Evidence map›Paper›PMID 41745776›Full record

ArticleToxins2026

Discovery of Two Novel Scorpion Venom Peptides Activating TRPML2 to Impair ZIKV Internalization.

Zhiqiang Xia, Xuhua Yang, Dangui He, Jiayuan Chang, Lixia Xie, Qian Liu, Jiahuan Jin, Bing Li, Alexandre K Tashima, Hang Fai Kwok and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Toxins, 2026. 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. Scorpion Peptides in Antiviral Drug Discovery: An In-depth Review.Probiotics and antimicrobial proteins · 2026
    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

11 authors.

Zhiqiang XiaSchool of Biological and Food Processing Engineering, Huanghuai University, Zhumadian 463000, China.
Xuhua YangNational "111" Center for Cellular Regulation and Molecular Pharmaceutics, Key Laboratory of Fermentation Engineering (Ministry of Education), School of Life and Health Sciences, Hubei University of Technology, Wuhan 430086, China.
Dangui HeDepartment of Biomedical Sciences, Faculty of Health Sciences, University of Macau, Taipa, Macau SAR, China.
Jiayuan ChangSchool of Biological and Food Processing Engineering, Huanghuai University, Zhumadian 463000, China.
Lixia XieSchool of Biological and Food Processing Engineering, Huanghuai University, Zhumadian 463000, China.
Qian LiuSchool of Biological and Food Processing Engineering, Huanghuai University, Zhumadian 463000, China.
Jiahuan JinSchool of Biological and Food Processing Engineering, Huanghuai University, Zhumadian 463000, China.
Bing LiZhumadian Huazhong Chia Tai Co., Ltd., Zhumadian 463000, China.
Alexandre K TashimaDepartment of Biochemistry, Paulista School of Medicine, Federal University of São Paulo, São Paulo 04023-062, Brazil.ORCID 0000-0002-1332-8895
Hang Fai KwokDepartment of Biomedical Sciences, Faculty of Health Sciences, University of Macau, Taipa, Macau SAR, China.ORCID 0000-0002-6349-4517
Zhijian CaoNational "111" Center for Cellular Regulation and Molecular Pharmaceutics, Key Laboratory of Fermentation Engineering (Ministry of Education), School of Life and Health Sciences, Hubei University of Technology, Wuhan 430086, China.

Funding

National Key Research and Development Program of China 2023YFF1304900National Natural Science Foundation of China 32370547National Natural Science Foundation of China 32561160088National Natural Science Foundation of China 32570597Science and Technology Development Fund of Macau S.A.R. 0069/2025/AFJ
6 · The paper itself

Abstract

The endo-lysosomal channel TRPML2 regulates key processes like membrane trafficking and autophagy, which are hijacked by many RNA viruses during endocytic entry. However, the development of TRPML2-targeted therapeutics has been hindered by a notable lack of high-affinity and selective peptide-based activators. Scorpion venom peptides, honed by evolution for exceptional specificity toward diverse membrane ion channels, represent a promising, underexplored natural library for discovering novel pharmacological probes and drug leads. Here, we screened and identified seven candidate peptides interacting with TRPML2 using co-immunoprecipitation combined with liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis of the

Indexed as

antiviral activityendo-lysosomal channelscorpion venom peptidesTRPML2 activatorZika virus

Identifiers

PMID41745776
PMCPMC12945122

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.