Evidence map›Paper›PMID 40828035›Full record

ReviewBiotechnology journal2025

Exploring Plant α-Amylase Inhibitors: Mechanisms and Potential Application for Insect Pest Control.

Marcos Fernando Basso, Arnubio Valencia-Jiménez, Fabrizio Lo Celso, Isabel Rodrigues Gerhardt, Thomas Joseph V Higgins, Maria Fatima Grossi-de-Sa

Abstract readReview
In one paragraph

Review in Biotechnology journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. 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

6 authors.

Marcos Fernando BassoEmbrapa Genetic Resources and Biotechnology Brasília Distrito, Federal, Brazil.
Arnubio Valencia-JiménezDepartamento De Producción Agropecuaria, University of Caldas, Manizales, Caldas, Colombia.
Fabrizio Lo CelsoDepartment of Physics and Chemical, University of Palermo, Palermo, Italy.
Isabel Rodrigues GerhardtEmbrapa Digital Agriculture, Campinas, São Paulo, Brazil.
Thomas Joseph V HigginsCommonwealth Scientific and Industrial Research Organisation (CSIRO), Agriculture and Food, Canberra, Australia.
Maria Fatima Grossi-de-SaEmbrapa Genetic Resources and Biotechnology Brasília Distrito, Federal, Brazil.ORCID https://orcid.org/0000-0001-8184-9599

Funding

CAPESCNPq 106655/2023-0CNPq 108646/2024-6EMBRAPAFAP-DFFAPESP 2016/23218-0FAPESP 2024/12315-0INCT PlantStress BiotechUCBUCDB
6 · The paper itself

Abstract

α-Amylases are found in microbes, plants, and animals, including insect pests. They play crucial roles in catalyzing the hydrolysis of α-1,4-glucan bonds within starch, glycogen, and related carbohydrates, forming shorter oligomers. In green plants, these enzymes are pivotal for starch degradation during photosynthesis and seed germination, whereas in phytophagous insect pests, they predominantly facilitate seed parasitism by degrading raw starch granules. Amylase inhibitors in plants appear to function as part of their defense against pests and pathogens. In the context of insect pests, some of these amylase inhibitors can target α-amylases in the digestive system of certain insects. Both mono- and dicotyledonous plants harbor multiple genes encoding proteinaceous α-amylase inhibitors. Previous studies have demonstrated that α-amylase inhibitors, whether produced in vitro or overexpressed in transgenic plants, can exhibit entomotoxic activity against certain insect pests. Field trials involving transgenic plants that overexpress α-amylase inhibitors have been conducted, laying the foundation for the potential commercialization of crops engineered with these genes. Herein, this review explores the molecular interactions between plant α-amylase inhibitors and insect α-amylases, shedding light on the underlying mechanisms of action, structural diversity, and assessing the broader biotechnological applications of this promising strategy.

Indexed as

alpha-AmylasesEnzyme InhibitorsInsectaInsect ControlPlant ProteinsPlantsAnimalsPlants, Genetically Modifiedalpha-AmylasesEnzyme InhibitorsPlant Proteinscrop protectioninsecticidal proteinstarch catabolismtransgenic plantsα‐amylase

Identifiers

PMID40828035
PMCPMC12363435

What OpenQuestion holds

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LicenceCC BY
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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.