Two-pore domain potassium channels (K2P) constitute major candidates for the regulation of background potassium currents in mammalian cells. Channels of the TREK subfamily are also well positioned to play an important role in sensory transduction due to their sensitivity to a large number of physiological and physical stimuli (pH, mechanical, temperature). Following our previous report describing the molecular expression of different K2P channels in the vagal sensory system, here we confirm that TREK channels are functionally expressed in neurons from the mouse nodose ganglion (mNG). Neurons were subdivided into three groups (A, Ah and C) based on their response to tetrodotoxin and capsaicin. Application of the TREK subfamily activator rilu...
The emergence of two pore potassium channels as a highly evolved and involved potassium conductance ...
The two-pore-domain potassium (K2P) channel TREK-2 serves to modulate plasma membrane potential in d...
Two-pore-domain K(+) (K(2P)) channel subunits are made up of four transmembrane segments and two por...
Two-pore domain potassium channels (K2P) constitute major candidates for the regulation of backgroun...
Two-pore domain potassium channels (K2P) constitute major candidates for the regulation of backgroun...
Background K2P channels play a key role in stabilizing the resting membrane potential, thereby modul...
Several types of neurons within the central and peripheral somatic nervous system express two-pore-d...
Bradykinin (BK), a hormone inducing pain and inflammation, is known to inhibit potassium M-currents ...
The distribution of two-pore-domain (2P-domain) K+ channels of the TREK subfamily was studied using ...
Recent evidence points to a pivotal contribution of a variety of different potassium channels, inclu...
Background K+ conductances are a major determinant of membrane resting potential and input resistanc...
The ionic mechanisms controlling the resting membrane potential (RMP) in superior cervical ganglion ...
Two-pore domain potassium (K2P) channels are expressed in cells throughout the body and give rise to...
Abstract Leak K+ currents are mediated by two-pore domain K+ (K2P) channels and are involved in cont...
The ionic mechanisms controlling the resting membrane potential (RMP) in superior cervical ganglion ...
The emergence of two pore potassium channels as a highly evolved and involved potassium conductance ...
The two-pore-domain potassium (K2P) channel TREK-2 serves to modulate plasma membrane potential in d...
Two-pore-domain K(+) (K(2P)) channel subunits are made up of four transmembrane segments and two por...
Two-pore domain potassium channels (K2P) constitute major candidates for the regulation of backgroun...
Two-pore domain potassium channels (K2P) constitute major candidates for the regulation of backgroun...
Background K2P channels play a key role in stabilizing the resting membrane potential, thereby modul...
Several types of neurons within the central and peripheral somatic nervous system express two-pore-d...
Bradykinin (BK), a hormone inducing pain and inflammation, is known to inhibit potassium M-currents ...
The distribution of two-pore-domain (2P-domain) K+ channels of the TREK subfamily was studied using ...
Recent evidence points to a pivotal contribution of a variety of different potassium channels, inclu...
Background K+ conductances are a major determinant of membrane resting potential and input resistanc...
The ionic mechanisms controlling the resting membrane potential (RMP) in superior cervical ganglion ...
Two-pore domain potassium (K2P) channels are expressed in cells throughout the body and give rise to...
Abstract Leak K+ currents are mediated by two-pore domain K+ (K2P) channels and are involved in cont...
The ionic mechanisms controlling the resting membrane potential (RMP) in superior cervical ganglion ...
The emergence of two pore potassium channels as a highly evolved and involved potassium conductance ...
The two-pore-domain potassium (K2P) channel TREK-2 serves to modulate plasma membrane potential in d...
Two-pore-domain K(+) (K(2P)) channel subunits are made up of four transmembrane segments and two por...