Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 5 of 5 for “"misfolded prion"”.
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Development of A High-Throughput System For Screening of Anti-Prion Molecules
<p>The misfolded prion protein causes and transmits disease in both humans and animals. As other infectious agents, prions display strain variation, which can generate different pathological outcomes in affected individuals. Unfortunately, there are no known therapies for these diseases, which at …
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Dilations of the Endoplasmic Reticulum Contribute to Spongiform Degeneration and Unlock a Door to a Unified Model of Neuropathological Features in Prion Diseases
Prion diseases are fatal neurodegenerative disorders characterized by spongiform degeneration, neuronal loss, and misfolded prion protein (PrPSc) deposition. The mechanistic origins of spongiform degeneration, which manifests as intracellular vacuolation in neurons, have remained unclear. We …
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The spread of pathological assemblies in neurodegenerative disease
… evidence that the direct propagation of misfolded proteins along neural pathways, in a manner reminiscent of misfolded prion protein, is a common principle across many neurodegenerative diseases. In particular, it has been hypothesised that Parkinson’s disease may originate with the …
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Probing Structural Differences of Recombinant Prion Isoforms Using Fluorescence Spectroscopy
Conversion of prion protein (PrP) from its normal, cellular isoform, PrPC, to an infectious, misfolded, fibrillar isoform, PrPSc, is responsible for various neurodegenerative diseases in a variety of mammalian hosts. Although the structure of PrPC is well studied, the structure of PrPSc is not …
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Probing Structural Differences of Recombinant Prion Isoforms Using Fluorescence Spectroscopy
Conversion of prion protein (PrP) from its normal, cellular isoform, PrPC, to an infectious, misfolded, fibrillar isoform, PrPSc, is responsible for various neurodegenerative diseases in a variety of mammalian hosts. Although the structure of PrPC is well studied, the structure of PrPSc is not …