Browse our anti-GLRA1 (GLRA1) Antibodies

Human Glycine Receptor, alpha 1 (GLRA1) interaction partners

1. The E103K startle mutation reduces the sensitivity of glycine receptor alpha 1 to both glycine and sarcosine and impairs channel gating.

2. 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.

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

4. 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

5. the TM3 (show TPM1 Antibodies)-4 loop length is critical for glycine receptor (show GLRB Antibodies) alpha1 desensitization and a direct neighborhood of both basic stretches changes receptor properties from non-desensitizing to desensitizing.

6. Mutations in the GLRA1 were identified in 16 Japanese patients with hyperekplexia.

7. The first X-ray structure of the TMD (show TTN Antibodies) 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.

8. 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.

9. Conformation and function of the human GLRA1 chloride channel (show CLCA1 Antibodies).

10. Analysis of hyperekplexia mutations identifies transmembrane domain rearrangements that mediate glycine receptor (show GLRB Antibodies) activation.

Zebrafish Glycine Receptor, alpha 1 (GLRA1) interaction partners

Mouse (Murine) Glycine Receptor, alpha 1 (GLRA1) interaction partners

1. Glra1 receptor Beta8-Beta9 loop is an essential regulator of conformational rearrangements in ion channel opening and closing.

2. Mutation of a zinc-binding residue in the glycine receptor (show GLRB Antibodies) alpha1 changes ethanol sensitivity in vitro and alcohol consumption in Glra1(D80A) knock-in mice.

3. TM3 (show TPM1 Antibodies)-4 loop subdomains are important for functional reconstitution of glycine receptors by independent domains

4. Mutations in the GlyR alpha-1 subunit, M287L and Q266I, resulted in a small but general impairment of glycine action, that is most evident in the glycine-induced maximal currents.

5. Mutations in the GlyR alpha-1 subunit, M287L and Q266I, decreased specific behavioral actions of ethanol and altered other nonethanol behaviors, demonstrating the importance of GlyR function in diverse neuronal systems.

6. The values of breathing frequency, tidal volume, and minute ventilation in newborn Glra1-deficient oscillator mice decrease rapidly during postnatal development.

7. The new Glra1 mutation appears to affect glycine's inhibitory neurotransmission in the central nervous system (CNS) of the nmf11 homozygotes, which suffer from a severe startle disease-related phenotype and die by postnatal day 21.

8. Thus, the hyperekplexia phenotype of Glra1(D80A) mice is due to the loss of Zn(2+) potentiation of alpha1 subunit containing GlyRs (show GARS Antibodies), indicating that synaptic Zn(2+) is essential for proper in vivo functioning of glycinergic neurotransmission.

9. These results show that insulin (show INS Antibodies) has a novel regulatory action on the potency of glycine for ionotropic glycine receptors.