SummaryPeptides comprising residues 106–126 of the human prion protein (PrP) exhibit many features of the full-length protein. PrP(106–126) induces apoptosis in neurons, forms fibrillar aggregates, and can mediate the conversion of native cellular PrP (PrPC) to the scrapie form (PrPSc). Despite a wide range of biochemical and biophysical studies on this peptide, including investigation of its propensity for aggregation, interactions with cell membranes, and PrP-like toxicity, the structure of amyloid fibrils formed by PrP(106–126) remains poorly defined. In this study we use solid-state nuclear magnetic resonance to define the secondary and quaternary structure of PrP(106–126) fibrils. Our results reveal that PrP(106–126) forms in-register ...
The principal event underlying the development of prion disease is the conversion of soluble cellula...
Mammalian prions propagate as distinct strains and are composed of multichain assemblies of misfolde...
A peptide encompassing the conserved hydrophobic region and the first β-strand of the prion protein ...
The formation of amyloid fibrils is a key characteristic of many neurodegenerative diseases includin...
AbstractMisfolded prion protein, PrPSc, is believed to be the pathogenic agens in transmissible spon...
AbstractConformational transitions are thought to be the prime mechanism of amyloid formation in pri...
The fibrillogenic peptide corresponding to the residues 106-126 of the prion protein sequence (PrP 1...
The self-association of prion protein (PrP) is a critical step in the pathology of prion diseases. I...
In the prion-related encephalopathies the prion protein is converted to an altered form, known as Pr...
The still elusive structural difference of non-infectious and infectious amyloid of the mammalian pr...
The self-association of prion protein (PrP) is a critical step in the pathology of prion diseases. I...
The conformational conversion of the cellular prion protein (PrPC) into a misfolded, aggregated and ...
Prion diseases are characterized by the conversion of the physiological cellular form of the prion p...
Transmissible spongiform encephalopathies (TSEs) or prion diseases are serious neurological ailments...
The conformational conversion of the cellular prion protein (PrPC) into a misfolded, aggregated and ...
The principal event underlying the development of prion disease is the conversion of soluble cellula...
Mammalian prions propagate as distinct strains and are composed of multichain assemblies of misfolde...
A peptide encompassing the conserved hydrophobic region and the first β-strand of the prion protein ...
The formation of amyloid fibrils is a key characteristic of many neurodegenerative diseases includin...
AbstractMisfolded prion protein, PrPSc, is believed to be the pathogenic agens in transmissible spon...
AbstractConformational transitions are thought to be the prime mechanism of amyloid formation in pri...
The fibrillogenic peptide corresponding to the residues 106-126 of the prion protein sequence (PrP 1...
The self-association of prion protein (PrP) is a critical step in the pathology of prion diseases. I...
In the prion-related encephalopathies the prion protein is converted to an altered form, known as Pr...
The still elusive structural difference of non-infectious and infectious amyloid of the mammalian pr...
The self-association of prion protein (PrP) is a critical step in the pathology of prion diseases. I...
The conformational conversion of the cellular prion protein (PrPC) into a misfolded, aggregated and ...
Prion diseases are characterized by the conversion of the physiological cellular form of the prion p...
Transmissible spongiform encephalopathies (TSEs) or prion diseases are serious neurological ailments...
The conformational conversion of the cellular prion protein (PrPC) into a misfolded, aggregated and ...
The principal event underlying the development of prion disease is the conversion of soluble cellula...
Mammalian prions propagate as distinct strains and are composed of multichain assemblies of misfolde...
A peptide encompassing the conserved hydrophobic region and the first β-strand of the prion protein ...