HONGO Kunihiro 本郷邦広

Researcher Number	80335504
Other IDs
Affiliation (Current)	2025: 鳥取大学, 工学部, 助教
Affiliation (based on the past Project Information) *help	2006: Tottori University, Faculty of Engineering, Assistant Professor 2005 – 2006: Tottori University, Faculty of Engineering, Associate Professor, 工学部, 助手 2004: 国立大学法人鳥取大学, 工学部, 助手 2002 – 2003: 鳥取大学, 工学部, 助手
Review Section/Research Field	Except Principal Investigator Structural biochemistry / Biological Sciences
Keywords	Except Principal Investigator Oligomeric protein / Amyloid fibril / Chaperonin / Molecular chaperone / 構造安定性 / αシヌクレイン / アミロイド線維形成 / 機能発現機構 / GroES / オリゴマー蛋白質 … More / アミロイド線維 / コンフォメーション変化 / シャペロニン / 分子シャペロン / Neurodegenerative disease / Functional mechanism / Molecular compactness / α-synuclein / シャペロニンGroES / 蛋白質の構造安定性 / 構造変化 / コンフォメーション病 / 脳神経変性病 / 分子のコンパクトさ / Ncurodegenerative disease / Thermostable enzyme / Folding / Conformational change / シャペロニンGroEL / オリゴマー酵素 / 耐熱性シャペロニン / 神経変性病 / 耐熱性酵素 / 構造形成反応 Less

Molecular study on large conformational changes of protein that relates biofunction and diseases
- Principal Investigator
  
  KAWATA Yasushi
- Project Period (FY)
  2003 – 2005
- Research Category
  
  Grant-in-Aid for Scientific Research (B)
- Research Field
  
  Structural biochemistry
- Research Institution
  Tottori University
Protein conformational changes and molecular chaperone
- Principal Investigator
  
  KAWATA Yasushi
- Project Period (FY)
  2002 – 2006
- Research Category
  
  Grant-in-Aid for Scientific Research on Priority Areas
- Review Section
  
  Biological Sciences
- Research Institution
  Tottori University

All 2006 2005 2004

All Journal Article

[Journal Article] Multiple structural transitions of the GroEL subunit are sensitive to intermolecular interactions with cochaperonin and refolding polypeptide2006
- Author(s)
  Tatsunari Yoshimi, Kunihiro Hongo, Tomohiro Mizobata, Yasushi Kawata
- Journal Title
  
  Journal of Biochemistry (印刷中)
- NAID
  10018846460
- Data Source
  KAKENHI-PROJECT-14037241
[Journal Article] A Novel ATP/ADP Hydrolysis Activity of Hyperthermostable Group II Chaperonin in the Presence of Cobalt or Manganese Ion2006
- Author(s)
  Kunihiro Hongo, Hidenori Hirai, Chisato Uemura, Shujiro Ono, Junjiro Tsunemi, Takashi Higurashi, Tomohiro Mizobata, Yasushi Kawata
- Journal Title
  
  FEBS Letters 580
  
  Pages: 34-40
- Description
  「研究成果報告書概要(欧文)」より
- Data Source
  KAKENHI-PROJECT-15370047
[Journal Article] Multiple structural transitions of the GroEL subunit are sensitive to intermolecular interactions with cochaperonin and refolding polypeptide2006
- Author(s)
  Tatsunari Yoshimi, Kunihiro Hongo, Tomohiro Mizobata, Yasushi Kawata
- Journal Title
  
  Journal of Biochemistry 139・3
  
  Pages: 407-419
- NAID
  10018846460
- Data Source
  KAKENHI-PROJECT-14037241
[Journal Article] A Novel ATP/ADP Hydrolysis Activity of Hyperthermostable Group II Chaperonin in the Presence of Cobalt or Manganese Ion2006
- Author(s)
  Kunihiro Hongo et al.
- Journal Title
  
  FEBS Letters 580
  
  Pages: 34-40
- Description
  「研究成果報告書概要(和文)」より
- Data Source
  KAKENHI-PROJECT-15370047
[Journal Article] A Novel ATP/ADP Hydrolysis Activity of Hyperthermostable Group II Chaperonin in the Presence of Cobalt or Manganese Ion2006
- Author(s)
  Kunihiro Hongo et al.
- Journal Title
  
  FEBS Letters 580
  
  Pages: 34-40
- Data Source
  KAKENHI-PROJECT-14037241
[Journal Article] Amyloid Fibril Formation of a-Synuclein is Accelerated by Preformed Amyloid Seeds of Other Proteins : Implications for the Mechanism of Transmissible Conformational Diseases2005
- Author(s)
  Hisashi Yagi, Eiko Kusaka, Kunihiro Hongo, Tomohiro Mizobata, Yasushi Kawata
- Journal Title
  
  Journal of Biological Chemistry 280(46)
  
  Pages: 38609-38616
- Description
  「研究成果報告書概要(欧文)」より
- Data Source
  KAKENHI-PROJECT-15370047
[Journal Article] Amyloid Fibril Formation of α-Synuclein is Accelerated by Preformed Amyloid Seeds of Other Proteins : Implications for the Mechanism of Transmissible Conformational Diseases2005
- Author(s)
  Hisashi Yagi, Eiko Kusaka, Kunihiro Hongo, Tomohiro Mizobata, Yasushi Kawata
- Journal Title
  
  Journal of Biological Chemistry 280・46
  
  Pages: 38609-38616
- Data Source
  KAKENHI-PROJECT-14037241
[Journal Article] Amyloid Fibril Formation of α-Synuclein is Accelerated by Preformed Amyloid Seeds of Other Proteins: Implications for the Mechanism of Transmissible Conformational Diseases2005
- Author(s)
  Hisashi Yagi, Eiko Kusaka, Kunihiro Hongo, Tomohiro Mizobata, Yasushi Kawata
- Journal Title
  
  Journal of Biological Chemistry 280(46)
  
  Pages: 38609-38616
- Description
  「研究成果報告書概要(欧文)」より
- Data Source
  KAKENHI-PROJECT-14037241
[Journal Article] Amyloid Fibril Formation of a-Synuclein is Accelerated by Preformed Amyloid Seeds of Other Proteins : Implications for the Mechanism of Transmissible Conformational Diseases2005
- Author(s)
  Hisashi Yagi, Eiko Kusaka, Kunihiro Hongo, Tomohiro Mizobata, Yasushi Kawata
- Journal Title
  
  Journal of Biological Chemistry 280・46
  
  Pages: 38609-38616
- Data Source
  KAKENHI-PROJECT-15370047
[Journal Article] Amyloid Fibril Formation of a-Synuclein is Accelerated by Preformed Amyloid Seeds of Other Proteins : Implications for the Mechanism of Transmissible Conformational Diseases2005
- Author(s)
  Hisashi Yagi, Eiko Kusaka, Kunihiro Hongo, Tomohiro Mizobana, Yasushi Kawata
- Journal Title
  
  J. Biol. Chem. 280・46
  
  Pages: 38609-38616
- Description
  「研究成果報告書概要(和文)」より
- Data Source
  KAKENHI-PROJECT-15370047
[Journal Article] Stopped-Flow Fluorescence Analysis of the Conformational Changes in the GroEL Apical Domain : Relationships between Movements in the Apical Domain and the Quaternary Structure of GroEL2004
- Author(s)
  Masaaki Taniguchi, Tatsunari Yoshimi, Kunihiro Hongo, Tomohiro Mizobata, Yasushi Kawata
- Journal Title
  
  Journal of Biological Chemistry 279(16)
  
  Pages: 16368-16376
- Description
  「研究成果報告書概要(欧文)」より
- Data Source
  KAKENHI-PROJECT-15370047
[Journal Article] Stopped-Flow Fluorescence Analysis of the Conformational Changes in the GroEL Apical Domain: Relationships between Movements in the Apical Domain and the Quaternary Structure of GroEL2004
- Author(s)
  Masaaki Taniguchi, Tatsunari Yoshimi, Kunihiro Hongo, Tomohiro Mizobata, Yasushi Kawata
- Journal Title
  
  Journal of Biological Chemistry 279(16)
  
  Pages: 16368-16376
- Description
  「研究成果報告書概要(欧文)」より
- Data Source
  KAKENHI-PROJECT-14037241

1. KAWATA Yasushi (40177697)

# of Collaborated Projects: 2 results

# of Collaborated Products: 10 results
2. MIZOBATA Tomohiro (50263489)

# of Collaborated Projects: 2 results

# of Collaborated Products: 9 results

HONGO Kunihiro 本郷 邦広

Research Projects

Research Products

Co-Researchers

Molecular study on large conformational changes of protein that relates biofunction and diseases

Principal Investigator

Project Period (FY)

Research Category

Research Field

Research Institution

Protein conformational changes and molecular chaperone

Principal Investigator

Project Period (FY)

Research Category

Review Section

Research Institution

[Journal Article] Multiple structural transitions of the GroEL subunit are sensitive to intermolecular interactions with cochaperonin and refolding polypeptide2006

Author(s)

Journal Title

NAID

Data Source

[Journal Article] A Novel ATP/ADP Hydrolysis Activity of Hyperthermostable Group II Chaperonin in the Presence of Cobalt or Manganese Ion2006

Author(s)

Journal Title

Description

Data Source

[Journal Article] Multiple structural transitions of the GroEL subunit are sensitive to intermolecular interactions with cochaperonin and refolding polypeptide2006

Author(s)

Journal Title

NAID

Data Source

[Journal Article] A Novel ATP/ADP Hydrolysis Activity of Hyperthermostable Group II Chaperonin in the Presence of Cobalt or Manganese Ion2006

Author(s)

Journal Title

Description

Data Source

[Journal Article] A Novel ATP/ADP Hydrolysis Activity of Hyperthermostable Group II Chaperonin in the Presence of Cobalt or Manganese Ion2006

Author(s)

Journal Title

Data Source

[Journal Article] Amyloid Fibril Formation of a-Synuclein is Accelerated by Preformed Amyloid Seeds of Other Proteins : Implications for the Mechanism of Transmissible Conformational Diseases2005

Author(s)

Journal Title

Description

Data Source

[Journal Article] Amyloid Fibril Formation of α-Synuclein is Accelerated by Preformed Amyloid Seeds of Other Proteins : Implications for the Mechanism of Transmissible Conformational Diseases2005

Author(s)

Journal Title

Data Source

[Journal Article] Amyloid Fibril Formation of α-Synuclein is Accelerated by Preformed Amyloid Seeds of Other Proteins: Implications for the Mechanism of Transmissible Conformational Diseases2005

Author(s)

Journal Title

Description

Data Source

[Journal Article] Amyloid Fibril Formation of a-Synuclein is Accelerated by Preformed Amyloid Seeds of Other Proteins : Implications for the Mechanism of Transmissible Conformational Diseases2005

Author(s)

Journal Title

Data Source

[Journal Article] Amyloid Fibril Formation of a-Synuclein is Accelerated by Preformed Amyloid Seeds of Other Proteins : Implications for the Mechanism of Transmissible Conformational Diseases2005

Author(s)

Journal Title

Description

Data Source

[Journal Article] Stopped-Flow Fluorescence Analysis of the Conformational Changes in the GroEL Apical Domain : Relationships between Movements in the Apical Domain and the Quaternary Structure of GroEL2004

Author(s)

Journal Title

Description

Data Source

[Journal Article] Stopped-Flow Fluorescence Analysis of the Conformational Changes in the GroEL Apical Domain: Relationships between Movements in the Apical Domain and the Quaternary Structure of GroEL2004

Author(s)

Journal Title

Description

Data Source

HONGO Kunihiro 本郷邦広