WZ
wenjuan zhang
Prion Unit (MRC), University College London
London, United Kingdom
About this Research Topic
This Research Topic is currently accepting articles, but is closing soon.
Background
Protein folding is essential for maintaining physiological functions, and improper folding can lead to the formation of toxic aggregates such as amyloids, implicated in various diseases including neurodegenerative disorders. To counteract these misfolded proteins, cells rely on an elaborate system of molecular chaperones that assist in both protein folding and disaggregation. Despite the critical role of chaperones, the transient and dynamic nature of their interactions with substrates leaves many aspects of their mode of action poorly understood. Recent advances in technologies like cryo-electron microscopy (cryo-EM) offer new opportunities to delve deeper into these interactions, especially for proteins larger than 50 kDa, potentially providing a clearer picture of intermediate chaperone-chaperone complexes.
This Research Topic aims to decipher the complex process of chaperone-mediated folding and disaggregation, emphasizing the mechanisms linked to neurodegeneration. While some insight into chaperone interactions has been achieved, a comprehensive understanding remains elusive, particularly concerning the full-size proteins and the transient states important in these processes. Additionally, understanding the kinetics of chaperone interactions with substrates is fundamental to linking their structural configurations to their biological functions, a crucial step in targeting these molecules as therapeutic agents in neurodegenerative diseases.
To further illuminate the intricacies of chaperone-substrate interactions, this Research Topic includes a wide range of contributions. Articles focusing on the following themes are particularly encouraged:
- Molecular mechanisms of chaperone-substrate interaction
- Kinetics of chaperone-mediated protein folding and disaggregation
- Advances in structural studies of chaperone-chaperone complexes and chaperone-substrate interactions
- Characterization of interactions between chaperones and amyloids
- Clinical potential of chaperones as therapeutic targets in neurodegeneration
Article types and fees
This Research Topic accepts the following article types, unless otherwise specified in the Research Topic description:
- Brief Research Report
- Editorial
- FAIR² Data
- General Commentary
- Hypothesis and Theory
- Methods
- Mini Review
- Opinion
- Original Research
Articles that are accepted for publication by our external editors following rigorous peer review incur a publishing fee charged to Authors, institutions, or funders.
Article types
This Research Topic accepts the following article types, unless otherwise specified in the Research Topic description:
- Brief Research Report
- Editorial
- FAIR² Data
- General Commentary
- Hypothesis and Theory
- Methods
- Mini Review
- Opinion
- Original Research
- Perspective
- Review
- Technology and Code
Keywords: chaperone, disaggregation, substrate, in vitro, in vivo, structure, kinetics
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.
