@article {156072,
	title = {Protein dynamics and the allosteric transitions of pentameric receptor channels},
	journal = {Biophys Rev},
	volume = {6},
	number = {3-4},
	year = {2014},
	note = {<p>Biophys Rev 2014. 6:311-321. 10.1007/s12551-014-0149-z</p>},
	month = {11/2014},
	pages = {311-321},
	abstract = {<p>The recent application of molecular dynamics (MD) methodology to investigate the allosteric transitions of the acetylcholine receptor and its prokaryotic and eukaryotic pentameric homologs has yielded new insights into the mechanisms of signal transduction by these receptors. Combined with available data on X-ray structures, MD techniques enable description of the dynamics of the conformational change at the atomic level, intra-molecular propagation of this signal transduction mechanism as a concerted stepwise process at physiological timescales and the control of this process by allosteric modulators, thereby offering new perspectives for drug design.</p>},
	keywords = {Acetylcholine receptor, Allosteric interactions, Conformational changes, Molecular dynamics},
	url = {http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4256460/},
	author = {Changeux, J.P.}
}
