Evidence map›Paper›PMID 42741776›Full record

ArticleThe journal of venomous animals and toxins including tropical diseases2026

Proteomic characterization of

Milena Del C Muñoz-Agames, Marcos H Salazar, Herlinda Clement, Lorena Hernández-Orihuela, Magdalena Hernández-Ortiz, Sergio Encarnación-Guevara, John Cleghorn, Hildaura Acosta, Gerardo Corzo

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Article in The journal of venomous animals and toxins including tropical diseases, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

9 authors.

Milena Del C Muñoz-AgamesUniversidad de Panama, Research and Information Center for Medicines and Toxic Substances, School of Medicine, Vice-Rectorate for Research and Graduate Studies, Panama City, Panama.
Marcos H SalazarUniversidad de Panama, Research and Information Center for Medicines and Toxic Substances, School of Medicine, Vice-Rectorate for Research and Graduate Studies, Panama City, Panama.
Herlinda ClementCenter for Genomic Sciences, National Autonomous University of Mexico, Cuernavaca, Morelos, Mexico.
Lorena Hernández-OrihuelaDepartment of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico, Cuernavaca, Morelos, Mexico.
Magdalena Hernández-OrtizCenter for Genomic Sciences, National Autonomous University of Mexico, Cuernavaca, Morelos, Mexico.
Sergio Encarnación-GuevaraCenter for Genomic Sciences, National Autonomous University of Mexico, Cuernavaca, Morelos, Mexico.
John CleghornUniversidad de Panama, Research and Information Center for Medicines and Toxic Substances, School of Medicine, Vice-Rectorate for Research and Graduate Studies, Panama City, Panama.
Hildaura AcostaUniversidad de Panama, Research and Information Center for Medicines and Toxic Substances, School of Medicine, Vice-Rectorate for Research and Graduate Studies, Panama City, Panama.
Gerardo CorzoDepartment of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico, Cuernavaca, Morelos, Mexico.ORCID https://orcid.org/0000-0002-9513-1622

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: Methods: Venom composition was analyzed by tandem mass spectrometry (MS/MS), enabling the identification of venom proteins. Subsequently, one of its primary lethal toxins (Tcham27) was identified and recombinantly expressed. Results: Proteomic analysis revealed that the most abundant family in the venom corresponded to metalloproteases, with 43 protein groups (17% of the total identifications), which are associated with processes such as hemorrhage, edema, inflammation, hypotension, and necrosis. CIIMET family toxins comprised 27 protein groups (11%). Among ion channel-acting toxins, 18 protein groups (7%) corresponded to sodium channel toxins and 14 (6%) to potassium channel toxins, homologous to components from geographically proximate species such as Conclusions: Proteomic characterization of

Indexed as

ProteinRecombinant expressionScorpion toxinSodium channelTityusVenom

Identifiers

PMID42741776
PMCPMC13574325

What OpenQuestion holds

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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.