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Autor:
Maikel C. Rheinstädter, Stine F. Pedersen, Kimmie Gauger, Elena Pedraz-Cuesta, Morten E. Pedersen, Katrine Bugge, Birthe B. Kragelund, Adree Khondker, Ersoy Cholak, Annette Eva Langkilde, Bente Vestergaard, Saskia Bucciarelli
Publikováno v:
The FASEB Journal
Cholak, E, Bugge, K, Khondker, A, Gauger, K, Pedraz-Cuesta, E, Pedersen, M E, Bucciarelli, S, Vestergaard, B, Pedersen, S F, Rheinstädter, M C, Langkilde, A E & Kragelund, B B 2020, ' Avidity within the N-terminal anchor drives α-synuclein membrane interaction and insertion ', FASEB journal : official publication of the Federation of American Societies for Experimental Biology, vol. 34, no. 6, pp. 7462-7482 . https://doi.org/10.1096/fj.202000107R
Cholak, E, Bugge, K, Khondker, A, Gauger, K, Pedraz-Cuesta, E, Pedersen, M E, Bucciarelli, S, Vestergaard, B, Pedersen, S F, Rheinstädter, M C, Langkilde, A E & Kragelund, B B 2020, ' Avidity within the N-terminal anchor drives α-synuclein membrane interaction and insertion ', FASEB journal : official publication of the Federation of American Societies for Experimental Biology, vol. 34, no. 6, pp. 7462-7482 . https://doi.org/10.1096/fj.202000107R
In the brain, α-synuclein (aSN) partitions between free unbound cytosolic and membrane bound forms modulating both its physiological and pathological role and complicating its study due to structural heterogeneity. Here, we use an interdisciplinary,