Misfolded proteins compromise cellular homeostasis and, eventually, lead to cell death. The accumulation of misfolded/aggregated proteins in the brain is a hallmark shared by several neurodegenerative diseases, like Parkinson’s, Alzheimer’s, and Huntington’s disease. Interestingly, the pathological aggregates have a fibrillar structure with similar morphology and sizes. Recently, it has been reported that the spreading of protein pathology resembles the templated conversion of proteins seen in prion diseases, which can be transmitted/propagated from cell-to-cell. However, our knowledge of the molecular underpinnings triggering the prion-like spreading of pathology in all these diseases is still unclear.
In this Research Topic issue focused on “Protein misfolding and spreading of pathology in neurodegenerative diseases” we aim to provide an update on the state-of-the-art of structural and molecular aspects of protein misfolding, with a special emphasis on those aspects which trigger/contribute for the spreading of pathology. Submissions that give new insights into the processes of misfolding/aggregation and spreading, and that identify ways of inhibiting these events are especially welcome. Further, submission of review articles focusing on the latest findings in this field is encouraged.
Potential topics include, but are not limited to the following:
- Protein aggregation
- Molecular mechanisms involved in protein spreading
- Comparison between different proteins/disease
- Novel methodological approaches (iPCS, mouse models, …)
- Biomarkers
- Parkinson’s disease/Synucleinopathies
- Alzheimer’s disease
- Huntington’s disease
- Amyotrophic lateral sclerosis
- Prion diseases
Misfolded proteins compromise cellular homeostasis and, eventually, lead to cell death. The accumulation of misfolded/aggregated proteins in the brain is a hallmark shared by several neurodegenerative diseases, like Parkinson’s, Alzheimer’s, and Huntington’s disease. Interestingly, the pathological aggregates have a fibrillar structure with similar morphology and sizes. Recently, it has been reported that the spreading of protein pathology resembles the templated conversion of proteins seen in prion diseases, which can be transmitted/propagated from cell-to-cell. However, our knowledge of the molecular underpinnings triggering the prion-like spreading of pathology in all these diseases is still unclear.
In this Research Topic issue focused on “Protein misfolding and spreading of pathology in neurodegenerative diseases” we aim to provide an update on the state-of-the-art of structural and molecular aspects of protein misfolding, with a special emphasis on those aspects which trigger/contribute for the spreading of pathology. Submissions that give new insights into the processes of misfolding/aggregation and spreading, and that identify ways of inhibiting these events are especially welcome. Further, submission of review articles focusing on the latest findings in this field is encouraged.
Potential topics include, but are not limited to the following:
- Protein aggregation
- Molecular mechanisms involved in protein spreading
- Comparison between different proteins/disease
- Novel methodological approaches (iPCS, mouse models, …)
- Biomarkers
- Parkinson’s disease/Synucleinopathies
- Alzheimer’s disease
- Huntington’s disease
- Amyotrophic lateral sclerosis
- Prion diseases
