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α-Conotoxins

open access: yesInternational Journal of Biochemistry and Cell Biology, 2000
Fil: Blanton, Michael P.
Hugo R Arias, Michael P Blanton
exaly   +3 more sources
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Metamorphoses of a Conotoxin

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

Transforming conotoxins into cyclotides: Backbone cyclization of P‐superfamily conotoxins

Peptide Science, 2015
ABSTRACT 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

Conotoxins down under

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

I‐conotoxin superfamily revisited

Journal of Peptide Science, 2006
AbstractThe 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, 2011
The 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

Molecular Engineering of Conotoxins: The Importance of Loop Size to α-Conotoxin Structure and Function

Journal of Medicinal Chemistry, 2008
Alpha-conotoxins are competitive antagonists of nicotinic acetylcholine receptors (nAChRs). The majority of currently characterized alpha-conotoxins have a 4/7 loop size, and the major features of neuronal alpha-conotoxins include a globular disulfide connectivity and a helical structure centered around the third of their four cysteine residues.
Jin, Ai-Hua   +8 more
openaire   +5 more sources

Advances in the synthesis and engineering of conotoxins

European Journal of Medicinal Chemistry
Conotoxins, isolated from the venom of carnivorous marine snails of the Conus genus, are disulfide-rich peptides and proteins with well-defined three-dimensional structures. Conotoxins' ability to target a wide range of ion channels and receptors, including voltage- and ligand-gated ion channels, G protein-coupled receptors, monoamine transporters, and
Thanh Hoa Tran   +2 more
exaly   +5 more sources

THE CHARACTERIZATION OF CONOTOXINS§

Journal of Toxicology: Toxin Reviews, 2000
Conotoxins are peptide toxins synthesized by marine cone snails for both prey entrapment and defense. The peptides, when injected into the prey, cause immobilization and death. Cone snails are widely distributed in tropical waters, their prey includes fish, worms and other marine snails. The peptide toxins have very high specificity and selectivity for
openaire   +1 more source

Conotoxins: Review and Docking Studies to determine potentials of Conotoxin as an Anticancer Drug Molecule

Current Topics in Medicinal Chemistry, 2012
It is known that potassium channels are important for cell proliferation. HERG, a potassium channel protein, is a transmembrane protein, which increases in concentration on the cell surface of cancer cells. Apart from cancer cells, this protein is found only in the brain & heart tissue, in very low number.
Kirtan, Dave, Anasuya, Lahiry
openaire   +2 more sources

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