Evidence map›Paper›PMID 22904323›Full record

ReviewThe Journal of biological chemistry2012

Structural basis for malfunction in complex II.

Tina M Iverson, Elena Maklashina, Gary Cecchini

Abstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Review
  2. Review
  3. A Novel Human SDHA-Knockout Cell Line Model for the Functional Analysis of Clinically Relevant SDHA Variants.Clinical cancer research : an official journal of the American Association for Cancer Research · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Functions of ROS in Macrophages and Antimicrobial Immunity.Antioxidants (Basel, Switzerland) · 2021
    Review
  10. Mitochondrial complex II and reactive oxygen species in disease and therapy.Redox report : communications in free radical research · 2020
    Review
  11. Article
  12. 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
  13. Maturation of the respiratory complex II flavoprotein.Current opinion in structural biology · 2019
    Review
  14. The assembly of succinate dehydrogenase: a key enzyme in bioenergetics.Cellular and molecular life sciences : CMLS · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

3 authors.

Tina M IversonDepartment of Pharmacology and Biochemistry, Vanderbilt University Medical Center, Nashville, Tennessee 37232. Electronic address: tina.iverson@vanderbilt.edu.
Elena MaklashinaMolecular Biology Division, Veterans Affairs Medical Center, San Francisco, California 94121; Department of Biochemistry and Biophysics, University of California, San Francisco, California 94158.
Gary CecchiniMolecular Biology Division, Veterans Affairs Medical Center, San Francisco, California 94121; Department of Biochemistry and Biophysics, University of California, San Francisco, California 94158. Electronic address: gary.cecchini@ucsf.edu.

Funding

Structure/Function of Complex ll OxidoreductasesR01GM061606 · NIGMS · NORTHERN CALIFORNIA INSTITUTE RES &EDUC · PI CECCHINI, GARY, IVERSON, T M · 2001 to 2022
$9.1M
Complexities of complex II: A versatile architecture for respirationR01GM079419 · NIGMS · VANDERBILT UNIVERSITY · PI IVERSON, T M · 2007 to 2011
$1.3M
THE ROLE OF ACETYLATION IN MITOCHONDRIAL FUNCTIONI01BX001077 · VA · VETERANS AFFAIRS MED CTR SAN FRANCISCO · PI CECCHINI, GARY · 2011 to 2014
–
BLRD VA I01 BX001077NIGMS NIH HHS GM61606NIGMS NIH HHS GM79419NIGMS NIH HHS R01 GM061606NIGMS NIH HHS R01 GM079419
6 · The paper itself

Abstract

Complex II couples oxidoreduction of succinate and fumarate at one active site with that of quinol/quinone at a second distinct active site over 40 Å away. This process links the Krebs cycle to oxidative phosphorylation and ATP synthesis. The pathogenic mutation or inhibition of human complex II or its assembly factors is often associated with neurodegeneration or tumor formation in tissues derived from the neural crest. This brief overview of complex II correlates the clinical presentations of a large number of symptom-associated alterations in human complex II activity and assembly with the biochemical manifestations of similar alterations in the complex II homologs from Escherichia coli. These analyses provide clues to the molecular basis for diseases associated with aberrant complex II function.

Indexed as

Adenosine TriphosphateAnimalsCitric Acid CycleElectron Transport Complex IIEscherichia coliEscherichia coli ProteinsHumansPhosphorylationStructure-Activity RelationshipAdenosine TriphosphateElectron Transport Complex IIEscherichia coli Proteins

Identifiers

PMID22904323
PMCPMC3471735

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.