Evidence map›Paper›PMID 27794026›Full record

ArticleGenetics2017

Histone H4 Facilitates the Proteolysis of the Budding Yeast CENP-ACse4 Centromeric Histone Variant.

Gary M R Deyter, Erica M Hildebrand, Adrienne D Barber, Sue Biggins

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 21% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Conformational flexibility of histone variant CENP-AThe Journal of biological chemistry · 2018
    Article
  10. 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 2 institutions in 1 country.

Gary M R DeyterHoward Hughes Medical Institute, Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98040.
Erica M HildebrandHoward Hughes Medical Institute, Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98040.
Adrienne D BarberHoward Hughes Medical Institute, Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98040.
Sue BigginsHoward Hughes Medical Institute, Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98040 sbiggins@fredhutch.org.ORCID 0000-0002-4499-6319
Fred Hutch Cancer Center · USUniversity of Washington · US

Funding

Chromosome Metabolism and Cancer Training GrantT32CA009657 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI EISENMAN, ROBERT NEIL · 1991 to 2020
$7.6M
Regulation of Centromeric ChromatinR01GM078069 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI BIGGINS, SUSAN · 2007 to 2015
$2.7M
NCI NIH HHS T32 CA009657NIGMS NIH HHS R01 GM078069
6 · The paper itself

Abstract

The incorporation of histone variants into nucleosomes can alter chromatin-based processes. CENP-A is the histone H3 variant found exclusively at centromeres that serves as an epigenetic mark for centromere identity and is required for kinetochore assembly. CENP-A mislocalization to ectopic sites appears to contribute to genomic instability, transcriptional misregulation, and tumorigenesis, so mechanisms exist to ensure its exclusive localization to centromeres. One conserved process is proteolysis, which is mediated by the Psh1 E3 ubiquitin ligase in Saccharomyces cerevisiae (budding yeast). To determine whether there are features of the CENP-A nucleosome that facilitate proteolysis, we performed a genetic screen to identify histone H4 residues that regulate CENP-A

Indexed as

AutoantigensCentromereCentromere Protein AChromatinChromosomal Proteins, Non-HistoneDNA-Binding ProteinsEuchromatinHistonesKinetochoresNucleosomesProtein BindingProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationUbiquitin-Protein LigasesAutoantigensCentromere Protein AChromatinChromosomal Proteins, Non-HistoneDNA-Binding ProteinsEuchromatinHistonesNucleosomesSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesCENP-ACse4centromereH4nucleosomeproteolysisPsh1

Identifiers

PMID27794026
PMCPMC5223497
OpenAlexW2545677203

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.