Evidence map›Paper›PMID 25996083›Full record

ArticleBiochemistry2015

Characterization of Novel Ribosome-Associated Endoribonuclease SLFN14 from Rabbit Reticulocytes.

Vera P Pisareva, Ilham A Muslimov, Andrew Tcherepanov, Andrey V Pisarev

Abstract read
In one paragraph

Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

42 citing papers in PubMed, 53 citations in OpenAlex.

  1. Trial
  2. Article
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  5. Article
  6. Article
  7. Human Schlafen 14 Cleavage of Short Double-Stranded RNAs Underpins its Antiviral Activity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  8. Article
  9. Article
  10. Novel mutationMolecular therapy. Nucleic acids · 2025
    Article
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  13. Review
  14. Article
  15. Review
  16. Article
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  19. Article
  20. Velcrin-induced selective cleavage of tRNANature chemical biology · 2023
    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

4 authors at 1 institution in 1 country.

Vera P Pisareva†Department of Cell Biology and ‡Department of Physiology and Pharmacology, SUNY Downstate Medical Center, 450 Clarkson Avenue, Brooklyn, New York 11203, United States.
Ilham A Muslimov†Department of Cell Biology and ‡Department of Physiology and Pharmacology, SUNY Downstate Medical Center, 450 Clarkson Avenue, Brooklyn, New York 11203, United States.
Andrew Tcherepanov†Department of Cell Biology and ‡Department of Physiology and Pharmacology, SUNY Downstate Medical Center, 450 Clarkson Avenue, Brooklyn, New York 11203, United States.
Andrey V Pisarev†Department of Cell Biology and ‡Department of Physiology and Pharmacology, SUNY Downstate Medical Center, 450 Clarkson Avenue, Brooklyn, New York 11203, United States.
SUNY Downstate Health Sciences University · US

Funding

Alternative mechanisms of different stages in eukaryotic translationR01GM097014 · NIGMS · SUNY DOWNSTATE MEDICAL CENTER · PI HELLEN, CHRISTOPHER ULRICH TRISTRAM · 2012 to 2022
$2.6M
NIGMS NIH HHS GM097014NIGMS NIH HHS R01 GM097014
6 · The paper itself

Abstract

Turnover of mRNA is a critical step that allows cells to control gene expression. Endoribonucleases, enzymes cleaving RNA molecules internally, are some of the key components of the degradation process. Here we provide a detailed characterization of novel endoribonuclease SLFN14 purified from rabbit reticulocyte lysate. Schlafen genes encode a family of proteins limited to mammals. Their cellular function is unknown or incompletely understood. In reticulocytes, SLFN14 is strongly overexpressed, represented exclusively by the short form, all tethered to ribosomes, and appears to be one of the major ribosome-associated proteins. SLFN14 binds to ribosomes and ribosomal subunits in the low part of the body and cleaves RNA but preferentially rRNA and ribosome-associated mRNA. This results in the degradation of ribosomal subunits. This process is strictly Mg(2+)- and Mn(2+)-dependent, NTP-independent, and sequence nonspecific. However, in other cell types, SLFN14 is a full-length solely nuclear protein, which lacks ribosomal binding and nuclease activities. Mutational analysis revealed the ribosomal binding site and the aspartate essential for the endonucleolytic activity of protein. Only few endoribonucleases participating in ribosome-mediated processes have been characterized to date. Moreover, none of them are shown to be directly associated with the ribosome. Therefore, our findings expand the general knowledge of endoribonucleases involved in mammalian translation control.

Indexed as

AnimalsBinding SitesEndoribonucleasesMutationRabbitsReticulocytesRibosomal ProteinsRibosomesRNA, RibosomalEndoribonucleasesRibosomal ProteinsRNA, Ribosomal

Identifiers

PMID25996083
PMCPMC4461289
OpenAlexW231638318

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.