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Amyloid oligomers: A joint experimental/computational perspective on Alzheimer's disease, Parkinson's disease, type II diabetes, and amyotrophic lateral sclerosis
Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …
Simulation studies of amyloidogenic polypeptides and their aggregates
Amyloids, fibrillar assembly of (poly) peptide chains, are associated with neurodegenerative
illnesses such as Alzheimer's and Parkinson's diseases, for which there are no cures. The …
illnesses such as Alzheimer's and Parkinson's diseases, for which there are no cures. The …
Energy landscapes of protein aggregation and conformation switching in intrinsically disordered proteins
The protein folding problem was apparently solved recently by the advent of a deep learning
method for protein structure prediction called AlphaFold. However, this program is not able …
method for protein structure prediction called AlphaFold. However, this program is not able …
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 …
Structures of the intrinsically disordered Aβ, tau and α-synuclein proteins in aqueous solution from computer simulations
PH Nguyen, P Derreumaux - Biophysical Chemistry, 2020 - Elsevier
Intrinsically disordered proteins (IDPs) play many biological roles in the human proteome
ranging from vesicular transport, signal transduction to neurodegenerative diseases. The Aβ …
ranging from vesicular transport, signal transduction to neurodegenerative diseases. The Aβ …
Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane
Mounting evidence suggests that the neuronal cell membrane is the main site of oligomer-
mediated neuronal toxicity of amyloid-β peptides in Alzheimer's disease. To gain a detailed …
mediated neuronal toxicity of amyloid-β peptides in Alzheimer's disease. To gain a detailed …
Key residue for aggregation of Amyloid-β peptides
It is known that oligomers of amyloid-β (Aβ) peptide are associated with Alzheimer's disease.
Aβ has two isoforms: Aβ40 and Aβ42. Although the difference between Aβ40 and Aβ42 is …
Aβ has two isoforms: Aβ40 and Aβ42. Although the difference between Aβ40 and Aβ42 is …
High-resolution structures of the amyloid-β 1–42 dimers from the comparison of four atomistic force fields
The dimer of the amyloid-β peptide Aβ of 42 residues is the smallest toxic species in
Alzheimer's disease, but its equilibrium structures are unknown. Here we determined the …
Alzheimer's disease, but its equilibrium structures are unknown. Here we determined the …
Advances in the simulation of protein aggregation at the atomistic scale
Protein aggregation into highly structured amyloid fibrils is associated with various diseases
including Alzheimer's disease, Parkinson's disease, and type II diabetes. Amyloids can also …
including Alzheimer's disease, Parkinson's disease, and type II diabetes. Amyloids can also …
An account of amyloid oligomers: facts and figures obtained from experiments and simulations
The deposition of amyloid in brain tissue in the context of neurodegenerative diseases
involves the formation of intermediate species—termed oligomers—of lower molecular mass …
involves the formation of intermediate species—termed oligomers—of lower molecular mass …