Evidence map›Paper›PMID 9171092›Full record

ArticleNucleic acids research1997

Chloroplast endoribonuclease p54 involved in RNA 3'-end processing is regulated by phosphorylation and redox state.

K Liere, G Link

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

12 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Sigma factor phosphorylation in the photosynthetic control of photosystem stoichiometry.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  4. Article
  5. Chloroplast RNA-binding proteins.Current genetics · 2003
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

2 authors.

K LierePlant Cell Physiology and Molecular Biology, University of Bochum, D-44780 Bochum, Germany.
G Link

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chloroplast RNA-binding protein p54 is an endoribonuclease required for 3'end-processing of plastid precursor transcripts. We find that purified p54 can serve as a phosphate acceptor for protein kinases in vitro. Both the processing and RNA-binding activities of p54 are enhanced by phosphorylation and decreased by dephosphorylation. In addition, the enzyme is activated by the oxidized form of glutathione and inhibited by the reduced form, whereas other redox reagents that were tested showed no effect. Kinase treatment of p54 prior to oxidation by glutathione resulted in highest levels of activation, suggesting that phosphorylation and redox state act together to control p54 activity in vitro and possibly also in vivo.

Indexed as

RNA Processing, Post-TranscriptionalChloroplast ProteinsChloroplastsEndoribonucleasesMustard PlantOxidation-ReductionPhosphorylationPlants, MedicinalPlastidsProtein Processing, Post-TranslationalRNA-Binding ProteinsRNA, PlantSubstrate SpecificityTranscription, GeneticChloroplast Proteinschloroplast RNA-binding protein p54EndoribonucleasesRNA-Binding ProteinsRNA, Plant

Identifiers

PMID9171092
PMCPMC146767
OpenAlexW2096049216

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.