Ryo Honda

488 total citations
36 papers, 363 citations indexed

About

Ryo Honda is a scholar working on Molecular Biology, Neurology and Nutrition and Dietetics. According to data from OpenAlex, Ryo Honda has authored 36 papers receiving a total of 363 indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 9 papers in Neurology and 8 papers in Nutrition and Dietetics. Recurrent topics in Ryo Honda's work include Prion Diseases and Protein Misfolding (14 papers), Neurological diseases and metabolism (9 papers) and Alzheimer's disease research and treatments (6 papers). Ryo Honda is often cited by papers focused on Prion Diseases and Protein Misfolding (14 papers), Neurological diseases and metabolism (9 papers) and Alzheimer's disease research and treatments (6 papers). Ryo Honda collaborates with scholars based in Japan, United States and Sweden. Ryo Honda's co-authors include Kazuo Kuwata, K. Yamaguchi, Tatsushi Nakayama, Yuji O. Kamatari, Heinrich Röder, Ming Xu, Nobuhiko Sugito, Hiroshi Ueda, Satoshi Endo and Yukihiro Akao and has published in prestigious journals such as Journal of Biological Chemistry, Angewandte Chemie International Edition and Journal of Clinical Investigation.

In The Last Decade

Ryo Honda

34 papers receiving 361 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ryo Honda Japan 11 247 62 59 53 37 36 363
Sonali Kumari India 8 137 0.6× 34 0.5× 84 1.4× 16 0.3× 23 0.6× 20 381
Lucas S. Dantas Brazil 8 172 0.7× 52 0.8× 16 0.3× 18 0.3× 28 0.8× 12 415
Yi‐Wen Lai Taiwan 9 155 0.6× 36 0.6× 49 0.8× 23 0.4× 21 0.6× 19 385
Abida Arshad Pakistan 8 200 0.8× 40 0.6× 19 0.3× 17 0.3× 14 0.4× 25 434
Mouadh Mihoub France 8 241 1.0× 107 1.7× 14 0.2× 40 0.8× 17 0.5× 11 523
Toni Kühl Germany 15 466 1.9× 92 1.5× 34 0.6× 23 0.4× 22 0.6× 32 692
S.R. Bharath India 12 319 1.3× 57 0.9× 16 0.3× 30 0.6× 10 0.3× 21 408
Kyoung-Chan Park South Korea 9 181 0.7× 27 0.4× 39 0.7× 21 0.4× 8 0.2× 11 347
César Millán‐Pacheco Mexico 12 311 1.3× 20 0.3× 42 0.7× 14 0.3× 15 0.4× 56 546
Soraia Pinto Portugal 11 122 0.5× 31 0.5× 27 0.5× 35 0.7× 34 0.9× 19 441

Countries citing papers authored by Ryo Honda

Since Specialization
Citations

This map shows the geographic impact of Ryo Honda'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 Ryo Honda with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Ryo Honda more than expected).

Fields of papers citing papers by Ryo Honda

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ryo Honda. 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 Ryo Honda. The network helps show where Ryo Honda may publish in the future.

Co-authorship network of co-authors of Ryo Honda

This figure shows the co-authorship network connecting the top 25 collaborators of Ryo Honda. A scholar is included among the top collaborators of Ryo Honda 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 Ryo Honda. Ryo Honda 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
2.
Honda, Ryo, Yuta Yoshino, Naohito Abe, et al.. (2025). Gnetin C sensitizes darolutamide-resistant prostate cancer cells by targeting NAD+ and energy metabolism. Biochemical and Biophysical Research Communications. 770. 152009–152009. 1 indexed citations
3.
Hijioka, Masanori, Yoshiaki Nomura, Ryo Honda, et al.. (2024). Galantamine suppresses α-synuclein aggregation by inducing autophagy via the activation of α7 nicotinic acetylcholine receptors. Journal of Pharmacological Sciences. 156(2). 102–114. 3 indexed citations
4.
Endo, Satoshi, Kazuya Fukasawa, Shigeo Takashima, et al.. (2023). ARL-17477 is a dual inhibitor of NOS1 and the autophagic-lysosomal system that prevents tumor growth in vitro and in vivo. Scientific Reports. 13(1). 10757–10757. 1 indexed citations
5.
Inden, Masatoshi, et al.. (2023). Development of TDP-43 RT-QuIC method. Proceedings for Annual Meeting of The Japanese Pharmacological Society. 97(0). 2–B. 1 indexed citations
6.
Heishima, Kazuki, Nobuhiko Sugito, Tomoyoshi Soga, et al.. (2021). Petasin potently inhibits mitochondrial complex I–based metabolism that supports tumor growth and metastasis. Journal of Clinical Investigation. 131(17). 22 indexed citations
7.
Heishima, Kazuki, et al.. (2021). Specific inhibition of oncogenic RAS using cell-permeable RAS-binding domains. Cell chemical biology. 28(11). 1581–1589.e6. 7 indexed citations
8.
Yamashita, Satoshi, Yuji O. Kamatari, Ryo Honda, et al.. (2021). Monomeric α-synuclein (αS) inhibits amyloidogenesis of human prion protein (hPrP) by forming a stable αS-hPrP hetero-dimer.. Prion. 15(1). 37–43. 2 indexed citations
10.
Ueda, Hiroshi, et al.. (2019). Structural and functional characterization of fast-cycling RhoF GTPase. Biochemical and Biophysical Research Communications. 513(2). 522–527. 4 indexed citations
11.
Kuwata, Kazuo, et al.. (2019). α-Synuclein chaperone suppresses nucleation and amyloidogenesis of prion protein. Biochemical and Biophysical Research Communications. 521(1). 259–264. 7 indexed citations
12.
Honda, Ryo. (2018). Role of the Disulfide Bond in Prion Protein Amyloid Formation: A Thermodynamic and Kinetic Analysis. Biophysical Journal. 114(4). 885–892. 21 indexed citations
13.
Niwa, Ayumi, Ryo Honda, K. Yamaguchi, et al.. (2018). A DISC1 point mutation promotes oligomerization and impairs information processing in a mouse model of schizophrenia. The Journal of Biochemistry. 165(4). 369–378. 7 indexed citations
14.
Yamaguchi, K., et al.. (2018). A valine-to-lysine substitution at position 210 induces structural conversion of prion protein into a β-sheet rich oligomer. Biochemical and Biophysical Research Communications. 506(1). 81–86. 8 indexed citations
15.
Tahoun, Amin, Trudi Gillespie, Ryo Honda, et al.. (2017). Capsular polysaccharide inhibits adhesion of Bifidobacterium longum 105-A to enterocyte-like Caco-2 cells and phagocytosis by macrophages. Gut Pathogens. 9(1). 27–27. 31 indexed citations
16.
Honda, Ryo & Kazuo Kuwata. (2017). The native state of prion protein (PrP) directly inhibits formation of PrP-amyloid fibrils in vitro. Scientific Reports. 7(1). 562–562. 13 indexed citations
17.
Endo, Satoshi, Ryo Honda, Kathrin Müller, et al.. (2016). Instability of C154Y variant of aldo-keto reductase 1C3. Chemico-Biological Interactions. 276. 194–202. 9 indexed citations
18.
Honda, Ryo, Ming Xu, K. Yamaguchi, Heinrich Röder, & Kazuo Kuwata. (2015). A Native-like Intermediate Serves as a Branching Point between the Folding and Aggregation Pathways of the Mouse Prion Protein. Structure. 23(9). 1735–1742. 32 indexed citations
19.
Honda, Ryo, K. Yamaguchi, & Kazuo Kuwata. (2014). Acid-induced Molten Globule State of a Prion Protein. Journal of Biological Chemistry. 289(44). 30355–30363. 45 indexed citations
20.
Honda, Ryo, et al.. (1964). Studies on the tasty substances of various foods. 2. On the tasty substances of prawn and shrimp.. 17. 268–274. 1 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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