Evidence map›Paper›PMID 33916241›Full record

ArticleMolecules (Basel, Switzerland)2021

Functional Characterization of an Anthocyanin Dimalonyltransferase in Maize.

Michael Paulsmeyer, John Juvik

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. 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
–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

3 citing papers in PubMed.

  1. Promiscuous Transferases Malonylate Furaneol Glucoside inJournal of agricultural and food chemistry · 2026
    Article
  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

2 authors.

Michael PaulsmeyerDepartment of Crop Sciences, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
John JuvikDepartment of Crop Sciences, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Anthocyanins are pigments with appealing hues that are currently being used as sources of natural colorants. The interaction of acylation on the stability of anthocyanin molecules has long been known. Maize is an abundant source of malonylglucoside and dimalonylglucoside anthocyanins. The enzyme Aat1 is an anthocyanin acyltransferase known to synthesize the majority of acylated anthocyanins in maize. In this paper, we characterize the substrate specificity and reaction kinetics of Aat1. It was found that Aat1 has anthocyanin 3-

Indexed as

AcyltransferasesAnthocyaninsChromatography, High Pressure LiquidEnzyme ActivationKineticsMass SpectrometryMolecular StructureRecombinant ProteinsStructure-Activity RelationshipSubstrate SpecificityZea maysAcyltransferasesAnthocyaninsRecombinant Proteinsacylationacyltransferasecyanidinenzyme kineticsmalonyltransferase

Identifiers

PMID33916241
PMCPMC8037723

What OpenQuestion holds

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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.