Evidence map›Paper›PMID 22514736›Full record

ArticlePloS one2012

Structural basis of the chromodomain of Cbx3 bound to methylated peptides from histone h1 and G9a.

Jianbin Ruan, Hui Ouyang, Maria F Amaya, Mani Ravichandran, Peter Loppnau, Jinrong Min, Jianye Zang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. The missing linkGenes & development · 2021
    Review
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  6. Article
  7. Article
  8. Article
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  10. Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8.Acta crystallographica. Section D, Biological crystallography · 2015
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. 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

7 authors at 4 institutions in 2 countries.

Jianbin RuanHefei National Laboratory for Physical Sciences, Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, People's Republic of China.
Hui Ouyang
Maria F Amaya
Mani Ravichandran
Peter Loppnau
Jinrong Min
Jianye Zang
University of Toronto · CAStructural Genomics Consortium · CAChinese Academy of Sciences · CNUniversity of Science and Technology of China · CN

Funding

Wellcome Trust
6 · The paper itself

Abstract

backgroundHP1 proteins are highly conserved heterochromatin proteins, which have been identified to be structural adapters assembling a variety of macromolecular complexes involved in regulation of gene expression, chromatin remodeling and heterochromatin formation. Much evidence shows that HP1 proteins interact with numerous proteins including methylated histones, histone methyltransferases and so on. Cbx3 is one of the paralogues of HP1 proteins, which has been reported to specifically recognize trimethylated histone H3K9 mark, and a consensus binding motif has been defined for the Cbx3 chromodomain. METHODOLOGY/PRINCIPAL

findingsHere, we found that the Cbx3 chromodomain can bind to H1K26me2 and G9aK185me3 with comparable binding affinities compared to H3K9me3. We also determined the crystal structures of the human Cbx3 chromodomain in complex with dimethylated histone H1K26 and trimethylated G9aK185 peptides, respectively. The complex structures unveil that the Cbx3 chromodomain specifically bind methylated histone H1K26 and G9aK185 through a conserved mechanism. CONCLUSIONS/SIGNIFICANCE: The Cbx3 chromodomain binds with comparable affinities to all of the methylated H3K9, H1K26 and G9aK185 peptides. It is suggested that Cbx3 may regulate gene expression via recognizing both histones and non-histone proteins.

Indexed as

CalorimetryChromosomal Proteins, Non-HistoneHistonesHumansMethylationPeptidesX-Ray DiffractionCBX3 protein, humanChromosomal Proteins, Non-HistoneHistonesPeptides

Identifiers

PMID22514736
PMCPMC3325965
OpenAlexW2060237924

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.