ArticleInsect biochemistry and molecular biology2017
Serpin-9 and -13 regulate hemolymph proteases during immune responses of Manduca sexta.
Article in Insect biochemistry and molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Serpin-4 Negatively Regulates Prophenoloxidase Activation and Antimicrobial Peptide Synthesis in the Silkworm,International journal of molecular sciences · 2023Article
- Parasitoid Serpins Evolve Novel Functions to Manipulate Host Homeostasis.Molecular biology and evolution · 2023Article
- A teratocyte-specific serpin from the endoparasitoid wasp Cotesia vestalis inhibits the prophenoloxidase-activating system of its host Plutella xylostella.Insect molecular biology · 2022Article
- Hemocyte Clusters Defined by scRNA-Seq inFrontiers in immunology · 2022Article
- Proteomic Analysis of the Hemolymph AfterFrontiers in immunology · 2021Article
- Article
- The Manduca sexta serpinome: Analysis of serpin genes and proteins in the tobacco hornworm.Insect biochemistry and molecular biology · 2018Article
- Manduca sexta serpin-12 controls the prophenoloxidase activation system in larval hemolymph.Insect biochemistry and molecular biology · 2018Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Serpins are a superfamily of proteins, most of which inhibit cognate serine proteases by forming inactive acyl-enzyme complexes. In the tobacco hornworm Manduca sexta, serpin-1, -3 through -7 negatively regulate a hemolymph serine protease system that activates precursors of the serine protease homologs (SPHs), phenoloxidases (POs), Spätzles, and other cytokines. Here we report the cloning and characterization of M. sexta serpin-9 and -13. Serpin-9, a 402-residue protein most similar to Drosophila Spn77Ba, has R
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Registered trials
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