Koichiro Ishimori

5.5k total citations
162 papers, 4.4k citations indexed

About

Koichiro Ishimori is a scholar working on Molecular Biology, Cell Biology and Pediatrics, Perinatology and Child Health. According to data from OpenAlex, Koichiro Ishimori has authored 162 papers receiving a total of 4.4k indexed citations (citations by other indexed papers that have themselves been cited), including 110 papers in Molecular Biology, 82 papers in Cell Biology and 24 papers in Pediatrics, Perinatology and Child Health. Recurrent topics in Koichiro Ishimori's work include Hemoglobin structure and function (77 papers), Heme Oxygenase-1 and Carbon Monoxide (38 papers) and Protein Structure and Dynamics (26 papers). Koichiro Ishimori is often cited by papers focused on Hemoglobin structure and function (77 papers), Heme Oxygenase-1 and Carbon Monoxide (38 papers) and Protein Structure and Dynamics (26 papers). Koichiro Ishimori collaborates with scholars based in Japan, United States and Singapore. Koichiro Ishimori's co-authors include Isao Morishima, Satoshi Takahashi, Takeshi Uchida, Shuji Akiyama, Shiro Yoshioka, Shingo Nagano, Motomasa Tanaka, Tetsunari Kimura, Haruto Ishikawa and Tetsuro Fujisawa 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

Koichiro Ishimori

160 papers receiving 4.3k citations

Peers

Koichiro Ishimori

SPECT

Marcelo A. Martí Argentina

Tetsutarō Iizuka Japan

A. Mitschler France

Pierre Moënne‐Loccoz United States

David B. Goodin United States

Carme Rovira Spain

Jean‐Paul Renaud France

A. Grant Mauk Canada

W.R. Montfort United States

Larry E. Vickery United States

Marcelo A. Martí Argentina

Koichiro Ishimori

3.4k ×1.3

1.6k ×1.1

732 ×0.9

479 ×0.7

391 ×0.9

SPECT

Citations per year, relative to Koichiro Ishimori Koichiro Ishimori (= 1×) peers Marcelo A. Martí

Countries citing papers authored by Koichiro Ishimori

Since Specialization

Citations

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

Fields of papers citing papers by Koichiro Ishimori

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Koichiro Ishimori

This figure shows the co-authorship network connecting the top 25 collaborators of Koichiro Ishimori. A scholar is included among the top collaborators of Koichiro Ishimori 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 Koichiro Ishimori. Koichiro Ishimori is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Mabuchi, Takuya, et al.. (2025). Mechanistic Insights Into Oxidative Response of Heat Shock Factor 1 Condensates. JACS Au. 5(2). 606–617. 1 indexed citations

Zhi, Du, Eunju Nam, Mannkyu Hong, et al.. (2023). Unveiling the impact of oxidation-driven endogenous protein interactions on the dynamics of amyloid-β aggregation and toxicity. Chemical Science. 14(20). 5340–5349. 10 indexed citations

Ishimori, Koichiro, et al.. (2022). Converting cytochrome c into a DyP-like metalloenzyme. Dalton Transactions. 51(33). 12641–12649. 3 indexed citations

Ishimori, Koichiro, et al.. (2021). Zinc-Dependent Oligomerization of Thermus thermophilus Trigger Factor Chaperone. Biology. 10(11). 1106–1106. 2 indexed citations

Rizzolo, Kamran, Sa Rang Kim, Koichiro Ishimori, et al.. (2021). Author Correction: Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex. Nature Communications. 12(1). 2753–2753. 1 indexed citations

Matsumoto, Yuki, et al.. (2020). Mechanistic insights into heme-mediated transcriptional regulation via a bacterial manganese-binding iron regulator, iron response regulator (Irr). Journal of Biological Chemistry. 295(32). 11316–11325. 7 indexed citations

Taniguchi, Makoto, Kazuma Uesaka, Kusol Pootanakit, et al.. (2019). Complete Genome Sequence of Staphylococcus arlettae Strain P2, Isolated from a Laboratory Environment. Microbiology Resource Announcements. 8(45). 6 indexed citations

Ishimori, Koichiro, et al.. (2019). A single mutation converts Alr5027 from cyanobacteria Nostoc sp. PCC 7120 to a heme-binding protein with heme-degrading ability. Journal of Inorganic Biochemistry. 203. 110916–110916. 1 indexed citations

Furukawa, Yoshiaki, Itsuki Anzai, Shuji Akiyama, et al.. (2015). Conformational Disorder of the Most Immature Cu, Zn-Superoxide Dismutase Leading to Amyotrophic Lateral Sclerosis. Journal of Biological Chemistry. 291(8). 4144–4155. 39 indexed citations

10.

Uzawa, Takanori, Takashi Isoshima, Yoshihiro Ito, et al.. (2013). Sequence and Temperature Dependence of the End-to-End Collision Dynamics of Single-Stranded DNA. Biophysical Journal. 104(11). 2485–2492. 20 indexed citations

11.

Uchida, Takeshi, et al.. (2007). Unique Peroxidase Reaction Mechanism in Prostaglandin Endoperoxide H Synthase-2. Journal of Biological Chemistry. 282(22). 16681–16690. 9 indexed citations

12.

Ishikawa, Haruto, Michiko Kato, Hiroshi Hori, et al.. (2005). Involvement of Heme Regulatory Motif in Heme-Mediated Ubiquitination and Degradation of IRP2. Molecular Cell. 19(2). 171–181. 131 indexed citations

13.

Uzawa, Takanori, Shuji Akiyama, Tetsunari Kimura, et al.. (2004). Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of α-helical content and compactness. Proceedings of the National Academy of Sciences. 101(5). 1171–1176. 132 indexed citations

14.

Egawa, Tsuyoshi, Shiro Yoshioka, Satoshi Takahashi, et al.. (2003). Kinetic and Spectroscopic Characterization of a Hydroperoxy Compound in the Reaction of Native Myoglobin with Hydrogen Peroxide. Journal of Biological Chemistry. 278(43). 41597–41606. 35 indexed citations

15.

Akiyama, Shuji, Satoshi Takahashi, Tetsunari Kimura, et al.. (2002). Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle x-ray scattering. Proceedings of the National Academy of Sciences. 99(3). 1329–1334. 203 indexed citations

16.

Akiyama, Shuji, Satoshi Takahashi, Koichiro Ishimori, & Isao Morishima. (2000). Stepwise formation of α-helices during cytochrome c folding. Nature Structural Biology. 7(6). 514–520. 123 indexed citations

17.

Akiyama, Shuji, Satoshi Takahashi, Koichiro Ishimori, & Isao Morishima. (1999). CD Measurements on the Early Folding Intermediates of Cytochrome c Using Fast Flow Mixer. Seibutsu Butsuri. 39(supplement). S149–S149. 1 indexed citations

18.

Shirai, Tsuyoshi, et al.. (1998). Design, construction, crystallization, and preliminary X-ray studies of a fine-tuning mutant (F133V) of module-substituted chimera hemoglobin. Proteins Structure Function and Bioinformatics. 32(3). 263–267. 2 indexed citations

19.

Uchida, Takeshi, Koichiro Ishimori, & Isao Morishima. (1997). The Effects of Heme Pocket Hydrophobicity on the Ligand Binding Dynamics in Myoglobin as Studied with Leucine 29 Mutants. Journal of Biological Chemistry. 272(48). 30108–30114. 35 indexed citations

20.

Unno, Masashi, Koichiro Ishimori, & Isao Morishima. (1990). High-pressure laser photolysis study of hemoproteins. Effects of pressure on carbon monoxide binding dynamics for R- and T-state hemoglobins. Biochemistry. 29(44). 10199–10205. 19 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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