These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Site-3 sea anemone toxins: molecular probes of gating mechanisms in voltage-dependent sodium channels.
    Author: Smith JJ, Blumenthal KM.
    Journal: Toxicon; 2007 Feb; 49(2):159-70. PubMed ID: 17095031.
    Abstract:
    Sea anemone toxins, whose biological function is the capture of marine prey, are invaluable tools for studying the structure and function of mammalian voltage-gated sodium channels. Their high degree of specificity and selectivity have allowed for detailed analysis of inactivation gating and assignment of molecular entities responsible for this process. Because of their ability to discriminate among channel isoforms, and their high degree of structural conservation, these toxins could serve as important lead compounds for future pharmaceutical design.
    [Abstract] [Full Text] [Related] [New Search]