 and results in increased proliferation of LNCaP as in the case of hPCL3S-WT. suggesting that this effect is not dependent on the reading H3K36me3 by the TUDOR domain.By contrast, a mutation in the PHD1 domain abolishes the effect on growth. This PHD1 domain is a protein-protein interaction domain that is very divergent between the 3 Polycomb-like orthologs, and could therefore have different functions. These results allow us to highlight the role of hPCL3S in prostate tumor progression and suggest that hPCL3S is a potential new therapeutic target in castration-resistant prostate cancer
Capoulade, Corinne. "MDM2 et p53 dans le lymphome de Burkitt : étude du mécanisme de surexpression de MDM2 et induction de l'apoptose par des oligonucléaires antisens." Paris 5, 1999. http://www.theses.fr/1999PA05N137.
Lincet, Hubert. "Potentialisation de l'effet cytotoxique de drogues anti-tumorales par surexpression de la protéine p21 WAF1/CIP1 dans les carcinomes ovariens humains in vitro." Caen, 2000. http://www.theses.fr/2000CAEN4042.
Hasan, Bou Issa Lama. "Étude des dépendances génomiques dans le myélome multiple surexprimant MYC." Electronic Thesis or Diss., Université de Lille (2022-....), 2024. http://www.theses.fr/2024ULILS011.
Multiple myeloma (MM) is a hematological malignancy that accounts for around 13% of hematological cancers and is characterized by the uncontrolled proliferation of malignant plasma cells in the bone marrow. MM progresses from precursor stages, known as monoclonal gammopathy of undetermined significance (MGUS) and smoldering multiple myeloma (SMM), to the symptomatic form, MM. It is an incurable malignancy in which heterogeneity and clonal evolution allow treatment escape and disease progression. MYC alterations play an essential role in this progression. However, MYC is not therapeutically targetable due to its nuclear localization and the protein's short half-life.To overcome this, we hypothesized that the proliferative advantage induced by MYC overexpression creates genomic dependencies on other signalling pathways that become essential for cell survival. To test this hypothesis, we applied a novel approach by leveraging large-scale loss of function screen (Achilles) and 1869 small molecules screen to identify MYC-induced genomic vulnerabilities. When identified, these vulnerabilities offer an opportunity to selectively target cancer cells harbouring this overexpression and spare normal cells.Our analyses demonstrate the dependence of MYC overexpressing cells on glutamine metabolism, in particular on the GLS1 (glutaminase). We validated and functionally delineated this dependence in vitro using different approaches.Our small molecule screen highlighted that NAD synthesis inhibitors had a preferential effect on the proliferation of MYC overexpressing cells. Considering that glutamine and NAD have closely interlinked metabolic networks, we investigated the possibility of a potential synergistic effect between GLS1 and NAMPT inhibitors. We demonstrated the effectiveness of this new synergistic combination to target MYC-driven MM cells in vitro and in vivo.These results establish a solid methodological basis that can be used to develop new therapeutic approaches to address unmet therapeutic needs to target MYC in MM
Giraud, Marie-France. "Etude de la sous-unité delta de l'ATP synthase mitochondriale de la levure Saccharomyces Cerevisiae : purification de la protéine, clonage et disruption du gène de structure, surexpression de la protéine chez Escherichia Coli." Bordeaux 2, 1996. http://www.theses.fr/1996BOR28434.
Mackenbach, Loue Petra. "Translocation nucléaire de la protéine kinase CK2 induite par les facteurs de croissance et surexpression d'une forme anormale de la kinase dans les tumeurs du sein." Université Joseph Fourier (Grenoble ; 1971-2015), 1997. http://www.theses.fr/1997GRE10164.