Ryo Kitahara

1.5k total citations
58 papers, 1.1k citations indexed

About

Ryo Kitahara is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Ryo Kitahara has authored 58 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 46 papers in Molecular Biology, 16 papers in Materials Chemistry and 15 papers in Spectroscopy. Recurrent topics in Ryo Kitahara's work include Protein Structure and Dynamics (31 papers), Enzyme Structure and Function (16 papers) and Hemoglobin structure and function (9 papers). Ryo Kitahara is often cited by papers focused on Protein Structure and Dynamics (31 papers), Enzyme Structure and Function (16 papers) and Hemoglobin structure and function (9 papers). Ryo Kitahara collaborates with scholars based in Japan, United Kingdom and Denmark. Ryo Kitahara's co-authors include Kazuyuki Akasaka, Shigeyuki Yokoyama, Hiroaki Yamada, Michael P. Williamson, Yuji O. Kamatari, Tomoshi Kameda, Kazuyuki Akasaka, Peter E. Wright, Kunihiko Gekko and Eiji Ohmae and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Ryo Kitahara

54 papers receiving 1.1k 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 Kitahara Japan 21 948 421 240 185 136 58 1.1k
Ryan Day United States 19 1.2k 1.3× 617 1.5× 177 0.7× 99 0.5× 145 1.1× 29 1.4k
Mohona Sarkar United States 9 1.2k 1.3× 510 1.2× 133 0.6× 260 1.4× 110 0.8× 10 1.5k
James O. Wrabl United States 18 1.9k 2.0× 600 1.4× 256 1.1× 205 1.1× 129 0.9× 41 2.2k
Christopher M. Dobson United Kingdom 12 1.2k 1.3× 580 1.4× 268 1.1× 197 1.1× 79 0.6× 12 1.4k
Nicholas P. Schafer United States 23 1.4k 1.5× 470 1.1× 101 0.4× 137 0.7× 109 0.8× 54 1.7k
Ulrich Weininger Germany 25 1.2k 1.3× 377 0.9× 270 1.1× 158 0.9× 39 0.3× 74 1.6k
Arthur M. Mandel United States 10 982 1.0× 307 0.7× 316 1.3× 121 0.7× 70 0.5× 15 1.3k
Diego U. Ferreiro Argentina 26 2.1k 2.2× 659 1.6× 155 0.6× 222 1.2× 67 0.5× 58 2.5k
Robin S. Dothager United States 14 1.2k 1.2× 627 1.5× 162 0.7× 156 0.8× 159 1.2× 17 1.5k
Timothy Sharpe Switzerland 22 1.1k 1.2× 368 0.9× 120 0.5× 117 0.6× 96 0.7× 43 1.4k

Countries citing papers authored by Ryo Kitahara

Since Specialization
Citations

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

Fields of papers citing papers by Ryo Kitahara

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ryo Kitahara

This figure shows the co-authorship network connecting the top 25 collaborators of Ryo Kitahara. A scholar is included among the top collaborators of Ryo Kitahara 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 Kitahara. Ryo Kitahara 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.
Kameda, Tomoshi, et al.. (2025). ATP as a Key Modulator of Fused-in-sarcoma Phase Separation and Aggregation: Insights into Amyotrophic Lateral Sclerosis Pathogenesis. Journal of Molecular Biology. 437(17). 169295–169295. 1 indexed citations
2.
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
3.
4.
Kobayashi, Kensuke, Ryo Kitahara, Katsunori Kitano, et al.. (2019). Gene delivery to cone photoreceptors by subretinal injection of rAAV2/6 in the mouse retina. Biochemical and Biophysical Research Communications. 515(1). 222–227. 5 indexed citations
5.
Xue, Mengjun, et al.. (2019). How internal cavities destabilize a protein. Proceedings of the National Academy of Sciences. 116(42). 21031–21036. 35 indexed citations
6.
Kitahara, Ryo, et al.. (2019). Pressure accelerates the circadian clock of cyanobacteria. Scientific Reports. 9(1). 12395–12395. 8 indexed citations
7.
Williamson, Michael P. & Ryo Kitahara. (2018). Characterization of low-lying excited states of proteins by high-pressure NMR. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1867(3). 350–358. 25 indexed citations
8.
Kawamura, Takahiro, et al.. (2017). Analysis of O 2 -binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A. Biophysical Journal. 112(9). 1820–1828. 5 indexed citations
9.
Kitahara, Ryo, Yuichi Yoshimura, Mengjun Xue, Tomoshi Kameda, & Frans A. A. Mulder. (2016). Detecting O2 binding sites in protein cavities. Scientific Reports. 6(1). 20534–20534. 20 indexed citations
10.
Kitahara, Ryo. (2015). High-Pressure NMR Spectroscopy Reveals Functional Sub-states of Ubiquitin and Ubiquitin-Like Proteins. Sub-cellular biochemistry. 72. 199–214. 2 indexed citations
11.
Ohmae, Eiji, et al.. (2013). Solvent environments significantly affect the enzymatic function of Escherichia coli dihydrofolate reductase: Comparison of wild-type protein and active-site mutant D27E. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1834(12). 2782–2794. 20 indexed citations
12.
Kitahara, Ryo, et al.. (2013). Pressure-induced chemical shifts as probes for conformational fluctuations in proteins. Progress in Nuclear Magnetic Resonance Spectroscopy. 71. 35–58. 50 indexed citations
13.
Akasaka, Kazuyuki, Ryo Kitahara, & Yuji O. Kamatari. (2012). Exploring the folding energy landscape with pressure. Archives of Biochemistry and Biophysics. 531(1-2). 110–115. 57 indexed citations
14.
Kitahara, Ryo, Akihiro Maeno, Kazuyuki Akasaka, et al.. (2010). Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH. Proteins Structure Function and Bioinformatics. 79(4). 1293–1305. 25 indexed citations
15.
Kitahara, Ryo, et al.. (2006). Real Time Rectangle Tracking Method for Geometric Correction on Mobile Terminals. IEICE Technical Report; IEICE Tech. Rep.. 106. 1 indexed citations
16.
Kitahara, Ryo, Shigeyuki Yokoyama, & Kazuyuki Akasaka. (2006). A New Paradigm of Protein Structures by Variable Pressure NMR. Journal of the Spectroscopical Society of Japan. 55(1). 10–20.
17.
Kitahara, Ryo, et al.. (2006). Cold denaturation of ubiquitin at high pressure. Magnetic Resonance in Chemistry. 44(S1). S108–S113. 37 indexed citations
18.
Kitahara, Ryo, Shigeyuki Yokoyama, & Kazuyuki Akasaka. (2005). NMR Snapshots of a Fluctuating Protein Structure: Ubiquitin at 30 bar–3 kbar. Journal of Molecular Biology. 347(2). 277–285. 127 indexed citations
19.
Kitahara, Ryo, Catherine A. Royer, Hiroaki Yamada, et al.. (2002). Equilibrium and Pressure-jump Relaxation Studies of the Conformational Transitions of P13MTCP1. Journal of Molecular Biology. 320(3). 609–628. 41 indexed citations
20.
Kitahara, Ryo, Hiroaki Yamada, Kazuyuki Akasaka, & Peter E. Wright. (2002). High Pressure NMR Reveals that Apomyoglobin is an Equilibrium Mixture from the Native to the Unfolded. Journal of Molecular Biology. 320(2). 311–319. 59 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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