Amyloid diseases: abnormal protein aggregation in neurodegeneration - PubMed (original) (raw)

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Amyloid diseases: abnormal protein aggregation in neurodegeneration

E H Koo et al. Proc Natl Acad Sci U S A. 1999.

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Figure 1

Figure 1

Atomic-force microscopy of Aβ1–40 demonstrating assembly of amyloid fibrils from protofibrils. Preincubated Aβ1–40 (100 μM) was seeded with preformed fibrils amounting to ≈1% of the initial Aβ1–40 concentration. The aggregates were analyzed 7 days later. In this image, protofibrils appear as smaller and more flexible aggregates (≈4 nm in height) whereas the amyloid fibrils are substantially longer and more rigid (≈8 nm). (Bar = 200 nm.) [Reproduced with permission from ref. (Copyright 1997).]

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