Heparin induces α-synuclein to form new fibril polymorphs with attenuated neuropathology
Cited by 63
Related Papers
Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
|Nature Communications|2019|225
Cryo-EM structure of full-length α-synuclein amyloid fibril with Parkinson’s disease familial A53T mutation
|Cell Research|2020|149
Parkinson’s disease associated mutation E46K of α-synuclein triggers the formation of a distinct fibril structure
|Nature Communications|2020|141
Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion
|Nature Communications|2022|49