anti-Glycine Receptor (GRD) Antibodies

Human Glycine Receptor (GRD) interaction partners

1. 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.

2. GLRB variants are associated with etiopathogenesis of fear and anxiety disorders.

3. A genome-wide significant association was found between ACQ and single non-coding nucleotide variants of the GLRB gene (rs78726293, P = 3.3 x 10 - 8; rs191260602, P = 3.9 x 10- 8).GLRB gene expression was found to be modulated by rs7688285 in brain tissue, as well as cell culture.

4. Whole-exome sequencing in ASD patients from each family identified a second rare inherited genetic variant, affecting GLRB expressed in inhibitory or in excitatory synapses.

5. GLRA1 and GLRB mutations are responsible for abnormal startled reactions in humans. (Review)

6. The N-terminal region of GABRA3 and the GlyR beta subunit occupies the same binding site of gephyrin.

7. We report novel GLRB mutations in hyperekplexia

8. p.E375X truncated subunits are incorporated into functional hGlyRs together with unmutated alpha1 or alpha1 plus beta subunits.

9. Systematic DNA sequencing of GLRB in individuals with hyperekplexia revealed new missense mutations in GLRB, resulting in M177R, L285R and W310C substitutions.

10. This study describes the definitive assignment of GLRB as the third major gene for hyperekplexia and impacts on the genetic stratification and biological causation of this neonatal/paediatric disorder.

11. investigated neural progenitor cells in respect to their glycine receptor function and subunit expression using electrophysiology, calcium imaging, immunocytochemistry, and quantitative real-time PCR

12. Distinct properties of glycine receptor beta+/alpha- interface: unambiguously characterizing heteromeric interface reconstituted in homomeric protein.

13. This study presents a large family with Hereditary hyperekplexia (HH) as a result of homozygous mutation in GLRB.

14. Hereditary hyperekplexia-causing mutations that modify alpha1 beta GlyR channel function are almost exclusively located in the alpha1 to the exclusion of the beta subunit.

15. The authors have identified a protein kinase C (PKC) phosphorylation site within the cytoplasmic domain of the beta-subunit of the GlyR (residue S403) that causes a reduction of the binding affinity between the receptor and gephyrin.

16. proton modulation of glycine receptor function is determined by extracellular domain in both the alpha1 and beta subunits

17. Stoichiometry of recombinant heteromeric glycine receptors revealed by a pore-lining region point mutation

18. Report interaction of androsterone and progesterone with inhibitory ligand-gated ion channels: a patch clamp study.