Evidence map›Paper›PMID 30057113›Full record

ArticleCell2018

Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109.

Lin Zhang, Albert Serra-Cardona, Hui Zhou, Mingzhu Wang, Na Yang, Zhiguo Zhang, Rui-Ming Xu

Abstract read
In one paragraph

Article in Cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. DiTSim: A Diffusion-Transformers Based Single-Cell ATAC-seq Data Simulator.Interdisciplinary sciences, computational life sciences · 2026
    Article
  2. Review
  3. Article
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  8. Article
  9. Mechanisms of chromatin-based epigenetic inheritance.Science China. Life sciences · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
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  20. Review
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.

Lin ZhangNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101 Beijing, China; University of Chinese Academy of Sciences, 100049 Beijing, China.
Albert Serra-CardonaInstitute for Cancer Genetics, Departments of Pediatrics and Genetics and Development and Irving Cancer Research Center, Vagelos College of Physicians and Surgeons, Columbia University, New York, NY 10032, USA.
Hui ZhouInstitute for Cancer Genetics, Departments of Pediatrics and Genetics and Development and Irving Cancer Research Center, Vagelos College of Physicians and Surgeons, Columbia University, New York, NY 10032, USA.
Mingzhu WangNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101 Beijing, China.
Na YangState Key Laboratory of Medicinal Chemical Biology, College of Pharmacy and Tianjin Key Laboratory of Molecular Drug Research, Nankai University, 300353 Tianjin, China.
Zhiguo ZhangInstitute for Cancer Genetics, Departments of Pediatrics and Genetics and Development and Irving Cancer Research Center, Vagelos College of Physicians and Surgeons, Columbia University, New York, NY 10032, USA. Electronic address: zz2401@cumc.columbia.edu.
Rui-Ming XuNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101 Beijing, China; University of Chinese Academy of Sciences, 100049 Beijing, China. Electronic address: rmxu@ibp.ac.cn.

Funding

Mechanisms of Epigenetic inheritanceR35GM118015 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Zhiguo Zhang · 2016 to 2026
$9.5M
NIGMS NIH HHS R35 GM118015
6 · The paper itself

Abstract

Rtt109 is a unique histone acetyltransferase acetylating histone H3 lysine 56 (H3K56), a modification critical for DNA replication-coupled nucleosome assembly and genome stability. In cells, histone chaperone Asf1 is essential for H3K56 acetylation, yet the mechanisms for H3K56 specificity and Asf1 requirement remain unknown. We have determined the crystal structure of the Rtt109-Asf1-H3-H4 complex and found that unwinding of histone H3 α

Indexed as

AcetylationAmino Acid SequenceAspergillus fumigatusHistone AcetyltransferasesHistonesLysineMolecular ChaperonesProtein ConformationSaccharomyces cerevisiaeSequence HomologySubstrate SpecificityHistone AcetyltransferasesHistonesLysineMolecular Chaperonesacetylationcrystal structureDNA damageDNA replicationhistonehistone chaperonenucleosome assembly

Identifiers

PMID30057113
PMCPMC6103222

What OpenQuestion holds

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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.