Structure-function relationships of the human glycine receptor: Insights from hyperekplexia mutations

Annals of the New York Academy of Sciences

Volumn 868, Issue , 1999, Pages 681-684

  Lewis, Trevor M ^a   Schofield, Peter R ^a  

^a GARVAN INSTITUTE OF MEDICAL RESEARCH   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

CHOLINERGIC RECEPTOR; GLYCINE RECEPTOR; ION CHANNEL; STRYCHNINE;

BRAIN STEM; CONFERENCE PAPER; CONFORMATIONAL TRANSITION; GENE MUTATION; MISSENSE MUTATION; SPINAL CORD; STARTLE EPILEPSY; STARTLE REFLEX; STRUCTURE ACTIVITY RELATION; TORPEDO;

STRYCHNOS TOXIFERA;

EID: 0032971436     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.1999.tb11345.x     Document Type: Conference Paper

References (4)

1. Vafa, B. & P.R. Schofield. 1998. Identification and functional analysis of heritable mutations in the glycine, γ-aminobutyric acid type A and nicotinic acetylcholine receptors provide new insights into the structure and function of the ligand-gated ion channel receptor superfamily. Int. Rev. Neurobiol. 42: 285-332.
2. Lynch, J.W., S. Rajendra, K.D. Pierce, C.A. Handford, P.H. Barry & P.R. Schofield. 1997. Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel. EMBO J. 16: 110-120.
3. Lewis, T.M., L.G. Sivilotti, D. Colquhoun, R.M. Gardiner, R. Schoepfer & M. Rees. 1998. Properties of human glycine receptors containing the hyperekplexia mutation α1(K276E), expressed in Xenopus oocytes. J. Physiol. 507: 25-40.
4. Unwin, N. 1995. Acetylcholine receptor channel imaged in the open state. Nature 373: 37-43.