Evidence map›Paper›PMID 30810978›Full record

ArticleNeurochemical research2019

The Effect of 2-Ketobutyrate on Mitochondrial Substrate-Level Phosphorylation.

David Bui, Dora Ravasz, Christos Chinopoulos

Open access · hybridAbstract read
In one paragraph

Article in Neurochemical research, 2019. 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
1.4field-weighted citation impact, top 19% 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.

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  12. Targeted and untargeted metabolomic approach for GDM diagnosis.Frontiers in molecular biosciences · 2022
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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

3 authors at 1 institution in 1 country.

David BuiDepartment of Medical Biochemistry, Semmelweis University, Tuzolto st. 37-47, Budapest, 1094, Hungary.
Dora RavaszDepartment of Medical Biochemistry, Semmelweis University, Tuzolto st. 37-47, Budapest, 1094, Hungary.
Christos ChinopoulosDepartment of Medical Biochemistry, Semmelweis University, Tuzolto st. 37-47, Budapest, 1094, Hungary. chinopoulos.christos@eok.sote.hu.ORCID http://orcid.org/0000-0003-0183-4149
Semmelweis University · HU

Funding

FIKP FIKP-61822-64888-EATVNemzeti Kutatási, Fejlesztési és Innovációs Hivatal KH129567
6 · The paper itself

Abstract

The reaction catalyzed by succinate-CoA ligase in the mitochondrial matrix yields a high-energy phosphate when operating towards hydrolysis of the thioester bond of succinyl-CoA, known as mitochondrial substrate-level phosphorylation (mSLP). The catabolism of several metabolites converge to succinyl-CoA but through different biochemical pathways. Among them, threonine, serine and methionine catabolize to succinyl-CoA through the common intermediate, 2-ketobutyrate. During the course of this pathway 2-ketobutyrate will become succinyl-CoA through propionyl-CoA catabolism, obligatorily passing through an ATP-consuming step substantiated by propionyl-CoA carboxylase. Here, by recording the directionality of the adenine nucleotide translocase while measuring membrane potential we tested the hypothesis that catabolism of 2-ketobutyrate negates mSLP due to the ATP-consuming propionyl-CoA carboxylase step in rotenone-treated, isolated mouse liver and brain mitochondria. 2-Ketobutyrate produced a less negative membrane potential compared to NADH or FADH

Indexed as

Acyl Coenzyme AAnimalsButyratesMiceMitochondriaPhosphorylationRotenoneSubstrate SpecificityAcyl Coenzyme Aalpha-ketobutyric acidButyratesRotenonesuccinyl-coenzyme A2-Oxobutanoate2-OxobutyrateAlpha-ketobutyrateSuccinyl-CoA

Identifiers

PMID30810978
PMCPMC6776489
OpenAlexW2916453292

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.