Results 31 to 40 of about 4,686 (201)

Structural and Functional Analyses of Cone Snail Toxins

Marine Drugs, 2019
Cone snails are marine gastropod mollusks with one of the most powerful venoms in nature. The toxins, named conotoxins, must act quickly on the cone snails´ prey due to the fact that snails are extremely slow, reducing their hunting capability ...
Harry Morales Duque, Simoni Campos Dias, Octávio Luiz Franco   +2 more
doaj   +1 more source

Characterization of the Native Disulfide Isomers of the Novel χ-Conotoxin PnID: Implications for Further Increasing Conotoxin Diversity

Marine Drugs, 2023
χ-Conotoxins are known for their ability to selectively inhibit norepinephrine transporters, an ability that makes them potential leads for treating various neurological disorders, including neuropathic pain.
Michael J. Espiritu, Jonathan K. Taylor, Christopher K. Sugai, Parashar Thapa, Nikolaus M. Loening, Emma Gusman, Zenaida G. Baoanan, Michael H. Baumann, Jon-Paul Bingham   +8 more
doaj   +1 more source

Conopeptides from Cape Verde Conus crotchii [PDF]

, 2013
Marine Cone snails of the genus Conus contain complex peptide toxins in their venom. Living in tropical habitats, they usually use the powerful venom for self-defense and prey capture.
Agostinho Antunes, Alexandre Campos, Biass, Cunha, Duda, Hu, Hugo Osório, Jorge Neves, Kalume, Luo, Mcintosh, Olivera, Olivera, Sechi, Vitor Vasconcelos   +14 more
core   +1 more source

µ-Conotoxins Targeting the Human Voltage-Gated Sodium Channel Subtype Na_V1.7

Toxins, 2022
µ-Conotoxins are small, potent, peptide voltage-gated sodium (NaV) channel inhibitors characterised by a conserved cysteine framework. Despite promising in vivo studies indicating analgesic potential of these compounds, selectivity towards the ...
Kirsten L. McMahon, Hue N. T. Tran, Jennifer R. Deuis, David J. Craik, Irina Vetter, Christina I. Schroeder   +5 more
doaj   +1 more source

Conotoxins: Therapeutic Potential and Application

Marine Drugs, 2006
The pharmacological variety of conotoxins, diverse peptides found in the venoms of marine cone snails, is well recognized. Venoms from each of the estimated 500 species of cone snails contain 50 to 200 distinct biologically active peptides.
Richard T. Layer, J. Michael McIntosh
doaj   +1 more source

The 3/4- and 3/6-Subfamily Variants of α-Conotoxins GI and MI Exhibit Potent Inhibitory Activity against Muscular Nicotinic Acetylcholine Receptors

Marine Drugs, 2021
α-Conotoxins GI and MI belong to the 3/5 subfamily of α-conotoxins and potently inhibit muscular nicotinic acetylcholine receptors (nAChRs). To date, no 3/4- or 3/6-subfamily α-conotoxins have been reported to inhibit muscular nAChRs.
Xiaoli Ma, Qiuyuan Huang, Shuo Yu, Shujing Xu, Yue Huang, Zhiming Zhao, Xinrong Xiao, Qiuyun Dai   +7 more
doaj   +1 more source

Hydrophobic residues at position 10 of α-conotoxin PnIA influence subtype selectivity between α7 and α3β2 neuronal nicotinic acetylcholine receptors [PDF]

, 2014
Neuronal nicotinic acetylcholine receptors (nAChRs) are a diverse class of ligand-gated ion channels involved in neurological conditions such as neuropathic pain and Alzheimer's disease.
Adams, David J., Alewood, Paul F., Hogg, Ron C., Hopping, Gene, Lewis, Richard J., Nevin, Simon T., Wang, C-I Anderson   +6 more
core   +1 more source

NMR structure of μ-conotoxin GIIIC : leucine 18 induces local repacking of the N-terminus resulting in reduced NaV channel potency [PDF]

, 2018
mu-Conotoxins are potent and highly specific peptide blockers of voltage-gated sodium channels. In this study, the solution structure of mu-conotoxin GIIIC was determined using 2D NMR spectroscopy and simulated annealing calculations.
Adams, David J, Craik, David J, Dash, Thomas S, Durek, Thomas, Finol-Urdaneta, Rocio K, Harvey, Peta J, Hill, Justine M, Kurniawan, Nyoman D, McArthur, Jeffrey R, Van Lysebetten, Dorien   +9 more
core   +1 more source

Novel conopeptides of the I-superfamily occur in several clades of cone snails [PDF]

, 2004
The I-superfamily of conotoxins represents a new class of peptides in the venom of some Conus species. These toxins are characterized by four disulfide bridges and inhibit or modify ion channels of nerve cells.
Huys, I., Kauferstein, S., Kuch, U., Mebs, D., Melaun, C., Tytgat, J.   +5 more
core   +1 more source

µ-Conotoxins as Leads in the Development of New Analgesics

Molecules, 2010
Voltage-gated sodium channels (VGSCs) contain a specific binding site for a family of cone shell toxins known as µ-conotoxins. As some VGSCs are involved in pain perception and µ-conotoxins are able to block these channels, µ-conotoxins show considerable
Raymond S. Norton
doaj   +1 more source