Amyloid fibril formation involves three steps; structural perturbation, nucleation and elongation. We have investigated amyloidogenesis using prion protein as a model system and UV-light as a structural perturbant. We find that UV-exposed prion protein fails to form amyloid fibrils. Interestingly, if provided with pre-formed fibrils as seeds, UV-exposed prion protein formed amyloid fibrils albeit with slightly different morphology. Atomic force microscopy and electron microscopic studies clearly show the formation of fibrils under these conditions. Circular dichroism study shows loss in helicity in UV-exposed protein. UV-exposed prion protein fails to form amyloid fibrils. However, it remains competent for fibril extension, suggesting that ...
Growth and deposition of amyloid fibrils, polymers of proteins with a cross beta-sheet structure, ar...
characterized by neurodegeneration and extracellular amyloidogenesis [5,6]. Subsequently, amyloid fo...
Protein aggregation into amyloid fibrils is linked to multiple neurodegenerative disorders, such as ...
Amyloid fibril formation involves three steps; structural perturbation, nucleation and elongation. W...
Amyloid fibril formation involves three steps; structural perturbation, nucleation and elongation. W...
Prion protein-mediated disorders appear to originate from the aggregation reactions of the prion pro...
The conversion of the alpha-helical, cellular isoform of the prion protein (PrP(C)) to the insoluble...
AbstractFibril formation has been considered a significant feature of amyloid proteins. However, it ...
AbstractThe chief and largely terminal element of normal blood clotting is considered to involve the...
AbstractThe assembly and misassembly of normally soluble proteins into fibrilar structures is though...
Increasing evidence suggests a central role for oxidative stress in the pathology of prion diseases,...
Amyloids consist of repetitions of a specific polypeptide chain in a regular cross-β-sheet conformat...
Amyloidoses are diseases, including some currently prominent such as Alzheimer's disease, bovine spo...
<div><p>The formation of β-sheet rich prion oligomers and fibrils from native prion protein (PrP) is...
AbstractBackground: Peptides derived from three of four putative α-helical regions of the prion prot...
Growth and deposition of amyloid fibrils, polymers of proteins with a cross beta-sheet structure, ar...
characterized by neurodegeneration and extracellular amyloidogenesis [5,6]. Subsequently, amyloid fo...
Protein aggregation into amyloid fibrils is linked to multiple neurodegenerative disorders, such as ...
Amyloid fibril formation involves three steps; structural perturbation, nucleation and elongation. W...
Amyloid fibril formation involves three steps; structural perturbation, nucleation and elongation. W...
Prion protein-mediated disorders appear to originate from the aggregation reactions of the prion pro...
The conversion of the alpha-helical, cellular isoform of the prion protein (PrP(C)) to the insoluble...
AbstractFibril formation has been considered a significant feature of amyloid proteins. However, it ...
AbstractThe chief and largely terminal element of normal blood clotting is considered to involve the...
AbstractThe assembly and misassembly of normally soluble proteins into fibrilar structures is though...
Increasing evidence suggests a central role for oxidative stress in the pathology of prion diseases,...
Amyloids consist of repetitions of a specific polypeptide chain in a regular cross-β-sheet conformat...
Amyloidoses are diseases, including some currently prominent such as Alzheimer's disease, bovine spo...
<div><p>The formation of β-sheet rich prion oligomers and fibrils from native prion protein (PrP) is...
AbstractBackground: Peptides derived from three of four putative α-helical regions of the prion prot...
Growth and deposition of amyloid fibrils, polymers of proteins with a cross beta-sheet structure, ar...
characterized by neurodegeneration and extracellular amyloidogenesis [5,6]. Subsequently, amyloid fo...
Protein aggregation into amyloid fibrils is linked to multiple neurodegenerative disorders, such as ...