Evidence map›Paper›PMID 23723239›Full record

ArticleScience (New York, N.Y.)2013

A conserved mechanism for centromeric nucleosome recognition by centromere protein CENP-C.

Hidenori Kato, Jiansheng Jiang, Bing-Rui Zhou, Marieke Rozendaal, Hanqiao Feng, Rodolfo Ghirlando, T Sam Xiao, Aaron F Straight, Yawen Bai

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 227 papers.

0numbers the graph read from it
0cells of the map it votes in
227citing papers in PubMed
15.0field-weighted citation impact, top 1% 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

227 citing papers in PubMed, 345 citations in OpenAlex.

  1. Structure and function of the centromere and inner kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
  3. Article
  4. Dual Roads of CENP-A for Centromere Identification.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  5. Article
  6. A Chromatin Biology Assessment of AlphaFold3.bioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Structure and dynamics of 2x(CENP-A/H4)Life science alliance · 2026
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

167 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 1 country.

Hidenori KatoLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, Bethesda, MD 20892, USA.
Jiansheng Jiang
Bing-Rui Zhou
Marieke Rozendaal
Hanqiao Feng
Rodolfo Ghirlando
T Sam Xiao
Aaron F Straight
Yawen Bai
National Cancer Institute · USNational Institute of Allergy and Infectious Diseases · USStanford University · USNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Nucleosome DynamicsZIABC010808 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BAI, YAWEN · 2009 to 2025
$26.5M
Mechanisms of Kinetochore AssemblyR01GM074728 · NIGMS · STANFORD UNIVERSITY · PI Aaron F Straight · 2005 to 2026
$6.6M
Structural Studies of Pattern Recognition ReceptorsZIAAI000960 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI XIAO, TSAN · 2009 to 2014
$6.1M
Biophysics of Macromolecular ComplexesZIADK033007 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2024
$4.9M
Intramural NIH HHS ZIA AI000960NCI NIH HHS Y1-CO-1020NIGMS NIH HHS R01 GM074728NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

Chromosome segregation during mitosis requires assembly of the kinetochore complex at the centromere. Kinetochore assembly depends on specific recognition of the histone variant CENP-A in the centromeric nucleosome by centromere protein C (CENP-C). We have defined the determinants of this recognition mechanism and discovered that CENP-C binds a hydrophobic region in the CENP-A tail and docks onto the acidic patch of histone H2A and H2B. We further found that the more broadly conserved CENP-C motif uses the same mechanism for CENP-A nucleosome recognition. Our findings reveal a conserved mechanism for protein recruitment to centromeres and a histone recognition mode whereby a disordered peptide binds the histone tail through hydrophobic interactions facilitated by nucleosome docking.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsAutoantigensBinding SitesCentromereCentromere Protein AChromosomal Proteins, Non-HistoneConserved SequenceDrosophilaHistonesHumansHydrophobic and Hydrophilic InteractionsMolecular Sequence DataNucleosomesProtein Structure, SecondaryAutoantigensCENPA protein, humanCentromere Protein Acentromere protein CChromosomal Proteins, Non-HistoneHistonesNucleosomes

Identifiers

PMID23723239
PMCPMC3763809
OpenAlexW2145579024

What OpenQuestion holds

Textmetadata
LicenceTDM
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.