Evidence map›Paper›PMID 20217058›Full record

ArticleJournal of molecular evolution2010

Recurrent emergence of catalytically inactive ornithine decarboxylase homologous forms that likely have regulatory function.

Ivaylo P Ivanov, Andrew E Firth, John F Atkins

Abstract read
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In one paragraph

Article in Journal of molecular evolution, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Roles of polyamines in translation.The Journal of biological chemistry · 2018
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. The Major Protein Arginine Methyltransferase inThe Journal of biological chemistry · 2017
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
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

3 authors at 2 institutions in 2 countries.

Ivaylo P IvanovBioSciences Institute, University College Cork, Ireland.
Andrew E Firth
John F Atkins
University College Cork · IEUniversity of Utah · US

Funding

The range of recoding and analysis of a 50 nt bypass to probe ribosomal functionR01GM079523 · NIGMS · UNIVERSITY OF UTAH · PI ATKINS, JOHN F. · 2007 to 2010
$1.3M
NIGMS NIH HHS R01 GM079523
6 · The paper itself

Abstract

Ornithine decarboxylase (ODC) catalyzes the first and rate limiting step in the biosynthesis of polyamines in most eukaryotes. Because polyamines have pleiotropic and often dramatic effects on cellular processes at both high and low concentrations, ODC expression is tightly controlled. ODC is regulated by a family of polyamine-induced proteins, antizymes, which bind to, and inactivate it. In mammals, and apparently most vertebrates, antizymes are in turn antagonized by proteins called antizyme inhibitors. Antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind antizyme, in most cases even more tightly than ODC. We present a phylogenetic analysis of over 200 eukaryotic homologs of ODC and evaluate their potential to be either true ODCs or catalytically inactive proteins that might be analogs of the previously identified antizyme inhibitors. This analysis yielded several orthologous groups of putative novel antizyme inhibitors each apparently arising independently. In the process we also identify previously unrecognized ODC paralogs in several evolutionary branches, including a previously unrecognized ODC paralog in mammals, and we evaluate their biochemical potential based on their pattern of amino acid conservation.

Indexed as

Evolution, MolecularSequence HomologyAnimalsCatalysisEnzyme ActivationHumansInvertebratesIsoenzymesOrnithine DecarboxylasePhylogenyProteinsRecurrenceStructure-Activity RelationshipVertebratesIsoenzymesOrnithine Decarboxylaseornithine decarboxylase antizymeProteins

Identifiers

PMID20217058
OpenAlexW2015892892

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.