Protein misfolding, functional amyloid, and human disease.
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Summary
The relative importance of the common main-chain and side-chain interactions in determining the propensities of proteins to aggregate is discussed and some of the evidence that the oligomeric fibril precursors are the primary origins of pathological behavior is described.
- Type
- review
- Published
- 2006-06-06
- Cited by
- 6,193
- References
- 202
- OpenAlex
- https://openalex.org/W2165186407
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:23797549
Keywords
Amyloid fibril, Protein aggregation, Amyloid (mycology), Fibril, Protein folding
References
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Cited by
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- Kinetic Characterization of the Coupled Folding and Binding Mechanism of Bacterial RNase P Protein: an Intrinsically Unstructured Protein
- Prevention of amyloid‐like aggregation as a driving force of protein evolution
- NMR Spectroscopic Investigation of Early Events in IAPP Amyloid Fibril Formation
- Fluorescent oligo and poly-thiophenes and their utilization for recording biological events of diverse origin—when organic chemistry meets biology
- A Condensation-Ordering Mechanism in Nanoparticle-Catalyzed Peptide Aggregation
- Amyloid-beta fibrillogenesis: structural insight and therapeutic intervention.
- Dynamic and supramolecular organisation of alpha-lactalbumin/lysozyme microspheres: A microscopic study.
- Transition of Tau Protein from Disordered to Misordered in Alzheimer’s Disease
- Structural and Dynamics Characteristics of Acylphosphatase from Sulfolobus solfataricus in the Monomeric State and in the Initial Native-like Aggregates*
- Elimination of the native structure and solubility of the hVAPB MSP domain by the Pro56Ser mutation that causes amyotrophic lateral sclerosis.
- In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells
- Extending the PRIME Model for Protein Aggregation to All Twenty Amino Acids
- Interactions between amyloidophilic dyes and their relevance to studies of amyloid inhibitors.
- Flexibility of the Ure2 prion domain is important for amyloid fibril formation.
- Acceleration of protein aggregation by amphiphilic peptides: Transformation of supramolecular structure of the aggregates
- Can Parkinson's disease pathology be propagated from one neuron to another?
- Serum Albumin Prevents Protein Aggregation and Amyloid Formation and Retains Chaperone-like Activity in the Presence of Physiological Ligands
- Molecular interaction of proteins and peptides with nanoparticles.
- Amyloid inspired self-assembled peptide nanofibers.
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