Evidence map›Paper›PMID 26372505›Full record

ArticleACS chemical biology2015

A Phenotypic Screen for Functional Mutants of Human Adenosine Deaminase Acting on RNA 1.

Yuru Wang, Jocelyn Havel, Peter A Beal

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
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  8. Review
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  13. Base editing: advances and therapeutic opportunities.Nature reviews. Drug discovery · 2020
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. RNA editing with CRISPR-Cas13.Science (New York, N.Y.) · 2017
    Article
  19. Article
  20. Article
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

3 authors at 1 institution in 1 country.

Yuru WangDepartment of Chemistry, University of California, Davis , 1 Shields Ave, Davis, California 95616, United States.
Jocelyn HavelDepartment of Chemistry, University of California, Davis , 1 Shields Ave, Davis, California 95616, United States.
Peter A BealDepartment of Chemistry, University of California, Davis , 1 Shields Ave, Davis, California 95616, United States.
University of California, Davis · US

Funding

The Bioorganic Chemistry Of RNA Editing By ADARSR01GM061115 · NIGMS · UNIVERSITY OF UTAH · PI BEAL, PETER A. · 2001 to 2020
$4.5M
NIGMS NIH HHS R01 GM061115NIGMS NIH HHS R01-GM061115
6 · The paper itself

Abstract

Adenosine deaminases acting on RNA (ADARs) are RNA-editing enzymes responsible for the conversion of adenosine to inosine at specific locations in cellular RNAs. ADAR1 and ADAR2 are two members of the family that have been shown to be catalytically active. Earlier, we reported a phenotypic screen for the study of human ADAR2 using budding yeast S. cerevisiae as the host system. While this screen has been successfully applied to the study of ADAR2, it failed with ADAR1. Here, we report a new reporter that uses a novel editing substrate and is suitable for the study of ADAR1. We screened plasmid libraries with randomized codons for two important residues in human ADAR1 (G1007 and E1008). The screening results combined with in vitro deamination assays led to the identification of mutants that are more active than the wild type protein. Furthermore, a screen of the ADAR1 E1008X library with a reporter construct bearing an A•G mismatch at the editing site suggests one role for the residue at position 1008 is to sense the identity of the base pairing partner for the editing site adenosine. This work has provided a starting point for future in vitro evolution studies of ADAR1 and led to new insight into ADAR's editing site selectivity.

Indexed as

MutationPhenotypeAdenosine DeaminaseAmino Acid SequenceCatalytic DomainGenetic TestingHumansMolecular Sequence DataProtein Structure, SecondaryRNARNA-Binding ProteinsADAR protein, humanAdenosine DeaminaseRNARNA-Binding Proteins

Identifiers

PMID26372505
PMCPMC4900682
OpenAlexW2414849856

What OpenQuestion holds

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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.