Results 281 to 290 of about 459,217 (330)
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Genome-Wide Analysis of A-to-I RNA Editing
Methods in molecular biology, 2016Adenosine (A)-to-inosine (I) RNA editing is a fundamental posttranscriptional modification that ensures the deamination of A-to-I in double-stranded (ds) RNA molecules. Intriguingly, the A-to-I RNA editing system is particularly active in the nervous system of higher eukaryotes, altering a plethora of noncoding and coding sequences.
Yiannis A, Savva +2 more
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A-to-I editing prevents self-RNA sensing
Nature Reviews Molecular Cell Biology, 2022Leilei Chen, Chen Leilei
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Identification of A-to-I RNA editing: Dotting the i’s in the human transcriptome
Biochemistry (Moscow), 2011The phenomenon of adenosine-to-inosine (A-to-I) RNA editing has attracted considerable attention from the scientific community due to its potential relationship to the evolution of cognition in animals. While A-to-I editing exists in all organisms with neurons, including those with primitive neuronal systems (hydra and nematodes), it is particularly ...
A, Kiran +3 more
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How RNA editing keeps an I on physiology
American Journal of Physiology-Cell Physiology, 2022Adenosine deaminases acting on RNAs convert adenosines (A) to inosines (I) in structured or double-stranded RNAs. In mammals, this process is widespread. In the human transcriptome, more than a million different sites have been identified that undergo an ADAR-mediated A-to-I exchange Inosines have an altered base pairing potential due to the missing ...
Marion Goldeck +5 more
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A-to-I RNA editing as a tuner of noncoding RNAs in cancer
Cancer Letters, 2020Recent advancement in RNA technology and computation biology shows the abundance and impact of RNA editing at the genome-wide level. Of RNA editing events, Adenosine-to-inosine (A-to-I) RNA editing is one of the most frequent types of RNA editing catalyzed by ADAR proteins.
Yuanfan Liao, Seung Ho Jung, Taewan Kim
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A-to-I editing of protein coding and noncoding RNAs
Critical Reviews in Biochemistry and Molecular Biology, 2012Adenosine deaminase acting on RNA (ADAR) catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) substrates. Inosine pairs preferentially with cytidine, as opposed to uridine; therefore, ADAR editing alters the sequence and base pairing properties of both protein-coding and non-coding RNA.
Arka, Mallela, Kazuko, Nishikura
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A-to-I RNA Editing is Induced Upon Hypoxia
Shock, 2011Regulating gene expression is part of a cell's response to hypoxia. A-to-I RNA editing is an epigenetic phenomenon that can contribute to RNA and protein levels and to isoform diversity. In this study, we identified alterations in the levels of RNA editing following hypoxic stress in three genes: MED13, STAT3, and F11R.
Yael, Nevo-Caspi +3 more
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Short-Chain Guide RNA for Site-Directed A-to-I RNA Editing
Nucleic Acid Therapeutics, 2021Site-directed RNA editing is a promising genetic modification technology for therapeutic and pharmaceutical applications. We previously constructed adenosine deaminases acting on RNA (ADAR)-guiding RNAs (AD-gRNAs) that direct A-to-I RNA editing activity of native human ADAR2 into a programmable target site.
Kanako, Nose +4 more
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Detection of A-to-I Hyper-edited RNA Sequences
2020Following A-to-I editing of double-stranded RNA (dsRNA) molecules, sequencing reactions interpret the edited inosine (I) as guanosine (G). For this reason, current methods to detect A-to-I editing sites work to align RNA sequences to their reference DNA sequence in order to reveal A-to-G mismatches.
Roni, Cohen-Fultheim, Erez Y, Levanon
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A-to-I RNA editing: The “ADAR” side of human cancer
Seminars in Cell & Developmental Biology, 2012Carcinogenesis is a complex, multi-stage process depending on both endogenous and exogenous factors. In the past years, DNA mutations provided important clues to the comprehension of the molecular pathways involved in numerous cancers. Recently, post-transcriptional modification events, such as RNA editing, are emerging as new players in several human ...
Galeano, Federica +3 more
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