Evidence map›Paper›PMID 23129636›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Mechanistic insights into editing-site specificity of ADARs.

Ashani Kuttan, Brenda L Bass

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
2.1field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

112 citing papers in PubMed, 179 citations in OpenAlex.

  1. Review
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  7. MEX3A Modulates PPARγ Pathway Activity and Colorectal Cancer Growth.Cellular and molecular gastroenterology and hepatology · 2026
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  12. Review
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  14. Phylogenetic and structural analysis of Hydra ADAR.Archives of biochemistry and biophysics · 2025
    Article
  15. Article
  16. Article
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  20. Article

52 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Ashani KuttanDepartment of Biochemistry, University of Utah, Salt Lake City, UT 84112, USA.
Brenda L Bass
University of Utah · US

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 1986 to 2026
$72.6M
The Biology and Biochemistry of ADAR RNA Editing EnzymesR01GM044073 · NIGMS · UNIVERSITY OF UTAH · PI BASS, BRENDA L. · 1990 to 2020
$3.6M
NCI NIH HHS P30 CA042014NCI NIH HHS P30CA042014NIGMS NIH HHS R01 GM044073NIGMS NIH HHS R01GM044073
6 · The paper itself

Abstract

Adenosine deaminases that act on RNA (ADARs) deaminate adenosines in dsRNA to produce inosines. ADARs are essential in mammals and are particularly important in the nervous system. Altered levels of adenosine-to-inosine (A-to-I) editing are observed in several diseases. The extent to which an adenosine is edited depends on sequence context. Human ADAR2 (hADAR2) has 5' and 3' neighbor preferences, but which amino acids mediate these preferences, and by what mechanism, is unknown. We performed a screen in yeast to identify mutations in the hADAR2 catalytic domain that allow editing of an adenosine within a disfavored triplet. Binding affinity, catalytic rate, base flipping, and preferences were monitored to understand the effects of the mutations on ADAR reactivity. Our data provide information on the amino acids that affect preferences and point to a conserved loop as being of key importance. Unexpectedly, our data suggest that hADAR2's preferences derive from differential base flipping rather than from direct recognition of neighboring bases. Our studies set the stage for understanding the basis of altered editing levels in disease and for developing therapeutic reagents.

Indexed as

RNA EditingAdenosine DeaminaseAmino Acid SequenceAnimalsBinding SitesCatalytic DomainModels, MolecularMolecular Sequence DataMutationRNA-Binding ProteinsSequence Homology, Amino AcidADARB1 protein, humanAdenosine DeaminaseRNA-Binding Proteins

Identifiers

PMID23129636
PMCPMC3511710
OpenAlexW2026284791

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.