Gotowa bibliografia na temat „Interaction domaine-motif”
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Rozprawy doktorskie na temat "Interaction domaine-motif"
Frenal, Karine. "Caractérisation structurale et fonctionnelle de TgDRE : une enzyme de réparation de l' ADN du parasite Toxoplasma gondii". Paris 6, 2006. http://www.theses.fr/2006PA066031.
Pełny tekst źródłaJané, Palli Pau. "Quantification des affinités PBM/PDZ et de leurs sites modulateurs par des approches expérimentales et informatiques à haut débit". Electronic Thesis or Diss., Strasbourg, 2020. http://www.theses.fr/2020STRAJ051.
Pełny tekst źródłaThis thesis focuses on PDZ domains, a family of globular domains that bind to conserved PDZ-Binding Motifs (called henceforth PBMs) generally situated at the extreme C-terminus of their partner proteins. Domain-motif networks are often modulated by reversible post-translational modifications (PTMs). We used synthetized PBMs to reproduce different conditions, such as a wild-type, acetylation or phosphorylation, addition of extra exosites or residue mimication of PTM in the literature. These peptides were used for interaction studies using the holdup assay, an assay originally developed in our laboratory. We evaluated the impact of diverse modifications of the PBM/PDZ interactions, which led to a global change of the PDZ-binding capability. These results provided quantitative information on the biological effects that such modifications may have in the context of full-length proteins
Takeuchi, Akiko. "Interactions ARN-protéines dans le mécanisme de biosynthèse des sélénoprotéines". Phd thesis, Université de Strasbourg, 2009. http://tel.archives-ouvertes.fr/tel-00455002.
Pełny tekst źródłaOguievetskaia, Ksenia. "Echafaudages moléculaires axogliaux des fibres myélinisées : interactions entre les protéines de la famille NCP et la protéine 4.1B". Paris 6, 2006. http://www.theses.fr/2006PA066395.
Pełny tekst źródłaClouaire, Thomas. "Caractérisation du domaine THAP, un nouveau domaine de liaison à l'ADN dépendant du zinc". Toulouse 3, 2005. http://www.theses.fr/2005TOU30118.
Pełny tekst źródłaWe have recently identified a novel evolutionarily conserved protein motif, the THAP domain, which defines a novel family of nuclear factors with 12 human members. We have identified more than a hundred THAP domain containing proteins in animals including the proapoptotic factors DAP4/THAP0 and THAP1, the transcriptional repressor THAP7, the fish orthologue of the cell cycle regulator E2F6 and the C. Elegans proteins HIM-17, LIN-36 and LIN-15B. The THAP domain exhibit striking similarities with the site-specific DNA-binding domain of Drosophila P element transposase. My thesis work demonstrates that the THAP domain of THAP1 is a sequence specific zinc dependent DNA-binding domain. Together with previous genetic data obtained in C. Elegans, our data suggest that the THAP proteins are sequence specific DNA binding factors with roles in cell cycle, apoptosis, chromosome segregation, chromatin modification and transcriptional repression
Rivière, Gwladys. "Étude par RMN de la créatine kinase musculaire et d’un nouveau domaine de liaison à l’ubiquitine dans la protéine STAM2". Thesis, Lyon 1, 2011. http://www.theses.fr/2011LYO10285/document.
Pełny tekst źródłaIn this thesis, we study two proteins by NMR: the muscular creatine kinase (CK-MM) and the SH3 domain of STAM2 protein, in the free and complexed forms. CK-MM is an active homodimeric enzyme which belongs to the guanidino-phosphagen-kinase family. This enzyme is involved in energetic process in the cell. The aim of this study is to elucidate the functional mode of the CK-MM. For this purpose, we measured R1 and R2 relaxation rates and chemical shit perturbation experiments on the substrate-free CK-MM, the CK-MM/MgADP complex, and the inhibitory ternary complex CK-MM/MgADP-creatine-nitrate. The experiments show that the loop 320s, specific recognition of the substrates, possesses a fast dynamic in absence of substrates (in the order of nano-picosecond) and a slower dynamic in presence of creatine-MgADP-nitrate ion. The binding of the substrate in the two active sites induces of significant conformational modification of the CK-MM. STAM2 protein consists in two ubiquitin binding domains (VHS and UIM) and a SH3 domain which interacts with deubiquinating enzymes AMSH and UBPY. This protein is involved in the lysosomal degradation pathway. The aim of this study is the characterization of the interaction between SH3 domain of STAM2 and ubiquitin. For this, we recorded the R1, R2, nOes relaxation experiments and chemical shift perturbation experiments on the UIM-SH3/ubiquitin complex. These experiments show that SH3 and UIM domains interact each with a single ubiquitin, with affinity of the order of hundred micromolars. The interface between these UBDs and ubiquitin, involves mainly hydrophobic and conserved amino-acids
Rivière, Gwladys. "Étude par RMN de la créatine kinase musculaire et d'un nouveau domaine de liaison à l'ubiquitine dans la protéine STAM2". Phd thesis, Université Claude Bernard - Lyon I, 2011. http://tel.archives-ouvertes.fr/tel-00861128.
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