Evidence map›Paper›PMID 41235125›Full record

ArticleRSC advances2025

A novel ene-reductase from

Lauriane Pillet, Cristina Lía Fernández Reguerio, Markus Richard Busch, David Roura Padrosa, Francesca Paradisi

Abstract read
In one paragraph

Article in RSC advances, 2025. 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
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.

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.

Lauriane PilletDepartment of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern Freiestrasse 3 CH-3012 Bern Switzerland francesca.paradisi@unibe.ch.
Cristina Lía Fernández ReguerioInSEIT AG Freiestrasse 3 CH-3012 Bern Switzerland.ORCID https://orcid.org/0000-0001-6709-2550
Markus Richard BuschDepartment of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern Freiestrasse 3 CH-3012 Bern Switzerland francesca.paradisi@unibe.ch.
David Roura PadrosaInSEIT AG Freiestrasse 3 CH-3012 Bern Switzerland.ORCID https://orcid.org/0000-0001-6324-8722
Francesca ParadisiDepartment of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern Freiestrasse 3 CH-3012 Bern Switzerland francesca.paradisi@unibe.ch.ORCID https://orcid.org/0000-0003-1704-0642

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In order to broaden the toolbox of enzymes available for biocatalytic reductions of carbon-carbon double bonds, we investigated four promising ene-reductases (ERs) stemming from extremophilic organisms or showing homology with thermophilic ERs. The novel ene-reductase from the halophilic organism

Identifiers

PMID41235125
PMCPMC12610393

What OpenQuestion holds

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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.