Evidence map›Paper›PMID 38963492›Full record

ReviewSub-cellular biochemistry2024

Mitochondrial Alpha-Keto Acid Dehydrogenase Complexes: Recent Developments on Structure and Function in Health and Disease.

Eszter Szabo, Balint Nagy, Andras Czajlik, Timea Komlodi, Oliver Ozohanics, Laszlo Tretter, Attila Ambrus

Abstract readReview
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In one paragraph

Review in Sub-cellular biochemistry, 2024. 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. Review
  2. Article
  3. The Role of Sirt3 in Kidney Health and Disease.Pharmaceuticals (Basel, Switzerland) · 2025
    Review
  4. Review
  5. Review
  6. Article
  7. Case Report: Biallelic variants inFrontiers in pediatrics · 2025
    Article
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

7 authors.

Eszter Szabo *Department of Biochemistry, Semmelweis University, Budapest, Hungary.
Balint Nagy *Department of Biochemistry, Semmelweis University, Budapest, Hungary.
Andras Czajlik *Department of Biochemistry, Semmelweis University, Budapest, Hungary.
Timea KomlodiDepartment of Biochemistry, Semmelweis University, Budapest, Hungary.
Oliver OzohanicsDepartment of Biochemistry, Semmelweis University, Budapest, Hungary.
Laszlo TretterDepartment of Biochemistry, Semmelweis University, Budapest, Hungary.
Attila AmbrusDepartment of Biochemistry, Semmelweis University, Budapest, Hungary. ambrus.attila@semmelweis.hu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The present work delves into the enigmatic world of mitochondrial alpha-keto acid dehydrogenase complexes discussing their metabolic significance, enzymatic operation, moonlighting activities, and pathological relevance with links to underlying structural features. This ubiquitous family of related but diverse multienzyme complexes is involved in carbohydrate metabolism (pyruvate dehydrogenase complex), the citric acid cycle (α-ketoglutarate dehydrogenase complex), and amino acid catabolism (branched-chain α-keto acid dehydrogenase complex, α-ketoadipate dehydrogenase complex); the complexes all function at strategic points and also participate in regulation in these metabolic pathways. These systems are among the largest multienzyme complexes with at times more than 100 protein chains and weights ranging up to ~10 million Daltons. Our chapter offers a wealth of up-to-date information on these multienzyme complexes for a comprehensive understanding of their significance in health and disease.

Indexed as

MitochondriaAnimalsCitric Acid CycleHumansKetoglutarate Dehydrogenase ComplexKetoglutarate Dehydrogenase ComplexAlpha-ketoadipate dehydrogenase complexAlpha-ketoglutarate dehydrogenase complexBranched-chain α-keto acid dehydrogenase complexMetabolic diseaseMitochondrionPathogenic mutationPyruvate dehydrogenase complexROSα-keto acid dehydrogenase complexes

Identifiers

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.