Results 51 to 60 of about 21,330 (214)
The Journal of Physiology, EarlyView.Abstract figure legend Stac2 adaptor protein is expressed in neurons and endocrine cells. Using a global Stac2 knockout mouse model here we investigated the role of endogenous Stac2 in adrenal gland mouse chromaffin cell (MCC) excitability and catecholamine vesicle exocytosis.
Stefanie M. Geisler +6 more
wiley +1 more source
Interaction of ω-conotoxin and the membrane calcium transport system of Escherichia coli
, 2000 ω-Conotoxin, a calcium channel blocker, inhibits chemotaxis by Escherichia coli. To test whether ω-conotoxin acts at the cytoplasmic membrane, the kinetics of 125I-ω-conotoxin binding was investigated.
Tisa, Louis S.
core +1 more source
Discovery Methodology of Novel Conotoxins from Conus Species
Marine Drugs, 2018 Cone snail venoms provide an ideal resource for neuropharmacological tools and drug candidates discovery, which have become a research hotspot in neuroscience and new drug development. More than 1,000,000 natural peptides are produced by cone snails, but
Ying Fu +5 more
doaj +1 more source
Diversity of Conopeptides and Their Precursor Genes of Conus Litteratus
Marine Drugs, 2020 The venom of various Conus species is composed of a rich variety of unique bioactive peptides, commonly referred to as conotoxins (conopeptides). Most conopeptides have specific receptors or ion channels as physiologically relevant targets. In this paper,
Xinjia Li +3 more
doaj +1 more source
Toxins, 2021 Venoms are complex mixtures of proteins that have evolved repeatedly in the animal kingdom. Cone snail venoms represent one of the best studied venom systems.
Samuel Abalde +2 more
doaj +1 more source
Pharmacological Inhibition of Cav2.2 Channels by Recombinant Phα1β Toxin (CTK01512‐2)
Basic &Clinical Pharmacology &Toxicology, Volume 139, Issue 2, August 2026.The recombinant Phα1β toxin (CTK01512‐2) partially and reversibly inhibits Cav2.2 calcium channels in HEK‐293 cells. CTK01512‐2 displays dose‐dependent inhibition of N‐type calcium currents, with an IC50 of 3.94 nM. In vivo, CTK01512‐2 effectively reduces mechanical allodynia in a neuropathic pain model, confirming its antinociceptive activity ...
Natália Virtude Carobin +5 more
wiley +1 more source
The M-superfamily of conotoxins: a review [PDF]
Cellular and Molecular Life Sciences, 2009 The focus of this review is the M-superfamily of Conus venom peptides. Disulfide rich peptides belonging to the M-superfamily have three loop regions and the cysteine arrangement: CC-C-C-CC, where the dashes represent loops one, two, and three, respectively.
Jacob, Reed B., McDougal, Owen M.
openaire +3 more sources
Research into the Bioengineering of a Novel α-Conotoxin from the Milked Venom of Conus obscurus
, 2022 The marine cone snail produces one of the fastest prey strikes in the animal kingdom. It injects highly efficacious venom, often causing prey paralysis and death within seconds.
Sean Wiere +19 more
core +1 more source
Chronic Pain: Epidemiology, Pathophysiology, and Clinical Management
MedComm, Volume 7, Issue 5, May 2026.The multidimensional nature of chronic pain is illustrated through four interconnected domains. (Left) Epidemiology and Global Burden: Chronic pain affects approximately one in five individuals globally, contributing to a rising trend in disability‐adjusted life years (YLDs) and a significant socioeconomic impact.
Zhihao Shang +12 more
wiley +1 more source
A Structure‐Informed Atlas of Venom‐Derived Peptides Reveals the Organization of Chemical Space
Molecular Informatics, Volume 45, Issue 5, May 2026.A structure‐informed atlas integrating sequence and AlphaFold‐derived features across 3,423 venom peptides reveals that chemical space is organized by disulfide‐stabilized compactness and electrostatic–hydrophobic balance, with functional classes clearly separated and convergent design principles overriding taxonomic origin.
Thaís Caroline Gonçalves +2 more
wiley +1 more source