Research Topic

Structural biology of misfolding proteins involved in neurodegenerative diseases

About this Research Topic

Neurodegenerative diseases include sporadic and genetic conditions but almost all involve abnormal protein deposition and accumulation intra- or extra-cellularly. The misfolded proteins assemble to form amyloid fibrils which share a common architecture. Recent advances in structural biology have led to an explosion in information regarding the structures of these amyloid fibrils involved in diseases including Alzheimer's; Parkinson's and amyotrophic lateral sclerosis as well as numerous tauopathies and synucleinopathies. This Research Topic will showcase the current understanding of the structure of these pathogenic fibrous molecules and provide information linking their structure to the downstream effects on disease progression.

Neurodegenerative diseases are extensively studied by neuroscientists and much progress has been made at the cellular level. However, there remains a gap in understanding between the structural biology of proteins associated with disease and their role in dysfunction in the brain. This Research Topic brings this important question to the forefront and provides a background in the structural biology of amyloid and amyloidogenic proteins associated with neurodegeneration to the general neuroscience field. Importantly, there remain many misunderstandings and misconceptions regarding the use of the word amyloid and its definition and this special issue will provide a broad and comprehensive set of information regarding the numerous amyloidogenic proteins that misfold in neurodegenerative disease.

We seek original research articles, reviews, mini-reviews, and methodological advances in the area of amyloidogenic proteins associated with neurodegeneration. We welcome manuscripts that describe structural polymorphism, the structural basis of strains, amyloidogenic model systems, and the relationship between structure and dysfunction in neurodegenerative diseases.

Topic Editor Prof. Louise Serpell received financial support from TauRX therapeutics Ltd. The other Topic Editors declare no competing interests with regard to the Research Topic subject.


Keywords: Protein misfolding, amyloid, aggregation, self-assembly, Alzheimer's disease, Neurodegenerative disease, Parkinson's disease


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

Neurodegenerative diseases include sporadic and genetic conditions but almost all involve abnormal protein deposition and accumulation intra- or extra-cellularly. The misfolded proteins assemble to form amyloid fibrils which share a common architecture. Recent advances in structural biology have led to an explosion in information regarding the structures of these amyloid fibrils involved in diseases including Alzheimer's; Parkinson's and amyotrophic lateral sclerosis as well as numerous tauopathies and synucleinopathies. This Research Topic will showcase the current understanding of the structure of these pathogenic fibrous molecules and provide information linking their structure to the downstream effects on disease progression.

Neurodegenerative diseases are extensively studied by neuroscientists and much progress has been made at the cellular level. However, there remains a gap in understanding between the structural biology of proteins associated with disease and their role in dysfunction in the brain. This Research Topic brings this important question to the forefront and provides a background in the structural biology of amyloid and amyloidogenic proteins associated with neurodegeneration to the general neuroscience field. Importantly, there remain many misunderstandings and misconceptions regarding the use of the word amyloid and its definition and this special issue will provide a broad and comprehensive set of information regarding the numerous amyloidogenic proteins that misfold in neurodegenerative disease.

We seek original research articles, reviews, mini-reviews, and methodological advances in the area of amyloidogenic proteins associated with neurodegeneration. We welcome manuscripts that describe structural polymorphism, the structural basis of strains, amyloidogenic model systems, and the relationship between structure and dysfunction in neurodegenerative diseases.

Topic Editor Prof. Louise Serpell received financial support from TauRX therapeutics Ltd. The other Topic Editors declare no competing interests with regard to the Research Topic subject.


Keywords: Protein misfolding, amyloid, aggregation, self-assembly, Alzheimer's disease, Neurodegenerative disease, Parkinson's disease


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

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Submission Deadlines

25 October 2021 Abstract
22 February 2022 Manuscript

Participating Journals

Manuscripts can be submitted to this Research Topic via the following journals:

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Topic Editors

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Submission Deadlines

25 October 2021 Abstract
22 February 2022 Manuscript

Participating Journals

Manuscripts can be submitted to this Research Topic via the following journals:

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