Structure of the cross-β spine of amyloid-like fibrils

2005/06/01 by Rebecca A. Nelson, Rebecca Nelson, M.R. Sawaya +6 · 8 citations
Biochemistry, Genetics and Molecular Biology · Medicine · Neuroscience · #Alzheimer's disease research and treatments #Neurological diseases and metabolism #Prion Diseases and Protein Misfolding

paper · doi:10.1038/nature03680

crossref issued 2005/06/01 · crossref published 2005/06/01 · crossref published-print 2005/06/01 · openalex publication_date 2005/06/01 · crossref created 2005/06/09 · openalex created_date 2016/06/24 · crossref deposited 2023/05/18 · crossref indexed 2026/07/31 · openalex updated_date 2026/08/01

Citations

• PROCHECK: a program to check the stereochemical quality of protein structures
• X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS
• Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation

Cited by

• Excited-State Proton Transfer of Photoacids Adsorbed on Biomaterials
• Atomic structures of peptide self-assembly mimics
• Minimalist design of water-soluble cross-β architecture
• The Amyloid State of Proteins in Human Diseases
• Cross-species transmission of CWD prions
• An extensively glycosylated archaeal pilus survives extreme conditions
• High hydrostatic pressure: a probing tool and a necessary parameter in biophysical chemistry
• Beta sheet [wikipedia]