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    Résumé/ stage

    Cours gratuits > Forum > Forum anglais: Questions sur l'anglais || En bas

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    Résumé/ stage
    Message de cemoulee posté le 03-06-2017 à 22:32:53 (S | E | F)
    Bonsoir,
    Je suis nouvelle sur ce site. J'ai fait très peu d'anglais durant mon cursus. Je suis actuellement en stage et je dois rédiger un résumé en anglais. Si quelqu'un pouvait me corriger je lui en serais reconnaissante.

    Apoptosis is a programmed cell death of cells that occurs naturally during embryogenesis and can be induced during a cellular stress such as hypoxia or free radicals. The deregulation of homeostasis between survival and cell death is found in cancers. These cells divert signaling pathways in their favor with high resistance to apoptosis and a high proliferation capacity. Apoptosis can be triggered by two distinct routes. The extrinsic pathway involves the death receptors of the TNF superfamily and the intrinsic pathway involving the mitochondria. The intrinsic pathway is controlled by proteins of the Bcl-2 family. Pro-apoptotic proteins such as Bax and Bak, as well as the anti-apoptotic proteins Bcl-2 and Bcl-xL, are distinguished. Pro-apoptotic proteins can be activated by BH3 proteins following a genotoxic stress. Their activation results in a change in conformation enabling them on the one hand to integrate into the mitochondrial membrane and / or on the other hand to form homo- or heterodimers. These dimers allow the formation of a mitochondrial pore and allows the release of apoptogenic molecules normally sequestered in the inter-mitochondrial space. For example, the release of cytochrome c into the cytosol will lead to the formation of a complex called the apoptosome responsible for the activation of caspase 9 which will activate other caspase cascades. The activation of these caspases can be inhibited by proteins of the IAP family. More particularly, cIAP1 is an E3 ubiquitin ligase that can bind partners via its domains of protein-BIR protein interactions and induce their ubiquitinylation via the RING domain. The action of pro-apoptotic proteins can be inhibited by the anti-apoptotic proteins Bcl-2 and Bcl-xL.
    My host team showed an interaction between cIAP1 and Bcl-xL by the GST-pull-down technique. During my internship I showed that cIAP1 could interact directly with Bcl-xL and that it was done via the domains BIR2 and BIR3. This interaction leads to a mono-ubiquitinylation or multi-mono-ubiquitinylation of Bcl-xL.cIAP1 leads to an increase in the expression of Bcl-xL or allows its stabilization. Functional analyzes showed that cIAP1 is able to inhibit changes in Bax conformation and block PARP cleavage. In collaborative work, we showed an interaction of the transcription factor E2F1 with the Bcl-xL protein. In order to respond to the requests of the experts, we undertook the search for the peptide region of E2F1 allowing this interaction.

    -------------------
    Modifié par lucile83 le 03-06-2017 22:34


    Réponse : Résumé/ stage de gerondif, postée le 03-06-2017 à 22:49:53 (S | E)
    Bonjour,
    ayant survécu à une première lecture, je vais vous indiquer deux trois erreurs , sur le fond, je vous fais confiance

    Apoptosis is a programmed cell death of cells(inutile après "cell-death") that occurs naturally during embryogenesis and can be induced during a cellular stress such as hypoxia or free radicals. The deregulation of homeostasis between survival and cell death is found in cancers. These cells divert (virgule?) signaling pathways in their favor with high resistance to apoptosis and a high proliferation capacity. Apoptosis can be triggered by two distinct routes. The extrinsic pathway involves the death receptors of the TNF superfamily and the intrinsic pathway involving(présent enes je suppose, en parallèle avec le premier) the mitochondria. The intrinsic pathway is controlled by proteins of the Bcl-2 family. Pro-apoptotic proteins such as Bax and Bak, as well as the anti-apoptotic proteins Bcl-2 and Bcl-xL, are distinguished(ça veut dire quoi, sont distinguées, sont mises à part, on peut les voir ? auquel cas je mettrais "can be seen"). Pro-apoptotic proteins can be activated by BH3 proteins following a genotoxic stress. Their activation results in a change in conformation enabling them on the one hand to integrate into the mitochondrial membrane and / or on the other hand to form homo- or heterodimers. These dimers allow the formation of a mitochondrial pore and allows(sujet pluriel, pas de s) the release of apoptogenic molecules normally sequestered in the inter-mitochondrial space. For example, the release of cytochrome c into the cytosol will lead to the formation of a complex called the apoptosome responsible for the activation of caspase 9 which will activate other caspase cascades. The activation of these caspases can be inhibited by proteins of the IAP family. More particularly, cIAP1 is an E3 ubiquitin ligase that can bind partners via its domains of protein-BIR protein interactions and induce their ubiquitinylation via the RING domain. The action of pro-apoptotic proteins can be inhibited by the anti-apoptotic proteins Bcl-2 and Bcl-xL.
    My host team showed an interaction between cIAP1 and Bcl-xL by (j'aurais mis through) the GST-pull-down technique. During my internship I showed that cIAP1 could interact directly with Bcl-xL and that it was done via the domains BIR2 and BIR3. This interaction leads to a mono-ubiquitinylation or multi-mono-ubiquitinylation of Bcl-xL. cIAP1 leads to an increase in the expression of Bcl-xL or allows its stabilization. Functional analyzes showed that cIAP1 is able to inhibit changes in Bax conformation and block PARP cleavage. In collaborative work, we showed an interaction of the transcription factor E2F1 with the Bcl-xL protein. In order to respond to the requests of the experts, we undertook the search (we started looking for)for the peptide region of E2F1 allowing this interaction.




    Réponse : Résumé/ stage de cemoulee, postée le 04-06-2017 à 10:50:35 (S | E)
    Je vous remercie de votre aide.




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