Sommer, Anselm ; Kordowski, Felix ; Büch, Joscha ; Maretzky, Thorsten 
; Evers, Astrid ; Andrä, Jörg ; Düsterhöft, Stefan ; Michalek, Matthias ; Lorenzen, Inken ; Somasundaram, Prasath ; Tholey, Andreas ; Sönnichsen, Frank D. ; Kunzelmann, Karl ; Heinbockel, Lena ; Nehls, Christian ; Gutsmann, Thomas ; Grötzinger, Joachim ; Bhakdi, Sucharit ; Reiss, Karina
; Evers, Astrid ; Andrä, Jörg ; Düsterhöft, Stefan ; Michalek, Matthias ; Lorenzen, Inken ; Somasundaram, Prasath ; Tholey, Andreas ; Sönnichsen, Frank D. ; Kunzelmann, Karl ; Heinbockel, Lena ; Nehls, Christian ; Gutsmann, Thomas ; Grötzinger, Joachim ; Bhakdi, Sucharit ; Reiss, Karina 
Zusammenfassung
ADAM17, a prominent member of the 'Disintegrin and Metalloproteinase' (ADAM) family, controls vital cellular functions through cleavage of transmembrane substrates. Here we present evidence that surface exposure of phosphatidylserine (PS) is pivotal for ADAM17 to exert sheddase activity. PS exposure is tightly coupled to substrate shedding provoked by diverse ADAM17 activators. PS dependency is ...
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