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Amyloid fibrils are a pathologically and functionally relevant state of protein folding, which is generally accessible to polypeptide chains and differs fund
PDF] Atomic structure and hierarchical assembly of a cross-β
Frontiers Exploring cryptic amyloidogenic regions in prion-like proteins from plants
Structural biology of misfolding proteins involved in
Targeting pathological and functional aggregates in heart failure.
Frontiers Supramolecular organizing centers at the interface of inflammation and neurodegeneration
Principal steps of the protein aggregation that are involved in the
The MicroED atomic structure of segment 19-29 S20G reveals pairs
α-Synuclein: An All-Inclusive Trip Around its Structure, Influencing Factors and Applied Techniques - Frontiers
PDF) General Principles Underpinning Amyloid Structure
Structural polymorphism of amyloid fibrils in cardiac ATTR
Interaction motifs - List of Frontiers' open access articles
PDF) Why amyloid fibrils have a limited width
Frontiers Deciphering the Structure and Formation of Amyloids in
Frontiers Functional Reciprocity of Amyloids and Antimicrobial
Frontiers Computational assessment of the impact of Cu(II) and