Conformational Changes in the Lower Palm Domain of ASIC1a Contribute to Desensitization and RFamide Modulation

@article{Frey2013ConformationalCI,
  title={Conformational Changes in the Lower Palm Domain of ASIC1a Contribute to Desensitization and RFamide Modulation},
  author={E. Frey and R. Pavlovicz and Clem John Wegman and C. Li and C. Askwith},
  journal={PLoS ONE},
  year={2013},
  volume={8}
}
Acid-sensing ion channel 1a (ASIC1a) is a proton-gated cation channel that contributes to fear and pain as well as neuronal damage following persistent cerebral acidosis. Neuropeptides can affect acid-induced neuronal injury by altering ASIC1a inactivation and/or steady-state desensitization. Yet, exactly how ASIC1a inactivation and desensitization occur or are modulated by peptides is not completely understood. We found that regions of the extracellular palm domain and the β11-12 linker are… Expand
17 Citations
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References

SHOWING 1-10 OF 66 REFERENCES
Asn415 in the β11-β12 Linker Decreases Proton-dependent Desensitization of ASIC1
Gating Transitions in the Palm Domain of ASIC1a*
Endogenous Arginine-Phenylalanine-Amide-related Peptides Alter Steady-state Desensitization of ASIC1a*
Alternative Splicing and Interaction with Di- and Polyvalent Cations Control the Dynamic Range of Acid-sensing Ion Channel 1 (ASIC1)*
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3
4
5
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