Evidence map›Paper›PMID 34199982›Full record

ReviewInternational journal of molecular sciences2021

The Mystery of Extramitochondrial Proteins Lysine Succinylation.

Christos Chinopoulos

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

30 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
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  7. Post-translational modifications regulating microglial inflammation in central nervous system disorders: a review.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2025
    Review
  8. Review
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  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. Impact of Lysine Succinylation on the Biology of Fungi.Current issues in molecular biology · 2024
    Review
  20. Dysregulation of protein succinylation and disease development.Frontiers in molecular biosciences · 2024
    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

1 author at 1 institution in 1 country.

Christos ChinopoulosDepartment of Biochemistry and Molecular Biology, Semmelweis University, 1094 Budapest, Hungary.ORCID 0000-0003-0183-4149
Semmelweis University · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine succinylation is a post-translational modification which alters protein function in both physiological and pathological processes. Mindful that it requires succinyl-CoA, a metabolite formed within the mitochondrial matrix that cannot permeate the inner mitochondrial membrane, the question arises as to how there can be succinylation of proteins outside mitochondria. The present mini-review examines pathways participating in peroxisomal fatty acid oxidation that lead to succinyl-CoA production, potentially supporting succinylation of extramitochondrial proteins. Furthermore, the influence of the mitochondrial status on cytosolic NAD

Indexed as

Protein Processing, Post-TranslationalHumansKetoglutarate Dehydrogenase ComplexLysineNeurogliaProteinsSirtuinsSuccinate DehydrogenaseKetoglutarate Dehydrogenase ComplexLysineProteinsSIRT5 protein, humanSirtuinsSuccinate Dehydrogenasefatty acid oxidationketoglutarate dehydrogenase complexlysineperoxisomespost-translational modificationsuccinyl-CoA

Identifiers

PMID34199982
PMCPMC8200203
OpenAlexW3167846570

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.