Koto Hayakawa

1.3k total citations
21 papers, 1.0k citations indexed

About

Koto Hayakawa is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Koto Hayakawa has authored 21 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 14 papers in Materials Chemistry and 3 papers in Genetics. Recurrent topics in Koto Hayakawa's work include Enzyme Structure and Function (14 papers), Protein Structure and Dynamics (4 papers) and Biochemical and Molecular Research (3 papers). Koto Hayakawa is often cited by papers focused on Enzyme Structure and Function (14 papers), Protein Structure and Dynamics (4 papers) and Biochemical and Molecular Research (3 papers). Koto Hayakawa collaborates with scholars based in Canada, United States and France. Koto Hayakawa's co-authors include Lora Swenson, M.E. Fraser, Steven F. Bellon, Paul Taslimi, Marc Jacobs, Mark Fleming, John Doran, Judith A. Lippke, Tianjun Sun and Bart Hazes and has published in prestigious journals such as Science, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Koto Hayakawa

21 papers receiving 985 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Koto Hayakawa Canada 12 789 147 120 107 88 21 1.0k
Hiroto Yamaguchi Japan 15 1.1k 1.4× 183 1.2× 146 1.2× 158 1.5× 74 0.8× 28 1.9k
Kun Xu China 21 918 1.2× 86 0.6× 97 0.8× 159 1.5× 151 1.7× 65 1.3k
Michael D. Scholle United States 18 1.2k 1.5× 148 1.0× 194 1.6× 133 1.2× 63 0.7× 27 1.6k
Bernardo Ochoa‐Montaño United Kingdom 9 822 1.0× 113 0.8× 57 0.5× 161 1.5× 124 1.4× 13 1.1k
Yehuda Goldgur United States 19 1.4k 1.7× 114 0.8× 180 1.5× 142 1.3× 53 0.6× 50 2.0k
Mei-Chu Lo United States 11 750 1.0× 97 0.7× 132 1.1× 74 0.7× 77 0.9× 19 957
David T. Chin United States 14 780 1.0× 71 0.5× 114 0.9× 156 1.5× 50 0.6× 16 1.3k
Carlos H. M. Rodrigues Australia 18 1.5k 1.9× 137 0.9× 85 0.7× 294 2.7× 289 3.3× 39 2.1k
Wenyan Wang China 16 847 1.1× 93 0.6× 94 0.8× 189 1.8× 20 0.2× 58 1.3k
S.M. Soisson United States 19 1.1k 1.4× 133 0.9× 192 1.6× 223 2.1× 74 0.8× 32 1.6k

Countries citing papers authored by Koto Hayakawa

Since Specialization
Citations

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

Fields of papers citing papers by Koto Hayakawa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Koto Hayakawa

This figure shows the co-authorship network connecting the top 25 collaborators of Koto Hayakawa. A scholar is included among the top collaborators of Koto Hayakawa 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 Koto Hayakawa. Koto Hayakawa 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.
Joyce, Michael, Koto Hayakawa, William T. Wolodko, & M.E. Fraser. (2012). Biochemical and structural characterization of the GTP-preferring succinyl-CoA synthetase fromThermus aquaticus. Acta Crystallographica Section D Biological Crystallography. 68(7). 751–762. 7 indexed citations
2.
Sun, Tianjun, Koto Hayakawa, & M.E. Fraser. (2011). ADP–Mg2+bound to the ATP-grasp domain of ATP-citrate lyase. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(10). 1168–1172. 21 indexed citations
3.
Sun, Tianjun, Koto Hayakawa, Katherine Bateman, & M.E. Fraser. (2010). Identification of the Citrate-binding Site of Human ATP-Citrate Lyase Using X-ray Crystallography. Journal of Biological Chemistry. 285(35). 27418–27428. 72 indexed citations
4.
Fraser, M.E., Koto Hayakawa, & William D. Brown. (2010). Catalytic Role of the Conformational Change in Succinyl-CoA:3-Oxoacid CoA Transferase on Binding CoA,. Biochemistry. 49(48). 10319–10328. 14 indexed citations
5.
Joyce, Michael, et al.. (2007). Cloning, expression, purification, crystallization and preliminary X-ray analysis ofThermus aquaticussuccinyl-CoA synthetase. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63(5). 399–402. 2 indexed citations
6.
Hayakawa, Koto, et al.. (2007). Participation of Cys123α ofEscherichia colisuccinyl-CoA synthetase in catalysis. Acta Crystallographica Section D Biological Crystallography. 63(8). 876–884. 9 indexed citations
7.
Fraser, M.E., et al.. (2006). Interactions of GTP with the ATP-grasp Domain of GTP-specific Succinyl-CoA Synthetase. Journal of Biological Chemistry. 281(16). 11058–11065. 32 indexed citations
8.
Jacobs, Marc, Koto Hayakawa, Lora Swenson, et al.. (2005). The Structure of Dimeric ROCK I Reveals the Mechanism for Ligand Selectivity. Journal of Biological Chemistry. 281(1). 260–268. 212 indexed citations
9.
Prasad, L. Guru, et al.. (2004). The structure of a universally employed enzyme: V8 protease fromStaphylococcus aureus. Acta Crystallographica Section D Biological Crystallography. 60(2). 256–259. 47 indexed citations
10.
Audette, Gerald F., et al.. (2004). Crystallization and preliminary diffraction studies of TraF, a component of theEscherichia colitype IV secretory system. Acta Crystallographica Section D Biological Crystallography. 60(11). 2025–2027. 5 indexed citations
11.
Bellon, Steven F., Jonathan D. Parsons, Yunyi Wei, et al.. (2004). Crystal Structures of Escherichia coli Topoisomerase IV ParE Subunit (24 and 43 Kilodaltons): a Single Residue Dictates Differences in Novobiocin Potency against Topoisomerase IV and DNA Gyrase. Antimicrobial Agents and Chemotherapy. 48(5). 1856–1864. 124 indexed citations
12.
Swenson, Lora, Matthew J. Fitzgibbon, Koto Hayakawa, et al.. (2002). Structure of Mitogen-activated Protein Kinase-activated Protein (MAPKAP) Kinase 2 Suggests a Bifunctional Switch That Couples Kinase Activation with Nuclear Export. Journal of Biological Chemistry. 277(40). 37401–37405. 99 indexed citations
13.
Hazes, Bart, et al.. (2000). Crystal structure of Pseudomonas aeruginosa PAK pilin suggests a main-chain-dominated mode of receptor binding 1 1Edited by R. Huber. Journal of Molecular Biology. 299(4). 1005–1017. 114 indexed citations
14.
Audette, Gerald F., Roswitha Engelmann, Wolfgang Hengstenberg, et al.. (2000). The 1.9 Å resolution structure of phospho-serine 46 HPr from Enterococcus faecalis 1 1Edited by P. Wright. Journal of Molecular Biology. 303(4). 545–553. 35 indexed citations
15.
Audette, Gerald F., J. Wilson Quail, Koto Hayakawa, et al.. (1999). Crystallization and preliminary X-ray diffraction studies of monomeric isocitrate dehydrogenase from Corynebacterium glutamicum. Acta Crystallographica Section D Biological Crystallography. 55(9). 1584–1585. 3 indexed citations
16.
Pieper, Ursula, Koto Hayakawa, Zhong Li, & Osnat Herzberg. (1997). Circularly Permuted β-Lactamase from Staphylococcus aureus PC1,. Biochemistry. 36(29). 8767–8774. 29 indexed citations
17.
Hayakawa, Koto, et al.. (1994). Crystallization of canine cardiac calsequestrin. Journal of Molecular Biology. 235(1). 357–360. 7 indexed citations
18.
Hayakawa, Koto, M. Fujinaga, M.E.P. Murphy, et al.. (1989). Structure of Recombinant Human Renin, a Target for Cardiovascular-Active Drugs, at 2.5 Å Resolution. Science. 243(4896). 1346–1351. 166 indexed citations
19.
Hayakawa, Koto, et al.. (1984). Crystallization of glycogen debranching enzyme. Journal of Molecular Biology. 174(3). 557–559. 5 indexed citations
20.
Boege, Ulrike, Douglas G. Scraba, Koto Hayakawa, Michael N.G. James, & John W. Erickson. (1984). Structure of the mengo virion. V11. Crystallization and preliminary X-ray diffraction analysis. Virology. 138(1). 162–167. 3 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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