Literatura académica sobre el tema "Acides ribonucléiques"
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Artículos de revistas sobre el tema "Acides ribonucléiques"
Bouloc, Philippe y Brice Felden. "Les acides ribonucléiques régulateurs du staphylocoque doré et leurs rôles dans la virulence". médecine/sciences 27, n.º 3 (marzo de 2011): 238–41. http://dx.doi.org/10.1051/medsci/2011273238.
Texto completoChaube, Ruchi. "Vaccin contre le SRAS-CoV-2 : défis et considérations". Relevé des maladies transmissibles au Canada 47, n.º 3 (31 de marzo de 2021): 141–44. http://dx.doi.org/10.14745/ccdr.v47i03a01f.
Texto completoSarnat, Naomi Beth y Harvey B. Sarnat. "Répartition tissulaire d'acide ribonucléique chez la planaire Dugesia tigrina: étude histochimique au fluorochrome acridine-orange". Canadian Journal of Zoology 65, n.º 5 (1 de mayo de 1987): 1135–39. http://dx.doi.org/10.1139/z87-177.
Texto completoTesis sobre el tema "Acides ribonucléiques"
Sibler-Gillig, Marie-Odile. "Rôle des nucléosides modifiés dans les acides ribonucléiques de transfert". Strasbourg 1, 1985. http://www.theses.fr/1985STR10482.
Texto completoGlasser, Anne-Lise. "Contribution à l'étude des relations structures-fonctions des acides ribonucléiques de transfert de cellules eucaryotes : analyse, identification et rôle de nouveaux nucléosides hypermodifiés". Dijon, 1993. http://www.theses.fr/1993DIJOS019.
Texto completoBoisbouvier, Jérôme. "Utilisation de la corrélation croisée CSA-Dipolaire pour l'étude RMN des acides ribonucléiques : détermination simultanée de la structure des protéines et de la topologie des ponts disulfures par modélisation moléculaire sous contraintes RMN". Université Joseph Fourier (Grenoble), 2000. http://www.theses.fr/2000GRE10062.
Texto completoGosset-Erard, Clarisse. "Développement méthodologique en CE-FTICR-MS pour l'étude de biomolécules à visée thérapeutique". Electronic Thesis or Diss., Université de Lorraine, 2022. http://www.theses.fr/2022LORR0219.
Texto completoMass spectrometry (MS) has emerged in recent years as benchmark method for the characterization of biomolecules. The development of new analyzers with ultra-high resolution and high mass accuracy, such as Fourier Transform Ion Cyclotron Resonance (FTICR), has improved the selectivity of the method. To ease the characterization of complex samples, MS can be coupled with separative methods such as capillary electrophoresis (CE). CE is the most powerful electrophoretic method in terms of resolution, efficiency and peak capacity, and is very fast. The CE-MS coupling has been developed for a large number of analytes and allows to obtain an optimal sensitivity of MS thanks to the use of a sheathless interface allowing the use of nanoflow rates. However, in order to combine the separation performances of CE, the high selectivity and sensitivity of the sheathless interface with the ultra-high resolution and the high mass accuracy of FTICR-MS, it is necessary to address the technical challenges related to the intrinsic properties of CE and FTICR such as the speed of separation, high peak efficiency and MS acquisition time. The work presented in this manuscript presents the implementation of the CE-FTICR-MS hyphenation and its application for the study of biomolecules, and in particular the characterization of post-transcriptional modifications of ribonucleic acids (RNA). A study of the CE-FTICR-MS hyphenation was first performed using standards, then a first method transfer was performed on biological samples already described in the literature. Various method developments are then presented such as the optimization of the sample preparation, and the development of new bioinformatics tools allowing to go further in the characterization of these modifications and in the complexity of the samples. Finally, the CE-FTICR-MS hyphenation as well as the latest method developments were applied on more complex samples, and whose post-transcriptional modifications are not described in the literature. The use of the CE-FTICR-MS hyphenation for the characterization of RNA enabled the identification of an unknown post-transcriptional modification in one of these complex samples that has not been previously studied in the literature
Refour, Philippe. "Bio-puce à ADN thématique de Plasmodium falciparum : mise au point et validation d'une technique de détection de deux radio-isotopes après hybridation différentielle sur lame de verre". Paris 6, 2005. http://www.theses.fr/2005PA066105.
Texto completoVicens, Quentin. "Structures cristallographiques de complexes entre des fragments d'acides ribonucléiques comportant le site A ribosomique et des antibiotiques de la famille des aminoglycosides". Phd thesis, Université Louis Pasteur - Strasbourg I, 2002. http://tel.archives-ouvertes.fr/tel-00003572.
Texto completoVanhoutteghem, Amandine. "Des kératinocytes de poulet à la basonucline 2". Paris 6, 2006. http://www.theses.fr/2006PA066221.
Texto completoBou, Nader Charles. "Structural and Functional characterization of flavoenzymes involved in posttranscriptional modification of tRNA". Thesis, Paris 6, 2017. http://www.theses.fr/2017PA066205/document.
Texto completoPosttranscriptional modification of ribonucleic acids (RNAs) is a crucial maturation step conserved in all domains of life. During my thesis, I have brought structural and functional insights on flavoenzymes involved in transfer RNA (tRNA) modifications: dihydrouridine synthase (Dus) responsible for dihydrouridine formation using flavin mononucleotide (FMN) and TrmFO responsible for C5 methylation of uridine position 54 relying on flavin adenosine dinucleotide (FAD) and methylenetetrahydrofolate. To elucidate the chemical mechanism of TrmFO we designed an apoprotein via a single mutation that could be reconstituted in vitro with FAD. Furthermore, we chemically synthesized the postulated intermediate active species consisting of a flavin iminium harboring a methylene moiety on the isoalloxazine N5 that was further characterized by mass spectrometry and UV-visible spectroscopy. Reconstitution of TrmFO with this molecule restored in vitro activity on a tRNA transcript proving that TrmFO uses FAD as a methylating agent via a reductive methylation.Dus2 reduces U20 and is comprised of a canonical Dus domain however, mammals have an additional double-stranded RNA-binding domain (dsRBD). To bring functional insight for this modular organization, we showed that only full length human Dus2 was active while its isolated domains were not. tRNA recognition is driven by the dsRBD via binding the acceptor and TΨ stem of tRNA with higher affinity then dsRNA as evidenced by NMR. We further solved the X-ray structures for both domains showing redistribution of surface positive charges justifying the involvement of this dsRBD for tRNA recognition in mammalian Dus2. This was attributed to a peculiar N-terminal extension proven by mutational analysis and an X-ray structure of dsRBD in complex with 22-nucleotide dsRNA. Altogether our work illustrates how during evolution, Dus2 enzymes acquired an engineered dsRBD for efficient tRNA binding via a ruler mechanism
Bourdet, Agnès. "Recherche de nouveaux acteurs impliqués dans l' inactivation du chromosome X : étude des transcriptomes d' embryons murins précoces mâles et femelles". Paris 7, 2003. http://www.theses.fr/2003PA077016.
Texto completoLecointe, François. "Étude d'enzymes de modification de nucléotides des ARNt et de leurs fonctions dans le métabolisme cellulaire chez Saccharomyces cerevisiae". Paris 6, 2002. http://www.theses.fr/2002PA066218.
Texto completoLibros sobre el tema "Acides ribonucléiques"
A, Clawson Gary y Hoffmann-La Roche inc, eds. Nucleic acid methylation: Proceedings of a Hoffman-La Rouche-UCLA Colloquium on Nucleic Acid Methylation held at Frisco, Colorado, March 31-April 7, 1989. New York, NY: Wiley-Liss, 1990.
Buscar texto completoMethylation, Hoffmann-LA Roche-UCLA Colloquium on Nucleic Acid, Dawn B. Willis, Arthur Weissbach y Gary A. Clawson. Nucleic Acid Methylation: Proceedings of a Hoffman-LA Roche-UCLA Colloquium on Nucleic Acid Methylation Held at Frisco, Colorado, March 31-April 7, (Ucla ... and Cellular Biology, New Ser., V. 128). Wiley-Liss, 1989.
Buscar texto completoEvolution of catalytic function. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory, 1987.
Buscar texto completoCold Spring Harbor Symposia on Quantitative Biology: Evolution of Catalytic Function. Cold Spring Harbor Laboratory Press, 1988.
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