Evidence map›Paper›PMID 38458818›Full record

ArticleFEBS open bio2024

Structural enzymology studies with the substrate 3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD.

Shruthi Sridhar, Tiila-Riikka Kiema, Werner Schmitz, Mikael Widersten, Rik K Wierenga

Open access · goldAbstract read
In one paragraph

Article in FEBS open bio, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 98% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

5 authors at 3 institutions in 3 countries.

Shruthi SridharFaculty of Biochemistry and Molecular Medicine, University of Oulu, Finland.ORCID 0000-0002-3546-2737
Tiila-Riikka KiemaBiocenter Oulu, University of Oulu, Finland.ORCID 0000-0002-7514-2316
Werner SchmitzTheodor Boveri Institute of Biosciences (Biocenter), University of Würzburg, Germany.ORCID 0000-0003-0485-7303
Mikael WiderstenDepartment of Chemistry - BMC, Uppsala University, Sweden.ORCID 0000-0002-3203-3793
Rik K WierengaFaculty of Biochemistry and Molecular Medicine, University of Oulu, Finland.ORCID 0000-0001-6554-471X
University of Oulu · FIUniversity of Würzburg · DEUppsala University · SE

Funding

Academy of Finland 339894Horizon2020 653706
6 · The paper itself

Abstract

Multifunctional enzyme, type-1 (MFE1) catalyzes the second and third step of the β-oxidation cycle, being, respectively, the 2E-enoyl-CoA hydratase (ECH) reaction (N-terminal part, crotonase fold) and the NAD

Indexed as

Enoyl-CoA HydrataseNADAnimalsCatalytic DomainGlutamic AcidHumansMultienzyme ComplexesOxidoreductasesRatsEhhadh protein, ratEnoyl-CoA HydrataseGlutamic AcidMultienzyme ComplexesNADOxidoreductasescrotonasecrystal structuredehydrogenasedynamical propertiesstopped‐flow

Identifiers

PMID38458818
PMCPMC10988713
OpenAlexW4392761096

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.