Direct Observation of Anisotropy-Driven Formation of Amyloid Protein Core-Shell Structures in Real-t...
Direct Observation of Anisotropy-Driven Formation of Amyloid Protein Core-Shell Structures in Real-time by Super-resolution Microscopy
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Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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English
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Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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Abstract Proteins misfolding and aggregation in the form of fibrils or amyloid containing spherulite-like structures, are involved in a spectrum of degenerative diseases. Current understanding of protein aggregation mechanism primarily relies on conventional spectrometric methods reporting the average growth rates and microscopy readouts of final s...
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Direct Observation of Anisotropy-Driven Formation of Amyloid Protein Core-Shell Structures in Real-time by Super-resolution Microscopy
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TN_cdi_proquest_journals_2564147851
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2564147851
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DOI
10.1101/2021.08.20.457097
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https://www.proquest.com/docview/2564147851?pq-origsite=primo&accountid=13902
