A novel hyperekplexia-causing mutation in the pre-transmembrane segment 1 of the human glycine receptor alpha1 subunit reduces membrane expression and impairs gating by agonists.
about
The impact of human hyperekplexia mutations on glycine receptor structure and functionGlycine receptor mouse mutants: model systems for human hyperekplexiaPore conformations and gating mechanism of a Cys-loop receptor.Subunit symmetry at the extracellular domain-transmembrane domain interface in acetylcholine receptor channel gating.A unified view of the role of electrostatic interactions in modulating the gating of Cys loop receptors.Establishing an ion pair interaction in the homomeric rho1 gamma-aminobutyric acid type A receptor that contributes to the gating pathway.Contributions of conserved residues at the gating interface of glycine receptors.Activation and desensitization induce distinct conformational changes at the extracellular-transmembrane domain interface of the glycine receptorCharacterization of two mutations, M287L and Q266I, in the α1 glycine receptor subunit that modify sensitivity to alcohols.Incompatibility between a pair of residues from the pre-M1 linker and Cys-loop blocks surface expression of the glycine receptorCharge and geometry of residues in the loop 2 β hairpin differentially affect agonist and ethanol sensitivity in glycine receptorsCross-linking of sites involved with alcohol action between transmembrane segments 1 and 3 of the glycine receptor following activationRoles for loop 2 residues of alpha1 glycine receptors in agonist activation.Mechanisms of homomeric alpha1 glycine receptor endocytosisLoop 2 structure in glycine and GABA(A) receptors plays a key role in determining ethanol sensitivity.The structural basis of function in Cys-loop receptors.Synaptic neurotransmitter-gated receptorsAn outline of desensitization in pentameric ligand-gated ion channel receptors.Additional acetylcholine (ACh) binding site at alpha4/alpha4 interface of (alpha4beta2)2alpha4 nicotinic receptor influences agonist sensitivity.The pre-M1 segment of the alpha1 subunit is a transduction element in the activation of the GABAA receptor.Role of aspartate 298 in mouse 5-HT3A receptor gating and modulation by extracellular Ca2+.Acetylcholine receptor gating at extracellular transmembrane domain interface: the "pre-M1" linker.Principal pathway coupling agonist binding to channel gating in nicotinic receptors.A missense mutation A384P associated with human hyperekplexia reveals a desensitization site of glycine receptors.Impaired Glycine Receptor Trafficking in Neurological Diseases
P2860
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P2860
A novel hyperekplexia-causing mutation in the pre-transmembrane segment 1 of the human glycine receptor alpha1 subunit reduces membrane expression and impairs gating by agonists.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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name
A novel hyperekplexia-causing ...... nd impairs gating by agonists.
@en
A novel hyperekplexia-causing ...... nd impairs gating by agonists.
@nl
type
label
A novel hyperekplexia-causing ...... nd impairs gating by agonists.
@en
A novel hyperekplexia-causing ...... nd impairs gating by agonists.
@nl
prefLabel
A novel hyperekplexia-causing ...... nd impairs gating by agonists.
@en
A novel hyperekplexia-causing ...... nd impairs gating by agonists.
@nl
P2093
P2860
P50
P356
P1476
A novel hyperekplexia-causing ...... and impairs gating by agonists
@en
P2093
Antonio Pascotto
Emanuele Miraglia Del Giudice
Giulia Bellini
James R Trudell
Maurizio Taglialatela
Neil L Harrison
Pasqualina Castaldo
Patrizia Stefanoni
P2860
P304
25598-25604
P356
10.1074/JBC.M311021200
P407
P577
2004-04-05T00:00:00Z