X-ray fibre diffraction studies of amyloid fibrils.
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Summary
The methods by which amyloid-like fibrils may be prepared to form a sample suitable for structural analysis are discussed and how data may be collected and then analysed to arrive at a potential model structure are described.
- Type
- article
- Published
- 2012-01-01
- Cited by
- 95
- References
- 38
- OpenAlex
- https://openalex.org/W111710589
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:36084818
Keywords
Fiber diffraction, Fibril, Amyloid fibril, Diffraction, Crystallography
References
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- Structural analysis of Alzheimer's beta(1-40) amyloid: protofilament assembly of tubular fibrils.
- The common architecture of cross-beta amyloid.
- An overview of the CCP4 project in protein crystallography: an example of a collaborative project.
- CONGO RED AS A STAIN FOR FLUORESCENCE MICROSCOPY OF AMYLOID
- Structural insights into the polymorphism of amyloid-like fibrils formed by region 20-29 of amylin revealed by solid-state NMR and X-ray fiber diffraction.
- Exploring the sequence determinants of amyloid structure using position-specific scoring matrices
- Amyloid plaque core protein in Alzheimer disease and Down syndrome.
- X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS
- A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR.
- CLEARER: a new tool for the analysis of X-ray fibre diffraction patterns and diffraction simulation from atomic structural models
- The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
Cited by
- Study of the aggregation process of the amyloid beta-protein associated to Alzheimer's disease. Examination of pharmaceutically important small molecules.
- CHARACTERIZATION AND DEVELOPMENT OF AMYLOID-REACTIVE PEPTIDES AS TRACERS FOR QUANTITATIVE MOLECULAR IMAGING
- Mechanical Properties and Failure of Biopolymers: Atomistic Reactions to Macroscale Response
- PROTEIN HYDROGELS AS TISSUE ENGINEERING SCAFFOLDS
- Two distinct β-sheet structures in Italian-mutant amyloid-beta fibrils: a potential link to different clinical phenotypes
- Silica Nanowires Templated by Amyloid‐like Fibrils
- The relationship between amyloid structure and cytotoxicity
- Amyloid β-protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies
- Antiparallel β-sheet structure within the C-terminal region of 42-residue Alzheimer’s β-amyloid peptides when they form 150 kDa oligomers
- Exploring the sequence–structure relationship for amyloid peptides
- Interactions in Bacterial Biofilm Development: A Structural Perspective
- What does make an amyloid toxic: morphology, structure or interaction with membrane?
- Computational de novo design of a self-assembling peptide with predefined structure.
- The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy
- Arrangement of fibril side chains studied by molecular dynamics and simulated infrared and vibrational circular dichroism spectra.
- Protein Fibrillar Nanopolymers: Molecular-Level Insights into Their Structural, Physical and Mechanical Properties
- Substoichiometric molecular control and amplification of the initiation and nature of amyloid fibril formation: lessons from and for blood clotting
- Proteins behaving badly. Substoichiometric molecular control and amplification of the initiation and nature of amyloid fibril formation: lessons from and for blood clotting.
- pH‐Responsive Self‐Organization of Metal‐Binding Protein Motifs from Biomolecular Junctions in Mussel Byssus
- Appraisal of role of the polyanionic inducer length on amyloid formation by 412-residue 1N4R Tau protein: A comparative study.
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