Satoru Itoh

助教/Assistant Professor

分子科学研究所/Institute for Molecular Science

Japan

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Satoru Itoh is an Assistant Professor at the Institute for Molecular Science in Japan. His research areas encompass molecular dynamics simulations, with a particular focus on amyloid-β aggregation, RNA-dependent RNA polymerase of SARS-CoV-2, and polyalanine aggregates. Recent publications highlight his contributions to understanding the mechanisms of fibrillization and the effects of environmental conditions on peptide behavior.

Articles (14)

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2023

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2023

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2023

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2022

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2022

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2022

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2022

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2022

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2021

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2021

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2021

Collaborators (3)

Maho Yagi-Utsumi

助教/Assistant Professor

自然科学研究機構　生命創成探究センター/Exploratory Research Center on Life and Living Systems

JAPAN

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HISASHI OKUMURA

准教授/Associate Professor

自然科学研究機構　生命創成探究センター/Exploratory Research Center on Life and Living Systems

JAPAN

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Masataka Yamauchi

ACS Computers in Chemistry

JAPAN

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Satoru Itoh

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Articles (14)

Dissociation process of polyalanine aggregates by free electron laser irradiation

The Double-Layered Structure of Amyloid-β Assemblage on GM1-Containing Membranes Catalytically Promotes Fibrillization

Ingenuity in performing replica permutation: How to order the state labels for improving sampling efficiency

Inhibition of amyloid-β(16–22) aggregation by polyphenols using replica permutation with solute tempering molecular dynamics simulation

State-of-the-Art Molecular Dynamics Simulation Studies of RNA-Dependent RNA Polymerase of SARS-CoV-2

Implementations of replica-permutation and replica sub-permutation methods into LAMMPS

Critical contributions of pre-S1 shoulder and distal TRP box in DAG-activated TRPC6 channel by PIP2 regulation

Molecular Dynamics Simulation Studies on the Aggregation of Amyloid-β Peptides and Their Disaggregation by Ultrasonic Wave and Infrared Laser Irradiation

Molecular dynamics simulations of amyloid-β peptides in heterogeneous environments.

Tardigrade Secretory-Abundant Heat-Soluble Protein Varies Entrance Propensity Depending on the Amino-Acid Sequence

Replica permutation with solute tempering for molecular dynamics simulation and its application to the dimerization of amyloid-β fragments

Tardigrade Secretory-Abundant Heat-Soluble Protein Has a Flexible β-Barrel Structure in Solution and Keeps This Structure in Dehydration

Role of Water Molecules and Helix Structure Stabilization in the Laser-Induced Disruption of Amyloid Fibrils Observed by Nonequilibrium Molecular Dynamics Simulations

Promotion and Inhibition of Amyloid-β Peptide Aggregation: Molecular Dynamics Studies

Collaborators (3)

Maho Yagi-Utsumi

HISASHI OKUMURA

Masataka Yamauchi

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Satoru Itoh

Research Interests

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Contact this professor

About

Articles (14)

Dissociation process of polyalanine aggregates by free electron laser irradiation

The Double-Layered Structure of Amyloid-β Assemblage on GM1-Containing Membranes Catalytically Promotes Fibrillization

Ingenuity in performing replica permutation: How to order the state labels for improving sampling efficiency

Inhibition of amyloid-β(16–22) aggregation by polyphenols using replica permutation with solute tempering molecular dynamics simulation

State-of-the-Art Molecular Dynamics Simulation Studies of RNA-Dependent RNA Polymerase of SARS-CoV-2

Implementations of replica-permutation and replica sub-permutation methods into LAMMPS

Critical contributions of pre-S1 shoulder and distal TRP box in DAG-activated TRPC6 channel by PIP2 regulation

Molecular Dynamics Simulation Studies on the Aggregation of Amyloid-&beta; Peptides and Their Disaggregation by Ultrasonic Wave and Infrared Laser Irradiation

Molecular dynamics simulations of amyloid-β peptides in heterogeneous environments.

Tardigrade Secretory-Abundant Heat-Soluble Protein Varies Entrance Propensity Depending on the Amino-Acid Sequence

Replica permutation with solute tempering for molecular dynamics simulation and its application to the dimerization of amyloid-β fragments

Tardigrade Secretory-Abundant Heat-Soluble Protein Has a Flexible β-Barrel Structure in Solution and Keeps This Structure in Dehydration

Role of Water Molecules and Helix Structure Stabilization in the Laser-Induced Disruption of Amyloid Fibrils Observed by Nonequilibrium Molecular Dynamics Simulations

Promotion and Inhibition of Amyloid-β Peptide Aggregation: Molecular Dynamics Studies

Collaborators (3)

Maho Yagi-Utsumi

HISASHI OKUMURA

Masataka Yamauchi

Make your next move.

Molecular Dynamics Simulation Studies on the Aggregation of Amyloid-β Peptides and Their Disaggregation by Ultrasonic Wave and Infrared Laser Irradiation