Nicotinic receptors at the amino acid level.

By P. Corringer, N. Novère, Jean-Pierre Changeux. Annual Review of Pharmacology and Toxicology, 2000

835 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/91c60b706d0ccfcdb11f88fca12fce8a7117b104

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In Cellular and Molecular Neuroscience

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Citations in the corpus

Structure and gating mechanism of the acetylcholine receptor pore (2003, background): “Mutations in the pore domain that would affect gating can be divided into three categories: (1) those that influence the coupling between the M2 helices and the ligandbinding domain; (2) those that influence the side-to-side interactions between the M2 helices; and (3) those in other regions that in”
GABAA Receptors: Subtypes Provide Diversity of Function and Pharmacology (2008, neutral): “…in the agonist binding loops at the b/a interface are homologous in all members of the superfamily (Smith and Olsen, 1995; Sigel and Buhr, 1997; Corringer et al., 2000) and are also homologous to those of the respective ‘‘loops’’ A, B, C, of the aþ and D, E, and F of the g side forming the…”
Molecular structure and function of the glycine receptor chloride channel. (2004, background): “Functional data suggest that nAChR activation is mediated by global intersubunit movements (74).”
International Union of Pharmacology. LXX. Subtypes of γ-Aminobutyric AcidA Receptors: Classification on the Basis of Subunit Composition, Pharmacology, and Function. Update (2008, background): “All members of the superfamily are homologous not only in the domains specifying membrane topology but also at the functional domain level, including ligand binding sites (Sigel and Buhr, 1997; Corringer et al., 2000; Olsen and Sawyer, 2004; Sine and Engel, 2006).”
Molecular and Physiological Diversity of Nicotinic Acetylcholine Receptors in the Midbrain Dopaminergic Nuclei (2001, positive): “We follow the rules currently accepted for assembly of functional nAChR oligomers (for review, see Corringer et al., 2000) and the recommended nomenclature (Lukas et al., 1999).”
Neuronal nicotinic receptors: from structure to pathology. (2004, background): “In heteromeric nAChRs, the principal component is carried by the a2–a4 and a6 subunits with the complementary site carried by the b2 or b4 subunits, whereas each subunit in the homomeric receptors contributes to both the principal and complementary components of the binding site (Changeux and Edelst”
Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors (2001, background): “Each subunit is divided into an N-terminal or ligand-binding domain (LBD), a transmembrane region and an intracellular regio”