Evidence map›Paper›PMID 24514906›Full record

ArticleGenetics2014

Degradation of centromeric histone H3 variant Cse4 requires the Fpr3 peptidyl-prolyl Cis-Trans isomerase.

Kentaro Ohkuni, Rashid Abdulle, Katsumi Kitagawa

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

27 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
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  6. Review
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  9. Article
  10. International journal of molecular sciences · 2020
    Article
  11. FKBP25 participates in DNA double-strand break repair.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2020
    Article
  12. Article
  13. Review
  14. Conformational flexibility of histone variant CENP-AThe Journal of biological chemistry · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Kentaro OhkuniCenter for Childhood Cancer, The Research Institute, Nationwide Children's Hospital, Columbus, Ohio 43205.
Rashid Abdulle
Katsumi Kitagawa
Nationwide Children's Hospital · US

Funding

Kinetochore Function and Cell Cycle Progression RevisionR01GM068418 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI KITAGAWA, KATSUMI · 2003 to 2012
$2.5M
NIGMS NIH HHS GM68418NIGMS NIH HHS R01 GM068418
6 · The paper itself

Abstract

The centromeric histone H3 variant Cse4 in Saccharomyces cerevisiae is polyubiquitylated and degraded in a proteasome-dependent manner. We report here that the proline isomerase Fpr3 regulates Cse4 proteolysis. Structural change in Cse4 by Fpr3 might be important for the interaction between Cse4 and the E3 ubiquitin ligase Psh1.

Indexed as

Chromosomal InstabilityChromosomal Proteins, Non-HistoneChromosomes, FungalDNA-Binding ProteinsImmunophilinsMitosisPeptide Elongation FactorsProteasome Endopeptidase ComplexProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationUbiquitin-Protein LigasesChromosomal Proteins, Non-HistoneCSE4 protein, S cerevisiaeDNA-Binding ProteinsFPR3 protein, S cerevisiaeImmunophilinsPeptide Elongation FactorsProteasome Endopeptidase ComplexPsh1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesCse4Fpr3isomerizationprotein degradationPsh1

Identifiers

PMID24514906
PMCPMC3982699
OpenAlexW2158045783

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.