Evidence map›Paper›PMID 35563006›Full record

ArticleInternational journal of molecular sciences2022

Role of Polyamine-Induced Dimerization of Antizyme in Its Cellular Functions.

Mervi T Hyvönen, Olga A Smirnova, Vladimir A Mitkevich, Vera L Tunitskaya, Maxim Khomutov, Dmitry S Karpov, Sergey P Korolev, Merja R Häkkinen, Marko Pietilä, Marina B Gottikh and 7 more

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

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Biomolecules · 2023
    Article
  3. 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

17 authors at 4 institutions in 3 countries.

Mervi T HyvönenSchool of Pharmacy, Biocenter Kuopio, University of Eastern Finland, Yliopistonranta 1B, 70210 Kuopio, Finland.
Olga A SmirnovaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia.
Vladimir A MitkevichEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia.ORCID 0000-0002-1517-1983
Vera L TunitskayaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia.
Maxim KhomutovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia.
Dmitry S KarpovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia.ORCID 0000-0001-5203-0787
Sergey P KorolevBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1, 119991 Moscow, Russia.ORCID 0000-0003-2278-4451
Merja R HäkkinenSchool of Pharmacy, Biocenter Kuopio, University of Eastern Finland, Yliopistonranta 1B, 70210 Kuopio, Finland.
Marko PietiläSchool of Medicine, Biocenter Kuopio, University of Eastern Finland, Yliopistonranta 1E, 70210 Kuopio, Finland.
Marina B GottikhBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1, 119991 Moscow, Russia.ORCID 0000-0002-4613-5096
Jouko VepsäläinenSchool of Pharmacy, Biocenter Kuopio, University of Eastern Finland, Yliopistonranta 1B, 70210 Kuopio, Finland.
Leena AlhonenSchool of Pharmacy, Biocenter Kuopio, University of Eastern Finland, Yliopistonranta 1B, 70210 Kuopio, Finland.
Alexander A MakarovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia.
Sergey N KochetkovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia.
Heather M WallaceSchool of Medicine, Medical Sciences and Nutrition, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, UK.ORCID 0000-0003-2804-3304
Tuomo A KeinänenSchool of Pharmacy, Biocenter Kuopio, University of Eastern Finland, Yliopistonranta 1B, 70210 Kuopio, Finland.ORCID 0000-0002-0659-5573
Alex R KhomutovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia.
Engelhardt Institute of Molecular Biology · RUUniversity of Eastern Finland · FILomonosov Moscow State University · RUUniversity of Aberdeen · GB

Funding

Academy of Finland 292574Academy of Finland 315487Russian Foundation for Basic Research 18-54-11008Russian Science Foundation 17-74-20049
6 · The paper itself

Abstract

The polyamines, spermine (Spm) and spermidine (Spd), are important for cell growth and function. Their homeostasis is strictly controlled, and a key downregulator of the polyamine pool is the polyamine-inducible protein, antizyme 1 (OAZ1). OAZ1 inhibits polyamine uptake and targets ornithine decarboxylase (ODC), the rate-limiting enzyme of polyamine biosynthesis, for proteasomal degradation. Here we report, for the first time, that polyamines induce dimerization of mouse recombinant full-length OAZ1, forming an (OAZ1)

Indexed as

PolyaminesSpermidineAnimalsDimerizationFrameshifting, RibosomalMiceOrnithine DecarboxylaseProteinsOrnithine Decarboxylaseornithine decarboxylase antizymePolyaminesProteinsSpermidineantizymedimerizationornithine decarboxylasepolyamine analoguespolyaminespolyamine uptakeribosomal frameshiftingα-difluoromethylornithine

Identifiers

PMID35563006
PMCPMC9104013
OpenAlexW4224243405

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.