Templating S100A9 amyloids on Aβ fibrillar surfaces revealed by charge detection mass spectrometry,...
Templating S100A9 amyloids on Aβ fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses
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Publisher
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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Contents
The mechanism of amyloid co-aggregation and its nucleation process are not fully understood in spite of extensive studies. Deciphering the interactions between proinflammatory S100A9 protein and Aβ42 peptide in Alzheimer's disease is fundamental since inflammation plays a central role in the disease onset. Here we use innovative charge detection ma...
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Templating S100A9 amyloids on Aβ fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses
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TN_cdi_proquest_journals_2407431966
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2407431966
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E-ISSN
2692-8205
DOI
10.1101/2020.05.26.116400
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https://www.proquest.com/docview/2407431966?pq-origsite=primo&accountid=13902
