ArticleThe protein journal2022
Purification and Characterization of Trehalase From Acyrthosiphon pisum, a Target for Pest Control.
Article in The protein journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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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.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- A fluorescent biosensor enables high-sensitivity quantification of hemolymph trehalose in individual aphids.BMC research notes · 2025Article
- Transgenerational Plasticity of Maternal Hemolymph Trehalose in Aphids.Archives of insect biochemistry and physiology · 2025Article
- The impact of three thioxothiazolidin compounds on trehalase activity and development ofPeerJ · 2024Article
- Silencing ofBiomolecules · 2023Article
- Article
- Synthesis of CFrontiers in chemistry · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Insect trehalases are glycoside hydrolases essential for trehalose metabolism and stress resistance. We here report the extraction and purification of Acyrthosiphon pisum soluble trehalase (ApTreh-1), its biochemical and structural characterization, as well as the determination of its kinetic properties. The protein has been purified by ammonium sulphate precipitation, first followed by an anion-exchange and then by an affinity chromatography. The SDS-PAGE shows a main band at 70 kDa containing two isoforms of ApTreh-1 (X1 and X2), identified by mass spectrometry and slightly contrasting in the C-terminal region. A phylogenetic tree, a multiple sequence alignment, as well as a modelled 3D-structure were constructed and they all reveal the ApTreh-1 similarity to other insect trehalases, i.e. the two signature motifs
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Registered trials
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