Evidence map›Paper›PMID 39462860›Full record

ReviewChembiochem : a European journal of chemical biology2025

Cracking Lysine Crotonylation (Kcr): Enlightening a Promising Post-Translational Modification.

Marinda Westerveld, Kosta Besermenji, David Aidukas, Nikita Ostrovitsa, Rita Petracca

Abstract readReview
In one paragraph

Review in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
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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

5 authors.

Marinda WesterveldDepartment of Pharmaceutical Sciences, Faculty of Science, Utrecht University, David De Wied Building, Universiteitsweg 99, 3584 CG, Utrecht, NL.
Kosta BesermenjiDepartment of Pharmaceutical Sciences, Faculty of Science, Utrecht University, David De Wied Building, Universiteitsweg 99, 3584 CG, Utrecht, NL.
David AidukasDepartment of Pharmaceutical Sciences, Faculty of Science, Utrecht University, David De Wied Building, Universiteitsweg 99, 3584 CG, Utrecht, NL.
Nikita OstrovitsaTrinity Biomedical Sciences Institute (TBSI), Trinity College Dublin (TCD), 152-160 Pearse St., Dublin, D02 R590, Ireland.
Rita PetraccaDepartment of Pharmaceutical Sciences, Faculty of Science, Utrecht University, David De Wied Building, Universiteitsweg 99, 3584 CG, Utrecht, NL.ORCID https://orcid.org/0000-0003-3671-1122

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine crotonylation (Kcr) is a recently discovered post-translational modification (PTM). Both histone and non-histone Kcr-proteins have been associated with numerous diseases including cancer, acute kidney injury, HIV latency, and cardiovascular disease. Histone Kcr enhances gene expression to a larger extend than the extensively studied lysine acetylation (Kac), suggesting Kcr as a novel potential therapeutic target. Although numerous scientific reports on crotonylation were published in the last years, relevant knowledge gaps concerning this PTM and its regulation still remain. To date, only few selective Kcr-interacting proteins have been identified and selective methods for the enrichment of Kcr-proteins in chemical proteomics analysis are still lacking. The development of new techniques to study this underexplored PTM could then clarify its function in health and disease and hopefully accelerate the development of new therapeutics for Kcr-related disease. Herein we briefly review what is known about the regulation mechanisms of Kcr and the current methods used to identify Kcr-proteins and their interacting partners. This report aims to highlight the significant potential of Kcr as a therapeutic target and to identify the existing scientific gaps that new research must address.

Indexed as

HistonesLysineProtein Processing, Post-TranslationalAcetylationAnimalsHumansHistonesLysineChemical proteomicsCrotonyl-CoAEnzymatic PTMs regulationPost-translational modifications (PTMs)

Identifiers

PMID39462860
PMCPMC11776371

What Socratic holds

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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 Socratic graph.