Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade.
Explore this paper's citation graph
Summary
This review describes this field of science with particular reference to the advances that have been made over the last decade in understanding of its fundamental nature and consequences and shows evidence that a complex proteostasis network actively combats protein aggregation.
- Type
- review
- Published
- 2017-06-27
- Cited by
- 2,267
- References
- 243
- Access
- Open access
- OpenAlex
- https://openalex.org/W2614053601
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:207599380
Keywords
Proteostasis, Amyloid (mycology), Amyloid fibril, Protein aggregation, Disease
References
- Quantifying the kinetic parameters of prion replication.
- Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
- Template-assisted filament growth by parallel stacking of tau.
- Prevention of amyloid‐like aggregation as a driving force of protein evolution
- Chemical classes of amyloid substance.
- X-ray fibre diffraction studies of amyloid fibrils.
- A new structural model of Aβ40 fibrils.
- Structural Insight into an Alzheimer’s Brain-Derived Spherical Assembly of Amyloid β by Solid-State NMR
- Role of Cholesterol and Phospholipids in Amylin Misfolding, Aggregation and Etiology of Islet Amyloidosis
- Analysis of protein aggregation kinetics.
- The structure of amyloid fibrils by electron microscopy and X-ray diffraction.
- Light chain deposition disease: novel biological insights and treatment advances
- Pathology and function of nuclear amyloid
- Substitutions at codon 22 of Alzheimer's abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells.
- A stop-codon mutation in the BRI gene associated with familial British dementia
- Vaccination with soluble Aβ oligomers generates toxicity‐neutralizing antibodies
- Metalloendoprotease cleavage triggers gelsolin amyloidogenesis
- Cell Biology of Prions and Prionoids: A Status Report.
- Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR.
- The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: Evidence from solid state NMR
Cited by
- Protein Misfolding Diseases.
- Tracing a protein’s folding pathway over evolutionary time using ancestral sequence reconstruction and hydrogen exchange
- β2-Type Amyloidlike Fibrils of Poly-l-glutamic Acid Convert into Long, Highly Ordered Helices upon Dissolution in Dimethyl Sulfoxide.
- Photosensitizing materials and platforms for light-triggered modulation of Alzheimer's β-amyloid self-assembly.
- Role of domain interactions in the aggregation of full-length immunoglobulin light chains
- Amyloidosis and Longevity: A Lesson from Plants
- Protein aggregation: From background to inhibition strategies.
- Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy
- Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies.
- Molecular Origins of the Compatibility between Glycosaminoglycans and Aβ40 Amyloid Fibrils
- The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseases.
- A review on protein misfolding, aggregation and strategies to prevent related ailments.
- Intrinsic Disorder, Protein-Protein Interactions, and Disease.
- Monomer-dependent secondary nucleation in amyloid formation
- Solid-state NMR spectroscopic trends for supramolecular assemblies and protein aggregates.
- Polyglutamine expansion diseases: More than simple repeats.
- A versatile platform for adding functional properties to amyloid fibrils.
- Lessons learned from protein aggregation: toward technological and biomedical applications
- Why Are Functional Amyloids Non-Toxic in Humans?
- How does solvation in the cell affect protein folding and binding?
Related papers
- Protein Chemistry of Amyloid Fibrils and Chaperones: Implications for Amyloid Formation and Disease
- Fundamentals of Enzymology: by N C Price and L Stevens. pp 447. Oxford University Press, Oxford. 1982. 20.00 or £9.95 paper
- Microbial Manipulation of the Amyloid Fold
- The formation, function and regulation of amyloids: insights from structural biology
- The metazoan protein disaggregase and amyloid depolymerase system
- Diagnostics for amyloid fibril formation: where to begin?
- High pressure modulates amyloid formation.
- Protein Misfolding Studies on Human Semenogelin-1 and Serum Albumin Proteins
- Screening for amyloid aggregation: in-silico, in-vitro and in-vivo detection.