Evidence map›Paper›PMID 42594255›Full record

ArticleArchives of insect biochemistry and physiology2026

Molecular Recognition of Odorant-Binding Proteins WmagOBP39280 and WmagOBP42531 to Wohlfahrtia magnifica Pheromones and Bactrian Camel Volatiles.

Yuting Bai, Leifen Li, Wuri Han, Huar Bao, Bin Yang, Baoxiang Han, Haobo Li, Yaning Li, Demtu Er

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Archives of insect biochemistry and physiology, 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. 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

9 authors.

Yuting BaiKey Laboratory of Clinical Diagnosis and Treatment Technology in Animal Disease, Ministry of Agriculture and Rural Affairs, College of Veterinary Medicine, Inner Mongolia Agricultural University, Hohhot, People's Republic of China.ORCID https://orcid.org/0000-0002-7775-1254
Leifen LiKey Laboratory of Clinical Diagnosis and Treatment Technology in Animal Disease, Ministry of Agriculture and Rural Affairs, College of Veterinary Medicine, Inner Mongolia Agricultural University, Hohhot, People's Republic of China.
Wuri HanQuality Safety Center for Agricultural and Animal Products of Inner Mongolia Autonomous Region, Hohhot, People's Republic of China.
Huar BaoKey Laboratory of Clinical Diagnosis and Treatment Technology in Animal Disease, Ministry of Agriculture and Rural Affairs, College of Veterinary Medicine, Inner Mongolia Agricultural University, Hohhot, People's Republic of China.
Bin YangKey Laboratory of Clinical Diagnosis and Treatment Technology in Animal Disease, Ministry of Agriculture and Rural Affairs, College of Veterinary Medicine, Inner Mongolia Agricultural University, Hohhot, People's Republic of China.
Baoxiang HanKey Laboratory of Clinical Diagnosis and Treatment Technology in Animal Disease, Ministry of Agriculture and Rural Affairs, College of Veterinary Medicine, Inner Mongolia Agricultural University, Hohhot, People's Republic of China.
Haobo LiKey Laboratory of Clinical Diagnosis and Treatment Technology in Animal Disease, Ministry of Agriculture and Rural Affairs, College of Veterinary Medicine, Inner Mongolia Agricultural University, Hohhot, People's Republic of China.
Yaning LiQuality Safety Center for Agricultural and Animal Products of Inner Mongolia Autonomous Region, Hohhot, People's Republic of China.
Demtu ErKey Laboratory of Clinical Diagnosis and Treatment Technology in Animal Disease, Ministry of Agriculture and Rural Affairs, College of Veterinary Medicine, Inner Mongolia Agricultural University, Hohhot, People's Republic of China.ORCID https://orcid.org/0000-0002-5705-665X

Funding

National Natural Science Foundation of China 32360862
6 · The paper itself

Abstract

Wohlfahrtia magnifica, a worldwide pest, causes myiasis in many domestic animals. Its pheromones and volatiles from Bactrian camels were reported to attract or repel W. magnifica, but the molecular mechanisms are still unclear. A small protein in the insect olfactory system, called odorant binding protein (OBP), plays a crucial role in odor reception. In this study, two W. magnifica odorant-binding proteins (WmagOBPs) genes, WmagOBP42531 and WmagOBP39280, were cloned from the antennae of W. magnifica, and then expressed and purified by prokaryotic expression. Fluorescence binding assays demonstrated that WmagOBP39280 exhibits high binding affinity to methylheptenone, butylbutyrate, p-ethylacetophenone, acetophenone (K

Indexed as

CamelusDipteraInsect ProteinsPheromonesReceptors, OdorantVolatile Organic CompoundsAmino Acid SequenceAnimalsArthropod AntennaeMolecular Docking SimulationInsect Proteinsodorant-binding proteinPheromonesReceptors, OdorantVolatile Organic Compoundsbinding affinitymolecular dockingmolecular dynamicsodorant‐binding proteinsWohlfahrtia magnifica

Identifiers

PMID42594255
PMCPMC13472500

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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.