...Samrat Mukhopadhyay; Pernilla Wittung-Stafshede Copper (Cu) ion dys-homeostasis and α-synclein amyloid deposits are two hallmarks of Parkinson’s disease (PD). Here, I will discuss the connections between these features, with a major focus on the role of Cu in the α-synuclein (aS) amyloid formation...

...Samrat Mukhopadhyay; Yong Xu; Roberto Maya-Martinez; Sheena E. Radford The pathological assembly of intrinsically disordered proteins/peptides (IDPs) into amyloid fibrils is associated with a range of human pathologies, including neurodegeneration, metabolic diseases and systemic amyloidosis...

... NTD. They are key players in the evasion of the host antiviral response and were shown to phase separate and to form amyloid-like fibrils in vitro . In this review, we summarize the available information on IDRs within the N, P, V and W proteins from these three model paramyxoviruses and describe...

... into protein aggregates, which have been widely implicated in Parkinson’s disease (PD) pathogenesis and other synucleinopathies. The self-assembly of α-Syn involves the structural conversion of soluble monomeric protein into oligomeric intermediates and eventually fibrillar aggregates of amyloids with cross-β...

... Society under a transformative agreement with JISC. Alzheimer's disease amyloid intrinsically disordered proteins liquid liquid phase separation protein misfolding tau Tau is a microtubule binding protein and an important component of the neuronal cytoskeleton as well as playing a role...

... Kirstein (email Kirstein@fmp-berlin.de ). 14 1 2016 7 3 2016 9 3 2016 © 2016 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society 2016 aggresome amyloid autophagy chaperones degradation deposition disaggregase misfolding polyQ...

... by the cellular pathways of protein degradation. Lysosomes are an important site for the degradation of misfolded proteins, which are trafficked to this organelle by the pathways of macroautophagy, chaperone-mediated autophagy and endocytosis. Conversely, amyloid diseases represent a failure in proteostasis...

...Sarah Perrett; Louise Serpell Amyloid fibrils are formed by numerous proteins and peptides that share little sequence homology. The structures formed are highly ordered and extremely stable, being composed of β-sheet structure and stabilized along their length by hydrogen bonding. The fibrils...

...Sarah Perrett; Chi L.L. Pham; Ann H. Kwan; Margaret Sunde Amyloids are insoluble fibrillar protein deposits with an underlying cross-β structure initially discovered in the context of human diseases. However, it is now clear that the same fibrillar structure is used by many organisms, from bacteria...