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 …
Complete phenotypic recovery of an Alzheimer's disease model by a quinone-tryptophan hybrid aggregation inhibitor
R Scherzer-Attali, R Pellarin, M Convertino… - PLoS one, 2010 - journals.plos.org
The rational design of amyloid oligomer inhibitors is yet an unmet drug development need.
Previous studies have identified the role of tryptophan in amyloid recognition, association …
Previous studies have identified the role of tryptophan in amyloid recognition, association …
Functional amyloid: turning swords into plowshares
D Otzen - Prion, 2010 - Taylor & Francis
Evidence is growing at an increasing pace that amyloid fibers are not just the result of
aberrant protein folding associated with neurodegenerative diseases, but are widespread in …
aberrant protein folding associated with neurodegenerative diseases, but are widespread in …
Amyloidogenic sequences in native protein structures
S Tzotzos, AJ Doig - Protein Science, 2010 - Wiley Online Library
Numerous short peptides have been shown to form β‐sheet amyloid aggregates in vitro.
Proteins that contain such sequences are likely to be problematic for a cell, due to their …
Proteins that contain such sequences are likely to be problematic for a cell, due to their …
Potential aggregation-prone regions in complementarity-determining regions of antibodies and their contribution towards antigen recognition: a computational …
Purpose To analyze contribution of short aggregation-prone regions (APRs), which may self-
associate via cross-β motif and were earlier identified in therapeutic mAbs, towards antigen …
associate via cross-β motif and were earlier identified in therapeutic mAbs, towards antigen …
Solubilization of aromatic and hydrophobic moieties by arginine in aqueous solutions
J Li, M Garg, D Shah, R Rajagopalan - The Journal of chemical physics, 2010 - pubs.aip.org
Experiments hold intriguing, circumstantial clues to the mechanisms behind arginine-
mediated solubilization of small organic drugs and suppression of protein aggregation …
mediated solubilization of small organic drugs and suppression of protein aggregation …
Fibrillation of α‐lactalbumin: Effect of crocin and safranal, two natural small molecules from Crocus sativus
MB Ebrahim‐Habibi, M Amininasab… - …, 2010 - Wiley Online Library
Formation of toxic amyloid structures is believed to be associated with various late‐onset
neurodegenerative disorders such as Alzheimer's and Parkinson's diseases. The fact that …
neurodegenerative disorders such as Alzheimer's and Parkinson's diseases. The fact that …
Experimental and Theoretical Investigation of the Aromatic− Aromatic Interaction in Isolated Capped Dipeptides
E Gloaguen, H Valdes, F Pagliarulo… - The Journal of …, 2010 - ACS Publications
Among the forces responsible for shaping proteins, interactions between side chains of
aromatic residues play an important role as they are involved in the secondary and the …
aromatic residues play an important role as they are involved in the secondary and the …
Effects of mutation on the amyloidogenic propensity of apolipoprotein C-II 60–70 peptide
N Todorova, A Hung, SM Maaser… - Physical Chemistry …, 2010 - pubs.rsc.org
Using experimental and computational methods we identified the effects of mutation on the
structure and dynamics of the amyloidogenic peptide apoC-II (60–70), in monomeric and …
structure and dynamics of the amyloidogenic peptide apoC-II (60–70), in monomeric and …
Self‐assembly of a modified amyloid peptide fragment: pH‐responsiveness and nematic phase formation
IW Hamley, V Castelletto, C Moulton… - Macromolecular …, 2010 - Wiley Online Library
The self‐assembly of peptide YYKLVFFC based on a fragment of the amyloid beta (Aβ)
peptide, Aβ16–20, KLVFF has been studied in aqueous solution. The peptide is designed …
peptide, Aβ16–20, KLVFF has been studied in aqueous solution. The peptide is designed …