Hierarchical Protofilament Intertwining Rules the Formation of Mixed‐Curvature Amyloid Polymorphs
Sign Up to like & getrecommendations! Published in 2024 at "Advanced Science"
DOI: 10.1002/advs.202402740
Abstract: Amyloid polymorphism is a hallmark of almost all amyloid species, yet the mechanisms underlying the formation of amyloid polymorphs and their complex architectures remain elusive. Commonly, two main mesoscopic topologies are found in amyloid polymorphs… read more here.
Keywords: polymorphs; mixed curvature; amyloid polymorphs; protofilament intertwining ... See more keywords
Amyloid polymorphs and pathological diversities
Sign Up to like & getrecommendations! Published in 2022 at "Neurochemistry International"
DOI: 10.1016/j.neuint.2022.105335
Abstract: The presence of protein aggregates within the central nervous system is intimately associated to debilitating neurodegenerative diseases. While the aggregation of proteins, that share no primary structure identity, is understandable in different diseases, that of… read more here.
Keywords: pathological diversities; amyloid polymorphs; polymorphs pathological;
Prion Amyloid Polymorphs – The Tag Might Change It All
Sign Up to like & getrecommendations! Published in 2020 at "Frontiers in Molecular Biosciences"
DOI: 10.3389/fmolb.2020.00190
Abstract: Sup35p is a protein from Saccharomyces cerevisiae. It can propagate using a prion-like mechanism, which means that it can recruit non-prion soluble Sup35p into insoluble fibrils. Sup35p is a large protein showing three distinct domains,… read more here.
Keywords: prion; poly histidine; prion amyloid; tag ... See more keywords