Evidence map›Paper›PMID 40943090›Full record

ArticleInternational journal of molecular sciences2025

Aptamers as Potential Inhibitors of Ethylene Biosynthesis: Identification and In Silico Selection.

Diana Laura Aparicio-Breceda, Cristian Patricia Cabrales-Arellano, Efren Delgado, Gerardo Antonio Pámanes-Carrasco, Jorge Iñaki Gamero-Barraza, Hiram Medrano-Roldán, Damián Reyes-Jáquez

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. 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

7 authors.

Diana Laura Aparicio-BrecedaDepartment of Chemical and Biochemical Engineering, National Technological Institute of Mexico (TecNM)-Durango Institute of Technology (ITD), Blvd. Felipe Pescador 1830, Nueva Vizcaya, Durango 34080, Durango, Mexico.
Cristian Patricia Cabrales-ArellanoDepartment of Biology, Eastern New Mexico University, 1500 S Ave K, Portales, NM 88130, USA.ORCID 0000-0003-4676-4762
Efren DelgadoFood Science and Technology, Department of Family and Consumer Sciences, New Mexico State University, P.O. Box 30001, Las Cruces, NM 88003, USA.ORCID 0000-0001-7359-6309
Gerardo Antonio Pámanes-CarrascoSECIHTI-Instituto de Silvicultura e Industria de la Madera, Universidad Juárez del Estado de Durango, Blvd. Guadiana No. 501, Cd. Universitaria, Durango 34120, Durango, Mexico.
Jorge Iñaki Gamero-BarrazaDepartment of Chemical and Biochemical Engineering, National Technological Institute of Mexico (TecNM)-Durango Institute of Technology (ITD), Blvd. Felipe Pescador 1830, Nueva Vizcaya, Durango 34080, Durango, Mexico.ORCID 0000-0002-8306-0855
Hiram Medrano-RoldánDepartment of Chemical and Biochemical Engineering, National Technological Institute of Mexico (TecNM)-Durango Institute of Technology (ITD), Blvd. Felipe Pescador 1830, Nueva Vizcaya, Durango 34080, Durango, Mexico.
Damián Reyes-JáquezDepartment of Chemical and Biochemical Engineering, National Technological Institute of Mexico (TecNM)-Durango Institute of Technology (ITD), Blvd. Felipe Pescador 1830, Nueva Vizcaya, Durango 34080, Durango, Mexico.ORCID 0000-0002-6033-8965

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Worldwide, 13.3% of food was wasted in 2020. Ethylene biosynthesis, responsible for fruit ripening, regulates key processes in plant growth and aging. Aptamers are DNA or RNA molecules with the capacity to bind with high affinity and specificity to proteins due to their three-dimensional structure. Therefore, conventional aptamer selection methods are often costly, inefficient, and time-consuming. In this context, in silico molecular docking offers an efficient alternative, enabling the evaluation of binding potential prior to experimental assays. This research identified aptamers with high predicted affinity for the 1-aminocyclopropane-1-carboxylate synthase (ACC synthase) and 1-aminocyclopropane-1-carboxylate oxidase (ACC oxidase) enzymes, essential in ethylene biosynthesis. Using ZDOCK for preliminary screening and HDOCK for refined analysis, aptamer-enzyme interactions were modeled. Aptamers AB451 and ABR6P.1 showed promising binding to ACC synthase, while RO33828 and O0O6O1 were optimal for ACC oxidase. These results represent a computational foundation for the development of aptamer-based inhibitors to potentially delay ripening and reduce postharvest losses. Experimental validation will be required to confirm their inhibitory function.

Indexed as

Aptamers, NucleotideEthylenesLyasesAmino Acid OxidoreductasesComputer SimulationMolecular Docking SimulationProtein Binding1-aminocyclopropane-1-carboxylic acid oxidase1-aminocyclopropanecarboxylate synthaseAmino Acid OxidoreductasesAptamers, NucleotideethyleneEthylenesLyasesACC oxidaseACC synthasemolecular dockingRNA aptamer

Identifiers

PMID40943090
PMCPMC12428408

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Registered trials

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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.