Interleukin‐11 (IL‐11) receptor cleavage by the rhomboid protease RHBDL2 induces IL‐11 trans‐signaling
Lydia Koch(Christian-Albrechts-Universität zu Kiel), Christoph Garbers(Christian-Albrechts-Universität zu Kiel)
Cited by 34
Related Papers
Inhibition of Classic Signaling Is a Novel Function of Soluble Glycoprotein 130 (sgp130), Which Is Controlled by the Ratio of Interleukin 6 and Soluble Interleukin 6 Receptor
|Journal of Biological Chemistry|2011|206
Proteolytic Origin of the Soluble Human IL-6R In Vivo and a Decisive Role of N-Glycosylation
|PLoS Biology|2017|133
Cleavage Site Localization Differentially Controls Interleukin-6 Receptor Proteolysis by ADAM10 and ADAM17
|Scientific Reports|2016|95
Activation of Toll-like Receptor 2 (TLR2) induces Interleukin-6 trans-signaling
|Scientific Reports|2019|64
Cathepsin S provokes interleukin-6 (IL-6) trans-signaling through cleavage of the IL-6 receptor in vitro
|Scientific Reports|2020|25