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Keywords: amyloid
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Articles
Essays Biochem (2022) 66 (7): 977–986.
Published: 16 December 2022
...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...
Articles
Essays Biochem (2022) 66 (7): 959–975.
Published: 16 December 2022
...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...
Articles
Essays Biochem (2022) 66 (7): 915–934.
Published: 16 December 2022
... 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...
Includes: Supplementary data
Articles
Essays Biochem (2022) 66 (7): 987–1000.
Published: 16 December 2022
... 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...
Articles
Essays Biochem (2022) 66 (7): 1001–1011.
Published: 16 December 2022
... to an ordered amyloid fibril remains unclear. Tau sequence is defined by the primary sequence which contains low-complexity domains which are often enriched in polar and charged amino acids (Gln, Ser, Pro, Glu and Lys) [ 55 ]. They also contain a low number of hydrophobic amino acids (Val, Leu, Ile, Met, Phe...
Articles
Essays Biochem (2016) 60 (2): 153–161.
Published: 15 October 2016
... 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...
Articles
Essays Biochem (2016) 60 (2): 173–180.
Published: 15 October 2016
... 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...
Articles
Essays Biochem (2014) 56: 1–10.
Published: 18 August 2014
...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...
Articles
Essays Biochem (2014) 56: 207–219.
Published: 18 August 2014
...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...