Literatura académica sobre el tema "Thiouridylase"
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Artículos de revistas sobre el tema "Thiouridylase"
Ogunkola, Moses, Lennart Wolff, Eric Asare Fenteng, Benjamin R. Duffus y Silke Leimkühler. "E. coli MnmA Is an Fe-S Cluster-Independent 2-Thiouridylase". Inorganics 12, n.º 3 (23 de febrero de 2024): 67. http://dx.doi.org/10.3390/inorganics12030067.
Texto completoBlack, Katherine A. y Patricia C. Dos Santos. "Abbreviated Pathway for Biosynthesis of 2-Thiouridine in Bacillus subtilis". Journal of Bacteriology 197, n.º 11 (30 de marzo de 2015): 1952–62. http://dx.doi.org/10.1128/jb.02625-14.
Texto completoСеменова, Н. А., П. Г. Цыганкова, Е. Л. Дадали, Т. В. Строкова, Н. Н. Таран, И. А. Кузьмичева y С. И. Куцев. "Clinical and diagnostic features of infantile liver failure caused by TRMU gene mutations". Nauchno-prakticheskii zhurnal «Medicinskaia genetika», n.º 7(216) (30 de julio de 2020): 95–96. http://dx.doi.org/10.25557/2073-7998.2020.07.95-96.
Texto completoSasarman, F., H. Antonicka, R. Horvath y E. A. Shoubridge. "The 2-thiouridylase function of the human MTU1 (TRMU) enzyme is dispensable for mitochondrial translation". Human Molecular Genetics 20, n.º 23 (1 de septiembre de 2011): 4634–43. http://dx.doi.org/10.1093/hmg/ddr397.
Texto completoPhilipp, Matthias, Florian John y Christoph Ringli. "The cytosolic thiouridylase CTU2 of Arabidopsis thaliana is essential for posttranscriptional thiolation of tRNAs and influences root development". BMC Plant Biology 14, n.º 1 (2014): 109. http://dx.doi.org/10.1186/1471-2229-14-109.
Texto completoYan, Han, Yushan Zuo, Huixia Zhang, Cuicui Liu, Jun Yang y Lijie Chen. "A cytosolic thiouridylase gene MoCTU2 in Magnaporthe oryzae is important for vegetative hyphal growth, conidiation, and responses to rapamycin and high temperature". Physiological and Molecular Plant Pathology 121 (septiembre de 2022): 101886. http://dx.doi.org/10.1016/j.pmpp.2022.101886.
Texto completoKemény-Beke, Á., E. Berényi, A. Facskó, J. Damjanovich, A. Horváth, A. Bodnár, A. Berta y J. Aradi. "Antiproliferative Effect of 4-Thiouridylate on OCM-1 Uveal Melanoma Cells". European Journal of Ophthalmology 16, n.º 5 (septiembre de 2006): 680–85. http://dx.doi.org/10.1177/112067210601600504.
Texto completoYan, Qingfeng y Min-Xin Guan. "Identification and characterization of mouse TRMU gene encoding the mitochondrial 5-methylaminomethyl-2-thiouridylate-methyltransferase". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1676, n.º 2 (enero de 2004): 119–26. http://dx.doi.org/10.1016/j.bbaexp.2003.11.010.
Texto completoAryal, Neeraj K., Anjana Sundarrajan, Scott Boiko, David Jenkins, Huayang Liu, Miika Ahdesmaki, Aurelie Bornot et al. "Elongator Complex Regulates MCL1 Dependency Via IRE1-XBP1 Axis of the ER Stress Response Pathway in Multiple Myeloma". Blood 138, Supplement 1 (5 de noviembre de 2021): 2275. http://dx.doi.org/10.1182/blood-2021-151194.
Texto completoYan, Qingfeng, Yelena Bykhovskaya, Ronghua Li, Emebet Mengesha, Mordechai Shohat, Xavier Estivill, Nathan Fischel-Ghodsian y Min-Xin Guan. "Human TRMU encoding the mitochondrial 5-methylaminomethyl-2-thiouridylate-methyltransferase is a putative nuclear modifier gene for the phenotypic expression of the deafness-associated 12S rRNA mutations". Biochemical and Biophysical Research Communications 342, n.º 4 (abril de 2006): 1130–36. http://dx.doi.org/10.1016/j.bbrc.2006.02.078.
Texto completoTesis sobre el tema "Thiouridylase"
Zhou, Jingjing. "Nouvelle fonction des centres [4Fe-4S] dans des réactions non-rédox : étude biochimique et structurale de thiouridylases d'ARN de transfert et d’une thiouracile désulfidase". Electronic Thesis or Diss., Sorbonne université, 2022. http://www.theses.fr/2022SORUS325.
Texto completoThe sulfur atom is an abundant and essential element for life. It is present in a wide variety of sulfur-containing biomolecules, such as certain essential amino acids - the cysteine and the methionine, which are at the center of various metabolic pathways -, transfer RNA thionucleosides, and certain essential cofactors participating in many biological processes, such as iron-sulfur centers [Fe-S]. The [Fe-S] centers are known for their redox activity and their role in electron transfer reactions. They have important cellular functions in photosynthesis, respiration, and regulation of gene translation under stress conditions. My thesis consisted of the study of two families of enzymes with [4Fe-4S] centers involved in sulfur metabolism: several transfer RNA thiouridylases (MnmA from E. coli, ThiI from archaea Methanococcus maripaludis), catalyzing sulfur insertion into tRNA uridines, as well as a ThioUracil DeSulfidase (TudS) catalyzing sulfur abstraction from thiouracil. By combining various biochemical (in vitro activity tests, site-directed mutagenesis) and biophysical (UV-visible spectroscopy, EPR, Mössbauer, X-ray crystallography) characterization methods, we were able to demonstrate the chemical nature and the role of the [4Fe-4S] cluster in the non-redox reactions catalyzed by these metalloenzymes. Identifying a reaction intermediate [4Fe-5S] in crystal, in the structure of the enzyme TudS, has confirmed a new function of the [4Fe-4S] clusters in the catalysis of non-redox reactions, previously proposed for transfer RNA thiouridylases (TtuA): the [4Fe-4S] cluster being liganded by only three amino acids, the fourth uncoordinated iron would play the role of Lewis acid by binding and activating the sulfur atom of the substrate (exogenous sulfide or thiouracil, respectively) to catalyze the reaction of thiolation (tRNA thiouridylases) or dethiolation (TudS)
Capítulos de libros sobre el tema "Thiouridylase"
Schomburg, Dietmar y Dörte Stephan. "tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase". En Enzyme Handbook 11, 263–65. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61030-1_58.
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