Effects of a hydrophilic/hydrophobic interface on amyloid-β peptides studied by molecular dynamics simulations and NMR experiments

SG Itoh, M Yagi-Utsumi, K Kato… - The Journal of Physical …, 2018 - ACS Publications
Oligomer formation of amyloid-β peptides (Aβ) is accelerated at a hydrophilic/hydrophobic
interface. However, details of the acceleration mechanism have not been elucidated. To …
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Effects of a Hydrophilic/Hydrophobic Interface on Amyloid-β Peptides Studied by Molecular Dynamics Simulations and NMR Experiments

SG Itoh, M Yagi-Utsumi, K Kato… - The journal of …, 2019 - pubmed.ncbi.nlm.nih.gov
Oligomer formation of amyloid-β peptides (Aβ) is accelerated at a hydrophilic/hydrophobic
interface. However, details of the acceleration mechanism have not been elucidated. To …
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[CITATION][C] Effects of a Hydrophilic/Hydrophobic Interface on Amyloid-β Peptides Studied by Molecular Dynamics Simulations and NMR Experiments

SG Itoh, M Yagi-Utsumi, K Kato… - The Journal of Physical …, 2018 - cir.nii.ac.jp
Effects of a Hydrophilic/Hydrophobic Interface on Amyloid-β Peptides Studied by Molecular
Dynamics Simulations and NMR Experiments | CiNii Research CiNii 国立情報学研究所 学術情報 …
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Effects of a Hydrophilic/Hydrophobic Interface on Amyloid-β Peptides Studied by Molecular Dynamics Simulations and NMR Experiments.

SG Itoh, M Yagi-Utsumi, K Kato… - The Journal of Physical …, 2019 - europepmc.org
Oligomer formation of amyloid-β peptides (Aβ) is accelerated at a hydrophilic/hydrophobic
interface. However, details of the acceleration mechanism have not been elucidated. To …
Cite

[CITATION][C] Effects of a Hydrophilic/Hydrophobic Interface on Amyloid-β Peptides Studied by Molecular Dynamics Simulations and NMR Experiments

SG Itoh, M Yagi-Utsumi, K Kato, H Okumura - 2018
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