English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Zendy Plus

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Zendy Tools

Zendy Open

Caenorhabditis elegans  is a widely accepted model system for parasitic nematodes, drug screening and developmental studies. Similar to parasitic worms,  C. elegans  expresses glycosphingolipids and glycoproteins carrying, in part, phosphorylcholine ( P Cho) substitutions, which might play important roles in nematode development, fertility and, at least in the case of parasites, survival within the host. With the exception of a major secretory/excretory product from  Acanthocheilonema viteae  (ES-62), no protein carrying this epitope has been studied in detail yet. Here we report on the identification, characterization and localization of the aspartyl protease ASP-6 of  C. elegans , which is excreted by the nematode in a  P Cho-substituted form. Within the worm, most prominent expression of the protein is observed in the intestine, while muscle and epithelial cells express  asp-6  to a lesser extent. In animals harboring an ASP-6::GFP fusion protein, diffuse fluorescence throughout the body cavity of adult worms indicates that the chimeric protein is secreted.

biological chemistry

First identification of a phosphorylcholine-substituted protein from  Caenorhabditis elegans : isolation and characterization of the aspartyl protease ASP-6