Results 41 to 50 of about 4,719 (211)
Bioactive Marine Drugs and Marine Biomaterials for Brain Diseases [PDF]
, 2014 Marine invertebrates produce a plethora of bioactive compounds, which serve as inspiration for marine biotechnology, particularly in drug discovery programs and biomaterials development.
Andrade, Paula B. +3 more
core +2 more sources
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 +7 more
doaj +1 more source
Rationally designed α-conotoxin analogues maintained analgesia activity and weakened side effects [PDF]
, 2019 A lack of specificity is restricting the further application of conotoxin from Conus bullatus (BuIA). In this study, an analogue library of BuIA was established and virtual screening was used, which identified high α7 nicotinic acetylcholine receptor ...
Gao, Xinmei +9 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
Conotoxin Prediction: New Features to Increase Prediction Accuracy
Toxins, 2023 Conotoxins are toxic, disulfide-bond-rich peptides from cone snail venom that target a wide range of receptors and ion channels with multiple pathophysiological effects. Conotoxins have extraordinary potential for medical therapeutics that include cancer,
Lyman K. Monroe +8 more
doaj +1 more source
Differential Cav2.1 and Cav2.3 channel inhibition by baclofen and α-conotoxin Vc1.1 via GABAB receptor activation [PDF]
, 2014 Neuronal Ca(v)2.1 (P/Q-type), Ca(v)2.2 (N-type), and Ca(v)2.3 (R-type) calcium channels contribute to synaptic transmission and are modulated through G protein-coupled receptor pathways. The analgesic. alpha-conotoxin Vc1.1 acts through.
Adams, David J. +4 more
core +1 more source
Less is more: Design of a highly stable disulfide-deleted mutant of analgesic cyclic alpha-conotoxin Vc1.1 [PDF]
, 2015 Cyclic alpha-conotoxin Vc1.1 (cVc1.1) is an orally active peptide with analgesic activity in rat models of neuropathic pain. It has two disulfide bonds, which can have three different connectivities, one of which is the native and active form.
Adams, D +7 more
core +3 more sources
The T-superfamily of Conotoxins [PDF]
Journal of Biological Chemistry, 1999 Nous rapportons la découverte et la caractérisation initiale de la super-famille T des conotoxines. Huit peptides différents de la superfamille T de cinq espèces de Conus ont été identifiés ; ils partagent une séquence de signal consensuelle et un arrangement conservé de résidus de cystéine (- -CC- -CC-).
Colin Walker +12 more
openaire +2 more sources
Identification and Characterization of a Novel Family of Cysteine-Rich Peptides (MgCRP-I) from Mytilus galloprovincialis [PDF]
, 2015 We report the identification of a novel gene family (named MgCRP-I) encoding short secreted cysteine-rich peptides in the Mediterranean mussel Mytilus galloprovincialis.
Benincasa, Monica +12 more
core +2 more sources
Conotoxins that Confer Therapeutic Possibilities [PDF]
Marine Drugs, 2012 Cone snails produce a distinctive repertoire of venom peptides that are used both as a defense mechanism and also to facilitate the immobilization and digestion of prey. These peptides target a wide variety of voltage- and ligand-gated ion channels, which make them an invaluable resource for studying the properties of these ion channels in normal and ...
Magbubah Essack +2 more
openaire +4 more sources