Evidence map›Paper›PMID 38882606›Full record

ReviewFrontiers in molecular biosciences2024

Dysregulation of protein succinylation and disease development.

Xiaoli Hou, Lijuan Zhu, Haiying Xu, Jie Shi, Shaoping Ji

Abstract readReview
In one paragraph

Review in Frontiers in molecular biosciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Biochemistry and regulation of histone lysine L-lactylation.Nature reviews. Molecular cell biology · 2026
    Review
  7. Review
  8. Review
  9. 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

5 authors.

Xiaoli HouCenter for Molecular Medicine, Zhengzhou Shuqing Medical College, Zhengzhou, Henan, China.
Lijuan ZhuZhengzhou Central Hospital Affiliated to Zhengzhou University, Zhengzhou, Henan, China.
Haiying XuCenter for Molecular Medicine, Zhengzhou Shuqing Medical College, Zhengzhou, Henan, China.
Jie ShiZhoukou Vocational and Technical College, Zhoukou, Henan, China.
Shaoping JiCenter for Molecular Medicine, Zhengzhou Shuqing Medical College, Zhengzhou, Henan, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As a novel post-translational modification of proteins, succinylation is widely present in both prokaryotes and eukaryotes. By regulating protein translocation and activity, particularly involved in regulation of gene expression, succinylation actively participates in diverse biological processes such as cell proliferation, differentiation and metabolism. Dysregulation of succinylation is closely related to many diseases. Consequently, it has increasingly attracted attention from basic and clinical researchers. For a thorough understanding of succinylation dysregulation and its implications for disease development, such as inflammation, tumors, cardiovascular and neurological diseases, this paper provides a comprehensive review of the research progress on abnormal succinylation. This understanding of association of dysregulation of succinylation with pathological processes will provide valuable directions for disease prevention/treatment strategies as well as drug development.

Indexed as

diseasedysregulationpost-translational modificationsuccinylasesuccinylation

Identifiers

PMID38882606
PMCPMC11176430

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.