The molecular basis of the structure and function of the 5-HT 3 receptor: a model ligand-gated ion channel (Review)

@article{Reeves2002TheMB,
  title={The molecular basis of the structure and function of the 5-HT 3 receptor: a model ligand-gated ion channel (Review)},
  author={D. C. Reeves and S. Lummis},
  journal={Molecular Membrane Biology},
  year={2002},
  volume={19},
  pages={11 - 26}
}
  • D. C. Reeves, S. Lummis
  • Published 2002
  • Chemistry, Medicine
  • Molecular Membrane Biology
  • The ligand-gated ion channel superfamily of neurotransmitter receptors are proteins responsible for rapid transmission of nerve impulses at the synapse and have, therefore, been the subject of intensive research for many years. The cys-loop family, of which the 5-HT3 receptor is a member, includes the nicotinic acetylcholine receptor, the GABAA receptor and the glycine receptor. A diverse range of endogenous and artificial ligands activate these receptors, but, nevertheless, the family shares… CONTINUE READING
    177 Citations
    The 5-HT3 receptor as a therapeutic target
    • 202
    • PDF
    The structural basis of function in Cys-loop receptors.
    • 253
    • PDF
    GABAA receptor structure-function studies: a reexamination in light of new acetylcholine receptor structures.
    • M. Akabas
    • Chemistry, Medicine
    • International review of neurobiology
    • 2004
    • 51
    The 5-HT3 Receptor
    • 14
    Characterization of the Ligand-binding Site of the Serotonin 5-HT3 Receptor
    • 31
    • PDF
    5-HT3 receptors.
    • 98

    References

    SHOWING 1-10 OF 230 REFERENCES
    Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • 1,613
    • Highly Influential
    • PDF
    Assigning functions to residues in the acetylcholine receptor channel region (review).
    • 9
    The selectivity of the channel coupled to the 5-HT3 receptor
    • 89
    • Highly Influential
    Evolutionary history of the ligand-gated ion-channel superfamily of receptors
    • 535
    • Highly Influential
    • PDF
    Mutations in the channel domain alter desensitization of a neuronal nicotinic receptor
    • 487
    The Pharmacological and Functional Characteristics of the Serotonin 5-HT3A Receptor Are Specifically Modified by a 5-HT3B Receptor Subunit*
    • 263
    • PDF