A natural point mutation changes both target selectivity and mechanism of action of sea anemone toxins-Reference-Cited by-同舟云学术

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A natural point mutation changes both target selectivity and mechanism of action of sea anemone toxins

Published:2012-09-12 Issue:12 Volume:26 Page:5141-5151
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:FASEB j.

Author:

Peigneur Steve¹,Béress László²³,Möller Carolina⁴,Marí Frank⁴,Forssmann Wolf‐Georg²³,Tytgat Jan¹

Affiliation:

1. Laboratory of ToxicologyUniversity of Leuven (Katholieke Universiteit Leuven)LeuvenBelgium

2. Department of Immunology and RheumatologyHannover Medical UniversityHannoverGermany

3. Pharis Biotec GmbHHannoverGermany

4. Department of Chemistry and BiochemistryFlorida Atlantic UniversityBoca RatonFloridaUSA

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.12-218479

Reference46 articles.

1. Overview of the voltage‐gated sodium channel family;Yu F. H.;Genome Biol.,2003

2. Analgesic Compound from Sea Anemone Heteractis crispa Is the First Polypeptide Inhibitor of Vanilloid Receptor 1 (TRPV1)

3. Peptide Toxins in Sea Anemones: Structural and Functional Aspects

4. Discovery and characterization of cnidarian peptide toxins that affect neuronal potassium ion channels

5. Sea anemone venom as a source of insecticidal peptides acting on voltage-gated Na+ channels

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