Evidence map›Paper›PMID 10781085›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Discovery of a spermatogenesis stage-specific ornithine decarboxylase antizyme: antizyme 3.

I P Ivanov, A Rohrwasser, D A Terreros, R F Gesteland, J F Atkins

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

57 citing papers in PubMed, 132 citations in OpenAlex.

  1. Protein degradation of antizyme depends on the N-terminal degrons.Protein science : a publication of the Protein Society · 2024
    Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Polyamines in mammalian pathophysiology.Cellular and molecular life sciences : CMLS · 2019
    Review
  13. Roles of polyamines in translation.The Journal of biological chemistry · 2018
    Review
  14. The antizyme family for regulating polyamines.The Journal of biological chemistry · 2018
    Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Structural basis of antizyme-mediated regulation of polyamine homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

I P IvanovDepartment of Human Genetics, University of Utah, 15 North 2030 East, Salt Lake City, UT 84112-5330, USA.
A Rohrwasser
D A Terreros
R F Gesteland
J F Atkins
United States Department of Veterans Affairs · USUniversity of Utah · US

Funding

RECODING--DYNAMIC REPROGRAMMING OF GENETIC READOUTR01GM048152 · NIGMS · UNIVERSITY OF UTAH · PI ATKINS, JOHN F. · 1992 to 2004
$2.1M
NIGMS NIH HHS R01 GM048152NIGMS NIH HHS R01-GM48152
6 · The paper itself

Abstract

Previous studies with mice overproducing ornithine decarboxylase have demonstrated the importance of polyamine homeostasis for normal mammalian spermatogenesis. The present study introduces a likely key player in the maintenance of proper polyamine homeostasis during spermatogenesis. Antizyme 3 is a paralog of mammalian ornithine decarboxylase antizymes. Like its previously described counterparts, antizymes 1 and 2, it inhibits ornithine decarboxylase, which catalyzes the synthesis of putrescine. Earlier work has shown that the coding sequences for antizymes 1 and 2 are in two different, partially overlapping reading frames. Ribosomes translate the first reading frame, and just before the stop codon for that frame, they shift to the second reading frame to synthesize a trans-frame product. The efficiency of this frameshifting depends on polyamine concentration, creating an autoregulatory circuit. Antizyme 3 cDNA has the same arrangement of reading frames and a potential shift site with definite, although limited, homology to its evolutionarily distant antizyme 1 and 2 counterparts. In contrast to antizymes 1 and 2, which are widely expressed throughout the body, antizyme 3 transcription is restricted to testis germ cells. Expression starts early in spermiogenesis and finishes in the late spermatid phase. The potential significance of antizyme 3 expression during spermatogenesis is discussed in this paper.

Indexed as

Ornithine Decarboxylase InhibitorsAdultAmino Acid SequenceAnimalsChickensDrosophila melanogasterEnzyme InhibitorsHumansIn Situ HybridizationMaleMiceMolecular Sequence DataOpen Reading FramesPhylogenyProteinsSeminiferous TubulesEnzyme Inhibitorsornithine decarboxylase antizymeOrnithine Decarboxylase InhibitorsProteins

Identifiers

PMID10781085
PMCPMC18314
OpenAlexW1993939352

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.