Evidence map›Paper›PMID 11972328›Full record

ArticleNucleic acids research2002

S6 phosphorylation-independent pathways regulate translation of 5'-terminal oligopyrimidine tract-containing mRNAs in differentiating hematopoietic cells.

Diane Barth-Baus, Carl A Stratton, Lou Parrott, Howard Myerson, Oded Meyuhas, Dennis J Templeton, Gary E Landreth, Jack O Hensold

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. AMPK represses TOP mRNA translation but not global protein synthesis in liver.Biochemical and biophysical research communications · 2008
    Article
  11. Article
  12. Review
  13. Article
  14. Amino acids as regulators of gene expression.Nutrition & metabolism · 2004
    Article
  15. Article
  16. 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

8 authors at 1 institution in 1 country.

Diane Barth-BausDepartment of Medicine and University/Ireland Cancer Center, Case Western Reserve University School of Medicine, Cleveland, OH 44106-4937, USA.
Carl A Stratton
Lou Parrott
Howard Myerson
Oded Meyuhas
Dennis J Templeton
Gary E Landreth
Jack O Hensold
Case Western Reserve University · US

Funding

NIDDK NIH HHS DK43414
6 · The paper itself

Abstract

Synthesis of new ribosomes is an energy costly and thus highly regulated process. Ribosomal protein synthesis is controlled by regulating translation of the corresponding ribosomal protein (rp)mRNAs. In mammalian cells a 5'-terminal oligopyrimidine tract (TOP) is a conserved feature of these mRNAs that has been demonstrated to be essential for their translational regulation. Translation of TOP mRNAs has been proposed to be regulated by phosphorylation of ribosomal protein S6, which is a common effect of mitogenic stimulation of cells. However, as demonstrated here, S6 phosphorylation is not detectable in murine erythroleukemia (MEL) or other hematopoietic cells. The absence of S6 phosphorylation appears to be due to the action of a phosphatase that acts downstream of S6 kinase, presumably on S6 itself. Despite the absence of changes in S6 phosphorylation, translation of TOP mRNAs is repressed during differentiation of MEL cells. These data demonstrate the existence of a mechanism for regulating S6 phosphorylation that is distinct from kinase activation, as well as the existence of mechanisms for regulating translation of TOP mRNAs that are independent of S6 phosphorylation.

Indexed as

Protein BiosynthesisSignal Transduction5' Flanking RegionAnimalsCell DifferentiationCell LineCell LineageDown-RegulationHematopoietic Stem CellsHumansMicePhosphorylationPyrimidinesRibosomal ProteinsRibosomal Protein S6Ribosomal Protein S6 KinasesPyrimidinesRibosomal ProteinsRibosomal Protein S6Ribosomal Protein S6 KinasesRNA, Messenger

Identifiers

PMID11972328
PMCPMC113832
OpenAlexW2098219133

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.