Kunihiro Hongo

772 total citations
35 papers, 633 citations indexed

About

Kunihiro Hongo is a scholar working on Molecular Biology, Materials Chemistry and Physiology. According to data from OpenAlex, Kunihiro Hongo has authored 35 papers receiving a total of 633 indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 20 papers in Materials Chemistry and 8 papers in Physiology. Recurrent topics in Kunihiro Hongo's work include Heat shock proteins research (26 papers), Protein Structure and Dynamics (20 papers) and Enzyme Structure and Function (20 papers). Kunihiro Hongo is often cited by papers focused on Heat shock proteins research (26 papers), Protein Structure and Dynamics (20 papers) and Enzyme Structure and Function (20 papers). Kunihiro Hongo collaborates with scholars based in Japan, Mexico and India. Kunihiro Hongo's co-authors include Yasushi Kawata, Tomohiro Mizobata, Hisashi Yagi, Naoya Fukui, Kodai Machida, Takuya Miyazaki, Hiroshi Kameda, Jun Nagai, Takashi Higurashi and Jun Nagai and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Journal of Molecular Biology.

In The Last Decade

Kunihiro Hongo

35 papers receiving 631 citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Kunihiro Hongo Japan 15 429 199 181 138 58 35 633
Francesca Munari Italy 17 483 1.1× 61 0.3× 200 1.1× 129 0.9× 86 1.5× 51 782
Yuichi Yoshimura Japan 17 602 1.4× 141 0.7× 478 2.6× 144 1.0× 63 1.1× 27 983
Md. Mamunul Haque South Korea 14 332 0.8× 118 0.6× 232 1.3× 25 0.2× 63 1.1× 32 722
Tomas Šneideris United Kingdom 17 451 1.1× 58 0.3× 324 1.8× 48 0.3× 37 0.6× 35 773
Claudia Parrini Italy 7 513 1.2× 85 0.4× 453 2.5× 84 0.6× 78 1.3× 7 741
Cecilia Wallin Sweden 15 329 0.8× 59 0.3× 398 2.2× 58 0.4× 21 0.4× 20 667
Gabriele Giachin Italy 20 825 1.9× 83 0.4× 182 1.0× 72 0.5× 33 0.6× 41 984
Karen E. Marshall United Kingdom 15 721 1.7× 136 0.7× 582 3.2× 41 0.3× 51 0.9× 30 1.1k
Antonia Stank Germany 7 584 1.4× 128 0.6× 73 0.4× 24 0.2× 130 2.2× 8 763
Tom Scheidt United Kingdom 10 299 0.7× 38 0.2× 258 1.4× 38 0.3× 45 0.8× 16 498

Countries citing papers authored by Kunihiro Hongo

Since Specialization
Citations

This map shows the geographic impact of Kunihiro Hongo's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Kunihiro Hongo with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Kunihiro Hongo more than expected).

Fields of papers citing papers by Kunihiro Hongo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Kunihiro Hongo. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Kunihiro Hongo. The network helps show where Kunihiro Hongo may publish in the future.

Co-authorship network of co-authors of Kunihiro Hongo

This figure shows the co-authorship network connecting the top 25 collaborators of Kunihiro Hongo. A scholar is included among the top collaborators of Kunihiro Hongo based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Kunihiro Hongo. Kunihiro Hongo is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Ogawa, Kenjirou, et al.. (2023). Effects of the Polyphenols Delphinidin and Rosmarinic Acid on the Inducible Intra-cellular Aggregation of Alpha-Synuclein in Model Neuron Cells. Applied Biochemistry and Biotechnology. 195(7). 4134–4147. 4 indexed citations
2.
Fukui, Naoya, Kunihiro Hongo, Tomohiro Mizobata, et al.. (2021). An α-synuclein decoy peptide prevents cytotoxic α-synuclein aggregation caused by fatty acid binding protein 3. Journal of Biological Chemistry. 296. 100663–100663. 12 indexed citations
3.
Hongo, Kunihiro, et al.. (2018). Acid-denatured small heat shock protein HdeA from Escherichia coli forms reversible fibrils with an atypical secondary structure. Journal of Biological Chemistry. 294(5). 1590–1601. 3 indexed citations
4.
Kameda, Hiroshi, Naoya Fukui, Kunihiro Hongo, et al.. (2016). Common structural features of toxic intermediates from α-synuclein and GroES fibrillogenesis detected using cryogenic coherent X-ray diffraction imaging. The Journal of Biochemistry. 161(1). 55–65. 6 indexed citations
5.
Fukui, Naoya, et al.. (2016). Modulating the Effects of the Bacterial Chaperonin GroEL on Fibrillogenic Polypeptides through Modification of Domain Hinge Architecture. Journal of Biological Chemistry. 291(48). 25217–25226. 12 indexed citations
6.
Ojha, Bimlesh, Naoya Fukui, Kunihiro Hongo, Tomohiro Mizobata, & Yasushi Kawata. (2016). Suppression of amyloid fibrils using the GroEL apical domain. Scientific Reports. 6(1). 31041–31041. 17 indexed citations
7.
Adachi, Masayuki, Kodai Machida, Kunihiro Hongo, et al.. (2015). Structural basis of Cu, Zn-superoxide dismutase amyloid fibril formation involves interaction of multiple peptide core regions. The Journal of Biochemistry. 159(2). 247–260. 18 indexed citations
8.
Kameda, Hiroshi, Naoya Fukui, Kunihiro Hongo, et al.. (2013). Bilberry Anthocyanins Neutralize the Cytotoxicity of Co-Chaperonin GroES Fibrillation Intermediates. Biochemistry. 52(51). 9202–9211. 8 indexed citations
9.
Kameda, Hiroshi, K. Hirakawa, Hisashi Yagi, et al.. (2012). Role of C‐terminal negative charges and tyrosine residues in fibril formation of α‐synuclein. Brain and Behavior. 2(5). 595–605. 65 indexed citations
10.
Hongo, Kunihiro, et al.. (2011). Varied effects of Pyrococcus furiosus prefoldin and P. furiosus chaperonin on the refolding reactions of substrate proteins. The Journal of Biochemistry. 151(4). 383–390. 3 indexed citations
11.
Meshitsuka, Shunsuke, et al.. (2011). Covalent Structural Changes in Unfolded GroES That Lead to Amyloid Fibril Formation Detected by NMR. Journal of Biological Chemistry. 286(24). 21796–21805. 9 indexed citations
12.
Yagi, Hisashi, Akihiro Yoshida, Masahiro Hara, et al.. (2008). Fibril Formation of hsp10 Homologue Proteins and Determination of Fibril Core Regions: Differences in Fibril Core Regions Dependent on Subtle Differences in Amino Acid Sequence. Journal of Molecular Biology. 377(5). 1593–1606. 11 indexed citations
13.
Machida, Kodai, et al.. (2008). Hydrophilic Residues 526KNDAAD531 in the Flexible C-terminal Region of the Chaperonin GroEL Are Critical for Substrate Protein Folding within the Central Cavity. Journal of Biological Chemistry. 283(11). 6886–6896. 33 indexed citations
14.
Hirai, Hiroshi, et al.. (2007). Functional Characterization of the Recombinant Group II Chaperonin   from Thermoplasma acidophilum. The Journal of Biochemistry. 143(4). 505–515. 8 indexed citations
15.
Hongo, Kunihiro, et al.. (2007). Structural Stability of Covalently Linked GroES Heptamer: Advantages in the Formation of Oligomeric Structure. Journal of Molecular Biology. 367(4). 1171–1185. 14 indexed citations
16.
Hongo, Kunihiro, et al.. (2005). A novel ATP/ADP hydrolysis activity of hyperthermostable group II chaperonin in the presence of cobalt or manganese ion. FEBS Letters. 580(1). 34–40. 18 indexed citations
17.
Taniguchi, Masaaki, et al.. (2004). Stopped-flow Fluorescence Analysis of the Conformational Changes in the GroEL Apical Domain. Journal of Biological Chemistry. 279(16). 16368–16376. 32 indexed citations
18.
Miyazaki, Takuya, et al.. (2002). GroEL-Substrate-GroES Ternary Complexes Are an Important Transient Intermediate of the Chaperonin Cycle. Journal of Biological Chemistry. 277(52). 50621–50628. 22 indexed citations
19.
Kawata, Yasushi, Kunihiro Hongo, Tomohiro Mizobata, & Jun Nagai. (1998). Chaperonin GroE-facilitated refolding of disulfide-bonded and reduced Taka-amylase A from Aspergillus oryzae. Protein Engineering Design and Selection. 11(12). 1293–1298. 13 indexed citations
20.
Kawata, Yasushi, et al.. (1995). The role of ATP hydrolysis in the function of the chaperonin GroEL: dynamic complex formation with GroES. FEBS Letters. 369(2-3). 283–286. 12 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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