Ontology highlight
ABSTRACT:
SUBMITTER: Yagi-Utsumi M
PROVIDER: S-EPMC7293247 | biostudies-literature | 2020
REPOSITORIES: biostudies-literature
Yagi-Utsumi Maho M Yanaka Saeko S Song Chihong C Satoh Tadashi T Yamazaki Chiaki C Kasahara Haruo H Shimazu Toru T Murata Kazuyoshi K Kato Koichi K
NPJ microgravity 20200612
Amyloid fibrils are self-assembled and ordered proteinaceous supramolecules structurally characterized by the cross-β spine. Amyloid formation is known to be related to various diseases typified by neurogenerative disorders and involved in a variety of functional roles. Whereas common mechanisms for amyloid formation have been postulated across diverse systems, the mesoscopic morphology of the fibrils is significantly affected by the type of solution condition in which it grows. Amyloid formatio ...[more]