Implications of peptide assemblies in amyloid diseases
Neurodegenerative disorders and type 2 diabetes are global epidemics compromising the
quality of life of millions worldwide, with profound social and economic implications. Despite …
quality of life of millions worldwide, with profound social and economic implications. Despite …
Self-organization of short peptide fragments: from amyloid fibrils to nanoscale supramolecular assemblies
Numerous supramolecular protein assemblies had been demonstrated to have either
physiological or pathological activities. The most significant case of disease-associated self …
physiological or pathological activities. The most significant case of disease-associated self …
Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology
Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …
considered only as pathological aggregates implicated in human neurodegenerative …
Modulating self‐assembly of amyloidogenic proteins as a therapeutic approach for neurodegenerative diseases: strategies and mechanisms
T Liu, G Bitan - ChemMedChem, 2012 - Wiley Online Library
Abnormal protein assembly causes multiple devastating disorders in the central nervous
system (CNS), such as Alzheimer's, Parkinson's, Huntington's, and prion diseases. Due to …
system (CNS), such as Alzheimer's, Parkinson's, Huntington's, and prion diseases. Due to …
[HTML][HTML] The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseases
N Cremades, CM Dobson - Neurobiology of Disease, 2018 - Elsevier
Many neurodegenerative disorders, including Alzheimer's, Parkinson's and the prion
diseases, are characterized by a conformational conversion of normally soluble proteins or …
diseases, are characterized by a conformational conversion of normally soluble proteins or …
Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity
M Fändrich - Journal of molecular biology, 2012 - Elsevier
Oligomeric intermediates are non-fibrillar polypeptide assemblies that occur during amyloid
fibril formation and that are thought to underlie the aetiology of amyloid diseases, such as …
fibril formation and that are thought to underlie the aetiology of amyloid diseases, such as …
Amyloid peptides and proteins in review
RS Harrison, PC Sharpe, Y Singh, DP Fairlie - Reviews of physiology …, 2007 - Springer
Amyloids are filamentous protein deposits ranging in size from nanometres to microns and
composed of aggregated peptide β-sheets formed from parallel or anti-parallel alignments of …
composed of aggregated peptide β-sheets formed from parallel or anti-parallel alignments of …
[HTML][HTML] Small molecule probes of protein aggregation
LM Young, AE Ashcroft, SE Radford - Current Opinion in Chemical Biology, 2017 - Elsevier
Highlights•A range of functionally and structurally unrelated proteins form amyloid.•Toxic
intermediates remain elusive, making their targeting a significant challenge.•Design and …
intermediates remain elusive, making their targeting a significant challenge.•Design and …
Protein misfolding, aggregation and mechanism of amyloid cytotoxicity: An overview and therapeutic strategies to inhibit aggregation
Protein and peptides are converted from their soluble forms into highly ordered fibrillar
aggregates under various conditions inside the cell. Such transitions confer diverse …
aggregates under various conditions inside the cell. Such transitions confer diverse …
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 …
unrelated origin. Recent research indicates that self‐assembled amyloid fibrils are also …