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Markus Rapedius

Researcher at University of Kiel

Publications -  41
Citations -  1527

Markus Rapedius is an academic researcher from University of Kiel. The author has contributed to research in topics: Gating & Ion channel. The author has an hindex of 20, co-authored 36 publications receiving 1329 citations. Previous affiliations of Markus Rapedius include University of Arizona & Schiller International University.

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KCNJ10 gene mutations causing EAST syndrome (epilepsy, ataxia, sensorineural deafness, and tubulopathy) disrupt channel function.

TL;DR: In summary, EAST mutations of KCNJ10 lead to impaired channel function and structural changes in distal convoluted tubules and the metabolic alkalosis present in patients carrying the R65P mutation possibly improves residual function of KC NJ10, which shows higher activity at alkaline pH.
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A Non-canonical Voltage-Sensing Mechanism Controls Gating in K2P K+ Channels

TL;DR: V voltage-dependent gating is common to most K2P channels and that this voltage sensitivity originates from the movement of three to four ions into the high electric field of an inactive selectivity filter, providing insight into the functional plasticity of a K+-selective filter.
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The pore structure and gating mechanism of K2P channels: K2P channel gating

TL;DR: In this paper, quaternary ammonium (QA) ions bind with high affinity deep within the pore of TREK-1 and have free access to their binding site before channel activation by intracellular pH or pressure.
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The pore structure and gating mechanism of K2P channels

TL;DR: It is reported that quaternary ammonium ions bind with high-affinity deep within the pore of TREK-1 and have free access to their binding site before channel activation by intracellular pH or pressure, demonstrating that, unlike most other K+ channels, the bundle-crossing gate in this K2P channel is constitutively open.

The Pore Structure and Gating Mechanism of K2P Channels

TL;DR: It is reported that quaternary ammonium ions bind with high‐affinity deep within the pore of TREK‐1 and have free access to their binding site before channel activation by intracellular pH or pressure, demonstrating that, unlike most other K+ channels, the bundle‐crossing gate in this K2P channel is constitutively open.