Kien Xuan NGO

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Assistant Professor

Kanazawa University

Japan

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About

Kien Xuan NGO is an Assistant Professor at Kanazawa University in Japan. His research focuses on actin function regulation, intrinsically disordered proteins, and the dynamics of protein interactions, as reflected in his recent articles. He employs advanced techniques such as high-speed atomic force microscopy to study molecular interactions and their implications in cellular processes.

Recent Grants

Grant: Close

Structures and dynamics of ABC transporters MsbA and LptB2FG in working with LptC during transport activities

Open Date: 2023-04-01

Close Date: 2026-03-01

Grant: Close

The mechanism of sparsely coupled actin-binding proteins regulate the function of the entire actin filament.

Open Date: 2023-04-01

Close Date: 2026-03-01

Grant: Close

Pore formation of alpha-toxin from Staphylococcus aureus and its toxoids investigated by Atomic Force Microscopy

Open Date: 2022-04-01

Close Date: 2023-03-01

Grant: Close

Temperature-modulated supramolecular nanomachinery for manipulating programmed cell death

Open Date: 2022-04-01

Close Date: 2023-03-01

Grant: Close

Structural Dynamics of ABC Transporter MsbA during Functional Activity

Open Date: 2019-04-01

Close Date: 2022-03-01

Articles (14)

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2025

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2024

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2024

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2024

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2024

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2024

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2024

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2023

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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 (15)

Noriyuki Kodera

Kanazawa University

JAPAN

Kien Xuan NGO

Research Interests

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About

Recent Grants

Articles (14)

Imaging oligomers of alpha-toxin (Hla) variants using high-speed AFM and neutralizing Hla hemolytic activity with their antisera

Multiple Mechanisms to Regulate Actin Functions: “Fundamental” Versus Lineage-Specific Mechanisms and Hierarchical Relationships

Deciphering the actin structure-dependent preferential cooperative binding of cofilin

Deciphering the actin structure-dependent preferential cooperative binding of cofilin

S100A11 promotes focal adhesion disassembly via myosin II-driven contractility and Piezo1-mediated Ca2+ entry

PQBP3/NOL7 is an intrinsically disordered protein

PQBP3 prevents senescence by suppressing PSME3-mediated proteasomal Lamin B1 degradation

High-Speed Atomic Force Microscopy for Filming Protein Molecules in Dynamic Action

Actin-binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II

Unraveling the host-selective toxic interaction of cassiicolin with lipid membranes and its cytotoxicity

High-speed atomic force microscopy reveals a three-state elevator mechanism in the citrate transporter CitS

GTP-dependent formation of straight tubulin oligomers leads to microtubule nucleation

GTP-dependent formation of straight tubulin oligomers leads to microtubule nucleation

Correlative AFM and fluorescence imaging demonstrate nanoscale membrane remodeling and ring-like and tubular structure formation by septins

Collaborators (15)

Noriyuki Kodera

Shinji Kamimura

Keiko Hirose

Kentaro Nakano

Stéphanie Mangenot

Aurélie Bertin

Clemens Franz

Taro QP Uyeda

Benoît Gigant

TOSHIO ANDO

Azuma Taoka

Masak Takaine

Kiyotaka Tokuraku

Dirk Jan Slotboom

Hidenori Homma

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