Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
Upon ligand binding at the subunit interfaces, the extracellular domain of the nicotinic
acetylcholine receptor undergoes conformational changes, and agonist binding …
acetylcholine receptor undergoes conformational changes, and agonist binding …
[PDF][PDF] Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
SB Hansen, G Sulzenbacher, T Huxford… - The EMBO …, 2005 - researchgate.net
Nicotinic acetylcholine receptors (nAChRs) are well-characterized transmembrane allosteric
proteins involved in rapid gating of ions elicited by acetylcholine. They belong to the 'Cys …
proteins involved in rapid gating of ions elicited by acetylcholine. They belong to the 'Cys …
[引用][C] Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive bin
SB Hansen, G Sulzenbacher, T Huxford, P Marchot… - EMBO J., 2005 - osti.gov
Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal
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Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
SB Hansen, G Sulzenbacher, T Huxford… - The EMBO …, 2005 - embopress.org
Upon ligand binding at the subunit interfaces, the extracellular domain of the nicotinic
acetylcholine receptor undergoes conformational changes, and agonist binding …
acetylcholine receptor undergoes conformational changes, and agonist binding …
Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
SB Hansen, G Sulzenbacher, T Huxford… - The EMBO …, 2005 - pubmed.ncbi.nlm.nih.gov
Upon ligand binding at the subunit interfaces, the extracellular domain of the nicotinic
acetylcholine receptor undergoes conformational changes, and agonist binding …
acetylcholine receptor undergoes conformational changes, and agonist binding …
Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
SB Hansen, G Sulzenbacher, T Huxford, P Marchot… - EMBO Journal, 2005 - hal.science
Upon ligand binding at the subunit interfaces, the extracellular domain of the nicotinic
acetylcholine receptor undergoes conformational changes, and agonist binding …
acetylcholine receptor undergoes conformational changes, and agonist binding …
[引用][C] Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
SB HANSEN - EMBO J., 2006 - cir.nii.ac.jp
Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal
distinctive binding interfaces and conformations | CiNii Research CiNii 国立情報学研究所 …
distinctive binding interfaces and conformations | CiNii Research CiNii 国立情報学研究所 …
[HTML][HTML] Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
SB Hansen, G Sulzenbacher, T Huxford… - The EMBO …, 2005 - ncbi.nlm.nih.gov
Upon ligand binding at the subunit interfaces, the extracellular domain of the nicotinic
acetylcholine receptor undergoes conformational changes, and agonist binding …
acetylcholine receptor undergoes conformational changes, and agonist binding …
Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations.
SB Hansen, G Sulzenbacher, T Huxford… - The EMBO …, 2005 - europepmc.org
Upon ligand binding at the subunit interfaces, the extracellular domain of the nicotinic
acetylcholine receptor undergoes conformational changes, and agonist binding …
acetylcholine receptor undergoes conformational changes, and agonist binding …
Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
SB Hansen, G Sulzenbacher, T Huxford, P Marchot… - EMBO Journal, 2005 - hal.science
Upon ligand binding at the subunit interfaces, the extracellular domain of the nicotinic
acetylcholine receptor undergoes conformational changes, and agonist binding …
acetylcholine receptor undergoes conformational changes, and agonist binding …