Evidence map›Paper›PMID 23665583›Full record

ArticleNature structural & molecular biology2013

Turning catalytically inactive human Argonaute proteins into active slicer enzymes.

Judith Hauptmann, Anne Dueck, Simone Harlander, Janina Pfaff, Rainer Merkl, Gunter Meister

Open access · greenAbstract readComparative Study
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

66 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
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  6. Review
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  9. Article
  10. The structural basis for RNA slicing by human Argonaute2.bioRxiv : the preprint server for biology · 2024
    Article
  11. Article
  12. Article
  13. Identification of an active RNAi pathway inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. NgAgo possesses guided DNA nicking activity.Nucleic acids research · 2021
    Article
  18. Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Judith HauptmannBiochemistry Center Regensburg, Laboratory for RNA Biology, University of Regensburg, Germany.
Anne Dueck
Simone Harlander
Janina Pfaff
Rainer Merkl
Gunter Meister
University of Regensburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Argonaute proteins interact with small RNAs that guide them to complementary target RNAs, thus leading to inhibition of gene expression. Some but not all Argonaute proteins are endonucleases and can cleave the complementary target RNA. Here, we have mutated inactive human Ago1 and Ago3 and generated catalytic Argonaute proteins. We find that two short sequence elements at the N terminus are important for activity. In addition, PIWI-domain mutations in Ago1 may misarrange the catalytic center. Our work helps in understanding of the structural requirements that make an Argonaute protein an active endonucleolytic enzyme.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionArgonaute ProteinsBase SequenceCatalysisEukaryotic Initiation FactorsHEK293 CellsHumansMicroRNAsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPoint MutationProtein ConformationProtein Structure, TertiaryRecombinant Fusion ProteinsAGO1 protein, humanAGO2 protein, humanAGO3 protein, humanAGO4 protein, humanArgonaute ProteinsEukaryotic Initiation FactorsMicroRNAsRecombinant Fusion Proteins

Identifiers

PMID23665583
OpenAlexW2090586656

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.