Structural analysis of Alzheimer's beta(1-40) amyloid: protofilament assembly of tubular fibrils.
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Summary
It is reported here that the birefringence of a small drop of peptide solution can supply information related to the cooperative packing of amyloid fibers and their capacity for magnetic orientation.
- Type
- article
- Published
- 1998-01-01
- Cited by
- 236
- References
- 42
- Access
- Open access
- OpenAlex
- https://openalex.org/W2008966525
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:23059689
Keywords
Amyloid fibril, Fibril, Amyloid (mycology), Amyloid β, Chemistry
References
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- Analysis of circular dichroism spectra.
- Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease. Analysis of circular dichroism spectra.
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- Solution structures of beta peptide and its constituent fragments: relation to amyloid deposition.
- "Cross-beta" conformation in proteins.
- Diamagnetic anisotropy of the peptide group.
- Formation of an infinite beta-sheet arrangement dominates the crystallization behavior of lambda-type antibody light chains.
- Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction.
- Deconvolution of disoriented fiber diffraction data using iterative convolution and local regression.
- Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic beta-protein fragments.
- Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro.
- Folding and function of the myelin proteins from primary sequence data
- The Diamagnetic Anisotropy of Aromatic Molecules
- pH-dependent structural transitions of Alzheimer amyloid peptides.
- New triple-helical model for the shaft of the adenovirus fibre.
- X-ray scattering from a discrete helix with cumulative angular and translational disorders.
- Scavenger receptor-mediated adhesion of microglia to β-amyloid fibrils
- RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
- Structural changes in transthyretin produced by the Ile 84 Ser mutation which result in decreased affinity for retinol-binding protein
Cited by
- Fibers of tau fragments, but not full length tau, exhibit a cross β‐structure: Implications for the formation of paired helical filaments
- The Contribution of Microscopy to the Study of Alzheimer’s Disease, Amyloid Plaques and Aβ Fibrillogenesis
- The effect of fluorescent labeling on α-synuclein fibril morphology.
- Structural Biology of PrP Prions.
- Multi-strand β-sheet of Alzheimer Aβ(1–40) folds to β-strip helix: implication for protofilament formation
- Solid-state nuclear magnetic resonance techniques for structural studies of amyloid fibrils.
- Modeling and Docking Studies of Anti-Anyloid Antibodies WOL and WOZ
- Cholesterol in Alzheimer's disease and other amyloidogenic disorders.
- X-ray fibre diffraction studies of amyloid fibrils.
- Potential covalent modification of amyloid-beta protein and its effect on aggregation
- Aggregated Beta Amyloid Peptide 1–40 Decreases Ca2+- and Cholinergic Receptor-Mediated Phosphoinositide Degradation by Alteration of Membrane and Cytosolic Phospholipase C in Brain Cortex
- TATA binding protein in Alzheimer's Disease
- Biophysical studies of the development of amyloid fibrils from a peptide fragment of cold shock protein B.
- Purification of polyglutamine proteins.
- Alzheimer's beta-amyloid: insights into fibril formation and structure from Congo red binding.
- Structural models of amyloid-like fibrils.
- Visualizing pathology deposits in the living brain of patients with Alzheimer's disease.
- Amyloid peptides and proteins in review.
- Atomic force microscopy investigations of peptide self-assembly
- X-ray fiber diffraction of amyloid fibrils.
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