Role of disulfide bridges in the folding, structure and biological activity of ω-conotoxin GVIA
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference42 articles.
1. Purification and sequence of a presynaptic peptide toxin from Conus geographus venom
2. ω-Conotoxin-sensitive voltage-operated calcium channels in vertebrate cells
3. Structure and Functional Expression of an ω-Conotoxin-Sensitive Human N-Type Calcium Channel
4. Antagonists of Neuronal Calcium Channels: Structure, Function, and Therapeutic Implications
5. Pharmacotherapeutic potential of omega-conotoxin MVIIA (SNX-111), an N-type neuronal calcium channel blocker found in the venom of Conus magus
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2. The Single Disulfide-Directed β-Hairpin Fold: Role of Disulfide Bond in Folding and Effect of an Additional Disulfide Bond on Stability;Australian Journal of Chemistry;2020
3. Cyclic analogues of α‐conotoxin Vc1.1 inhibit colonic nociceptors and provide analgesia in a mouse model of chronic abdominal pain;British Journal of Pharmacology;2018-02-13
4. The Single Disulfide-Directed β-Hairpin Fold. Dynamics, Stability, and Engineering;Biochemistry;2017-05-02
5. Molecular Engineering of Conus Peptides as Therapeutic Leads;Peptides and Peptide-based Biomaterials and their Biomedical Applications;2017
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