Hidekazu Hiroaki

Professor

Nagoya University

Japan

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Professor Hidekazu Hiroaki serves at Nagoya University in Japan. His research primarily focuses on molecular biology, particularly related to Wnt signaling processes, protein interactions, and the molecular mechanisms of amyloid-β peptide formation. He has contributed to significant findings regarding the inhibition of tight junctions and the potential therapeutic roles of the p53 tumor suppressor. His recent articles reflect a strong interest in the biochemical pathways and molecular interactions that are critical in various biological processes.

Articles (14)

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2025

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2023

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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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2020

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2020

Collaborators (3)

Shota Suzuki

project assistant profoassor

Institute of Science Tokyo

JAPAN

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Emi Hibino

Assistant Professor

Nagoya University

JAPAN

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Nobutaka Numoto

Special-Appointment Associate Professor

Okayama University

JAPAN

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Hidekazu Hiroaki

Research Interests

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Articles (14)

A Unique Trimeric Assembly of Human Dishevelled 1 PDZ Domain in Crystal: Implication of Homo- and Hetero-Oligomerization During Wnt Signaling Process

A Cost-Effective Immobilization Method for MBP Fusion Proteins on Microtiter Plates Using a Gelatinized Starch–Agarose Mixture and Its Application for Convenient Protein–Protein Interaction Analysis

Pharmacologic Comparison of High-Dose Hesperetin and Quercetin on MDCK II Cell Viability, Tight Junction Integrity, and Cell Shape

Small-Molecule-Mediated Suppression of BMP Signaling by Selective Inhibition of BMP1-Dependent Chordin Cleavage

Molecular mechanisms of amyloid-β peptide fibril and oligomer formation: NMR-based challenges

A cryptic phosphate-binding pocket on the SPFH domain of human stomatin that regulates a novel fibril-like self-assembly

Direct inhibition of the first PDZ domain of ZO-1 by glycyrrhizin is a possible mechanism of tight junction opening of Caco-2 cells

Potential of rescue and reactivation of tumor suppressor p53 for cancer therapy

Relevance of Amorphous and Amyloid-Like Aggregates of the p53 Core Domain to Loss of its DNA-Binding Activity

Direct inhibition of the first PDZ domain of ZO-1 by glycyrrhizin is a possible mechanism of tight junction opening of Caco-2 cells

NMR-Guided Repositioning of Non-Steroidal Anti-Inflammatory Drugs into Tight Junction Modulators

Cryoprotective activities of FK20, a human genome-derived intrinsically disordered peptide against cryosensitive enzymes without a stereospecific molecular interaction

Opposing Effect of Naringenin and Quercetin on the Junctional Compartment of MDCK II Cells to Modulate the Tight Junction

High dose of baicalin or baicalein can reduce tight junction integrity by partly targeting the first PDZ domain of zonula occludens-1 (ZO-1)

Collaborators (3)

Shota Suzuki

Emi Hibino

Nobutaka Numoto

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