Evidence map›Paper›PMID 32068790›Full record

ArticleBioscience reports2020

Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse.

Alexander K H Weiss, Andreas Naschberger, Elia Cappuccio, Christina Metzger, Lorenza Mottes, Max Holzknecht, Jill von Velsen, Matthew W Bowler, Bernhard Rupp, Pidder Jansen-Dürr

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bioscience reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 51% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
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

10 authors at 3 institutions in 2 countries.

Alexander K H WeissUniversity of Innsbruck, Research Institute for Biomedical Aging Research, Rennweg 10, Innsbruck A-6020, Austria.
Andreas NaschbergerMedical University of Innsbruck, Division of Genetic Epidemiology, Schöpfstrasse 41, Innsbruck A-6020, Austria.
Elia CappuccioUniversity of Innsbruck, Research Institute for Biomedical Aging Research, Rennweg 10, Innsbruck A-6020, Austria.
Christina MetzgerUniversity of Innsbruck, Research Institute for Biomedical Aging Research, Rennweg 10, Innsbruck A-6020, Austria.
Lorenza MottesUniversity of Innsbruck, Research Institute for Biomedical Aging Research, Rennweg 10, Innsbruck A-6020, Austria.
Max HolzknechtUniversity of Innsbruck, Research Institute for Biomedical Aging Research, Rennweg 10, Innsbruck A-6020, Austria.
Jill von VelsenEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, CS 90181, Grenoble 38042, France.
Matthew W BowlerEuropean Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, CS 90181, Grenoble 38042, France.
Bernhard RuppMedical University of Innsbruck, Division of Genetic Epidemiology, Schöpfstrasse 41, Innsbruck A-6020, Austria.
Pidder Jansen-DürrUniversity of Innsbruck, Research Institute for Biomedical Aging Research, Rennweg 10, Innsbruck A-6020, Austria.
Universität Innsbruck · ATEuropean Molecular Biology Laboratory · FRInnsbruck Medical University · AT

Funding

Austrian Science Fund FWF P 28395Austrian Science Fund FWF P 31582
6 · The paper itself

Abstract

FAH domain containing protein 1 (FAHD1) is a mammalian mitochondrial protein, displaying bifunctionality as acylpyruvate hydrolase (ApH) and oxaloacetate decarboxylase (ODx) activity. We report the crystal structure of mouse FAHD1 and structural mapping of the active site of mouse FAHD1. Despite high structural similarity with human FAHD1, a rabbit monoclonal antibody (RabMab) could be produced that is able to recognize mouse FAHD1, but not the human form, whereas a polyclonal antibody recognized both proteins. Epitope mapping in combination with our deposited crystal structures revealed that the epitope overlaps with a reported SIRT3 deacetylation site in mouse FAHD1.

Indexed as

AcetoacetatesAnimalsCarboxy-LyasesCatalytic DomainCrystallography, X-RayEpitope MappingHumansHydrolasesMiceMitochondriaMitochondrial ProteinsStructure-Activity RelationshipAcetoacetatesCarboxy-LyasesFAHD1 protein, humanFahd2a protein, mousefumarylacetoacetateHydrolasesMitochondrial Proteinsoxaloacetate decarboxylasecrystallographyFAHD1SIRT3

Identifiers

PMID32068790
PMCPMC7056447
OpenAlexW3007422766

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.