Evidence map›Paper›PMID 39940919›Full record

ArticleInternational journal of molecular sciences2025

Analysis of Protein Inhibitors of Trypsin in Quinoa, Amaranth and Lupine Seeds. Selection and Deep Structure-Function Characterization of the

Martha Hernández de la Torre, Giovanni Covaleda-Cortés, Laura Montesinos, Daniela Covaleda, Juan C Ortiz, Jaume Piñol, José M Bautista, J Patricio Castillo, David Reverter, Francesc Xavier Avilés

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Protein Fraction and Derived Peptides fromInternational journal of molecular sciences · 2026
    Article
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.

Martha Hernández de la TorreFacultad de Ciencias Forestales, Universidad de Concepción, Concepción 4030000, Chile.ORCID 0000-0001-8191-3597
Giovanni Covaleda-CortésDepartment of Chemical, Biological and Environmental Engineering, Universitat Autònoma de Barcelona, 08193 Barcelona, Spain.ORCID 0000-0002-7621-852X
Laura MontesinosInstitute of Food and Agricultural Technology-CIDSAV-XaRTA, University of Girona, 17004 Girona, Spain.ORCID 0000-0003-4291-1227
Daniela CovaledaInstitut de Biotecnologia i Biomedicina, Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193 Barcelona, Spain.ORCID 0009-0007-4919-0377
Juan C OrtizInstitut de Biotecnologia i Biomedicina, Departament de Genètica i Microbiologia, Universitat Autònoma de Barcelona, 08193 Barcelona, Spain.ORCID 0000-0001-6672-4763
Jaume PiñolInstitut de Biotecnologia i Biomedicina, Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193 Barcelona, Spain.
José M BautistaDepartment of Biochemistry and Molecular Biology, Universidad Complutense de Madrid, 28040 Madrid, Spain.ORCID 0000-0001-8926-881X
J Patricio CastilloDepartamento de Ciencias Nucleares, Escuela Politécnica Nacional, Quito 170143, Ecuador.ORCID 0000-0002-9902-9262
David ReverterInstitut de Biotecnologia i Biomedicina, Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193 Barcelona, Spain.ORCID 0000-0002-5347-0992
Francesc Xavier AvilésInstitut de Biotecnologia i Biomedicina, Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193 Barcelona, Spain.ORCID 0000-0002-1399-6789

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protease inhibitors are biomolecules with growing biotechnological and biomedical relevance, including those derived from plants. This study investigated strong trypsin inhibitors in quinoa, amaranth, and lupine seeds, plant grains traditionally used in Andean South America. Amaranth seeds displayed the highest trypsin inhibitory activity, despite having the lowest content of aqueous soluble and thermostable protein material. This activity, directly identified by enzymatic assay, HPLC, intensity-fading mass spectrometry (IF-MS), and MS/MS, was attributed to a single protein of 7889.1 Da, identified as identical in

Indexed as

AmaranthusChenopodium quinoaLupinusPlant ProteinsSeedsTrypsinTrypsin InhibitorsAnimalsCattleStructure-Activity RelationshipPlant ProteinsTrypsinTrypsin InhibitorsamaranthAmaranthus caudatusAmaranthus hybridusHPLClupine seedsMS and X-ray analysisplant defenceplant trypsin inhibitorsquinoastructure–function characterisation

Identifiers

PMID39940919
PMCPMC11817793

What Socratic 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 Socratic graph.