Use of venom peptides to probe ion channel structure and function

Dutertre, Sébastien and Lewis, Richard J. (2010) Use of venom peptides to probe ion channel structure and function. Journal of Biological Chemistry, 285 18: 13315-13320. doi:10.1074/jbc.R109.076596

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
HERDC_checklist.pdf HERDC checklist – not publicly available application/pdf 60.79KB 1
UQ204978_OA.pdf Full text (open access) application/pdf 2.58MB 0

Author Dutertre, Sébastien
Lewis, Richard J.
Title Use of venom peptides to probe ion channel structure and function
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 2010-04-30
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1074/jbc.R109.076596
Open Access Status File (Publisher version)
Volume 285
Issue 18
Start page 13315
End page 13320
Total pages 6
Editor Herbert Tabor
Place of publication Bethesda, MD, U.S.A.
Publisher American Society for Biochemistry and Molecular Biology
Collection year 2011
Language eng
Formatted abstract
Venoms of snakes, scorpions, spiders, insects, sea anemones, and cone snails are complex mixtures of mostly peptides and small proteins that have evolved for prey capture and/or defense. These deadly animals have long fascinated scientists and the public. Early studies isolated lethal components in the search for cures and understanding of their mechanisms of action. Ion channels have emerged as targets for many venom peptides, providing researchers highly selective and potent molecular probes that have proved invaluable in unraveling ion channel structure and function. This minireview highlights molecular details of their toxin-receptor interactions and opportunities for development of peptide therapeutics.
© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.
Keyword Nicotinic-acetylcholine-receptor
Gated sodium-channels
Alpha-conotoxin binding
D-aspartate receptor
Shaker K+ channel
II voltage sensor
Potassium channel
Calcium-channels
Scorpion toxin
NMDA receptor
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Published under "Minireview".

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Official 2011 Collection
Institute for Molecular Bioscience - Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 69 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 73 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Sun, 09 May 2010, 00:03:44 EST