ArticleInsect molecular biology2013
Identification and biochemical characterization of Laodelphax striatellus neutral ceramidase.
Article in Insect molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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.
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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.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Insect Lipids: Structure, Classification and Function.Advances in experimental medicine and biology · 2026Review
- Alkaline ceramidase (Frontiers in physiology · 2023Article
- Study of tyramine-binding mechanism and insecticidal activity of oil extracted from Eucalyptus againstFrontiers in chemistry · 2022Article
- Neutral Ceramidase Is Required for the Reproduction of Brown Planthopper,Frontiers in physiology · 2021Article
- A neutral ceramidase, NlnCDase, is involved in the stress responses of brown planthopper, Nilaparvata lugens (Stål).Scientific reports · 2018Article
- Rice Stripe Virus Infection Alters mRNA Levels of Sphingolipid-Metabolizing Enzymes and Sphingolipids Content in Laodelphax striatellus.Journal of insect science (Online) · 2017Article
Corrections and comments
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Authors and funding
12 authors at 7 institutions in 3 countries.
Funding
Abstract
Ceramidases are a group of enzymes that catalyse hydrolysis of ceramides to generate fatty acid and sphingosine. In this study, we report the cloning and characterization of the rice small brown planthopper Laodelphax striatellus neutral ceramidase (nCDase), LsnCer. LsnCer was identified by sequencing the transcriptome of L. striatellus and is a protein of 717 amino acids with a predicted molecular weight of 79.3 kDa. Similarly to other known nCDases, the optimum pH for LsnCer is 8.0 and the optimum temperature is 37 °C for its in vitro activity. LsnCer activity is inhibited by Zn(2+) significantly and Fe(2+) slightly. LsnCer has broad substrate specificity with a preference for ceramides with a medium acyl-chain or a monounsaturated long acyl-chain. Infection with rice strip virus (RSV) or treatment with insecticides significantly increased LsnCer mRNA expression and its enzymatic activity in L. striatellus. These results suggest that LsnCer is a bona fide nCDase that may have a role in adaption of L. striatellus to environmental stresses.
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Registered trials
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