Misfolding of the amyloid β‐protein: a molecular dynamics study
D Flöck, S Colacino, G Colombo… - … : Structure, Function, and …, 2006 - Wiley Online Library
Amyloid β‐proteins spontaneously aggregate and build plaques in the brains of Alzheimer's
disease patients. The polypeptide has been the subject of extensive in vitro and …
disease patients. The polypeptide has been the subject of extensive in vitro and …
Molecular simulations of amyloid beta assemblies
G Grasso, A Danani - Advances in Physics: X, 2020 - Taylor & Francis
Several neurodegenerative disorders arise from the abnormal protein aggregation in the
nervous tissue leading tointracellular inclusions or extracellular aggregates in specific brain …
nervous tissue leading tointracellular inclusions or extracellular aggregates in specific brain …
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 …
A molecular dynamics approach to the structural characterization of amyloid aggregation
M Cecchini, R Curcio, M Pappalardo, R Melki… - Journal of Molecular …, 2006 - Elsevier
A novel computational approach to the structural analysis of ordered β-aggregation is
presented and validated on three known amyloidogenic polypeptides. The strategy is based …
presented and validated on three known amyloidogenic polypeptides. The strategy is based …
Thermodynamics and dynamics of amyloid peptide oligomerization are sequence dependent
Y Lu, P Derreumaux, Z Guo… - Proteins: Structure …, 2009 - Wiley Online Library
Aggregation of the full‐length amyloid‐β (Aβ) and β2‐microglobulin (β2m) proteins is
associated with Alzheimer's disease and dialysis‐related amyloidosis, respectively. This …
associated with Alzheimer's disease and dialysis‐related amyloidosis, respectively. This …
Structure of the 21–30 fragment of amyloid β‐protein
A Baumketner, SL Bernstein, T Wyttenbach… - Protein …, 2006 - Wiley Online Library
Folding and self‐assembly of the 42‐residue amyloid β‐protein (Aβ) are linked to
Alzheimer's disease (AD). The 21–30 region of Aβ, Aβ (21–30), is resistant to proteolysis …
Alzheimer's disease (AD). The 21–30 region of Aβ, Aβ (21–30), is resistant to proteolysis …
Simulation of pH‐dependent edge strand rearrangement in human β‐2 microglobulin
Amyloid fibrils formed from unrelated proteins often share morphological similarities,
suggesting common biophysicalmechanisms for amyloidogenesis. Biochemical studies of …
suggesting common biophysicalmechanisms for amyloidogenesis. Biochemical studies of …
[HTML][HTML] Investigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer
The aggregation of amyloid beta (Aβ) peptides plays an important role in the development of
Alzheimer's disease. Despite extensive effort, it has been difficult to characterize the …
Alzheimer's disease. Despite extensive effort, it has been difficult to characterize the …
A Study of the α-Helical Intermediate Preceding the Aggregation of the Amino-Terminal Fragment of the β Amyloid Peptide (Aβ1–28)
The β amyloid (Aβ) peptide aggregates to form β-rich structures that are known to trigger
Alzheimer's disease. Experiments suggest that an α-helical intermediate precedes the …
Alzheimer's disease. Experiments suggest that an α-helical intermediate precedes the …
[HTML][HTML] Competition between intramolecular and intermolecular interactions in an amyloid-forming protein
KE Routledge, GG Tartaglia, GW Platt… - Journal of molecular …, 2009 - Elsevier
Despite much progress in understanding the folding and the aggregation processes of
proteins, the rules defining their interplay have yet to be fully defined. This problem is of …
proteins, the rules defining their interplay have yet to be fully defined. This problem is of …