Evidence map›Paper›PMID 28108585›Full record

ArticleGenetics2017

Histone H3K4 and H3K36 Methylation Independently Recruit the NuA3 Histone Acetyltransferase in

Benjamin J E Martin, Kristina L McBurney, Vicki E Maltby, Kristoffer N Jensen, Julie Brind'Amour, LeAnn J Howe

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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 28 citations in OpenAlex.

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  5. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
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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

6 authors at 2 institutions in 2 countries.

Benjamin J E MartinDepartment of Biochemistry and Molecular Biology, University of British Columbia, Vancouver V6T 1Z3, Canada.
Kristina L McBurneyDepartment of Biochemistry and Molecular Biology, University of British Columbia, Vancouver V6T 1Z3, Canada.
Vicki E MaltbySchool of Biomedical Sciences and Pharmacy, University of Newcastle, 2308, Australia.
Kristoffer N JensenHunter Medical Research Institute, University of Newcastle, 2308, Australia.
Julie Brind'AmourHunter Medical Research Institute, University of Newcastle, 2308, Australia.
LeAnn J HoweDepartment of Biochemistry and Molecular Biology, University of British Columbia, Vancouver V6T 1Z3, Canada ljhowe@mail.ubc.ca.
University of British Columbia · CAUniversity of Newcastle Australia · AU

Funding

CIHR
6 · The paper itself

Abstract

Histone post-translational modifications (PTMs) alter chromatin structure by promoting the interaction of chromatin-modifying complexes with nucleosomes. The majority of chromatin-modifying complexes contain multiple domains that preferentially interact with modified histones, leading to speculation that these domains function in concert to target nucleosomes with distinct combinations of histone PTMs. In

Indexed as

Protein Processing, Post-TranslationalAcetylationHistone AcetyltransferasesHistonesMethylationNucleosomesProtein DomainsProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHistone AcetyltransferasesHistonesNucleosomesProtein SubunitsSaccharomyces cerevisiae Proteinshistone acetylationhistone acetyltransferasehistone methylationNuA3Saccharomyces cerevisiae

Identifiers

PMID28108585
PMCPMC5340327
OpenAlexW2575820897

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.