Evidence map›Paper›PMID 30093404›Full record

ArticleThe Journal of biological chemistry2018

Arginine 107 of yeast ATP synthase subunit g mediates sensitivity of the mitochondrial permeability transition to phenylglyoxal.

Lishu Guo, Michela Carraro, Geppo Sartori, Giovanni Minervini, Ove Eriksson, Valeria Petronilli, Paolo Bernardi

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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.5field-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

27 citing papers in PubMed, 47 citations in OpenAlex.

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  15. Frontiers in microbiology · 2022
    Article
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  19. Cryo-EM structure of the entire mammalian F-type ATP synthase.Nature structural & molecular biology · 2020
    Article
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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

7 authors at 1 institution in 1 country.

Lishu GuoFrom the Consiglio Nazionale delle Ricerche Institute of Neuroscience and Department of Biomedical Sciences, University of Padova, Padova 35131, Italy and.
Michela CarraroFrom the Consiglio Nazionale delle Ricerche Institute of Neuroscience and Department of Biomedical Sciences, University of Padova, Padova 35131, Italy and.
Geppo SartoriFrom the Consiglio Nazionale delle Ricerche Institute of Neuroscience and Department of Biomedical Sciences, University of Padova, Padova 35131, Italy and.
Giovanni MinerviniFrom the Consiglio Nazionale delle Ricerche Institute of Neuroscience and Department of Biomedical Sciences, University of Padova, Padova 35131, Italy and.
Ove Erikssonthe Department of Biochemistry and Developmental Biology, Faculty of Medicine, University of Helsinki, Helsinki 00290, Finland.ORCID 0000-0002-3565-4106
Valeria PetronilliFrom the Consiglio Nazionale delle Ricerche Institute of Neuroscience and Department of Biomedical Sciences, University of Padova, Padova 35131, Italy and.ORCID 0000-0003-4026-6404
Paolo BernardiFrom the Consiglio Nazionale delle Ricerche Institute of Neuroscience and Department of Biomedical Sciences, University of Padova, Padova 35131, Italy and bernardi@bio.unipd.it.ORCID 0000-0001-9187-3736
University of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Modification with arginine-specific glyoxals modulates the permeability transition (PT) of rat liver mitochondria, with inhibitory or inducing effects that depend on the net charge of the adduct(s). Here, we show that phenylglyoxal (PGO) affects the PT in a species-specific manner (inhibition in mouse and yeast, induction in human and

Indexed as

Mitochondrial Membrane Transport ProteinsAnimalsArginineCalciumCatalysisDimerizationDrosophilaHEK293 CellsHumansMiceMitochondriaMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesPhenylglyoxalSaccharomyces cerevisiaeSpecies SpecificityArginineCalciumMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesPhenylglyoxalATP synthasebioenergeticscalciummitochondriamitochondrial permeability transition (MPT)

Identifiers

PMID30093404
PMCPMC6153276
OpenAlexW2886685732

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.