Atomic structures of amyloid cross-β spines reveal varied steric zippers

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Analysis of oligomeric complexes of the amyloid-forming FYLLYY peptide by collision-induced dissociation with electrospray ionization mass spectrometry - Ryu Ho Choi, Ho-Tae Kim, 2020

Advances in AFM Imaging Applications for Characterizing the Biophysical Properties of Amyloid Fibrils

Structural identification of individual helical amyloid filaments by integration of cryo-electron microscopy-derived maps in comparative morphometric atomic force microscopy image analysis

Heterogeneous Seeding of a Prion Structure by a Generic Amyloid Form of the Fungal Prion-forming Domain HET-s(218–289)* - Journal of Biological Chemistry

Identifying amyloid-related diseases by mapping mutations in low-complexity protein domains to pathologies. - Abstract - Europe PMC

Frontiers Diverse Misfolded Conformational Strains and Cross-seeding of Misfolded Proteins Implicated in Neurodegenerative Diseases

PDF] Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils

Dynamics of locking of peptides onto growing amyloid fibrils

Fiber Diffraction and Small-Angle Scattering for Structural Investigation of Bacterial Amyloids

Between Amyloids and Aggregation Lies a Connection with Strength and Adhesion

PDF] Thermodynamic Selection of Steric Zipper Patterns in the Amyloid Cross-β Spine

Advances in AFM Imaging Applications for Characterizing the Biophysical Properties of Amyloid Fibrils

Structural identification of individual helical amyloid filaments by integration of cryo-electron microscopy-derived maps in comparative morphometric atomic force microscopy image analysis