Solid State NMR Reveals a pH-dependent Antiparallel β-Sheet Registry in Fibrils Formed by a β-Amyloid Peptide
- 2 January 2004
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 335 (1), 247-260
- https://doi.org/10.1016/j.jmb.2003.10.044
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Constraints on Supramolecular Structure in Amyloid Fibrils from Two-Dimensional Solid-State NMR Spectroscopy with Uniform Isotopic LabelingJournal of the American Chemical Society, 2003
- Insights into the Amyloid Folding Problem from Solid-State NMRBiochemistry, 2003
- Supramolecular Structural Constraints on Alzheimer's β-Amyloid Fibrils from Electron Microscopy and Solid-State Nuclear Magnetic ResonanceBiochemistry, 2002
- Supramolecular Structure in Full-Length Alzheimer's β-Amyloid Fibrils: Evidence for a Parallel β-Sheet Organization from Solid-State Nuclear Magnetic ResonanceBiophysical Journal, 2002
- Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrilsProceedings of the National Academy of Sciences of the United States of America, 2000
- Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMRBiochemistry, 2000
- Structure of the β-Amyloid(10-35) FibrilJournal of the American Chemical Society, 2000
- Two-Dimensional Structure of β-Amyloid(10−35) FibrilsBiochemistry, 2000
- Propagating structure of Alzheimer’s β-amyloid (10–35) is parallel β-sheet with residues in exact registerProceedings of the National Academy of Sciences of the United States of America, 1998
- From the globular to the fibrous state: protein structure and structural conversion in amyloid formationQuarterly Reviews of Biophysics, 1998