Unfolding Aggregation: Pathological and Functional Roles of Amyloids in Neurodegeneration and Beyond

  • 342

    Total downloads

  • 5,334

    Total views and downloads

About this Research Topic

This Research Topic is currently accepting articles, but is closing soon.

Background

The Prion 2025 Congress will take place from November 3–7, 2025, at the Hotel Atlântico Búzios in Armação dos Búzios, Rio de Janeiro, Brazil. Organized by the NeuroPrion Association, this international meeting will bring together scientists, clinicians, and industry experts to discuss advances in prion diseases and other protein misfolding disorders. To highlight this event, Frontiers in Neuroscience is launching this Research Topic to spotlight themes emerging from the conference and the wider field of protein aggregation in neurodegeneration.

Protein aggregation is a hallmark of neurodegenerative diseases, including prion diseases, Alzheimer’s, Parkinson’s, and related disorders. Misfolded proteins such as PrP, α-synuclein, amyloid-β, and tau form aggregates that disrupt neuronal function, spread pathology across the nervous system, and drive disease progression. At the same time, recent studies show that amyloid-like assemblies can also serve physiological roles in cellular regulation, highlighting a duality between pathological and functional amyloids.

This Research Topic will gather original research and review articles exploring the mechanisms, molecular and cellular consequences, and therapeutic implications of amyloid aggregation in neurodegenerative disease. Submissions are welcome from both Prion 2025 participants and the wider research community.

We invite contributions addressing, but not limited to:

• Structural and biophysical insights into amyloid formation and propagation in neurodegeneration

• Molecular pathways linking aggregation to neuronal dysfunction and disease progression

• Functional or adaptive roles of amyloids in nervous system physiology

• Diagnostic, biomarker, and therapeutic strategies targeting amyloid aggregation

• Comparative and cross-disease perspectives, including prion and prion-like mechanisms

• Insights from patient-derived models, in vivo systems, or translational approaches to intervention

By aligning with Prion 2025, this Research Topic provides a platform to disseminate the latest discoveries in protein aggregation biology. It will highlight how prion research informs broader neurodegenerative fields, and how advances in one disease can accelerate progress in others. By integrating pathological and functional perspectives, this collection seeks to deepen our understanding of amyloids and their multifaceted roles in health, disease, and therapy.

Topic Editor Prof. Holger Wille is co-founder of Solenoid Biosciences LLC and holds related patents. The other Topic Editors declare no competing interests with regard to the Research Topic subject

Article types and fees

This Research Topic accepts the following article types, unless otherwise specified in the Research Topic description:

  • Brief Research Report
  • Data Report
  • Editorial
  • FAIR² Data
  • FAIR² DATA Direct Submission
  • General Commentary
  • Hypothesis and Theory
  • Methods
  • Mini Review

Articles that are accepted for publication by our external editors following rigorous peer review incur a publishing fee charged to Authors, institutions, or funders.

Keywords: protein aggregation, amyloids, prion diseases, neurodegeneration, protein misfolding, functional amyloids

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.

Topic editors

Manuscripts can be submitted to this Research Topic via the main journal or any other participating journal.

Impact

  • 5,334Topic views
  • 2,431Article views
  • 342Article downloads
View impact