Evidence map›Paper›PMID 42130197›Full record

ArticleJournal of agricultural and food chemistry2026

Fungal Rutinosidase─Engineering of a Side Tunnel Steers Its Transglycosylation Potential.

Lucie Petrásková, Michael Kotik, Natalia Kulik, Andrea Vopálenská, Anna Šidáková, Katerina Brodsky, Vladimír Křen, Pavla Bojarová

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of agricultural and food chemistry, 2026. 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

8 authors.

Lucie PetráskováInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, Prague 4, CZ 142 00, Czech Republic.ORCID 0000-0002-7052-5115
Michael KotikInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, Prague 4, CZ 142 00, Czech Republic.ORCID 0000-0003-4519-5983
Natalia KulikInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, Prague 4, CZ 142 00, Czech Republic.ORCID 0000-0003-2005-8165
Andrea VopálenskáInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, Prague 4, CZ 142 00, Czech Republic.
Anna ŠidákováInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, Prague 4, CZ 142 00, Czech Republic.
Katerina BrodskyInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, Prague 4, CZ 142 00, Czech Republic.
Vladimír KřenInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, Prague 4, CZ 142 00, Czech Republic.ORCID 0000-0002-1091-4020
Pavla BojarováInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, Prague 4, CZ 142 00, Czech Republic.ORCID 0000-0001-7069-0973

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rutinosidases (α-l-rhamnosyl-β-d-glucosidases) are glycosidases (EC 3.2.1.168) that cleave the glycosidic bond between the aglycone and the disaccharide residue rutinose. Their dual substrate specificity is reflected in their activity toward both rutin (rutinosylated) and isoquercitrin (glucosylated) substrates. The structure of rutinosidase from

Indexed as

Aspergillus nigerAspergillus oryzaeFungal ProteinsGlycoside HydrolasesCatalytic DomainGlycosylationKineticsRutinSubstrate SpecificityFungal ProteinsGlycoside HydrolasesRutinactive siteAspergillus nigerAspergillus oryzaemutagenesisrutinosidasetrans-glycosylation

Identifiers

PMID42130197
PMCPMC13237774

What OpenQuestion holds

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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.