Evidence map›Paper›PMID 36983519›Full record

ArticleJournal of fungi (Basel, Switzerland)2023

Yeast Ribonucleotide Reductase Is a Direct Target of the Proteasome and Provides Hyper Resistance to the Carcinogen 4-NQO.

Daria S Spasskaya, Kirill A Kulagin, Evgenia N Grineva, Pamila J Osipova, Svetlana V Poddubko, Julia A Bubis, Elizaveta M Kazakova, Tomiris T Kusainova, Vladimir A Gorshkov, Frank Kjeldsen and 3 more

Open access · goldAbstract read
In one paragraph

Article in Journal of fungi (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 51% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. 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

13 authors at 4 institutions in 2 countries.

Daria S SpasskayaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.
Kirill A KulaginEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.
Evgenia N GrinevaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.ORCID 0000-0002-3099-3029
Pamila J OsipovaInstitute of Medical and Biological Problems, Russian Academy of Sciences, 123007 Moscow, Russia.
Svetlana V PoddubkoInstitute of Medical and Biological Problems, Russian Academy of Sciences, 123007 Moscow, Russia.ORCID 0000-0003-4926-8289
Julia A BubisV.L. Talrose Institute for Energy Problems of Chemical Physics, N.N. Semenov Federal Research Center of Chemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia.
Elizaveta M KazakovaV.L. Talrose Institute for Energy Problems of Chemical Physics, N.N. Semenov Federal Research Center of Chemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia.
Tomiris T KusainovaV.L. Talrose Institute for Energy Problems of Chemical Physics, N.N. Semenov Federal Research Center of Chemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia.
Vladimir A GorshkovDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, 5230 Odense M, Denmark.ORCID 0000-0003-0170-5785
Frank KjeldsenDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, 5230 Odense M, Denmark.
Vadim L KarpovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.
Irina A TarasovaV.L. Talrose Institute for Energy Problems of Chemical Physics, N.N. Semenov Federal Research Center of Chemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia.
Dmitry S KarpovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.ORCID 0000-0001-5203-0787
Engelhardt Institute of Molecular Biology · RUSemenov Institute of Chemical Physics · RUInstitute of Biomedical Problems · RUUniversity of Southern Denmark · DK

Funding

Russian Science Foundation 22-24-01065VILLUM Center for Bioanalytical Sciences and PRO-MS: Danish National Mass Spec-trometry Platform for Functional Proteomics 5072-00007B
6 · The paper itself

Abstract

Various external and internal factors damaging DNA constantly disrupt the stability of the genome. Cells use numerous dedicated DNA repair systems to detect damage and restore genomic integrity in a timely manner. Ribonucleotide reductase (RNR) is a key enzyme providing dNTPs for DNA repair. Molecular mechanisms of indirect regulation of yeast RNR activity are well understood, whereas little is known about its direct regulation. The study was aimed at elucidation of the proteasome-dependent mechanism of direct regulation of RNR subunits in

Indexed as

4-NQOproteasomeribonucleotide reductaseS. cerevisiaeshotgun proteomics

Identifiers

PMID36983519
PMCPMC10057556
OpenAlexW4324149941

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.