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Torsten K. Roepke

Researcher at Charité

Publications -  31
Citations -  2558

Torsten K. Roepke is an academic researcher from Charité. The author has contributed to research in topics: KCNE2 & Potassium channel. The author has an hindex of 17, co-authored 31 publications receiving 2393 citations. Previous affiliations of Torsten K. Roepke include Cornell University & Max Delbrück Center for Molecular Medicine.

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Human cardiovascular progenitor cells develop from a KDR + embryonic-stem-cell-derived population

TL;DR: Analysis of the development of the cardiovascular lineages in human embryonic stem cell differentiation cultures identifies a human cardiovascular progenitor that defines one of the earliest stages of human cardiac development.
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The KCNE2 potassium channel ancillary subunit is essential for gastric acid secretion

TL;DR: It is demonstrated that KCNE2 is essential for gastric acid secretion, the first genetic evidence that a member of the KCNE gene family is required for normal gastrointestinal function.
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Kcne2 deletion uncovers its crucial role in thyroid hormone biosynthesis

TL;DR: It is shown that the potassium channel subunits KCNQ1 and KCNE2 form a thyroid-stimulating hormone–stimulated, constitutively active, thyrocyte K+ channel required for normal thyroid hormone biosynthesis.
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Calcium-sensing receptor abrogates secretagogue- induced increases in intestinal net fluid secretion by enhancing cyclic nucleotide destruction.

TL;DR: The authors showed that colonic CaSR signaling stimulates the degradation of cyclic nucleotides by phosphodiesterases and described the ability of receptor activation to reverse the fluid and electrolyte secretory actions of cAMP-and cGMP-generating secretagogues, including cholera toxin and heat stable Escherichia coli enterotoxin STa.
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Targeted deletion of kcne2 impairs ventricular repolarization via disruption of I(K,slow1) and I(to,f).

TL;DR: Targeted disruption of kcne2 has revealed a novel cardiac partner for MiRP1, a novel role for MiRPs in α subunit targeting in vivo, and a role forMiRP1 in murine ventricular repolarization with parallels to that proposed for the human heart.