Yoichi Osawa

5.6k total citations · 1 hit paper
107 papers, 4.6k citations indexed

About

Yoichi Osawa is a scholar working on Molecular Biology, Physiology and Cell Biology. According to data from OpenAlex, Yoichi Osawa has authored 107 papers receiving a total of 4.6k indexed citations (citations by other indexed papers that have themselves been cited), including 73 papers in Molecular Biology, 31 papers in Physiology and 26 papers in Cell Biology. Recurrent topics in Yoichi Osawa's work include Heat shock proteins research (27 papers), Nitric Oxide and Endothelin Effects (24 papers) and Hemoglobin structure and function (21 papers). Yoichi Osawa is often cited by papers focused on Heat shock proteins research (27 papers), Nitric Oxide and Endothelin Effects (24 papers) and Hemoglobin structure and function (21 papers). Yoichi Osawa collaborates with scholars based in United States, Japan and Brazil. Yoichi Osawa's co-authors include William B. Pratt, Yoshihiro Morishima, Roger K. Sunahara, Andrew T. Bender, Dragomir Draganov, Andrew P. Lieberman, David A. Wink, Bert N. La Du, John F. Teiber and Hwei‐Ming Peng and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Yoichi Osawa

104 papers receiving 4.5k citations

Hit Papers

Human paraoxonases (PON1, PON2, and PON3) are lactonases ... 2005 2026 2012 2019 2005 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Yoichi Osawa United States 36 2.4k 1.2k 782 550 546 107 4.6k
Rick G. Schnellmann United States 44 3.1k 1.3× 881 0.7× 580 0.7× 523 1.0× 534 1.0× 174 6.3k
Dennis R. Petersen United States 53 4.4k 1.8× 1.4k 1.2× 981 1.3× 588 1.1× 1.0k 1.9× 177 9.2k
Thomas D. Hurley United States 48 3.9k 1.6× 795 0.7× 820 1.0× 295 0.5× 767 1.4× 114 7.2k
Kozo Utsumi Japan 43 3.3k 1.4× 1.1k 0.9× 414 0.5× 481 0.9× 444 0.8× 246 6.4k
Grant M. Hatch Canada 50 4.1k 1.7× 1.1k 0.9× 506 0.6× 235 0.4× 829 1.5× 187 6.6k
Anna Colell Spain 50 4.9k 2.0× 1.4k 1.2× 887 1.1× 308 0.6× 1.3k 2.4× 93 8.8k
Montserrat Marı́ Spain 46 3.6k 1.5× 1.1k 0.9× 705 0.9× 185 0.3× 914 1.7× 81 6.9k
Todd D. Williams United States 44 3.7k 1.5× 1.2k 1.0× 636 0.8× 487 0.9× 886 1.6× 138 7.1k
Zezong Gu United States 33 3.3k 1.4× 1.8k 1.5× 684 0.9× 789 1.4× 545 1.0× 75 6.3k
Albert Morales Spain 50 4.6k 1.9× 1.2k 1.0× 854 1.1× 224 0.4× 1.2k 2.1× 90 8.5k

Countries citing papers authored by Yoichi Osawa

Since Specialization
Citations

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

Fields of papers citing papers by Yoichi Osawa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Yoichi Osawa

This figure shows the co-authorship network connecting the top 25 collaborators of Yoichi Osawa. A scholar is included among the top collaborators of Yoichi Osawa 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 Yoichi Osawa. Yoichi Osawa 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.
Huang, Xiaoqiang, et al.. (2025). Computational design of CYP102A1 variants for the biosynthesis of a next-generation antiplatelet drug DT-678. bioRxiv (Cold Spring Harbor Laboratory).
2.
Huang, Xiaoqiang, et al.. (2023). Computational redesign of cytochrome P450 CYP102A1 for highly stereoselective omeprazole hydroxylation by UniDesign. Journal of Biological Chemistry. 299(8). 105050–105050. 13 indexed citations
3.
Huang, Xiaoqiang, et al.. (2023). The Versatile Biocatalyst of Cytochrome P450 CYP102A1: Structure, Function, and Engineering. Molecules. 28(14). 5353–5353. 5 indexed citations
4.
Pospiech, Thomas H., Yoshihiro Morishima, Haoming Zhang, et al.. (2023). Mapping interactions of calmodulin and neuronal NO synthase by crosslinking and mass spectrometry. Journal of Biological Chemistry. 300(1). 105464–105464. 7 indexed citations
5.
Morishima, Yoshihiro, Miranda Lau, William B. Pratt, & Yoichi Osawa. (2022). Dynamic cycling with a unique Hsp90/Hsp70-dependent chaperone machinery and GAPDH is needed for heme insertion and activation of neuronal NO synthase. Journal of Biological Chemistry. 299(2). 102856–102856. 5 indexed citations
6.
Mehta, Ranjit K., Merna Sitto, Theresa P. Devasia, et al.. (2020). Low-Dose Hsp90 Inhibitor Selectively Radiosensitizes HNSCC and Pancreatic Xenografts. Clinical Cancer Research. 26(19). 5246–5257. 17 indexed citations
7.
Su, Min, et al.. (2020). Cryo-EM reveals the architecture of the dimeric cytochrome P450 CYP102A1 enzyme and conformational changes required for redox partner recognition. Journal of Biological Chemistry. 295(6). 1637–1645. 35 indexed citations
8.
Morishima, Yoshihiro, Ranjit K. Mehta, Miranda Lau, et al.. (2018). Chaperone Activity and Dimerization Properties of Hsp90α and Hsp90β in Glucocorticoid Receptor Activation by the Multiprotein Hsp90/Hsp70-Dependent Chaperone Machinery. Molecular Pharmacology. 94(3). 984–991. 16 indexed citations
9.
Lauver, Adam, Hui Wang, Dandan Sun, et al.. (2016). Significant Improvement of Antithrombotic Responses to Clopidogrel by Use of a Novel Conjugate as Revealed in an Arterial Model of Thrombosis. Journal of Pharmacology and Experimental Therapeutics. 359(1). 11–17. 10 indexed citations
10.
Ingelman‐Sundberg, Magnus, Xiao‐bo Zhong, Oliver Hankinson, et al.. (2013). Potential Role of Epigenetic Mechanisms in the Regulation of Drug Metabolism and Transport. Drug Metabolism and Disposition. 41(10). 1725–1731. 54 indexed citations
11.
Peng, Hwei‐Ming, Gary J. Jenkins, Michael Ford, et al.. (2012). Ubiquitination of Neuronal Nitric-oxide Synthase in the Calmodulin-binding Site Triggers Proteasomal Degradation of the Protein. Journal of Biological Chemistry. 287(51). 42601–42610. 10 indexed citations
12.
Pratt, William B., Yoshihiro Morishima, & Yoichi Osawa. (2008). The Hsp90 Chaperone Machinery Regulates Signaling by Modulating Ligand Binding Clefts. Journal of Biological Chemistry. 283(34). 22885–22889. 122 indexed citations
13.
Wakabayashi, Kanako, Ai Tamura, Hiroshi Nakagawa, et al.. (2008). Major SNP (Q141K) Variant of Human ABC Transporter ABCG2 Undergoes Lysosomal and Proteasomal Degradations. Pharmaceutical Research. 26(2). 469–479. 120 indexed citations
14.
Kamada, Yasuhiko, et al.. (2004). Ubiquitination and Degradation of Neuronal Nitric-Oxide Synthase in Vitro: Dimer Stabilization Protects the Enzyme from Proteolysis. Molecular Pharmacology. 66(4). 964–969. 39 indexed citations
15.
Noguchi, Soichi, Suree Jianmongkol, Andrew T. Bender, et al.. (2000). Guanabenz-mediated Inactivation and Enhanced Proteolytic Degradation of Neuronal Nitric-oxide Synthase. Journal of Biological Chemistry. 275(4). 2376–2380. 48 indexed citations
16.
Olken, Norman M., Yoichi Osawa, & Michael A. Marletta. (1994). Characterization of the Inactivation of Nitric Oxide Synthase by NG-Methyl-L-arginine: Evidence for Heme Loss. Biochemistry. 33(49). 14784–14791. 57 indexed citations
17.
Korzekwa, Kenneth R., et al.. (1993). Studies on the mechanism of aromatase and other cytochrome P450 mediated deformylation reactions. The Journal of Steroid Biochemistry and Molecular Biology. 44(4-6). 367–373. 33 indexed citations
19.
Osawa, Yoichi & Lance R. Pohl. (1989). Covalent bonding of the prosthetic heme to protein: a potential mechanism for the suicide inactivation or activation of hemoproteins. Chemical Research in Toxicology. 2(3). 131–141. 66 indexed citations
20.
Osawa, Yoichi & Minor J. Coon. (1987). Radiometric assay for cytochrome P-450-catalyzed progesterone 16α-hydroxylation and determination of an apparent isotope effect. Analytical Biochemistry. 164(2). 355–361. 2 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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