Outlines of the pore in open and closed conformations describe the gating mechanism of ASIC1

Asp433in the closing gate of ASIC1 determines stability of the open state without changing properties of the selectivity filter or Ca2+block

(2011) Tianbo Li et al.   JOURNAL OF GENERAL PHYSIOLOGY

Ion selectivity in channels and transporters

(2011) Benoît Roux et al.   JOURNAL OF GENERAL PHYSIOLOGY

Two residues in the extracellular domain convert a nonfunctional ASIC1 into a proton-activated channel

(2010) Tianbo Li et al.   AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY

Pore architecture and ion sites in acid-sensing ion channels and P2X receptors

(2009) Eric B. Gonzales et al.   NATURE

Crystal structure of the ATP-gated P2X4 ion channel in the closed state

(2009) Toshimitsu Kawate et al.   NATURE

Gating the pore of P2X receptor channels

(2008) Mufeng Li et al.   NATURE NEUROSCIENCE