Evidence map›Paper›PMID 28862252›Full record

ArticleCell research2017

Genome-wide identification of histone H2A and histone variant H2A.Z-interacting proteins by bPPI-seq.

Yi Zhang, Wai Lim Ku, Shuai Liu, Kairong Cui, Wenfei Jin, Qingsong Tang, William Lu, Bing Ni, Keji Zhao

Open access · bronzeAbstract read
In one paragraph

Article in Cell research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Genome-Wide Identification ofMarine drugs · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Epigenetic regulation of renal development.Seminars in cell & developmental biology · 2019
    Review
  11. The histone variant H2A.Z in gene regulation.Epigenetics & chromatin · 2019
    Review
  12. Article
  13. Catching global interactions in vivo.Cell & bioscience · 2017
    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

9 authors at 2 institutions in 2 countries.

Yi ZhangInstitute of Immunology PLA, Third Military Medical University, Chongqing 400038, China.
Wai Lim KuSystems Biology Center, Division of Intramural Research, NHLBI, NIH, Bethesda, MD 20892, USA.
Shuai LiuSystems Biology Center, Division of Intramural Research, NHLBI, NIH, Bethesda, MD 20892, USA.
Kairong CuiSystems Biology Center, Division of Intramural Research, NHLBI, NIH, Bethesda, MD 20892, USA.
Wenfei JinSystems Biology Center, Division of Intramural Research, NHLBI, NIH, Bethesda, MD 20892, USA.
Qingsong TangSystems Biology Center, Division of Intramural Research, NHLBI, NIH, Bethesda, MD 20892, USA.
William LuSystems Biology Center, Division of Intramural Research, NHLBI, NIH, Bethesda, MD 20892, USA.
Bing NiInstitute of Immunology PLA, Third Military Medical University, Chongqing 400038, China.
Keji ZhaoSystems Biology Center, Division of Intramural Research, NHLBI, NIH, Bethesda, MD 20892, USA.
Center for Systems Biology · USArmy Medical University · CN

Funding

Genome-wide mapping of histone modificationsZIAHL005801 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ZHAO, KEJI · 2009 to 2025
$24.0M
Epigenetic Regulation of Hematopoietic Stem CellsZIAHL006031 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ZHAO, KEJI · 2009 to 2025
$16.6M
6 · The paper itself

Abstract

H2A is a nucleosome core subunit involved in organizing DNA into a chromatin structure that is often inaccessible to regulatory enzymes. Replacement of H2A by its variant H2A.Z renders chromatin accessible at enhancers and promoters. However, it remains unclear how H2A.Z functions so differently from canonical H2A. Here we report the genome-wide identification of proteins that directly interact with H2A and H2A.Z in vivo using a novel strategy, bPPI-seq. We show that bPPI-seq is a sensitive and robust technique to identify protein-protein interactions in vivo. Our data indicate that H2A.Z-interacting proteins and H2A-interacting proteins participate in distinct biological processes. In contrast to H2A-interacting proteins, the H2A.Z-interacting proteins are involved in transcriptional regulation. We found that the transcription factor Osr1 interacts with H2A.Z both in vitro and in vivo. It also mediates H2A.Z incorporation to a large number of target sites and regulates gene expression. Our data indicate that bPPI-seq can be widely applied to identify genome-wide interacting proteins under physiological conditions.

Indexed as

AnimalsChromatinGene Expression RegulationGenomeHistonesHumansMiceNIH 3T3 CellsNucleosomesPromoter Regions, GeneticProtein Interaction MapsTranscription FactorsChromatinhistone H2A.F-ZHistonesNucleosomesOsr1 protein, mouseTranscription Factors

Identifiers

PMID28862252
PMCPMC5630678
OpenAlexW2752522035

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.