Evidence map›Paper›PMID 33996767›Full record

ReviewFrontiers in chemistry2021

Ubiquinone Binding and Reduction by Complex I-Open Questions and Mechanistic Implications.

Etienne Galemou Yoga, Jonathan Schiller, Volker Zickermann

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Understanding coenzyme Q.Physiological reviews · 2024
    Review
  7. Article
  8. Article
  9. Highly Accessible Computational Prediction andOxidative medicine and cellular longevity · 2023
    Article
  10. Article
  11. Binding of Natural Inhibitors to Respiratory Complex I.Pharmaceuticals (Basel, Switzerland) · 2022
    Review
  12. Article
  13. 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

3 authors at 1 institution in 1 country.

Etienne Galemou YogaInstitute of Biochemistry II, University Hospital, Goethe University, Frankfurt, Germany.
Jonathan SchillerInstitute of Biochemistry II, University Hospital, Goethe University, Frankfurt, Germany.
Volker ZickermannInstitute of Biochemistry II, University Hospital, Goethe University, Frankfurt, Germany.
Goethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

nadhubiquinone oxidoreductase (complex I) is the first enzyme complex of the respiratory chain. Complex I is a redox-driven proton pump that contributes to the proton motive force that drives ATP synthase. The structure of complex I has been analyzed by x-ray crystallography and electron cryo-microscopy and is now well-described. The ubiquinone (Q) reduction site of complex I is buried in the peripheral arm and a tunnel-like structure is thought to provide access for the hydrophobic substrate from the membrane. Several intermediate binding positions for Q in the tunnel were identified in molecular simulations. Structural data showed the binding of native Q molecules and short chain analogs and inhibitors in the access pathway and in the Q reduction site, respectively. We here review the current knowledge on the interaction of complex I with Q and discuss recent hypothetical models for the coupling mechanism.

Indexed as

electron transferinhibitorNADH dehydrogenaseoxidative phosphorylationproton pumpingrespiratory chainsemiquinone

Identifiers

PMID33996767
PMCPMC8119997
OpenAlexW3157748334

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.