Jon Lindstrom

TL;DR: Correlation of the fractional occupancy of ligand binding sites by cobratoxin with inhibition of receptor function is used to demonstrate that in the reconstituted system the doubly liganded acetylcholine receptor prevails in controlling channel gating.

TL;DR: The concept that receptors from the electric organs of several species and probably also from muscle share a similarly complex subunit structure is supported, indicating the presence of an unexpected structural similarity in receptor from eel.

TL;DR: Crystallography and cryo-electron-microscopy are providing increasing insights into the structures and functions of AChRs, however, much remains to be learned about both AChR structure and function, the in vivo functional roles of some A ChR subtypes, and the development of better pharmacological tools directed at A ChRs to treat addiction, pain, inflammation, and other medically important issues.

TL;DR: It is demonstrated that after reduction with dithiothreitol (DTT) the AChRs can be specifically labelled with the acetylcholine‐binding site directed reagent 4‐(N‐maleimido)benzyltri [3H]methylammonium iodide, suggesting that although neuronal nicotinic ACh Rs have some structural homologies to AChR from muscle and electric organs, the A chRs from these sources are quite distant relatives in

TL;DR: In this work, matrix-assisted laser desorption ionization time-of-flight tandem mass spectrometry is used to uncover protein interactions of the intracellular loop of the β2 subunit and components of immunoprecipitated β2–nAChR complexes from mouse brain and suggest a link between nAChRs and cellular G protein pathways.