Relevant bibliographies by topics / Dihydrouridine

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters

Academic literature on the topic 'Dihydrouridine'

Author: Grafiati
Published: 16 November 2024
Last updated: 31 July 2025

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Journal articles on the topic "Dihydrouridine"

1

Kasprzak, Joanna M., Anna Czerwoniec, and Janusz M. Bujnicki. "Molecular evolution of dihydrouridine synthases." BMC Bioinformatics 13, no. 1 (2012): 153. http://dx.doi.org/10.1186/1471-2105-13-153.

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Byrne, Robert T., Huw T. Jenkins, Daniel T. Peters, et al. "Major reorientation of tRNA substrates defines specificity of dihydrouridine synthases." Proceedings of the National Academy of Sciences 112, no. 19 (2015): 6033–37. http://dx.doi.org/10.1073/pnas.1500161112.

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The reduction of specific uridines to dihydrouridine is one of the most common modifications in tRNA. Increased levels of the dihydrouridine modification are associated with cancer. Dihydrouridine synthases (Dus) from different subfamilies selectively reduce distinct uridines, located at spatially unique positions of folded tRNA, into dihydrouridine. Because the catalytic center of all Dus enzymes is conserved, it is unclear how the same protein fold can be reprogrammed to ensure that nucleotides exposed at spatially distinct faces of tRNA can be accommodated in the same active site. We show t
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3

Whelan, Fiona, Huw T. Jenkins, Samuel C. Griffiths, Robert T. Byrne, Eleanor J. Dodson, and Alfred A. Antson. "From bacterial to human dihydrouridine synthase: automated structure determination." Acta Crystallographica Section D Biological Crystallography 71, no. 7 (2015): 1564–71. http://dx.doi.org/10.1107/s1399004715009220.

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The reduction of uridine to dihydrouridine at specific positions in tRNA is catalysed by dihydrouridine synthase (Dus) enzymes. Increased expression of human dihydrouridine synthase 2 (hDus2) has been linked to pulmonary carcinogenesis, while its knockdown decreased cancer cell line viability, suggesting that it may serve as a valuable target for therapeutic intervention. Here, the X-ray crystal structure of a construct of hDus2 encompassing the catalytic and tRNA-recognition domains (residues 1–340) determined at 1.9 Å resolution is presented. It is shown that the structure can be determined
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Dixit, Sameer, and Samie R. Jaffrey. "Expanding the epitranscriptome: Dihydrouridine in mRNA." PLOS Biology 20, no. 7 (2022): e3001720. http://dx.doi.org/10.1371/journal.pbio.3001720.

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5

House, Christopher H., and Stanley L. Miller. "Hydrolysis of Dihydrouridine and Related Compounds." Biochemistry 35, no. 1 (1996): 315–20. http://dx.doi.org/10.1021/bi951577+.

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6

Savage, Dan F., Valérie de Crécy-Lagard, and Anthony C. Bishop. "Molecular determinants of dihydrouridine synthase activity." FEBS Letters 580, no. 22 (2006): 5198–202. http://dx.doi.org/10.1016/j.febslet.2006.08.062.

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7

Dyubankova, N., E. Sochacka, K. Kraszewska, B. Nawrot, P. Herdewijn, and E. Lescrinier. "Contribution of dihydrouridine in folding of the D-arm in tRNA." Organic & Biomolecular Chemistry 13, no. 17 (2015): 4960–66. http://dx.doi.org/10.1039/c5ob00164a.

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8

Feng, Pengmian, Zhaochun Xu, Hui Yang, Hao Lv, Hui Ding, and Li Liu. "Identification of D Modification Sites by Integrating Heterogeneous Features in Saccharomyces cerevisiae." Molecules 24, no. 3 (2019): 380. http://dx.doi.org/10.3390/molecules24030380.

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As an abundant post-transcriptional modification, dihydrouridine (D) has been found in transfer RNA (tRNA) from bacteria, eukaryotes, and archaea. Nonetheless, knowledge of the exact biochemical roles of dihydrouridine in mediating tRNA function is still limited. Accurate identification of the position of D sites is essential for understanding their functions. Therefore, it is desirable to develop novel methods to identify D sites. In this study, an ensemble classifier was proposed for the detection of D modification sites in the Saccharomyces cerevisiae transcriptome by using heterogeneous fe
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9

Yu, F., Y. Tanaka, K. Yamashita, et al. "Molecular basis of dihydrouridine formation on tRNA." Proceedings of the National Academy of Sciences 108, no. 49 (2011): 19593–98. http://dx.doi.org/10.1073/pnas.1112352108.

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10

Bishop, Anthony C., Jimin Xu, Reid C. Johnson, Paul Schimmel, and Valérie de Crécy-Lagard. "Identification of the tRNA-Dihydrouridine Synthase Family." Journal of Biological Chemistry 277, no. 28 (2002): 25090–95. http://dx.doi.org/10.1074/jbc.m203208200.

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Dissertations / Theses on the topic "Dihydrouridine"

1

Toubdji, Sabrine. "Biological and biochemical characterization of dihydrouridilation in bacterial ribosomal RNA." Electronic Thesis or Diss., Sorbonne université, 2024. http://www.theses.fr/2024SORUS236.

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La dihydrouridine (D) est une modification répandue et conservée au cours de l'évolution que l'on trouve principalement dans les ARNt et, dans une moindre mesure, dans les ARNm. Chez E. coli, elle s'étend jusqu'à la position 2449 de l'ARNr 23S, stratégiquement située près du centre peptidyltransférase du ribosome. Malgré l'existence de dihydrouridine synthases (DUS) connues, qui utilisent le NADPH et le FMN, l'enzyme responsable de la biosynthèse de D2449 est restée insaisissable.Cette étude présente une méthode rapide de détection de la D dans l'ARNr, impliquant le blocage de la transcriptase
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Lee, Ming-Hsun, та 李明訓. "Synthesis of 4'-α/β-aminomethyl dihydrouridine analogs construction of libraries via amide-bond formation". Thesis, 2008. http://ndltd.ncl.edu.tw/handle/18482427631937005984.

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Books on the topic "Dihydrouridine"

1

Hydrolysis of dihydrouridine and related compounds. National Aeronautics and Space Administration, 1996.

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Book chapters on the topic "Dihydrouridine"

1

"Dihydrouridine (5,6-dihydro-2,4-dihydroxyuracil nucleo-side)." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics. Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_4475.

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2

"Dd." In Biochemistry and Molecular biology, edited by Dr AD Smith, SP Datta, Dr G. H. Smith, et al. Oxford University PressOxford, 1997. http://dx.doi.org/10.1093/oso/9780198547686.003.0004.

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Abstract d- abbr. for dextro- used (formerly) as symbol denoting dextrorotatory;( + )- should now be used. See optical isomerism.D symbol for 1 a residue of the a-amino acid L-aspartic acid. 2 aresidue of an incompletely specified base in a nucleic-acid sequencethat may be adenine, guanine, or either thymine (inDNA) or uracil (in RNA). 3 a residue of the ribonucleoside(5,6-)dihydrouridine. 4 debye. 5 deuterium (use deprecated).D600 gallopamil, 5-methoxyverapamil, a-(3-{[2-(3,4-dimethoxyphenyl)ethyl] methylamino }propyl)-3,4,5-trimethoxy-a-(l-methylethyl) benzeneacetonitrile; a drug used in the
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3

Draycott, Austin S., Cassandra Schaening-Burgos, Maria F. Rojas-Duran, and Wendy V. Gilbert. "D-Seq: Genome-wide detection of dihydrouridine modifications in RNA." In Methods in Enzymology. Elsevier, 2023. http://dx.doi.org/10.1016/bs.mie.2023.09.001.

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4

Marchand, Virginie, Valérie Bourguignon-Igel, Mark Helm, and Yuri Motorin. "Mapping of 7-methylguanosine (m7G), 3-methylcytidine (m3C), dihydrouridine (D) and 5-hydroxycytidine (ho5C) RNA modifications by AlkAniline-Seq." In Methods in Enzymology. Elsevier, 2021. http://dx.doi.org/10.1016/bs.mie.2021.06.001.

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Journal articles
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