Evidence map›Paper›PMID 29463709›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Identification of the YEATS domain of GAS41 as a pH-dependent reader of histone succinylation.

Yi Wang, Jing Jin, Matthew Wai Heng Chung, Ling Feng, Hongyan Sun, Quan Hao

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

51 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. [Role of succinylation modification in central nervous system diseases].Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2025
    Review
  5. Article
  6. [Prediction of protein Kbhb sites based on learnable feature embedding].Sheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi · 2025
    Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Review
  16. Review
  17. Impact of Lysine Succinylation on the Biology of Fungi.Current issues in molecular biology · 2024
    Review
  18. Small-molecule tools for YEATS domain proteins.Current opinion in chemical biology · 2023
    Review
  19. Review
  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

6 authors at 3 institutions in 2 countries.

Yi WangSchool of Biomedical Sciences, University of Hong Kong, Hong Kong, China.
Jing JinSchool of Biomedical Sciences, University of Hong Kong, Hong Kong, China.
Matthew Wai Heng ChungSchool of Biomedical Sciences, University of Hong Kong, Hong Kong, China.
Ling FengDepartment of Chemistry, City University of Hong Kong, Hong Kong, China.
Hongyan SunDepartment of Chemistry, City University of Hong Kong, Hong Kong, China.
Quan HaoSchool of Biomedical Sciences, University of Hong Kong, Hong Kong, China; qhao@hku.hk.
University of Hong Kong · HKCity University of Hong Kong · HKCity University of Hong Kong, Shenzhen Research Institute · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine succinylation is a newly discovered posttranslational modification with distinctive physical properties. However, to date rarely have studies reported effectors capable of interpreting this modification on histones. Following our previous study of SIRT5 as an eraser of succinyl-lysine (Ksuc), here we identified the GAS41 YEATS domain as a reader of Ksuc on histones. Biochemical studies showed that the GAS41 YEATS domain presents significant binding affinity toward H3K122suc upon a protonated histidine residue. Furthermore, cellular studies showed that GAS41 had prominent interaction with H3K122suc on histones and also demonstrated the coenrichment of GAS41 and H3K122suc on the

Indexed as

HistonesProtein Processing, Post-TranslationalSuccinic AcidTranscription FactorsCrystallographyHeLa CellsHistidineHistone AcetyltransferasesHumansLysineModels, MolecularProtein DomainsSaccharomyces cerevisiae ProteinsHistidineHistone AcetyltransferasesHistonesLysineSaccharomyces cerevisiae ProteinsSuccinic AcidTranscription FactorsYAF9 protein, S cerevisiaeYEATS4 protein, humanGAS41readersuccinyl-lysine

Identifiers

PMID29463709
PMCPMC5877980
OpenAlexW2788462335

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.