Evidence map›Paper›PMID 22354986›Full record

ArticleMolecular and cellular biology2012

Polyamine-regulated translation of spermidine/spermine-N1-acetyltransferase.

Oscar Perez-Leal, Carlos A Barrero, Allen B Clarkson, Robert A Casero, Salim Merali

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 40 citations in OpenAlex.

  1. Trial
  2. Article
  3. Activation of polyamine catabolism promotes glutamine metabolism and creates a targetable vulnerability in lung cancer.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Metabolomic Reprogramming of C57BL/6-Macrophages during Early Infection withInternational journal of molecular sciences · 2021
    Article
  11. Polyamine Homeostasis in Development and Disease.Medical sciences (Basel, Switzerland) · 2021
    Review
  12. Article
  13. Polyamine Catabolism in Acute Kidney Injury.International journal of molecular sciences · 2019
    Review
  14. Article
  15. Roles of polyamines in translation.The Journal of biological chemistry · 2018
    Review
  16. Article
  17. Article
  18. 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

5 authors at 3 institutions in 1 country.

Oscar Perez-LealDepartment of Biochemistry, Temple University School of Medicine, Philadelphia, Pennsylvania, USA.
Carlos A Barrero
Allen B Clarkson
Robert A Casero
Salim Merali
Temple University · USJohns Hopkins University · USNew York University · US

Funding

Spermine N1-Acetylase Induction in Lung CancersR01CA051085 · NCI · JOHNS HOPKINS UNIVERSITY · PI CASERO, ROBERT A. · 1990 to 2013
$4.7M
S-Adenosylmethionine and Pneumocystis treatmentR01AI064017 · NIAID · TEMPLE UNIV OF THE COMMONWEALTH · PI MERALI, SALIM · 2005 to 2009
$1.8M
NCI NIH HHS R01 CA051085NIAID NIH HHS R01 AI064017NIAID NIH HHS R01AI064017
6 · The paper itself

Abstract

Rapid synthesis of the polyamine catabolic enzyme spermidine/spermine-N(1)-acetyltransferase (SSAT) in response to increased polyamines is an important polyamine homeostatic mechanism. Indirect evidence has suggested that there is an important control mechanism involving the release of a translational repressor protein that allows the immediate initiation of SSAT protein synthesis without RNA transcription, maturation, or translocation. To identify a repressor protein, we used a mass spectroscopy-based RNA-protein interaction system and found six proteins that bind to the coding region of SSAT mRNA. Individual small interfering RNA (siRNA) experiments showed that nucleolin knockdown enhances SSAT translation. Nucleolin exists in several isoforms, and we report that the isoform that binds to SSAT mRNA undergoes autocatalysis in the presence of polyamines, a result suggesting that there is a negative feedback system that helps control the cellular content of polyamines. Preliminary molecular interaction data show that a nucleolin isoform binds to a 5' stem-loop of the coding region of SSAT mRNA. The glycine/arginine-rich C terminus of nucleolin is required for binding, and the four RNA recognition motif domains are included in the isoform that blocks SSAT translation. Understanding SSAT translational control mechanisms has the potential for the development of therapeutic strategies against cancer and obesity.

Indexed as

Protein BiosynthesisAcetyltransferasesCell LineDiamine N-AcetyltransferaseHumansNucleolinPhosphoproteinsPolyaminesProtein BindingProtein IsoformsRNA-Binding ProteinsRNA, Small InterferingAcetyltransferasesDiamine N-AcetyltransferaseNucleolinPhosphoproteinsPolyaminesProtein IsoformsRNA-Binding ProteinsRNA, Small Interfering

Identifiers

PMID22354986
PMCPMC3318587
OpenAlexW2081556765

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.