Amyloid-type protein aggregation and prion-like properties of amyloids

D Willbold, B Strodel, GF Schröder, W Hoyer… - Chemical …, 2021 - ACS Publications
This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …

[HTML][HTML] Structure–activity relationship of amyloid fibrils

SK Maji, L Wang, J Greenwald, R Riek - FEBS letters, 2009 - Elsevier
Protein aggregation is a process in which proteins self-associate into imperfectly ordered
macroscopic entities. Such aggregates are generally classified as either amorphous or …

Formation of distinct prion protein amyloid fibrils under identical experimental conditions

M Ziaunys, T Sneideris, V Smirnovas - Scientific reports, 2020 - nature.com
Protein aggregation into amyloid fibrils is linked to multiple neurodegenerative disorders,
such as Alzheimer's, Parkinson's or Creutzfeldt-Jakob disease. A better understanding of the …

Formation of mixed fibrils demonstrates the generic nature and potential utility of amyloid nanostructures

CE MacPhee, CM Dobson - Journal of the American Chemical …, 2000 - ACS Publications
The aggregation of proteins and peptides in the form of stable and highly ordered amyloid
fibrils is most commonly associated with pathological conditions such as Alzheimer's …

Structure and aggregation mechanisms in amyloids

ZL Almeida, RMM Brito - Molecules, 2020 - mdpi.com
The aggregation of a polypeptide chain into amyloid fibrils and their accumulation and
deposition into insoluble plaques and intracellular inclusions is the hallmark of several …

Visualization and classification of amyloid β supramolecular assemblies

H Yagi, T Ban, K Morigaki, H Naiki, Y Goto - Biochemistry, 2007 - ACS Publications
Deposition of amyloid β (Aβ) fibrils has been suggested to play a central role in Alzheimer's
disease. In clarifying the mechanism by which fibrils form and moreover in developing new …

Amyloid fibrils from the viewpoint of protein folding

S Ohnishi, K Takano - Cellular and Molecular Life Sciences CMLS, 2004 - Springer
In amyloid related diseases, proteins form fibrillar aggregates with highly ordered β-sheet
structure regardless of their native conformations. Formation of such amyloid fibrils can be …

Structural models of amyloid‐like fibrils

R Nelson, D Eisenberg - Advances in protein chemistry, 2006 - Elsevier
Amyloid fibrils are elongated, insoluble protein aggregates deposited in vivo in amyloid
diseases, and amyloid‐like fibrils are formed in vitro from soluble proteins. Both of these …

A new era for understanding amyloid structures and disease

MG Iadanza, MP Jackson, EW Hewitt… - … reviews Molecular cell …, 2018 - nature.com
The aggregation of proteins into amyloid fibrils and their deposition into plaques and
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …

[PDF][PDF] Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases

JW Kelly - Structure, 1997 - cell.com
The assembly and misassembly of normally soluble proteins into fibrilar structures is thought
to be a causative agent in a variety of human amyloid and prion diseases. Structural and …