@article {187,
	title = {Towards improved acetylcholinesterase inhibitors: a structural and computational approach},
	journal = {Mini reviews in medicinal chemistry},
	volume = {1},
	year = {2001},
	month = {2001/09//},
	pages = {255 - 266},
	abstract = {During the last years, solving the X-ray crystallographic structure of both the unliganded acetylcholinesterase (AChE) and AChE complexes with various inhibitors has provided valuable knowledge of the interactions that mediate inhibitor binding. This structural information allows us to rationalize differences in binding affinities for related analogues, and more importantly opens new strategies to design compounds with improved pharmacological properties. This is illustrated in the case of the recently reported huprines, which are a new class of very potent and selective acetylcholinesterase inhibitors.},
	keywords = {Acetylcholinesterase/chemistry; Alzheimer Disease/drug therapy; Animals; Cholinesterase Inhibitors/chemical synthesis/chemistry/therapeutic use; Computational Biology/methods; Drug Design; Humans; Models, Molecular; Protein Conformation; Structure-Activity Relationship; Torpedo},
	author = {Barril, Xavier and M. Orozco and F. J. Luque}
}
