| Four Turkish families with hyperekplexia: A missense mutation and the exon 1-7 deletion in the GLRA1 gene. | Four Turkish families with hyperekplexia: A missense mutation and the exon 1-7 deletion in the GLRA1 gene.
Tezen D, Şimşir G, Çokar Ö, Demirbilek V, Başak AN, Yapıcı Z. | 12/17/2022 |
| The startle disease mutation alpha1S270T predicts shortening of glycinergic synaptic currents. | The startle disease mutation α1S270T predicts shortening of glycinergic synaptic currents.
Wu Z, Lape R, Jopp-Saile L, O'Callaghan BJ, Greiner T, Sivilotti LG., Free PMC Article | 04/17/2021 |
| A Novel Glycine Receptor Variant with Startle Disease Affects Syndapin I and Glycinergic Inhibition. | A Novel Glycine Receptor Variant with Startle Disease Affects Syndapin I and Glycinergic Inhibition.
Langlhofer G, Schaefer N, Maric HM, Keramidas A, Zhang Y, Baumann P, Blum R, Breitinger U, Strømgaard K, Schlosser A, Kessels MM, Koch D, Qualmann B, Breitinger HG, Lynch JW, Villmann C., Free PMC Article | 10/31/2020 |
| The synthetic cannabinoid dehydroxylcannabidiol restores the function of a major GABAA receptor isoform in a cell model of hyperekplexia. | The synthetic cannabinoid dehydroxylcannabidiol restores the function of a major GABA(A) receptor isoform in a cell model of hyperekplexia.
Zou G, Xia J, Han Q, Liu D, Xiong W., Free PMC Article | 09/12/2020 |
| data implicated that ubiquitin modification of GlyRs-alpha1 represented an important way for peripheral inflammation to reduce spinal glycinergic inhibition and that interference with HUWE1 activity generated analgesic action by resuming GlyRs-alpha1-mediated synaptic transmission. | Ubiquitination and inhibition of glycine receptor by HUWE1 in spinal cord dorsal horn.
Zhang ZY, Guo Z, Li HL, He YT, Duan XL, Suo ZW, Yang X, Hu XD. | 12/28/2019 |
| Study found significant associations between the minor alleles of three SNPs (rs2915885, rs11167557, and rs1428159) within the glycine receptor alpha 1 subunit (GLRA1) and dimensional schizotypy, specifically with the disorganized symptoms dimension. However, there were no significant associations between any of the SNPs and the categorical diagnosis of schizotypal personality disorder. | Dimensional Traits of Schizotypy Associated With Glycine Receptor GLRA1 Polymorphism: An Exploratory Candidate-Gene Association Study.
Vora AK, Fisher AM, New AS, Hazlett EA, McNamara M, Yuan Q, Zhou Z, Hodgkinson C, Goldman D, Siever LJ, Roussos P, Perez-Rodriguez MM., Free PMC Article | 11/23/2019 |
| Data show that the same mutation in GLRA1 could have different phenotypic expressions, suggesting an underling mechanism of variable expressivity, even in the same pedigree. | Clinical features and genetic analysis of two siblings with startle disease in an Italian family: a case report.
Sprovieri T, Ungaro C, Sivo S, Quintiliani M, Contaldo I, Veredice C, Citrigno L, Muglia M, Cavalcanti F, Cavallaro S, Mercuri E, Battaglia D., Free PMC Article | 08/24/2019 |
| Using quantitative photoactivated localisation microscopy the authors found that alpha-1 and alpha-3 containing glycine receptors display the same alpha3:beta2 stoichiometry and gephyrin binding. | Alpha subunit-dependent glycine receptor clustering and regulation of synaptic receptor numbers.
Patrizio A, Renner M, Pizzarelli R, Triller A, Specht CG., Free PMC Article | 05/25/2019 |
| The data of this study demonstrated increased pain sensitivity and impaired central pain modulation in hyperekplexia patients with GLRA1 mutation. | Mutations affecting glycinergic neurotransmission in hyperekplexia increase pain sensitivity.
Vuilleumier PH, Fritsche R, Schliessbach J, Schmitt B, Arendt-Nielsen L, Zeilhofer HU, Curatolo M. | 03/30/2019 |
| results suggest that many extracellular domains are important for GlyR function | Multiple regions in the extracellular domain of the glycine receptor determine receptor activity.
Tang B, Lummis SCR., Free PMC Article | 03/2/2019 |
| Results support the notion that the efficacies of ligands for the alpha1 GlyR are determined by conformational changes that occur within and near the ligand-binding domain: disruption of the D97-R119 interaction may be an important element in receptor activation and that agonists may break this putative intersubunit bond in order to destabilize the initial shut state and facilitate transitions towards the open state. | Disruption of a putative intersubunit electrostatic bond enhances agonist efficacy at the human α1 glycine receptor.
Welsh BT, Todorovic J, Kirson D, Allen HM, Bayly MD, Mihic SJ., Free PMC Article | 08/5/2017 |
| The E103K startle mutation reduces the sensitivity of glycine receptor alpha 1 to both glycine and sarcosine and impairs channel gating. | The Startle Disease Mutation E103K Impairs Activation of Human Homomeric α1 Glycine Receptors by Disrupting an Intersubunit Salt Bridge across the Agonist Binding Site.
Safar F, Hurdiss E, Erotocritou M, Greiner T, Lape R, Irvine MW, Fang G, Jane D, Yu R, Dämgen MA, Biggin PC, Sivilotti LG., Free PMC Article | 06/24/2017 |
| gain-of-function GLRA1 mutations also cause hyperekplexia, although the mechanism is unknown. Here we identify two new gain-of-function mutations (I43F and W170S) and characterize these along with known gain-of-function mutations (Q226E, V280M, and R414H) to identify how they cause hyperekplexia. | Investigating the Mechanism by Which Gain-of-function Mutations to the α1 Glycine Receptor Cause Hyperekplexia.
Zhang Y, Bode A, Nguyen B, Keramidas A, Lynch JW., Free PMC Article | 05/7/2017 |
| GLRA1 and GLRB mutations are responsible for abnormal startled reactions in humans. (Review) | [GLYCINE RECEPTOR: MOLECULAR ORGANIZATION AND PATHOLOGY].
Maleeva GV, Bregestovski PD. | 03/5/2016 |
| in two sisters with hyperekplexia a compound heterozygosis of 2 novel mutations of GLRA1 gene was found - heterozygous for a C-to-G base transition resulting in a phenylalanine to leucine amino acid change in position 235 and for a T-to-C base transition resulting in a cysteine to arginine amino acid change in position 237 | Novel mutations in the glycine receptor alpha subunit gene in two sisters with hyperekplexia.
Ursitti F, Ulgiati F, Papetti L, Nicita F, Lovardi E, Vecchi C, Di Marino V, Bertola F, Spalice A. | 12/12/2015 |
| the TM3-4 loop length is critical for glycine receptor alpha1 desensitization and a direct neighborhood of both basic stretches changes receptor properties from non-desensitizing to desensitizing. | Length of the TM3-4 loop of the glycine receptor modulates receptor desensitization.
Langlhofer G, Janzen D, Meiselbach H, Villmann C. | 10/24/2015 |
| Self-declared ethnicity can predict gene-screening outcomes. Cultural practices influence the inheritance patterns and a Caucasian founder is postulated for R271 mutations. | Ethnicity can predict GLRA1 genotypes in hyperekplexia.
Thomas RH, Drew CJ, Wood SE, Hammond CL, Chung SK, Rees MI. | 05/16/2015 |
| Mutations in the GLRA1 were identified in 16 Japanese patients with hyperekplexia. | Clinical and genetic investigation of 17 Japanese patients with hyperekplexia.
Mine J, Taketani T, Yoshida K, Yokochi F, Kobayashi J, Maruyama K, Nanishi E, Ono M, Yokoyama A, Arai H, Tamaura S, Suzuki Y, Otsubo S, Hayashi T, Kimura M, Kishi K, Yamaguchi S. | 05/16/2015 |
| Data indicate that alpha1Q-26'E-containing glycine receptors have longer active periods and lower conductances. | Correlating structural and energetic changes in glycine receptor activation.
Scott S, Lynch JW, Keramidas A., Free PMC Article | 05/16/2015 |
| The first X-ray structure of the TMD of the alpha1GlyR solved here using GLIC as a scaffold paves the way for mechanistic investigation and design of allosteric modulators of a human receptor. | Allosteric and hyperekplexic mutant phenotypes investigated on an α1 glycine receptor transmembrane structure.
Moraga-Cid G, Sauguet L, Huon C, Malherbe L, Girard-Blanc C, Petres S, Murail S, Taly A, Baaden M, Delarue M, Corringer PJ., Free PMC Article | 05/9/2015 |
| In GlyRA1 mutants, a portion of them can be transported to the plasma membrane but don't form funtional channels; a possible cause for hyperekplexia. | Disturbed neuronal ER-Golgi sorting of unassembled glycine receptors suggests altered subcellular processing is a cause of human hyperekplexia.
Schaefer N, Kluck CJ, Price KL, Meiselbach H, Vornberger N, Schwarzinger S, Hartmann S, Langlhofer G, Schulz S, Schlegel N, Brockmann K, Lynch B, Becker CM, Lummis SC, Villmann C., Free PMC Article | 03/21/2015 |
| Comparison of glycine-mediated conformational changes in the extracellular M2-M3 domain finds significantly different structures between GlyR alpha3 and GlyR alpha1 isoforms. | Phosphorylation of α3 glycine receptors induces a conformational change in the glycine-binding site.
Han L, Talwar S, Wang Q, Shan Q, Lynch JW., Free PMC Article | 05/31/2014 |
| Conformation and function of the human GLRA1 chloride channel. | Open-channel structures of the human glycine receptor α1 full-length transmembrane domain.
Mowrey DD, Cui T, Jia Y, Ma D, Makhov AM, Zhang P, Tang P, Xu Y., Free PMC Article | 05/17/2014 |
| Analysis of hyperekplexia mutations identifies transmembrane domain rearrangements that mediate glycine receptor activation. | Analysis of hyperekplexia mutations identifies transmembrane domain rearrangements that mediate glycine receptor activation.
Bode A, Lynch JW., Free PMC Article | 02/8/2014 |
| p.E375X truncated subunits are incorporated into functional hGlyRs together with unmutated alpha1 or alpha1 plus beta subunits. | New hyperekplexia mutations provide insight into glycine receptor assembly, trafficking, and activation mechanisms.
Bode A, Wood SE, Mullins JGL, Keramidas A, Cushion TD, Thomas RH, Pickrell WO, Drew CJG, Masri A, Jones EA, Vassallo G, Born AP, Alehan F, Aharoni S, Bannasch G, Bartsch M, Kara B, Krause A, Karam EG, Matta S, Jain V, Mandel H, Freilinger M, Graham GE, Hobson E, Chatfield S, Vincent-Delorme C, Rahme JE, Afawi Z, Berkovic SF, Howell OW, Vanbellinghen JF, Rees MI, Chung SK, Lynch JW., Free PMC Article | 02/8/2014 |