Results 21 to 30 of about 917,242 (94)

Solution conformation of a neuronal nicotinic acetylcholine receptor antagonist α-conotoxin OmIA that discriminates α3 vs. α6 nAChR subtypes

open access: yes, 2006
α-Conotoxin OmIA from Conus omaria is the only α-conotoxin that shows a ∼20-fold higher affinity to the α3β2 over the α6β2 subtype of nicotinic acetylcholine receptor.
Do-heyoung Kim   +4 more
core   +1 more source

Stability and Structure-Forming Properties of the Two Disulfide Bonds of α-Conotoxin GI

open access: yes, 2016
α-Conotoxin GI is a 13 residue snail toxin peptide cross-linked by Cys2−Cys7 and Cys3−Cys13 disulfide bridges. The formation of the two disulfide bonds by thiol/disulfide exchange with oxidized glutathione (GSSG) has been characterized.
Andreas Kaerner (2140825)   +1 more
core   +1 more source

A novel α-conotoxin, PeIA, cloned from Conus pergrandis, discriminates between Rat α9α10 and α7 nicotinic cholinergic receptors [PDF]

open access: yes, 2005
The α9 and α10 nicotinic cholinergic subunits assemble to form the receptor believed to mediate synaptic transmission between efferent olivocochlear fibers and hair cells of the cochlea, one of the few examples of postsynaptic function for a non-muscle ...
McIntosh, J. Michael   +11 more
core   +1 more source

Structure and Activity of (2,8)-Dicarba-(3,12)-cystino α-ImI, an α-Conotoxin Containing a Nonreducible Cystine Analogue

open access: yes, 2016
The α-conotoxins are potent and selective antagonists of nicotinic acetylcholine receptors (nAChR). Exploitation of these and other peptides in research and clinical settings has been hampered by the lability of the disulfide bridges that are essential ...
Jayamini Illesinghe (2392780)   +7 more
core   +1 more source

Nuclear magnetic resonance solution conformation of α-conotoxin AuIB, an α3β4 subtype-selective neuronal nicotinic acetylcholine receptor antagonist

open access: yes, 2000
The neuronal nicotinic acetylcholine receptors constitute a highly diverse group, with subtypes consisting of pentameric combinations of α and β subunits, α-Conotoxins are a homologous series of small peptides that antagonize these receptors.
K Hun Mok   +5 more
core   +1 more source

Nuclear magnetic resonance solution conformation of α-conotoxin AuIB, an α3ß4 subtype-selective neuronal nicotinic acetylcholine receptor antagonist [PDF]

open access: yes, 2000
journal articleThe neuronal nicotinic acetylcholine receptors constitute a highly diverse group, with subtypes consisting of pentameric combinations of α and ß subunits.
Cho, Jee-Hyun; Mok, K. Hun; Park, Kyu-Hwan; Han, Kyou-Hoon   +1 more
core  

α-Conotoxin dendrimers have enhanced potency and selectivity for homomeric nicotinic acetylcholine receptors

open access: yes, 2015
Covalently attached peptide dendrimers can enhance binding affinity and functional activity. Homogenous di- and tetravalent dendrimers incorporating the α7-nicotinic receptor blocker α-conotoxin ImI (α-ImI) with polyethylene glycol spacers were designed ...
Adams, David J.   +23 more
core   +1 more source

Interactions between the presynaptically active neurotoxins α-latrotoxin and ω-conotoxin GVIA: studies on calcium fluxes and binding parameters in rat and chicken synaptosomes

open access: yes, 1990
Possible interactions between α-latrotoxin, an activator of synaptosomal calcium uptake, and ω-conotoxin GVIA, an inhibitor of voltage-sensitive calcium channels of the N-type, were investigated in rat and chicken synaptosomal preparations.
H. W. Scheer
core   +1 more source

α-Conotoxin AuIB Selectively Blocks α3β4 Nicotinic Acetylcholine Receptors and Nicotine-Evoked Norepinephrine Release

open access: yes, 1998
Neuronal nicotinic acetylcholine receptors (nAChRs) with putative α3β4-subunits have been implicated in the mediation of signaling in various systems, including ganglionic transmission peripherally and nicotine-evoked neurotransmitter release centrally ...
Siqin Luo   +6 more
core   +1 more source

Solution conformation of alpha-conotoxin EI, a neuromuscular toxin specific for the α₁/δ subunit interface of Torpedo nicotinic acetylcholine receptor

open access: yes, 2001
A high resolution structure of α-conotoxin EI has been determined by 1H NMR spectroscopy and molecular modeling. α-Conotoxin EI has the same disulfide framework as α4/7 conotoxins targeting neuronal nicotinic acetylcholine receptors but antagonizes the ...
Jae Eun Suk   +5 more
core   +1 more source

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