A new era for understanding amyloid structures and disease

2018/09/20 by M.G. Iadanza, Matthew G. Iadanza, Matthew P. Jackson +3 · 2 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Medicine · Nursing · #Alzheimer's disease #Alzheimer's disease research and treatments #Amyloid (mycology) #Amyloid disease #Amyloid fibril #Amyloid precursor protein #Amyloid β #Amyloidosis #Biochemistry #Biology #Biophysics #Cell biology #Chemistry #Disease #Fibril #Intracellular #Medicine #P3 peptide #Pathology #Prion Diseases and Protein Misfolding #Protein aggregation #Trace Elements in Health

paper · doi:10.1038/s41580-018-0060-8

crossref issued 2018/09/20 · crossref published 2018/09/20 · crossref published-online 2018/09/20 · openalex publication_date 2018/09/20 · crossref created 2018/09/20 · crossref published-print 2018/12/01 · crossref deposited 2023/05/20 · openalex created_date 2025/10/10 · crossref indexed 2026/08/05 · openalex updated_date 2026/08/05

Citations

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• Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy
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• The characterization of soluble amyloid prepared in water
• ATR-FTIR: A “rejuvenated” tool to investigate amyloid proteins
• Structure of the cross-β spine of amyloid-like fibrils
• Aging renders the brain vulnerable to amyloid β-protein neurotoxicity
• Cryo-EM structures of tau filaments from Alzheimer’s disease

Cited by

• Inhibitor-based modulation of huntingtin aggregation mechanisms mitigates fibril-induced cellular stress
• Structural biology [wikipedia]