Evidence map›Paper›PMID 40384981›Full record

ArticleFrontiers in cellular and infection microbiology2025

Screening and identification of protein 29 of

Zailing Shang, Fei Qiao, Yaning Li, Xuelin Ma, Mingxia Wang, Wenji Yang, Tianyu He, Haixia Ma, Yana Wang

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Article in Frontiers in cellular and infection microbiology, 2025. 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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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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4 · The record

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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.

Zailing Shang *Basic Medical Institute of Ningxia Medical University, Yinchuan, China.
Fei Qiao *Basic Medical Institute of Ningxia Medical University, Yinchuan, China.
Yaning LiBasic Medical Institute of Ningxia Medical University, Yinchuan, China.
Xuelin MaBasic Medical Institute of Ningxia Medical University, Yinchuan, China.
Mingxia WangBasic Medical Institute of Ningxia Medical University, Yinchuan, China.
Wenji YangBasic Medical Institute of Ningxia Medical University, Yinchuan, China.
Tianyu HeBasic Medical Institute of Ningxia Medical University, Yinchuan, China.
Haixia MaSchool of Clinical Medicine of Ningxia Medical University, Yinchuan, China.
Yana WangBasic Medical Institute of Ningxia Medical University, Yinchuan, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Introduction: Eg.P29 is a specific protein of Methods: Some basic information about Eg.P29 through bioinformatics software. A total of 50 molecules interacting with Eg.P29 were screened by three immunoprecipitation-combined liquid chromatography-tandem mass spectrometry intersections. The Results: Eg.P29 is a soluble cytoplasmic protein containing a BAR structural domain that may play a role in actin polarity and endocytosis. Cells in the Eg.P29 group showed marked morphological changes in the form of rounded, or oval shapes, which were attributed to changes in actin distribution. Seven molecules interacting with Eg.P29 were mainly actin and actin-related proteins (ACTG1, ACTN4, VCL, ARPC1A, LIMA1, FLNB and MYH10), and their mRNA and protein levels were significantly affected by Eg.P29. Yeast two-hybridization experiments showed that VCL did not interact with Eg.P29, whereas the other molecules interacted with Eg.P29. The interaction of LIMA1 and actin with Eg.P29 was verified by co-immunoprecipitation. Additionally, Eg.P29 and Eg.actin had the same histological location on rostellum, and suckers of the protoscolex. Additionally, the seven molecules were all discovered their homologous proteins in Discussion: In this study, we confirmed LIMA1 and actin were Eg.P29-interacting molecules, they were forming a compound regulation system to affect cytoskeleton formation. And we also deduced that Eg.P29 interacts with Eg.actin in

Indexed as

Echinococcus granulosusHelminth ProteinsActinsAnimalsChromatography, LiquidComputational BiologyHumansImmunoprecipitationMiceProtein BindingProtein Interaction MappingSheepTandem Mass SpectrometryTwo-Hybrid System TechniquesActinsHelminth Proteinscytoskeletonimmunoprecipitationmass spectrometryP29 of Echinococcus granulosusprotein-protein interactions

Identifiers

PMID40384981
PMCPMC12081405

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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.