Markus Hanner

TL;DR: The deduced amino acid sequence was structurally unrelated to known mammalian proteins but it shared homology with fungal proteins involved in sterol synthesis, in agreement with the known ability of sigma1-binding sites to interact with steroids, such as progesterone.

TL;DR: Potassium channels represent the largest and most diverse family of ion channels and are postulated to be involved in a variety of physiologic processes, such as control of cell excitability, release of neurotransmitters, secretion of hormones, regulation of fluid secretion, and clonal expansion of cells of the immune system.

TL;DR: The results obtained suggest that oxidation enhances specific voltage-dependent opening transitions and slows the rate-limiting closing transition in the Slo channel, and may represent an important link between cellular electrical excitability and metabolism.

TL;DR: In vivo subunit coassembly provides the structural basis for toxin binding pharmacology and can lead to the association of as many as three distinct channel subunits to form functional K+channels in vivo.

TL;DR: Investigating if sterol C8–C7 isomerase inhibitors are high affinity ligands for the (+)‐[3H]‐pentazocine labelled sigma1‐binding site demonstrates that sigma 1‐binding protein and yeast isomerases are not only structurally but also pharmacologically related.