Synthesis and characterization of an N-terminal-specific125I-photoaffinity derivative of μ-Conotoxin GIIIA which binds to the voltage-dependent sodium channel
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(90)80471-T/fullpdf
Reference16 articles.
1. PEPTIDE TOXINS FROM VENOMOUS CONUS SNAILS
2. Specific inhibition of [3H] saxitoxin binding to skeletal muscle sodium channels by geographutoxin II, a polypeptide channel blocker.
3. Structure and Function of Voltage-Sensitive Ion Channels
4. .mu.-Conotoxin GIIIA, a peptide ligand for muscle sodium channels: chemical synthesis, radiolabeling and receptor characterization
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1. A tyrosine-containing analog of mu-conotoxin GIIIA as ligand in the receptor binding assay for paralytic shellfish poisons;Toxicon;2015-06
2. μ-Conotoxin Giiia Interactions with the Voltage-Gated Na+ Channel Predict a Clockwise Arrangement of the Domains;Journal of General Physiology;2000-10-30
3. Photoactivatable derivatives of peptide and protein ligands in the study of neuroreceptor structure;Russian Journal of Bioorganic Chemistry;2000-01
4. [30] Pore-blocking toxins as probes of voltage-dependent channels;Methods in Enzymology;1999
5. Predominant Interactions between μ-Conotoxin Arg-13 and the Skeletal Muscle Na+ Channel Localized by Mutant Cycle Analysis;Biochemistry;1998-03-01
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