Evidence map›Paper›PMID 29610278›Full record

ArticleThe Journal of biological chemistry2018

The unassembled flavoprotein subunits of human and bacterial complex II have impaired catalytic activity and generate only minor amounts of ROS.

Elena Maklashina, Sany Rajagukguk, T M Iverson, Gary Cecchini

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Alteration of Flavin Cofactor Homeostasis in Human Neuromuscular Pathologies.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  10. Mitochondrial complex II and reactive oxygen species in disease and therapy.Redox report : communications in free radical research · 2020
    Review
  11. The roles of SDHAF2 and dicarboxylate in covalent flavinylation of SDHA, the human complex II flavoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Review
  13. Article
  14. Maturation of the respiratory complex II flavoprotein.Current opinion in structural biology · 2019
    Review
  15. The assembly of succinate dehydrogenase: a key enzyme in bioenergetics.Cellular and molecular life sciences : CMLS · 2019
    Review
  16. 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

4 authors at 2 institutions in 1 country.

Elena MaklashinaFrom the Molecular Biology Division, San Francisco Veterans Affairs Health Care System, San Francisco, California 94121.
Sany RajagukgukFrom the Molecular Biology Division, San Francisco Veterans Affairs Health Care System, San Francisco, California 94121.
T M Iversonthe Departments of Pharmacology and.
Gary CecchiniFrom the Molecular Biology Division, San Francisco Veterans Affairs Health Care System, San Francisco, California 94121, Gary.Cecchini@ucsf.edu.ORCID 0000-0002-0571-1747
San Francisco VA Medical Center · USVanderbilt University · US

Funding

Structure/Function of Complex ll OxidoreductasesR01GM061606 · NIGMS · NORTHERN CALIFORNIA INSTITUTE RES &EDUC · PI CECCHINI, GARY, IVERSON, T M · 2001 to 2022
$9.1M
THE ROLE OF ACETYLATION IN MITOCHONDRIAL FUNCTIONI01BX001077 · VA · VETERANS AFFAIRS MED CTR SAN FRANCISCO · PI CECCHINI, GARY · 2011 to 2014
–
BLRD VA I01 BX001077BLRD VA IK6 BX004215NIGMS NIH HHS R01 GM061606
6 · The paper itself

Abstract

Complex II (SdhABCD) is a membrane-bound component of mitochondrial and bacterial electron transport chains, as well as of the TCA cycle. In this capacity, it catalyzes the reversible oxidation of succinate. SdhABCD contains the SDHA protein harboring a covalently bound FAD redox center and the iron-sulfur protein SDHB, containing three distinct iron-sulfur centers. When assembly of this complex is compromised, the flavoprotein SDHA may accumulate in the mitochondrial matrix or bacterial cytoplasm. Whether the unassembled SDHA has any catalytic activity, for example in succinate oxidation, fumarate reduction, reactive oxygen species (ROS) generation, or other off-pathway reactions, is not known. Therefore, here we investigated whether unassembled

Indexed as

Bacterial ProteinsCatalysisCrystallography, X-RayElectron Transport Complex IIEscherichia coliFlavoproteinsHumansModels, MolecularOxidation-ReductionProtein ConformationProtein SubunitsReactive Oxygen SpeciesBacterial ProteinsElectron Transport Complex IIFlavoproteinsProtein SubunitsReactive Oxygen SpeciesSdhA protein, BacteriaSDHA protein, humanelectron transfer complexflavoproteinmitochondrial respiratory chain complexprotein assemblyprotein domainprotein evolutionstructure-function

Identifiers

PMID29610278
PMCPMC5961047
OpenAlexW2796360169

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.