Nicotine and Carbamylcholine Binding to Nicotinic Acetylcholine Receptors as Studied in AChBP Crystal Structures

doi:10.1016/S0896-6273(04)00115-1

Paper

Nicotine and Carbamylcholine Binding to Nicotinic Acetylcholine Receptors as Studied in AChBP Crystal Structures

Published Mar 25, 2004 · P. Celie, S. E. V. Rossum-fikkert, W. Dijk

Neuron

Q1 SJR score

784

Citations

61

Influential Citations

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Abstract

Abstract hidden due to publisher request; this does not indicate any issues with the research. Click the full text link above to read the abstract and view the original source.

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Study Snapshot

Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors is driven by enthalpy and accompanied by conformational changes, providing valuable tools for developing new drugs for nicotinic receptor-associated diseases.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

Nicotine and Carbamylcholine Binding to Nicotinic Acetylcholine Receptors as Studied in AChBP Crystal Structures

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References

Citations

Conformational dynamics of a nicotinic receptor neurotransmitter site

The low-to-high affinity conformational change at the Torpedo - nicotinic receptor neurotransmitter site involves rotation of the agonist, downward displacement of loop C, and formation of a stable high-affinity pocket.

Tabernanthalog and ibogainalog inhibit the α7 and α9α10 nicotinic acetylcholine receptors via different mechanisms and with higher potency than the GABAA receptor and CaV2.2 channel.

Tabernanthalog and ibogainalog effectively inhibit nicotinic acetylcholine receptors (nAChRs) through noncompetitive and competitive mechanisms, with higher potency than the GABAA receptor and CaV2.2 channel.

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The spiroimine core of marine macrocyclic toxins is sufficient to bind to nicotinic acetylcholine receptors, dictating antagonism and determining receptor-subtype selectivity.

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The LEXSY system effectively expresses the receptor-binding domain of SARS-CoV-2 and the acetylcholine-binding protein from Lymnaea stagnalis, providing valuable tools for research and medical purposes.

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