Role of water in protein aggregation and amyloid polymorphism
A variety of neurodegenerative diseases are associated with amyloid plaques, which begin
as soluble protein oligomers but develop into amyloid fibrils. Our incomplete understanding …
as soluble protein oligomers but develop into amyloid fibrils. Our incomplete understanding …
Polymorphism in Alzheimer Aβ amyloid organization reflects conformational selection in a rugged energy landscape
Amyloids can have normal biological functions. 1r3 However, amyloidogenic proteins can
also form unwanted oligomeric or polymeric aggregates when disturbed from their native …
also form unwanted oligomeric or polymeric aggregates when disturbed from their native …
Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils
Abstract The amyloid-β1–42 (Aβ42) peptide rapidly aggregates to form oligomers, protofibils
and fibrils en route to the deposition of amyloid plaques associated with Alzheimer's …
and fibrils en route to the deposition of amyloid plaques associated with Alzheimer's …
Assessing the stability of Alzheimer's amyloid protofibrils using molecular dynamics
Amyloid fibrils represent a stable form of many misfolded proteins associated with numerous
diseases. Among these are Parkinson's disease (α-synuclein), Type II diabetes (islet …
diseases. Among these are Parkinson's disease (α-synuclein), Type II diabetes (islet …
Pathways of amyloid-β aggregation depend on oligomer shape
One of the main research topics related to Alzheimer's disease is the aggregation of the
amyloid-β peptide, which was shown to follow different pathways for the two major alloforms …
amyloid-β peptide, which was shown to follow different pathways for the two major alloforms …
Toward a molecular theory of early and late events in monomer to amyloid fibril formation
Quantitative understanding of the kinetics of fibril formation and the molecular mechanism of
transition from monomers to fibrils is needed to obtain insights into the growth of amyloid …
transition from monomers to fibrils is needed to obtain insights into the growth of amyloid …
Elucidating ATP's role as solubilizer of biomolecular aggregate
Proteins occurring in significantly high concentrations in cellular environments (over 100
mg/ml) and functioning in crowded cytoplasm, often face the prodigious challenges of …
mg/ml) and functioning in crowded cytoplasm, often face the prodigious challenges of …
Amyloid β-protein monomer folding: free-energy surfaces reveal alloform-specific differences
M Yang, DB Teplow - Journal of molecular biology, 2008 - Elsevier
Alloform-specific differences in structural dynamics between amyloid β-protein (Aβ) 40 and
Aβ42 appear to underlie the pathogenesis of Alzheimer's disease. To elucidate these …
Aβ42 appear to underlie the pathogenesis of Alzheimer's disease. To elucidate these …
Dynamics of an intrinsically disordered protein reveal metastable conformations that potentially seed aggregation
Amyloid fibril deposits of the intrinsically disordered hIAPP peptide are found in 95% of type
II diabetes patients, and the aggregation of this peptide is suggested to induce apoptotic cell …
II diabetes patients, and the aggregation of this peptide is suggested to induce apoptotic cell …
Inhibition of aggregation of amyloid peptides by beta-sheet breaker peptides and their binding affinity
The effects of beta-sheet breaker peptides KLVFF and LPFFD on the oligomerization of
amyloid peptides were studied by all-atom simulations. It was found that LPFFD interferes …
amyloid peptides were studied by all-atom simulations. It was found that LPFFD interferes …