In Vitro Analyses of Novel HCN4 Gene Mutations

Autor: Melina Möller, Nicole Silbernagel, Eva Wrobel, Birgit Stallmayer, Elsie Amedonu, Susanne Rinné, Stefan Peischard, Sven G. Meuth, Bernhard Wünsch, Nathalie Strutz-Seebohm, Niels Decher, Eric Schulze-Bahr, Guiscard Seebohm

Publikováno v: Cellular Physiology and Biochemistry, Vol 49, Iss 3, Pp 1238-1248 (2018)

Background/Aims: The hyperpolarization-activated cyclic nucleotide-gated cation channel HCN4 contributes significantly to the generation of basic cardiac electrical activity in the sinus node and is a mediator of modulation by β–adrenergic stimula

Externí odkaz: https://doaj.org/article/aea5423fac8c48d99316e6c83049191e

Structural interplay of KV7.1 and KCNE1 is essential for normal repolarization and is compromised in short QT syndrome 2 (KV7.1-A287T)

Autor: Ina Rothenberg, PhD, Ilaria Piccini, PhD, Eva Wrobel, PhD, Birgit Stallmeyer, PhD, Jovanca Müller, MD, Boris Greber, PhD, Nathalie Strutz-Seebohm, PhD, Eric Schulze-Bahr, MD, Nicole Schmitt, PhD, Guiscard Seebohm, PhD

Publikováno v: HeartRhythm Case Reports, Vol 2, Iss 6, Pp 521-529 (2016)

Externí odkaz: https://doaj.org/article/4c26f8f9dc8347bd90dc911ca0158446

A benzodiazepine activator locks K

Autor: Julian A, Schreiber, Melina, Möller, Mark, Zaydman, Lu, Zhao, Zachary, Beller, Sebastian, Becker, Nadine, Ritter, Panpan, Hou, Jingyi, Shi, Jon, Silva, Eva, Wrobel, Nathalie, Strutz-Seebohm, Niels, Decher, Nicole, Schmitt, Sven G, Meuth, Martina, Düfer, Bernhard, Wünsch, Jianmin, Cui, Guiscard, Seebohm

Publikováno v: Communications biology. 5(1)

Loss-of-function mutations in K

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::887806817ade2c0976cacfab4bb80d12
https://pubmed.ncbi.nlm.nih.gov/35365746

Structural basis of PI(4,5)P2-dependent regulation of GluA1 by phosphatidylinositol-5-phosphate 4-kinase, type II, alpha (PIP5K2A)

Autor: Fabian Hertel, Michael Pusch, Eric Schulze-Bahr, Nathalie Strutz-Seebohm, Lutz Pott, Markus Dicks, Veronika Matschke, Jan Terhag, Guiscard Seebohm, Ina Rothenberg, Florian Lang, Michael Hollmann, Eva Wrobel, Oana N. Ursu, Raphael Stoll

Publikováno v: Pflügers Archiv 466 (2014): 1885–1897. doi:10.1007/s00424-013-1424-8
info:cnr-pdr/source/autori:Seebohm, Guiscard; Wrobel, Eva; Pusch, Michael; Dicks, Markus; Terhag, Jan; Matschke, Veronika; Rothenberg, Ina; Ursu, Oana N.; Hertel, Fabian; Pott, Lutz; Lang, Florian; Schulze-Bahr, Eric; Hollmann, Michael; Stoll, Raphael; Strutz-Seebohm, Nathalie/titolo:Structural basis of PI(4,5)P-2-dependent regulation of GluA1 by phosphatidylinositol-5-phosphate 4-kinase, type II, alpha (PIP5K2A)/doi:10.1007%2Fs00424-013-1424-8/rivista:Pflügers Archiv/anno:2014/pagina_da:1885/pagina_a:1897/intervallo_pagine:1885–1897/volume:466
Pflugers Archiv

Ionotropic glutamate receptors are the most important excitatory receptors in the central nervous system, and their impairment can lead to multiple neuronal diseases. Here, we show that glutamate-induced currents in oocytes expressing GluA1 are incre

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87f0f26c808eae95328f6c12b747b2ff
https://doi.org/10.1007/s00424-013-1424-8

KCNE1 induces fenestration in the Kv7.1/KCNE1 channel complex that allows for highly specific pharmacological targeting

Autor: Karina Eckey, Tao Yang, Christoph Krisp, Ina Rothenberg, Dan M. Roden, Nathalie Strutz-Seebohm, Michael Pusch, Eric Schulze-Bahr, Harley T. Kurata, Joannes T. M. Linders, Rob Towart, Dirk Wolters, Guiscard Seebohm, Eva Wrobel, Benjamin Fraenzel, Lutz Pott, Franziska Hundt, David J. Gallacher

Publikováno v: Nature communications 7 (2016). doi:10.1038/ncomms12795
info:cnr-pdr/source/autori:Wrobel E, Rothenberg I, Krisp C, Hundt F, Fraenzel B, Eckey K, Linders JT, Gallacher DJ, Towart R, Pott L, Pusch M, Yang T, Roden DM, Kurata HT, Schulze-Bahr E, Strutz-Seebohm N, Wolters D, Seebohm G/titolo:KCNE1 induces fenestration in the Kv7.1%2FKCNE1 channel complex that allows for highly specific pharmacological targeting/doi:10.1038%2Fncomms12795/rivista:Nature communications/anno:2016/pagina_da:/pagina_a:/intervallo_pagine:/volume:7
Nature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
Nature Communications

Most small-molecule inhibitors of voltage-gated ion channels display poor subtype specificity because they bind to highly conserved residues located in the channel's central cavity. Using a combined approach of scanning mutagenesis, electrophysiology

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a7b21cbf9257e48ed4bd20e6d4cb4ee
http://www.scopus.com/inward/record.url?eid=2-s2.0-84991508551&partnerID=q2rCbXpz