Evidence map›Paper›PMID 31236625›Full record

ReviewCellular and molecular life sciences : CMLS2019

The assembly of succinate dehydrogenase: a key enzyme in bioenergetics.

Behrooz Moosavi, Edward A Berry, Xiao-Lei Zhu, Wen-Chao Yang, Guang-Fu Yang

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing 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

64 citing papers in PubMed.

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  7. Energy metabolism and adenylate system in Mytilus galloprovincialis (Lamarck, 1819) tissues under acute hypoxia.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2026
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4 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

5 authors.

Behrooz MoosaviKey Laboratory of Pesticide and Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University, Wuhan, 430079, People's Republic of China.
Edward A BerryDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY, 13210, USA.
Xiao-Lei ZhuKey Laboratory of Pesticide and Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University, Wuhan, 430079, People's Republic of China.
Wen-Chao YangKey Laboratory of Pesticide and Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University, Wuhan, 430079, People's Republic of China.
Guang-Fu YangKey Laboratory of Pesticide and Chemical Biology, Ministry of Education, College of Chemistry, Central China Normal University, Wuhan, 430079, People's Republic of China. gfyang@mail.ccnu.edu.cn.

Funding

National Key Research and Development Program of China 2017YFA0505200National Natural Science Foundation of China (CN) 21837001
6 · The paper itself

Abstract

Succinate dehydrogenase (SDH) also known as complex II or succinate:quinone oxidoreductase is an enzyme involved in both oxidative phosphorylation and tricarboxylic acid cycle; the processes that generate energy. SDH is a multi-subunit enzyme which requires a series of proteins for its proper assembly at several steps. This enzyme has medical significance as there is a broad range of human diseases from cancers to neurodegeneration related to SDH malfunction. Some of these disorders have recently been linked to defective assembly factors, reinvigorating further research in this area. Apart from that this enzyme has agricultural importance as many fungicides have been/will be designed targeting specifically this enzyme in plant fungal pathogens. In addition, we speculate it might be possible to design novel fungicides specifically targeting fungal assembly factors. Considering the medical and agricultural implications of SDH, the aim of this review is an overview of the SDH assembly factors and critical analysis of controversial issues around them.

Indexed as

AnimalsCitric Acid CycleCoenzymesFlavin-Adenine DinucleotideFungal ProteinsFungiFungicides, IndustrialGene ExpressionHumansMembrane Transport ProteinsMitochondriaMolecular ChaperonesNeoplasmsNeurodegenerative DiseasesOxidative PhosphorylationPlantsCoenzymesFlavin-Adenine DinucleotideFLX1 protein, S cerevisiaeFungal ProteinsFungicides, IndustrialMembrane Transport ProteinsMolecular ChaperonesProtein IsoformsProteinsProtein SubunitsSaccharomyces cerevisiae ProteinsSDHAF1 protein, humanSuccinate DehydrogenaseComplex IIFumarate reductaseMitochondriaOxidative phosphorylationSuccinate:quinone oxidoreductasesTricarboxylic acid cycle

Identifiers

PMID31236625
PMCPMC11105593

What OpenQuestion holds

Textmetadata
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.