Mechanisms of amyloid fibril self‐assembly and inhibition: Model short peptides as a key research tool

E Gazit - The FEBS journal, 2005 - Wiley Online Library
The formation of amyloid fibrils is associated with various human medical disorders of
unrelated origin. Recent research indicates that self‐assembled amyloid fibrils are also …

Mechanistic studies of the process of amyloid fibrils formation by the use of peptide fragments and analogues: implications for the design of fibrillization inhibitors

E Gazit - Current medicinal chemistry, 2002 - ingentaconnect.com
The process of amyloid fibrils formation is a common mechanism of a large number of
unrelated infectious, genetic and spontaneous diseases. A partial list includes the bovine …

A possible role for π‐stacking in the self‐assembly of amyloid fibrils

E Gazit - The FASEB Journal, 2002 - Wiley Online Library
Amyloid fibril formation is assumed to be the molecular basis for a variety of diseases of
unrelated origin. Despite its fundamental clinical importance, the mechanism of amyloid …

Self assembly of short aromatic peptides into amyloid fibrils and related nanostructures

E Gazit - Prion, 2007 - Taylor & Francis
The formation of amyloid fibrils is the hallmark of more than twenty human disorders of
unrelated etiology. In all these cases, ordered fibrillar protein assemblies with a diameter of …

Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis

A Lakshmanan, DW Cheong… - Proceedings of the …, 2013 - National Acad Sciences
The self-assembly of abnormally folded proteins into amyloid fibrils is a hallmark of many
debilitating diseases, from Alzheimer's and Parkinson diseases to prion-related disorders …

Exploring amyloid formation by a de novo design

RA Kammerer, D Kostrewa, J Zurdo… - Proceedings of the …, 2004 - National Acad Sciences
Protein deposition as amyloid fibrils underlies many debilitating human disorders. The
complexity and size of disease-related polypeptides, however, often hinders a detailed …

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 …

Self-organization of short peptide fragments: from amyloid fibrils to nanoscale supramolecular assemblies

S Gilead, E Gazit - Supramolecular Chemistry, 2005 - Taylor & Francis
Numerous supramolecular protein assemblies had been demonstrated to have either
physiological or pathological activities. The most significant case of disease-associated self …

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 …

Implications of peptide assemblies in amyloid diseases

PC Ke, MA Sani, F Ding, A Kakinen, I Javed… - Chemical Society …, 2017 - pubs.rsc.org
Neurodegenerative disorders and type 2 diabetes are global epidemics compromising the
quality of life of millions worldwide, with profound social and economic implications. Despite …