Combinatorial mutations in loops D and F strongly influence responses of the α7 nicotinic acetylcholine receptor to imidacloprid

Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors

Katjuša Brejc, Willem J. van Dijk, Remco V. Klaassen et al. · Nature · 2001 · 1.8K citations

Life Sciences, Biophysics, Molecular Biology +17

MMFF VI. MMFF94s option for energy minimization studies

Thomas A. Halgren · Journal of Computational Chemistry · 1999 · 1.2K citations

Natural Sciences, Biophysics, Chemistry +14

A neuronal nicotinic acetylcholine receptor subunit (α7) is developmentally regulated and forms a homo-oligomeric channel blocked by α-BTX

S. Couturier, Daniel Bertrand, Jean‐Marc Matter et al. · Neuron · 1990 · 934 citations · Full text

Life Sciences, Neurobiology, Neuroscience +13

α9: An acetylcholine receptor with novel pharmacological properties expressed in rat cochlear hair cells

Ana B. Elgoyhen, David S. Johnson, Jim Boulter et al. · Cell · 1994 · 889 citations

Life Sciences, Neuroscience, Pharmacology +16

MMFF VII. Characterization of MMFF94, MMFF94s, and other widely available force fields for conformational energies and for intermolecular-interaction energies and geometries

Thomas A. Halgren · Journal of Computational Chemistry · 1999 · 719 citations

Natural Sciences, Biophysics, Chemistry +13