Two distinct amyloid beta-protein (Abeta) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology, and toxicity analyses.

@article{Matsumura2011TwoDA,
  title={Two distinct amyloid beta-protein (Abeta) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology, and toxicity analyses.},
  author={Satoko Matsumura and Keiko Shinoda and Mayumi Yamada and Satoshi Yokojima and Masafumi Inoue and Takayuki Ohnishi and Tetsuya Shimada and Kazuya Kikuchi and Dai Masui and Shigeki Hashimoto and Michio Sato and Akane Ito and Manami Akioka and Shinsuke Takagi and Yoshihiro Nakamura and Kiyokazu Nemoto and Yutaka Hasegawa and Hisayoshi Takamoto and Haruo Inoue and Shinichiro Nakamura and Yo-ichi Nabeshima and David B Teplow and Masataka Kinjo and Minako M Hoshi},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 13},
  pages={11555-62}
}
Nonfibrillar assemblies of amyloid β-protein (Aβ) are considered to play primary roles in Alzheimer disease (AD). Elucidating the assembly pathways of these specific aggregates is essential for understanding disease pathogenesis and developing knowledge-based therapies. However, these assemblies cannot be monitored in vivo, and there has been no reliable in vitro monitoring method at low protein concentration. We have developed a highly sensitive in vitro monitoring method using fluorescence… CONTINUE READING

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