Prion diseases are characterized by the transmission of infectious protein species that can cause clinical symptoms. Monomeric prion proteins (PrPC) adopting alternative conformations, namely PrPSC, are capable of self-templating and propagate in neurons via synaptic connections. Ample evidence suggests distinct conformational strains of PrPSC molecules are associated with different prion diseases. Currently, it is believed many neurodegenerative diseases, such as Alzheimer’s, Parkinson’s, amyotrophic lateral sclerosis, and frontotemporal lobar degenerations share the misfolded protein transmission phenomena with the prion diseases. The misfolded proteins aggregate to adopt a amyloid-like ordered fold and show a similar filamentous nature across different neurodegenerative diseases. However, recent advances in structural biology have led to an increase in structural information about these filaments, showing differences in their packing at high resolution in different disease types, suggesting a link between the structure and biological function of protein aggregates in different disease forms. This research topic will showcase the current understanding of the structure and transmission property of these filamentous molecules linking the effect of conformational strains to the disease progression.
The goal of this topic is to combine the cellular, molecular, and structural basis of understanding on prion -like transmissions of misfolded proteins associated with different neurodegenerative diseases.
We welcome original manuscripts that describe the following aspects
• The structural basis of toxicity of different strains
• Strain polymorphism
• Prion -like transmission in cellular and animal models
• Relationship between toxicity and prion -like transmission of misfolded proteins.
We also welcome reviews, mini-reviews, and methodological advances in protein misfolding linked to neurodegeneration research.
Prion diseases are characterized by the transmission of infectious protein species that can cause clinical symptoms. Monomeric prion proteins (PrPC) adopting alternative conformations, namely PrPSC, are capable of self-templating and propagate in neurons via synaptic connections. Ample evidence suggests distinct conformational strains of PrPSC molecules are associated with different prion diseases. Currently, it is believed many neurodegenerative diseases, such as Alzheimer’s, Parkinson’s, amyotrophic lateral sclerosis, and frontotemporal lobar degenerations share the misfolded protein transmission phenomena with the prion diseases. The misfolded proteins aggregate to adopt a amyloid-like ordered fold and show a similar filamentous nature across different neurodegenerative diseases. However, recent advances in structural biology have led to an increase in structural information about these filaments, showing differences in their packing at high resolution in different disease types, suggesting a link between the structure and biological function of protein aggregates in different disease forms. This research topic will showcase the current understanding of the structure and transmission property of these filamentous molecules linking the effect of conformational strains to the disease progression.
The goal of this topic is to combine the cellular, molecular, and structural basis of understanding on prion -like transmissions of misfolded proteins associated with different neurodegenerative diseases.
We welcome original manuscripts that describe the following aspects
• The structural basis of toxicity of different strains
• Strain polymorphism
• Prion -like transmission in cellular and animal models
• Relationship between toxicity and prion -like transmission of misfolded proteins.
We also welcome reviews, mini-reviews, and methodological advances in protein misfolding linked to neurodegeneration research.
