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GRD encodes the beta subunit of the glycine receptor, which is a pentamer composed of alpha and beta subunits.
Showing 5 out of 5 products:
Human Polyclonal GRD Primary Antibody for IHC (fro), WB - ABIN361432
Beckstead, Phelan, Mihic: Antagonism of inhalant and volatile anesthetic enhancement of glycine receptor function. in The Journal of biological chemistry 2001
Show all 7 references for ABIN361432
Rat (Rattus) Polyclonal GRD Primary Antibody for WB - ABIN306940
Fischer, Kneussel, Tintrup, Haverkamp, Rauen, Betz, Wässle: Reduced synaptic clustering of GABA and glycine receptors in the retina of the gephyrin null mutant mouse. in The Journal of comparative neurology 2000
Show all 6 references for ABIN306940
GLRA1 (show GLRA1 Antibodies) and GLRB (show GLRB Antibodies) mutations are responsible for abnormal startled reactions in humans. (Review)
The N-terminal region of GABRA3 (show GABRA3 Antibodies) and the GlyR beta subunit (show POLG Antibodies) occupies the same binding site of gephyrin (show GPHN Antibodies).
We report novel GLRB (show GLRB Antibodies) mutations in hyperekplexia
Systematic DNA sequencing of GLRB (show GLRB Antibodies) in individuals with hyperekplexia revealed new missense mutations in GLRB (show GLRB Antibodies), resulting in M177R, L285R and W310C substitutions.
This study describes the definitive assignment of GLRB (show GLRB Antibodies) as the third major gene for hyperekplexia and impacts on the genetic stratification and biological causation of this neonatal/paediatric disorder.
investigated neural progenitor cells in respect to their glycine receptor (show GLRB Antibodies) function and subunit expression using electrophysiology, calcium imaging, immunocytochemistry, and quantitative real-time PCR
Distinct properties of glycine receptor beta (show GLRB Antibodies)+/alpha- interface: unambiguously characterizing heteromeric interface reconstituted in homomeric protein.
This study presents a large family with Hereditary hyperekplexia (HH) as a result of homozygous mutation in GLRB (show GLRB Antibodies).
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 (show POLG Antibodies).
The authors have identified a protein kinase C (PKC (show PKC Antibodies)) phosphorylation site within the cytoplasmic domain of the beta-subunit (show POLG Antibodies) of the GlyR (residue S403) that causes a reduction of the binding affinity between the receptor and gephyrin (show GPHN Antibodies).
This gene encodes the beta subunit of the glycine receptor, which is a pentamer composed of alpha and beta subunits. The receptor functions as a neurotransmitter-gated ion channel, which produces hyperpolarization via increased chloride conductance due to the binding of glycine to the receptor. Mutations in this gene cause startle disease, also known as hereditary hyperekplexia or congenital stiff-person syndrome, a disease characterized by muscular rigidity. Alternative splicing results in multiple transcript variants.
glycine receptor 58 kDa subunit
, glycine receptor subunit beta
, glycine receptor, beta subunit