Research Topic

Clearance of Neurodegenerative Disease-associated Misfolded Proteins

About this Research Topic

Neurodegenerative disorders are characterized by progressive loss of selectively vulnerable populations of neurons. A common pathological feature among neurodegenerative diseases is the aggregation of toxic misfolded proteins. Although the roles of misfolded-protein aggregates are still debated, the formation of aggregates suggests the deficient clearance of misfolded proteins in brain cells. Furthermore, growing evidence indicates that neuronal and glial cells have differing capacities to the extent that they can remove misfolded proteins and that these misfolded proteins, such as mutant huntingtin, have different degradation rates in differential subcellular compartments of neurons. Thus, investigating the turnover of misfolded proteins could advance our knowledge of pathogenesis of neurodegenerative disorders. Moreover, the development of new techniques, such as CRISPR/Cas9 and antisense oligonucleotides, enables researchers to reduce the expression level of target toxic misfolded proteins, which has therapeutic potentials for neurodegenerative disorders.

This Research Topic aims to understand mechanisms that regulate the aggregation and clearance of neurodegenerative disease-associated misfolded proteins, and how these misfolded proteins affect proteolytic machineries. For developing new potential therapeutic approaches, we are also interested in the development and application of new strategies to reduce the expression of misfolded proteins. We seek Original Research Articles, Reviews, Mini-Reviews, Methods that cover, but are not limited to, the following topics:

1) Turnover of misfolded proteins, especially the study of degradation of misfolded protein at subcellular levels
2) Impact of misfolded proteins on ubiquitin-proteasome system, chaperones and autophagy
3) Reducing misfolded proteins with DNA-targeting approaches (ZFPs, TALENs, CRISPR/Cas9 et al.)
4) Reducing misfolded proteins with RNA-targeting approaches (RNAi, antisense oligonucleotides et al.)
5)Reducing misfolded proteins with protein clearance approaches by activating protein degradation machineries.
6) Dynamics of proteasome and autophagy


Keywords: Neurodegeneration, misfolded proteins, aggregates, degradation, subcellular compartments


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 disorders are characterized by progressive loss of selectively vulnerable populations of neurons. A common pathological feature among neurodegenerative diseases is the aggregation of toxic misfolded proteins. Although the roles of misfolded-protein aggregates are still debated, the formation of aggregates suggests the deficient clearance of misfolded proteins in brain cells. Furthermore, growing evidence indicates that neuronal and glial cells have differing capacities to the extent that they can remove misfolded proteins and that these misfolded proteins, such as mutant huntingtin, have different degradation rates in differential subcellular compartments of neurons. Thus, investigating the turnover of misfolded proteins could advance our knowledge of pathogenesis of neurodegenerative disorders. Moreover, the development of new techniques, such as CRISPR/Cas9 and antisense oligonucleotides, enables researchers to reduce the expression level of target toxic misfolded proteins, which has therapeutic potentials for neurodegenerative disorders.

This Research Topic aims to understand mechanisms that regulate the aggregation and clearance of neurodegenerative disease-associated misfolded proteins, and how these misfolded proteins affect proteolytic machineries. For developing new potential therapeutic approaches, we are also interested in the development and application of new strategies to reduce the expression of misfolded proteins. We seek Original Research Articles, Reviews, Mini-Reviews, Methods that cover, but are not limited to, the following topics:

1) Turnover of misfolded proteins, especially the study of degradation of misfolded protein at subcellular levels
2) Impact of misfolded proteins on ubiquitin-proteasome system, chaperones and autophagy
3) Reducing misfolded proteins with DNA-targeting approaches (ZFPs, TALENs, CRISPR/Cas9 et al.)
4) Reducing misfolded proteins with RNA-targeting approaches (RNAi, antisense oligonucleotides et al.)
5)Reducing misfolded proteins with protein clearance approaches by activating protein degradation machineries.
6) Dynamics of proteasome and autophagy


Keywords: Neurodegeneration, misfolded proteins, aggregates, degradation, subcellular compartments


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

15 January 2021 Abstract
15 September 2021 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

15 January 2021 Abstract
15 September 2021 Manuscript

Participating Journals

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

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