Kosuke Maki

1.7k total citations
44 papers, 1.4k citations indexed

About

Kosuke Maki is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Kosuke Maki has authored 44 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 38 papers in Molecular Biology, 20 papers in Materials Chemistry and 6 papers in Cell Biology. Recurrent topics in Kosuke Maki's work include Protein Structure and Dynamics (27 papers), Enzyme Structure and Function (20 papers) and RNA and protein synthesis mechanisms (10 papers). Kosuke Maki is often cited by papers focused on Protein Structure and Dynamics (27 papers), Enzyme Structure and Function (20 papers) and RNA and protein synthesis mechanisms (10 papers). Kosuke Maki collaborates with scholars based in Japan, United States and Russia. Kosuke Maki's co-authors include Heinrich Röder, Kunihiro Kuwajima, Hong Cheng, Masahiro Iwakura, Munehito Arai, T. Nakamura, Tomonao Inobe, S. Orito, Flemming M. Poulsen and Birthe B. Kragelund and has published in prestigious journals such as Chemical Reviews, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Kosuke Maki

43 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kosuke Maki Japan 21 1.2k 593 129 118 117 44 1.4k
Mohona Sarkar United States 9 1.2k 1.0× 510 0.9× 110 0.9× 133 1.1× 260 2.2× 10 1.5k
Christopher M. Dobson United Kingdom 12 1.2k 1.0× 580 1.0× 79 0.6× 268 2.3× 197 1.7× 12 1.4k
S. Jordan Kerns United States 8 1.4k 1.2× 390 0.7× 136 1.1× 189 1.6× 131 1.1× 8 1.8k
Madeleine B. Borgia Switzerland 13 1.4k 1.2× 559 0.9× 191 1.5× 137 1.2× 174 1.5× 20 1.7k
Jaby Jacob United States 15 1.3k 1.1× 562 0.9× 132 1.0× 200 1.7× 129 1.1× 17 1.7k
Atsuo Tamura Japan 22 1.3k 1.1× 437 0.7× 184 1.4× 210 1.8× 137 1.2× 65 1.8k
M. Delaye France 16 1.0k 0.9× 284 0.5× 139 1.1× 131 1.1× 124 1.1× 28 1.5k
John W. Shriver United States 26 1.4k 1.2× 468 0.8× 109 0.8× 194 1.6× 109 0.9× 54 1.8k
Philipp Neudecker Germany 26 1.6k 1.4× 555 0.9× 80 0.6× 459 3.9× 137 1.2× 48 2.3k
F. Cipriani France 21 1.3k 1.1× 1.1k 1.8× 58 0.4× 160 1.4× 95 0.8× 39 1.9k

Countries citing papers authored by Kosuke Maki

Since Specialization
Citations

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

Fields of papers citing papers by Kosuke Maki

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kosuke Maki

This figure shows the co-authorship network connecting the top 25 collaborators of Kosuke Maki. A scholar is included among the top collaborators of Kosuke Maki 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 Kosuke Maki. Kosuke Maki 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.
2.
Itoh, Satoru, Teikichi Ikura, Kunio Ihara, et al.. (2020). Energetics and kinetics of substrate analog-coupled staphylococcal nuclease folding revealed by a statistical mechanical approach. Proceedings of the National Academy of Sciences. 117(33). 19953–19962. 7 indexed citations
3.
4.
Mukaiyama, Atsushi, Takashi Nakamura, Koki Makabe, et al.. (2012). The Molten Globule of β2-Microglobulin Accumulated at pH 4 and Its Role in Protein Folding. Journal of Molecular Biology. 425(2). 273–291. 20 indexed citations
5.
Tomoyori, Katsuaki, et al.. (2012). Sequential four‐state folding/unfolding of goat α‐lactalbumin and its N‐terminal variants. Proteins Structure Function and Bioinformatics. 80(9). 2191–2206. 4 indexed citations
6.
Mukaiyama, Atsushi, Takashi Nakamura, Koki Makabe, et al.. (2012). Native-State Heterogeneity of β2-Microglobulin as Revealed by Kinetic Folding and Real-Time NMR Experiments. Journal of Molecular Biology. 425(2). 257–272. 19 indexed citations
7.
Maki, Kosuke, et al.. (2011). Salt bridges in prion proteins are necessary for high-affinity binding to the monoclonal antibody T2. Biophysical Chemistry. 156(2-3). 140–145. 3 indexed citations
8.
Nakamura, Takashi, Koki Makabe, Katsuaki Tomoyori, et al.. (2010). Different Folding Pathways Taken by Highly Homologous Proteins, Goat α-Lactalbumin and Canine Milk Lysozyme. Journal of Molecular Biology. 396(5). 1361–1378. 22 indexed citations
9.
Latypov, Ramil F., Kosuke Maki, Hong Cheng, Stanley Luck, & Heinrich Röder. (2008). Folding Mechanism of Reduced Cytochrome c: Equilibrium and Kinetic Properties in the Presence of Carbon Monoxide. Journal of Molecular Biology. 383(2). 437–453. 32 indexed citations
10.
Ishii, Takaaki, Yoshihiro Murayama, Atsuto Katano, et al.. (2008). Probing force-induced unfolding intermediates of a single staphylococcal nuclease molecule and the effect of ligand binding. Biochemical and Biophysical Research Communications. 375(4). 586–591. 8 indexed citations
11.
Tsukamoto, Seiichi, Yoshiteru Yamada, Kazuo Fujiwara, et al.. (2008). Non‐native α‐helix formation is not necessary for folding of lipocalin: Comparison of burst‐phase folding between tear lipocalin and β‐lactoglobulin. Proteins Structure Function and Bioinformatics. 76(1). 226–236. 11 indexed citations
12.
Iizuka, Ryo, Kazunobu Takahashi, Kosuke Maki, et al.. (2008). Sequential Action of ATP-dependent Subunit Conformational Change and Interaction between Helical Protrusions in the Closure of the Built-in Lid of Group II Chaperonins. Journal of Biological Chemistry. 283(50). 34773–34784. 23 indexed citations
13.
Maki, Kosuke, Hong Cheng, Д. А. Долгих, & Heinrich Röder. (2007). Folding Kinetics of Staphylococcal Nuclease Studied by Tryptophan Engineering and Rapid Mixing Methods. Journal of Molecular Biology. 368(1). 244–255. 25 indexed citations
14.
Maki, Kosuke, Tomonao Inobe, Kazunobu Takahashi, et al.. (2006). The Equilibrium Unfolding Intermediate Observed at pH 4 and its Relationship with the Kinetic Folding Intermediates in Green Fluorescent Protein. Journal of Molecular Biology. 361(5). 969–982. 38 indexed citations
15.
Kato, Atsushi, Kosuke Maki, Teppei Ebina, et al.. (2006). Mutational analysis of protein solubility enhancement using short peptide tags. Biopolymers. 85(1). 12–18. 81 indexed citations
16.
Maki, Kosuke, Hong Cheng, Д. А. Долгих, M.C.R. Shastry, & Heinrich Röder. (2004). Early Events During Folding of Wild-type Staphylococcal Nuclease and a Single-tryptophan Variant Studied by Ultrarapid Mixing. Journal of Molecular Biology. 338(2). 383–400. 48 indexed citations
17.
Zhu, Yongjin, Darwin O. V. Alonso, Kosuke Maki, et al.. (2003). Ultrafast folding of α 3 D: A de novo designed three-helix bundle protein. Proceedings of the National Academy of Sciences. 100(26). 15486–15491. 135 indexed citations
18.
Arai, Munehito, Tomonao Inobe, Kosuke Maki, et al.. (2003). Denaturation and reassembly of chaperonin GroEL studied by solution X‐ray scattering. Protein Science. 12(4). 672–680. 19 indexed citations
19.
Teilum, Kaare, Kosuke Maki, Birthe B. Kragelund, Flemming M. Poulsen, & Heinrich Röder. (2002). Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing. Proceedings of the National Academy of Sciences. 99(15). 9807–9812. 83 indexed citations
20.
Maki, Kosuke & S. Orito. (1998). Hadron colliders as the “neutralino factory”: Search for a slow decay of the lightest neutralino at the CERN LHC. Physical review. D. Particles, fields, gravitation, and cosmology/Physical review. D. Particles and fields. 57(1). 554–566. 11 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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