Evidence map›Paper›PMID 30903449›Full record

ReviewNeurochemical research2019

Succinylation Links Metabolism to Protein Functions.

Yun Yang, Gary E Gibson

Open access · greenAbstract readReview
In one paragraph

Review in Neurochemical research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers.

0numbers the graph read from it
0cells of the map it votes in
136citing papers in PubMed
8.8field-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

136 citing papers in PubMed, 224 citations in OpenAlex.

  1. Article
  2. Review
  3. Stage-Specific H3K14 and H3K23 Succinylation Orchestrates Insect Metamorphosis and Oogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Review
  5. Article
  6. Mechanisms Involved in Pathological Succinate-Mediated Signaling.International journal of molecular sciences · 2026
    Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Multi-omics reveals that genes linked to succinylation regulate the onset of epilepsy through metabolic reprogramming.Mammalian genome : official journal of the International Mammalian Genome Society · 2025
    Article

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

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

2 authors at 2 institutions in 2 countries.

Yun YangIntegrated Medicine Research Center for Neurological Rehabilitation, College of Medicine, Jiaxing University, Jiaxing, 314001, China.
Gary E GibsonBrain and Mind Research Institute, Weill Cornell Medicine, Burke Neurological Institute, 785 Mamaroneck Avenue, White Plains, NY, 10605, USA. ggibson@med.cornell.edu.ORCID http://orcid.org/0000-0003-2549-2876
Cornell University · USJiaxing University · CN

Funding

TRANSCRIPTIONAL RESPONSES TO MITOCHONDRIAL DYSFUNCTIONP01AG014930 · NIA · WINIFRED MASTERSON BURKE MED RES INST · PI GIBSON, GARY E · 1999 to 2020
$30.7M
NIA NIH HHS AG014930NIA NIH HHS P01 AG014930
6 · The paper itself

Abstract

Post-translational modifications (PTMs) are important regulators of protein function, and integrate metabolism with physiological and pathological processes. Phosphorylation and acetylation are particularly well studied PTMs. A relatively recently discovered novel PTM is succinylation in which metabolically derived succinyl CoA modifies protein lysine groups. Succinylation causes a protein charge flip from positive to negative and a relatively large increase in mass compared to other PTMs. Hundreds of protein succinylation sites are present in proteins of multiple tissues and species, and the significance is being actively investigated. The few completed studies demonstrate that succinylation alters rates of enzymes and pathways, especially mitochondrial metabolic pathways. Thus, succinylation provides an elegant and efficient mechanism to coordinate metabolism and signaling by utilizing metabolic intermediates as sensors to regulate metabolism. Even though the brain is one of the most metabolically active organs, an understanding of the role succinylation in the nervous system is largely unknown. Data from other tissues and other PTMs suggest that succinylation provides a coupling between metabolism and protein function in the nervous system and in neurological diseases. This review provides a new insight into metabolism in neurological diseases and suggests that the drug development for these diseases requires a better understanding of succinylation and de-succinylation in the brain and other tissues.

Indexed as

Acyl Coenzyme AAnimalsHumansLysineMetabolic Networks and PathwaysMitochondriaProtein Processing, Post-TranslationalProteomeAcyl Coenzyme ALysineProteomesuccinyl-coenzyme AMetabolismMitochondriaSirtuinsSuccinlyation

Identifiers

PMID30903449
PMCPMC6755074
OpenAlexW2941046634

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.