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A-to-I editing of protein coding and noncoding RNAs

Critical Reviews in Biochemistry and Molecular Biology, 2012
Adenosine 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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RNA A-to-I editing, environmental exposure, and human diseases

Critical Reviews in Toxicology, 2021
Epigenetic modifications have gained attention since they can be potentially changed with environmental stimuli and can be associated with adverse health outcomes. Epitranscriptome field has begun to attract attention with several aspects since RNA modifications have been linked with critical biological processes and implicated in diseases. Several RNA
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A-to-I RNA Editing in Human Cells

2021
A thesis presented to the faculty of The Rockefeller University in partial fulfillment of the requirements for the degree of Doctor of ...
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Aptazyme-directed A-to-I RNA editing

As a promising therapeutic approach, the RNA editing process can correct pathogenic mutations and is reversible and tunable, without permanently altering the genome. RNA editing mediated by human ADAR proteins offers unique advantages, including high specificity and low immunogenicity.
Xilei, Ai, Zhuo, Tang
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A-to-I editing of microRNAs: Regulating the regulators?

Seminars in Cell & Developmental Biology, 2012
An important epigenetic mechanism in mammals is adenosine deamination, which generates transcriptome variety through the conversion of single adenosines into inosines in RNA molecules. Inosine is interpreted as guanosine by the translational machinery, and when A-to-I RNA editing occurs in the coding region of pre-mRNA molecules this substitution can ...
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Nanopore sequencing to detect A-to-I editing sites

Adenosine-to-inosine (A-to-I) RNA editing, mediated by the ADAR family of enzymes, is pervasive in metazoans and functions as an important mechanism to diversify the proteome and control gene expression. Over the years, there have been multiple efforts to comprehensively map the editing landscape in different organisms and in different disease states ...
Jia Wei Joel, Heng, Meng How, Tan
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A-to-I and C-to-U editing within transfer RNAs

Biochemistry (Moscow), 2011
A significant number of post-transcriptional changes occur during the generation of mature transfer RNAs (tRNAs). These changes within precursor-tRNA molecules include the processing of 5' and 3' termini, the introduction of modifications, and also RNA editing. In this review, we will detail the reported cases of A-to-I and C-to-U tRNA editing.
Su, A., Randau, L.
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A-to-I RNA editing: The “ADAR” side of human cancer

Seminars in Cell & Developmental Biology, 2012
Carcinogenesis 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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Bioinformatic Approaches for Identification of A-to-I Editing Sites

2011
The first discoveries of mammalian A-to-I RNA editing have been serendipitous. In conjunction with the fast advancement in sequencing technology, systematic methods for prediction and detection of editing sites have been developed, leading to the discovery of thousands of A-to-I editing sites.
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Perturbing A-to-I RNA Editing Using Genetics and Homologous Recombination

2011
Evidence for the chemical conversion of adenosine-to-inosine (A-to-I) in messenger RNA (mRNA) has been detected in numerous metazoans, especially those "most successful" phyla: Arthropoda, Mollusca, and Chordata. The requisite enzymes for A-to-I editing, ADARs (adenosine deaminases acting on RNA) are highly conserved and are present in every higher ...
Cynthia J, Staber   +3 more
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