Alpha-selenoconotoxins, a new class of potent alpha7 neuronal nicotinic receptor antagonists. - Wikidata - wikimedia - TriplyDB

Alpha-selenoconotoxins, a new class of potent alpha7 neuronal nicotinic receptor antagonists.

Alpha-selenoconotoxins, a new class of potent alpha7 neuronal nicotinic receptor antagonists.

http://www.wikidata.org/entity/Q46962955

about

Structure and function of μ-conotoxins, peptide-based sodium channel blockers with analgesic activity Distinct Disulfide Isomers of μ-Conotoxins KIIIA and KIIIB Block Voltage-Gated Sodium Channels Transforming conotoxins into cyclotides: Backbone cyclization of P-superfamily conotoxins Investigation of Elemental Mass Spectrometry in Pharmacology for Peptide Quantitation at Femtomolar Levels High throughput electrophysiology with Xenopus oocytes Alpha-conotoxins as pharmacological probes of nicotinic acetylcholine receptors.μ-conotoxin KIIIA derivatives with divergent affinities versus efficacies in blocking voltage-gated sodium channels.Electrophilic aromatic selenylation: new OPRT inhibitors.Dissecting a role of evolutionary-conserved but noncritical disulfide bridges in cysteine-rich peptides using ω-conotoxin GVIA and its selenocysteine analogs.Oxidative folding and preparation of α-conotoxins for use in high-throughput structure-activity relationship studies.Understanding the structure/activity relationships of the iron regulatory peptide hepcidin.Expanding chemical diversity of conotoxins: peptoid-peptide chimeras of the sodium channel blocker μ-KIIIA and its selenopeptide analogues Synthesis and activity of thioether-containing analogues of the complement inhibitor compstatin.The use of 2,2'-dithiobis(5-nitropyridine) (DTNP) for deprotection and diselenide formation in protected selenocysteine-containing peptides.The Cystine Knot Is Responsible for the Exceptional Stability of the Insecticidal Spider Toxin ω-Hexatoxin-Hv1a High Proteolytic Resistance of Spider-Derived Inhibitor Cystine Knots Tumor-targeted liposomal drug delivery mediated by a diseleno bond-stabilized cyclic peptide.Use of lantibiotic synthetases for the preparation of bioactive constrained peptides Strategies for the development of conotoxins as new therapeutic leads.Integrating the discovery pipeline for novel compounds targeting ion channels.Venoms as a platform for human drugs: translating toxins into therapeutics.Synthetic α-conotoxin mutants as probes for studying nicotinic acetylcholine receptors and in the development of novel drug leads.A chemical method for investigating disulfide-coupled peptide and protein folding.Therapeutic potential of conopeptides.Incorporation of post-translational modified amino acids as an approach to increase both chemical and biological diversity of conotoxins and conopeptides.Peptide ligation chemistry at selenol amino acids.Chemical methods and approaches to the regioselective formation of multiple disulfide bonds.Future of the Genetic Code.Redox-stable cyclic peptide inhibitors of the SPSB2-iNOS interaction.Total Chemical Synthesis of an Intra-A-Chain Cystathionine Human Insulin Analogue with Enhanced Thermal Stability.Enhancing the therapeutic potential of peptide toxins.Rational design of alpha-conotoxin analogues targeting alpha7 nicotinic acetylcholine receptors: improved antagonistic activity by incorporation of proline derivatives.Rapid total synthesis of DARPin pE59 and barnase.Site-specific effects of diselenide bridges on the oxidative folding of a cystine knot peptide, omega-selenoconotoxin GVIA.Evolving tRNA(Sec) for efficient canonical incorporation of selenocysteine.Harnessing selenocysteine reactivity for oxidative protein folding.The Role of Disulfide Bond Replacements in Analogues of the Tarantula Toxin ProTx-II and Their Effects on Inhibition of the Voltage-Gated Sodium Ion Channel Nav1.7.Disulfide-Depleted Selenoconopeptides: a Minimalist Strategy to Oxidative Folding of Cysteine-Rich Peptides.Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency.Reagentless oxidative folding of disulfide-rich peptides catalyzed by an intramolecular diselenide.

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P2860

Alpha-selenoconotoxins, a new class of potent alpha7 neuronal nicotinic receptor antagonists.

http://www.wikidata.org/entity/Q46962955

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2006 nî lūn-bûn

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Alpha-selenoconotoxins, a new ...... icotinic receptor antagonists.

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Christopher J Armishaw

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Paul F Alewood

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Simon T Nevin

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P2860

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

NMR solution structure of alpha-conotoxin ImI and comparison to other conotoxins specific for neuronal nicotinic acetylcholine receptors

Solution structure of alpha-conotoxin ImI by 1H nuclear magnetic resonance

NMR spatial structure of alpha-conotoxin ImI reveals a common scaffold in snail and snake toxins recognizing neuronal nicotinic acetylcholine receptors

Twists, knots, and rings in proteins. Structural definition of the cyclotide framework

Structure determination of the three disulfide bond isomers of alpha-conotoxin GI: a model for the role of disulfide bonds in structural stability

Torsion angle dynamics for NMR structure calculation with the new program DYANA

Human thioredoxin reductase from HeLa cells: selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin

The Cambridge Structural Database: a quarter of a million crystal structures and rising

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