Evidence map›Paper›PMID 29932303›Full record

ArticleProteomics2018

Quantitative Crotonylome Analysis Expands the Roles of p300 in the Regulation of Lysine Crotonylation Pathway.

He Huang, Dan-Li Wang, Yingming Zhao

Abstract read
In one paragraph

Article in Proteomics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed, 1 pooled it
3.2field-weighted citation impact, top 7% 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

53 citing papers in PubMed, 1 synthesis or guideline pooled it, 82 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
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  5. Review
  6. Article
  7. Risk Stratification and Prognosis Determination Based on Protein Lysine Crotonylation in Patients with Resected Pancreatic Cancer: A Multicenter Study.Clinical cancer research : an official journal of the American Association for Cancer Research · 2025
    Article
  8. Review
  9. Article
  10. Review
  11. Histone crotonylation in tumors (Review).Molecular and clinical oncology · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. Article
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  18. Review
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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

3 authors at 2 institutions in 2 countries.

He HuangBen May Department for Cancer Research, The University of Chicago, 60637 Chicago, IL, USA.
Dan-Li WangSchool of Marine Sciences, Ningbo University, 315211 Ningbo, China.
Yingming ZhaoBen May Department for Cancer Research, The University of Chicago, 60637 Chicago, IL, USA.
University of Chicago · USNingbo University · CN

Funding

SIRT6 and lysine fatty acylation in macrophage inflammationR01DK107868 · NIDDK · CORNELL UNIVERSITY · PI LIN, HENING, ZHAO, YINGMING · 2016 to 2019
$2.0M
Systems-wide analysis of histone lysine 2-hydroxyisobutyrylation pathwayR01GM115961 · NIGMS · UNIVERSITY OF CHICAGO · PI ZHAO, YINGMING · 2016 to 2019
$1.8M
NIDDK NIH HHS R01 DK107868NIGMS NIH HHS R01 GM115961
6 · The paper itself

Abstract

Lysine crotonylation (Kcr) is a recently identified post-translational modification (PTM) that is regulated by an acetyltransferase, p300. The p300-catalyzed histone Kcr is able to stimulate transcription to a greater degree than the well-studied histone lysine acetylation (Kac). Despite these progresses, the global Kcr substrates regulated by p300 remain largely unknown, hindering efforts to establish mechanistic links between Kcr and p300-mediated phenotypes. Here, a quantitative proteomics study to characterize the p300-regulated lysine crotonylome is reported. A total of 816 unique endogenous crotonylation sites are identified across 392 proteins, with 88 sites from 69 proteins being decreased by more than 0.7-fold (log2 < 0.5) and 31 sites from 17 proteins being increased by more than 1.4-fold (log2 > 0.5) in response to p300 knockout (KO). The most downregulated crotonylome alterations under p300 deficiency concern components of the nonsense-mediated decay, infectious disease, and viral/eukaryotic translation pathways. Moreover, some p300-targeted Kcr substrates are potentially linked to diseases such as cancer. Taken together, this study reveals the lysine crotonylome in response to p300, which sheds light on the role for lysine crotonylation in regulation of diverse cellular processes and provides new insights into mechanisms of p300 functions.

Indexed as

Protein Processing, Post-TranslationalAcyl Coenzyme AE1A-Associated p300 ProteinHistonesHumansLysineMass SpectrometryProtein Interaction MapsProteomeAcyl Coenzyme Acrotonyl-coenzyme AE1A-Associated p300 ProteinEP300 protein, humanHistonesLysineProteomeacetyltransferaselysine crotonylationp300post-translational modificationquantitative proteomics

Identifiers

PMID29932303
PMCPMC6420807
OpenAlexW2809468490

What OpenQuestion holds

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Registered trials

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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.