Evidence map›Paper›PMID 38242919›Full record

ArticleScientific reports2024

Residual Complex I activity and amphidirectional Complex II operation support glutamate catabolism through mtSLP in anoxia.

Dora Ravasz, David Bui, Sara Nazarian, Gergely Pallag, Noemi Karnok, Jennie Roberts, Bryan P Marzullo, Daniel A Tennant, Bennett Greenwood, Alex Kitayev and 13 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

11 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. 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

23 authors at 6 institutions in 5 countries.

Dora RavaszDepartment of Biochemistry, Semmelweis University, Budapest, 1094, Hungary.
David BuiDepartment of Biochemistry, Semmelweis University, Budapest, 1094, Hungary.
Sara NazarianDepartment of Biochemistry, Semmelweis University, Budapest, 1094, Hungary.
Gergely PallagDepartment of Biochemistry, Semmelweis University, Budapest, 1094, Hungary.
Noemi KarnokDepartment of Biochemistry, Semmelweis University, Budapest, 1094, Hungary.
Jennie RobertsInstitute of Metabolism and Systems Research, College of Medical and Dental Sciences, University of Birmingham, Birmingham, B15 2TT, UK.
Bryan P MarzulloInstitute of Metabolism and Systems Research, College of Medical and Dental Sciences, University of Birmingham, Birmingham, B15 2TT, UK.
Daniel A TennantInstitute of Metabolism and Systems Research, College of Medical and Dental Sciences, University of Birmingham, Birmingham, B15 2TT, UK.
Bennett GreenwoodBERG, Framingham, MA, 01701, USA.
Alex KitayevBERG, Framingham, MA, 01701, USA.
Collin HillBERG, Framingham, MA, 01701, USA.
Timea KomlódiDepartment of Biochemistry, Semmelweis University, Budapest, 1094, Hungary.
Carolina DoerrierOroboros Instruments, Innsbruck, Austria.
Kristyna CunatovaDepartment of Biomedical Sciences, University of Padova, 35131, Padova, Italy.
Erika Fernandez-VizarraDepartment of Biomedical Sciences, University of Padova, 35131, Padova, Italy.
Erich GnaigerOroboros Instruments, Innsbruck, Austria.
Michael A KiebishBERG, Framingham, MA, 01701, USA.
Alexandra RaskaDepartment of Biochemistry, Semmelweis University, Budapest, 1094, Hungary.
Krasimir KolevDepartment of Biochemistry, Semmelweis University, Budapest, 1094, Hungary.
Bence CzumbelDepartment of Biochemistry, Semmelweis University, Budapest, 1094, Hungary.
Niven R NarainBERG, Framingham, MA, 01701, USA.
Thomas N SeyfriedBiology Department, Boston College, Chestnut Hill, Boston, MA, 02467, USA.
Christos ChinopoulosDepartment of Biochemistry, Semmelweis University, Budapest, 1094, Hungary. chinopoulos.christos@semmelweis.hu.
Semmelweis University · HUFramingham State University · USUniversity of Birmingham · GBOroboros Instruments (Austria) · ATUniversity of Padua · ITBoston College · US

Funding

Cancer Research UK 24757Horizon 2020 Framework Programme No. 859770Nemzeti Kutatási Fejlesztési és Innovációs Hivatal EFOP-3.6.3-VEKOP-16-2017-00009Nemzeti Kutatási Fejlesztési és Innovációs Hivatal K137563Nemzeti Kutatási Fejlesztési és Innovációs Hivatal KH129567
6 · The paper itself

Abstract

Anoxia halts oxidative phosphorylation (OXPHOS) causing an accumulation of reduced compounds in the mitochondrial matrix which impedes dehydrogenases. By simultaneously measuring oxygen concentration, NADH autofluorescence, mitochondrial membrane potential and ubiquinone reduction extent in isolated mitochondria in real-time, we demonstrate that Complex I utilized endogenous quinones to oxidize NADH under acute anoxia.

Indexed as

MitochondriaNADElectron Transport Complex IHumansHypoxiaOxidation-ReductionOxidative PhosphorylationQuinonesSuccinatesElectron Transport Complex INADQuinonesSuccinates

Identifiers

PMID38242919
PMCPMC10798963
OpenAlexW4391023797

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.