Evidence map›Paper›PMID 28357293›Full record

ArticleMicrobial cell (Graz, Austria)2015

Polyamines directly promote antizyme-mediated degradation of ornithine decarboxylase by the proteasome.

R R Beenukumar, Daniela Gödderz, R Palanimurugan, R J Dohmen

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Microbial cell (Graz, Austria), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

8 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. A safety catch for ornithine decarboxylase degradation.Microbial cell (Graz, Austria) · 2015
    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

4 authors at 1 institution in 2 countries.

R R BeenukumarInstitute for Genetics, University of Cologne, Biocenter, Zülpicher Str. 47a, D-50674 Cologne, Germany.
Daniela GödderzInstitute for Genetics, University of Cologne, Biocenter, Zülpicher Str. 47a, D-50674 Cologne, Germany. ; Present address: Karolinska Institute, Department for Cell- and Molecular Biology, Von Eulers väg 3, 171 77 Stockholm.
R PalanimuruganInstitute for Genetics, University of Cologne, Biocenter, Zülpicher Str. 47a, D-50674 Cologne, Germany. ; Present address: Center for Cellular and Molecular Biology (CCMB), Uppal Road, Hyderabad 500007, India.
R J DohmenInstitute for Genetics, University of Cologne, Biocenter, Zülpicher Str. 47a, D-50674 Cologne, Germany.
University of Cologne · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ornithine decarboxylase (ODC), a ubiquitin-independent substrate of the proteasome, is a homodimeric protein with a rate-limiting function in polyamine biosynthesis. Polyamines regulate ODC levels by a feedback mechanism mediated by ODC antizyme (OAZ). Higher cellular polyamine levels trigger the synthesis of OAZ and also inhibit its ubiquitin-dependent proteasomal degradation. OAZ binds ODC monomers and targets them to the proteasome. Here, we report that polyamines, aside from their role in the control of OAZ synthesis and stability, directly enhance OAZ-mediated ODC degradation by the proteasome. Using a stable mutant of OAZ, we show that polyamines promote ODC degradation in

Indexed as

antizymeODCpolyaminesproteasomeubiquitin

Identifiers

PMID28357293
PMCPMC5349141
OpenAlexW2130012853

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.