6 research outputs found
Ion channel diversity, channel expression and function in the choroid plexuses
Knowledge of the diversity of ion channel form and function has increased enormously over the last 25 years. The initial impetus in channel discovery came with the introduction of the patch clamp method in 1981. Functional data from patch clamp experiments have subsequently been augmented by molecular studies which have determined channel structures. Thus the introduction of patch clamp methods to study ion channel expression in the choroid plexus represents an important step forward in our knowledge understanding of the process of CSF secretion
Ion channel diversity, channel expression and function in the choroid plexuses-0
<p><b>Copyright information:</b></p><p>Taken from "Ion channel diversity, channel expression and function in the choroid plexuses"</p><p>http://www.cerebrospinalfluidresearch.com/content/4/1/8</p><p>Cerebrospinal Fluid Research 2007;4():8-8.</p><p>Published online 20 Sep 2007</p><p>PMCID:PMC2072944.</p><p></p>s, B) 6TMD-1P voltage-gated Kchannels and C) 4TMD-2P twin pore domain Kchannels. Functional channels are a tetramer of α-subunits (or dimer in the case of the 4TMD-2P), arranged so the extracellular P loops form the pore region of the channel. The charged TMD S4 in the 6TMD-1P structure is thought to be involved in the voltage-gating of these channels. Channel gating may also be modified by the presence of auxiliary β-subunits
Ion channel diversity, channel expression and function in the choroid plexuses-1
<p><b>Copyright information:</b></p><p>Taken from "Ion channel diversity, channel expression and function in the choroid plexuses"</p><p>http://www.cerebrospinalfluidresearch.com/content/4/1/8</p><p>Cerebrospinal Fluid Research 2007;4():8-8.</p><p>Published online 20 Sep 2007</p><p>PMCID:PMC2072944.</p><p></p>s, B) 6TMD-1P voltage-gated Kchannels and C) 4TMD-2P twin pore domain Kchannels. Functional channels are a tetramer of α-subunits (or dimer in the case of the 4TMD-2P), arranged so the extracellular P loops form the pore region of the channel. The charged TMD S4 in the 6TMD-1P structure is thought to be involved in the voltage-gating of these channels. Channel gating may also be modified by the presence of auxiliary β-subunits