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The Parkinson's disease-associated H50Q mutation accelerates α-Synuclein aggregation in vitro.
α-Synuclein (α-Syn) aggregation is directly linked with Parkinson's disease (PD) pathogenesis. Here, we analyzed the aggregation of newly discovered α-Syn missense mutant H50Q in vitro and found thatExpand
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CSF Biomarkers for Alzheimer's Disease Diagnosis
Alzheimer's disease (AD) is the most common form of dementia that affects several million people worldwide. The major neuropathological hallmarks of AD are the presence of extracellular amyloidExpand
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Nanomaterials: amyloids reflect their brighter side
Amyloid fibrils belong to the group of ordered nanostructures that are self-assembled from a wide range of polypeptides/proteins. Amyloids are highly rigid structures possessing a high mechanicalExpand
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Glycosaminoglycans have variable effects on α-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrils
Parkinson's disease is mainly a sporadic disorder in which both environmental and cellular factors play a major role in the initiation of this disease. Glycosaminoglycans (GAG) are integralExpand
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Elucidating the Role of Disulfide Bond on Amyloid Formation and Fibril Reversibility of Somatostatin-14
Background: Peptide/protein hormones are stored as amyloids within endocrine secretory granules. Results: Disulfide bond cleavage enhances conformational dynamics and aggregation kinetics inExpand
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Familial Parkinson Disease-associated Mutations Alter the Site-specific Microenvironment and Dynamics of α-Synuclein*
Background: Aggregation of α-Syn is associated with PD pathogenesis. Results: Despite being natively unfolded, a site-specific structure exists in α-Syn that is significantly altered by familialExpand
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Characterization of amyloid formation by glucagon-like peptides: role of basic residues in heparin-mediated aggregation.
Glycosaminoglycans (GAGs) have been reported to play a significant role in amyloid formation of a wide range of proteins/peptides either associated with diseases or native biological functions. TheExpand
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Amyloid formation of growth hormone in presence of zinc: Relevance to its storage in secretory granules
Amyloids are cross-β-sheet fibrillar aggregates, associated with various human diseases and native functions such as protein/peptide hormone storage inside secretory granules of neuroendocrine cells.Expand
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Complexation of amyloid fibrils with charged conjugated polymers.
It has been suggested that conjugated charged polymers are amyloid imaging agents and promising therapeutic candidates for neurological disorders. However, very less is known about their efficacy inExpand
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Site-specific fluorescence dynamics of α-synuclein fibrils using time-resolved fluorescence studies: effect of familial Parkinson's disease-associated mutations.
α-Synuclein (α-Syn) aggregation is directly implicated in both the initiation and spreading of Parkinson's Diseases (PD) pathogenesis. Although the familial PD-associated mutations (A53T, E46K, andExpand
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