Results 161 to 170 of about 21,330 (214)
<i>PIONOCONUS</i>: A PISCIVOROUS SUBGENUS OF <i>CONUS</i> GASTROPODS. [PDF]
Watkins M +6 more
europepmc +1 more source
Conotoxins: Chemistry and Biology [PDF]
The venom of the marine predatory cone snails (genus Conus) has evolved for prey capture and defense, providing the basis for survival and rapid diversification of the now estimated 750+ species. A typical Conus venom contains hundreds to thousands of bioactive peptides known as conotoxins.
Ai-Hua Jin +7 more
openaire +4 more sources
α-Conotoxin OmIA from Conus omaria is the only α-conotoxin that shows a ∼20-fold higher affinity to the α3β2 over the α6β2 subtype of nicotinic acetylcholine receptor.
Seung-Wook Chi +2 more
exaly +2 more sources
Influence of ω-conotoxin on morphine analgesia and withdrawal syndrome in rats
The effect of ω-conotoxin on opiate analgesia and withdrawal syndrome was investigated in rats. ω-Conotoxin given i.c.v. and i.p. caused weak analgesia in the tail-flick test. When the toxin (20 ng/rat) was given i.c.v.
Daniela Parolaro +2 more
exaly +2 more sources
Background: The venoms of Conus snails contain small, disulfide-rich inhibitors of voltage-dependent sodium channels. Conotoxin GS is a 34-residue polypeptide isolated from Conus geographus that interacts with the extracellular entrance of skeletal ...
Paul F Alewood, David J Craik
exaly +2 more sources
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1996
Venom is a mixture of various substances produced in a specific gland in the body of the venomous animal and introduced through a piercing injecting mechanism into the body of another animal in order to paralyze it or to kill it. In nature, venoms are employed by slow predatory animals in order to capture through an immediate paralysis their relatively
E, Zlotkin +3 more
openaire +2 more sources
Venom is a mixture of various substances produced in a specific gland in the body of the venomous animal and introduced through a piercing injecting mechanism into the body of another animal in order to paralyze it or to kill it. In nature, venoms are employed by slow predatory animals in order to capture through an immediate paralysis their relatively
E, Zlotkin +3 more
openaire +2 more sources
Transforming conotoxins into cyclotides: Backbone cyclization of P‐superfamily conotoxins
Peptide Science, 2015ABSTRACT Peptide backbone cyclization is a widely used approach to improve the activity and stability of small peptides but until recently it had not been applied to peptides with multiple disulfide bonds. Conotoxins are disulfide‐rich conopeptides derived from the venoms of cone snails that have applications in drug design and ...
Akcan, Muharrem +9 more
openaire +5 more sources
Toxicon, 2006
In the four decades since toxinologists in Australia and elsewhere started to investigate the active constituents of venomous cone snails, a wealth of information has emerged on the various classes of peptides and proteins that make their venoms such potent bioactive cocktails.
Raymond S, Norton, Baldomero M, Olivera
openaire +2 more sources
In the four decades since toxinologists in Australia and elsewhere started to investigate the active constituents of venomous cone snails, a wealth of information has emerged on the various classes of peptides and proteins that make their venoms such potent bioactive cocktails.
Raymond S, Norton, Baldomero M, Olivera
openaire +2 more sources
I‐conotoxin superfamily revisited
Journal of Peptide Science, 2006AbstractThe I‐conotoxin superfamily (I‐Ctx) is known to have four disulfide bonds with the cysteine arrangement C‐C‐CC‐CC‐C‐C, and the members inhibit or modify ion channels of nerve cells. Recently, Olivera and co‐workers (FEBS J. 2005; 272: 4178–4188) have suggested that the previously described I‐Ctx should now be divided into two different gene ...
Gough, Julie; id_orcid 0000-0002-1270-0616 +4 more
openaire +3 more sources
Engineering of Conotoxins for the Treatment of Pain
Current Pharmaceutical Design, 2011The peptides present in the venoms of marine snails are used by the snails to capture prey, but they have also attracted the interest of drug designers because of their potent activity against therapeutically important targets. These peptides are typically disulfiderich and target a wide range of ion channels, transporters and receptors with exquisite ...
Carstens, Bodil B. +5 more
openaire +5 more sources

