Virtual Issue: Amyloids, prions and protein oligomers

Virtual Issue: Amyloids, prions and protein oligomers

Protein aggregation into amyloid oligomers and fibrils plays a key role in a wide range of diseases as well as normal biological function. The editors at JBC are proud to support the community studying amyloidogenic proteins and their connections to both neurological disorders and the rapidly expanding area of functional amyloids. To honor this field, we’ve assembled a collection of research papers published in 2015-2018 that advance our understanding of amyloid structure, aggregation pathways and cell-to-cell propagation. We hope you enjoy this collection and thank all the authors who have contributed to JBC.

The cover art shows the common structural architecture of amyloid-β and human islet amyloid polypeptide sequences, along with models of peptide inhibitors of hIAPP fibril formation, as reported by Krotee et al. Artwork created by Valery Masterson.

Assembled by Paul Fraser and Catherine Goodman; published March 2018

Find more virtual issues

Amyloid aggregation and neurodegeneration

Tau and synuclein pathways

Prion oligomers and prion-like propagation

Functional amyloids and phase transitions

Amyloid-based therapies, tools and techniques

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