Shedding Light on Alzheimer's β‐Amyloid Aggregation with Chemical Tools | Zendy

Kapurniotu Aphrodite | Zendy

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Shedding Light on Alzheimer's β‐Amyloid Aggregation with Chemical Tools

Author(s) -

Kapurniotu Aphrodite

Publication year - 2012

Publication title -

chembiochem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.05

H-Index - 126

eISSN - 1439-7633

pISSN - 1439-4227

DOI - 10.1002/cbic.201100631

Subject(s) - fibril , amyloid (mycology) , peptide , biophysics , chemistry , amyloid fibril , p3 peptide , fluorescence , in vitro , amyloid β , β amyloid , alzheimer's disease , biochemistry , amyloid precursor protein , biology , disease , medicine , pathology , inorganic chemistry , physics , quantum mechanics

Early steps in self‐assembly: Kelly and co‐workers have presented a fluorescence‐based assay system that differentially detects the early oligomers and fibrils formed by the Alzheimer's disease β‐amyloid peptide, Aβ, and provided evidence that in vitro Aβ amyloidogenesis proceeds through a nucleated conformational conversion of nonfibrillar oligomers into amyloid fibrils.

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