Evidence map›Paper›PMID 35563503›Full record

ArticleInternational journal of molecular sciences2022

Proline Oxidation Supports Mitochondrial ATP Production When Complex I Is Inhibited.

Gergely Pallag, Sara Nazarian, Dora Ravasz, David Bui, Timea Komlódi, Carolina Doerrier, Erich Gnaiger, Thomas N Seyfried, Christos Chinopoulos

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
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  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Complex II ambiguities-FADHThe Journal of biological chemistry · 2024
    Review
  14. Article
  15. Article
  16. Mitochondrial Bioenergetics in Different Pathophysiological Conditions 2.0.International journal of molecular sciences · 2022
    Article
  17. 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

9 authors at 3 institutions in 3 countries.

Gergely PallagDepartment of Biochemistry and Molecular Biology, Semmelweis University, 1094 Budapest, Hungary.
Sara NazarianDepartment of Biochemistry and Molecular Biology, Semmelweis University, 1094 Budapest, Hungary.
Dora RavaszDepartment of Biochemistry and Molecular Biology, Semmelweis University, 1094 Budapest, Hungary.
David BuiDepartment of Biochemistry and Molecular Biology, Semmelweis University, 1094 Budapest, Hungary.
Timea KomlódiOroboros Instruments, 6020 Innsbruck, Austria.
Carolina DoerrierOroboros Instruments, 6020 Innsbruck, Austria.ORCID 0000-0002-7969-6762
Erich GnaigerOroboros Instruments, 6020 Innsbruck, Austria.ORCID 0000-0003-3647-5895
Thomas N SeyfriedBiology Department, Boston College, Chestnut Hill, MA 02467, USA.
Christos ChinopoulosDepartment of Biochemistry and Molecular Biology, Semmelweis University, 1094 Budapest, Hungary.ORCID 0000-0003-0183-4149
Semmelweis University · HUOroboros Instruments (Austria) · ATBoston College · US

Funding

European Union's Horizon 2020 research and innovation programme 859770Hungarian Scientific Research Fund K_135027Hungarian Scientific Research Fund KH_129567National Research, Development and Innovation Office 2017-2.3.4-TET-RU-2017-00003National Research, Development and Innovation Office FIKP-61822-64888-EATVNational Research, Development and Innovation Office [TKP2021-EGA-25]National Research, Development and Innovation Office VEKOP 2.3.3-15-2016-00012
6 · The paper itself

Abstract

The oxidation of proline to pyrroline-5-carboxylate (P5C) leads to the transfer of electrons to ubiquinone in mitochondria that express proline dehydrogenase (ProDH). This electron transfer supports Complexes CIII and CIV, thus generating the protonmotive force. Further catabolism of P5C forms glutamate, which fuels the citric acid cycle that yields the reducing equivalents that sustain oxidative phosphorylation. However, P5C and glutamate catabolism depend on CI activity due to NAD

Indexed as

Proline OxidaseUbiquinoneAdenosine TriphosphatasesAdenosine TriphosphateAnimalsElectron Transport Complex IGlutamic AcidMiceMitochondriaProlineAdenosine TriphosphatasesAdenosine TriphosphateElectron Transport Complex IGlutamic AcidProlineProline OxidaseUbiquinonecoenzyme Qproline dehydrogenasereducing equivalentsubstrate-level phosphorylation

Identifiers

PMID35563503
PMCPMC9106064
OpenAlexW4225401898

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.