A partially folded structure of amyloid-beta (1–40) in an aqueous environment
S Vivekanandan, JR Brender, SY Lee… - Biochemical and …, 2011 - Elsevier
Aggregation of the Aβ1–40 peptide is linked to the development of extracellular plaques
characteristic of Alzheimer's disease. While previous studies commonly show the Aβ1–40 is …
characteristic of Alzheimer's disease. While previous studies commonly show the Aβ1–40 is …
Atomic-level characterization of the ensemble of the Aβ (1–42) monomer in water using unbiased molecular dynamics simulations and spectral algorithms
NG Sgourakis, M Merced-Serrano, C Boutsidis… - Journal of molecular …, 2011 - Elsevier
Aβ (1–42) is the highly pathologic isoform of amyloid-β, the peptide constituent of fibrils and
neurotoxic oligomers involved in Alzheimer's disease. Recent studies on the structural …
neurotoxic oligomers involved in Alzheimer's disease. Recent studies on the structural …
Differences in β-strand populations of monomeric Aβ40 and Aβ42
Using homonuclear 1 H NOESY spectra, with chemical shifts, 3 JHNH α scalar couplings,
residual dipolar couplings, and 1 H-15 N NOEs, we have optimized and validated the …
residual dipolar couplings, and 1 H-15 N NOEs, we have optimized and validated the …
Effect of zinc binding on β-amyloid structure and dynamics: implications for Aβ aggregation
N Rezaei-Ghaleh, K Giller, S Becker, M Zweckstetter - Biophysical journal, 2011 - cell.com
Assembly of β-amyloid (Aβ) peptide into toxic oligomers is widely believed to initiate
Alzheimer's disease pathogenesis. Under in vitro physiological conditions, zinc (Zn (II)) can …
Alzheimer's disease pathogenesis. Under in vitro physiological conditions, zinc (Zn (II)) can …
Identification of small-molecule binding pockets in the soluble monomeric form of the Aβ42 peptide
M Zhu, A De Simone, D Schenk, G Toth… - The Journal of …, 2013 - pubs.aip.org
The aggregation of intrinsically disordered peptides and proteins is associated with a wide
range of highly debilitating neurological and systemic disorders. In this work we explored the …
range of highly debilitating neurological and systemic disorders. In this work we explored the …
Characterizing amyloid‐beta protein misfolding from molecular dynamics simulations with explicit water
Extracellular deposition of amyloid‐beta (Aβ) protein, a fragment of membrane glycoprotein
called β‐amyloid precursor transmembrane protein (βAPP), is the major characteristic for the …
called β‐amyloid precursor transmembrane protein (βAPP), is the major characteristic for the …
Comparison of structure determination methods for intrinsically disordered amyloid-β peptides
Intrinsically disordered proteins (IDPs) represent a new frontier in structural biology since the
primary characteristic of IDPs is that structures need to be characterized as diverse …
primary characteristic of IDPs is that structures need to be characterized as diverse …
Reorientational dynamics of amyloid-β from NMR spin relaxation and molecular simulation
N Rezaei-Ghaleh, G Parigi… - The Journal of Physical …, 2019 - ACS Publications
Amyloid-β (Aβ) aggregation is a hallmark of Alzheimer's disease. As an intrinsically
disordered protein, Aβ undergoes extensive dynamics on multiple length and time scales …
disordered protein, Aβ undergoes extensive dynamics on multiple length and time scales …
The hazardous effects of the environmental toxic gases on amyloid beta-peptide aggregation: A theoretical perspective
Alzheimer's disease (AD) is one of the leading causes of dementia in elderly people. It has
been well documented that the exposure to environmental toxins such as CO, CO 2, SO 2 …
been well documented that the exposure to environmental toxins such as CO, CO 2, SO 2 …
Characterizing the structural and thermodynamic properties of Aβ42 and Aβ40
The self-assembly of amyloid-beta (Aβ) proteins in aqueous extracellular environments is
implicated in Alzheimer's disease. Among several alloforms of Aβ proteins differing in …
implicated in Alzheimer's disease. Among several alloforms of Aβ proteins differing in …