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Keywords: amyloid
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Articles
Biosci Rep (2022) 42 (5): BSR20211297.
Published: 18 May 2022
... (PMDs) and involves human islet amyloid polypeptide (hIAPP) misfolding and accumulating in parts of the body, primarily in the pancreas, causing damage to islet cells and affecting glucose regulation. In this review, we have summarised our current understanding of what causes hIAPP to misfold, what...
Includes: Supplementary data
Articles
Biosci Rep (2019) 39 (3): BSR20190327.
Published: 06 March 2019
... concentration. Cofactors such as glycosaminoglycans and metal ions have been found associated with amyloid deposits in vivo and shown to affect protein assembly kinetics in vitro. Cofactor interactions with the amyloidogenic process are an area of great interest for therapeutic intervention for the wide range...
Articles
Biosci Rep (2019) 39 (2): BSR20182345.
Published: 12 February 2019
... that is defined by four sequence motifs and a highly conserved tertiary structure. A common structure–function relationship for this domain is hitherto unknown. A characteristic of several CAP proteins is their formation of amyloid-like structures in the presence of lipids. Here we investigate the structural...
Includes: Supplementary data
Articles
Biosci Rep (2016) 36 (3): e00334.
Published: 20 May 2016
...Alexandr G. Bobylev; Oxana V. Galzitskaya; Roman S. Fadeev; Liya G. Bobyleva; Darya A. Yurshenas; Nikolay V. Molochkov; Nikita V. Dovidchenko; Olga M. Selivanova; Nikita V. Penkov; Zoya A. Podlubnaya; Ivan M. Vikhlyantsev Amyloids are insoluble fibrous protein aggregates, and their accumulation...
Articles
Biosci Rep (2013) 33 (4): e00054.
Published: 25 July 2013
..., the CTD (C-terminal domain) and the core domain (p53C) that constitutes the sequence-specific DBD (DNA-binding region). Most p53 mutations related to cancer development are found in the DBD. Aggregation of p53 into amyloid oligomers and fibrils has been shown. Moreover, amyloid aggregates of both...