Christoph Korbmacher

Friedrich-Alexander-Universität Erlangen-Nürnberg — Germany

Biochemistry, Genetics and Molecular Biology · Life Sciences

46h-index5.9kcitations205works1.62yr avg
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Research Topics

Ion Transport and Channel Regulation(88), Ion channel regulation and function(76), Electrolyte and hormonal disorders(26), Ion Channels and Receptors(15), Neuroscience and Neuropharmacology Research(13)

Publications201 total

Differential modulation of polycystin-2 gain-of-function channels by cysteine-reactive compounds, amphiphilic substances, and S4-S5 linker mutations
Journal of Biological Chemistry·2025Open Access
Acute activation of human epithelial sodium channel (ENaC) by serum and glucocorticoid inducible kinase 1 (SGK1) requires prior cleavage of the channel’s γ-subunit at its proximal cleavage site
Pflügers Archiv - European Journal of Physiology·2025Open Access
Ion channel function of polycystin‐2/polycystin‐1 heteromer revealed by structure‐guided mutagenesis
FEBS Letters·2025· 1 citedOpen Access
Automated patch-clamp recordings for detecting activators and inhibitors of the epithelial sodium channel (ENaC)
Pflügers Archiv - European Journal of Physiology·2025Open Access
Author response for "Ion channel function of polycystin‐2/polycystin‐1 heteromer revealed by structure‐guided mutagenesis"
2025
Ion channel function of polycystin-2/polycystin-1 heteromer revealed by structure-guided mutagenesis
2024Open Access
Transmembrane Serine Protease 2 and Proteolytic Activation of the Epithelial Sodium Channel in Mouse Kidney
Journal of the American Society of Nephrology·2024· 7 citedOpen Access
Electrophysiological Analysis of a Gain-of-Function Polycystin-1/Polycystin-2 Ion Channel
Journal of the American Society of Nephrology·2024
Disease-associated missense mutations in the pore loop of polycystin-2 alter its ion channel function in a heterologous expression system
Journal of Biological Chemistry·2024· 7 citedOpen Access
Activation of the Human Epithelial Sodium Channel (ENaC) by the Peptidomimetic S3969 Involves a Specific Binding Pocket in the Channel’s β-Subunit
Physiology·2024
The small molecule activator S3969 stimulates the epithelial sodium channel by interacting with a specific binding pocket in the channel's β-subunit
Journal of Biological Chemistry·2024· 3 citedOpen Access
In mouse kidney endogenous transmembrane serine protease 2 (TMPRSS2) contributes to proteolytic processing and activation of the epithelial sodium channel (ENaC)
Physiology·2023
Funktion und Interaktion von Zellen
Physiologie·2023· 1 cited
Lipophilic Methanethiosulfonate (MTS) Reagents Inhibit Ion Channel Function of Polycystin-2 With a Gain-of-Function Mutation (F604P)
Journal of the American Society of Nephrology·2022
Electrophysiological Characterization of Polycystin-2 Mutants With Disease-Associated Missense Mutations in the Channel's Pore Loop
Journal of the American Society of Nephrology·2022
Regulation of distal tubule sodium transport: mechanisms and roles in homeostasis and pathophysiology
Pflügers Archiv - European Journal of Physiology·2022· 47 citedOpen Access
Correction to: Two adjacent phosphorylation sites in the C-terminus of the channel’s α-subunit have opposing effects on epithelial sodium channel (ENaC) activity
Pflügers Archiv - European Journal of Physiology·2022· 1 citedOpen Access
Two adjacent phosphorylation sites in the C-terminus of the channel’s α-subunit have opposing effects on epithelial sodium channel (ENaC) activity
Pflügers Archiv - European Journal of Physiology·2022· 6 citedOpen Access
Transmembrane serine protease 2 (TMPRSS2) proteolytically activates the epithelial sodium channel (ENaC) by cleaving the channel’s γ-subunit
Journal of Biological Chemistry·2022· 24 citedOpen Access
Epithelialer Natriumkanal (ENaC) im distalen Nephron
Der Nephrologe·2022
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Frequent Co-authors

Silke Haerteis(13), Marko Bertog(11), Nigel W. Bunnett(7), Bettina Krueger(6), Alexei Diakov(6), R. D. Rauh(5), John E. Cuffe(4), Viatcheslav Nesterov(4), Jan‐Peter Koch(4), Angelos-Aristeidis Konstas(4), Michael Wiederholt(4), TinaMarie Lieu(3), Peishen Zhao(3), Dane D. Jensen(3), Matteus Krappitz(3), Johannes Loffing(3), B. Letz(3), Andreas Bielfeld‐Ackermann(3), A S Segal(3), Emile L. Boulpaep(3)