Tomoo Ohashi

2.6k total citations
53 papers, 2.2k citations indexed

About

Tomoo Ohashi is a scholar working on Molecular Biology, Cell Biology and Immunology and Allergy. According to data from OpenAlex, Tomoo Ohashi has authored 53 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 15 papers in Cell Biology and 12 papers in Immunology and Allergy. Recurrent topics in Tomoo Ohashi's work include Cell Adhesion Molecules Research (12 papers), Cellular Mechanics and Interactions (11 papers) and Force Microscopy Techniques and Applications (6 papers). Tomoo Ohashi is often cited by papers focused on Cell Adhesion Molecules Research (12 papers), Cellular Mechanics and Interactions (11 papers) and Force Microscopy Techniques and Applications (6 papers). Tomoo Ohashi collaborates with scholars based in United States, Japan and United Kingdom. Tomoo Ohashi's co-authors include Harold Erickson, Daniel P. Kiehart, Maria A. Schumacher, Seiji KUSUHARA, Riddhi Shah, Naga Babu Chinnam, Stéphane Galiacy, Gina Briscoe, Lisa Schering and Elke Albrecht and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and The Journal of Cell Biology.

In The Last Decade

Tomoo Ohashi

51 papers receiving 2.1k citations

Peers

Tomoo Ohashi

PHYSI

GENET

Robert M. Ezzell United States

Ewald Hannappel Germany

Therese Schulthess Switzerland

Philip G. Allen United States

Shin Lin United States

Dale Moulding United Kingdom

Renaud Poincloux France

Sandrine Bourdoulous France

P A Detmers United States

M Bubb United States

Robert M. Ezzell United States

Tomoo Ohashi

1.7k ×2.1

1.5k ×2.5

485 ×0.9

291 ×0.7

PHYSI

250 ×1.0

GENET

Citations per year, relative to Tomoo Ohashi Tomoo Ohashi (= 1×) peers Robert M. Ezzell

Countries citing papers authored by Tomoo Ohashi

Since Specialization

Citations

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

Fields of papers citing papers by Tomoo Ohashi

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Tomoo Ohashi

This figure shows the co-authorship network connecting the top 25 collaborators of Tomoo Ohashi. A scholar is included among the top collaborators of Tomoo Ohashi 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 Tomoo Ohashi. Tomoo Ohashi 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

Schumacher, Maria A., et al.. (2020). High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP. Acta Crystallographica Section F Structural Biology Communications. 76(2). 94–102. 22 indexed citations

Mangan, Riley J., Lisa Stamper, Tomoo Ohashi, et al.. (2019). Determinants of Tenascin-C and HIV-1 envelope binding and neutralization. Mucosal Immunology. 12(4). 1004–1012. 20 indexed citations

Shah, Riddhi, Tomoo Ohashi, Harold Erickson, & Terrence G. Oas. (2016). Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange. Journal of Biological Chemistry. 292(3). 955–966. 8 indexed citations

Stamper, Lisa, Frederick H. Jaeger, Genevieve G. Fouda, et al.. (2016). The Presence and Anti-HIV-1 Function of Tenascin C in Breast Milk and Genital Fluids. PLoS ONE. 11(5). e0155261–e0155261. 16 indexed citations

Albrecht, Elke, Frode Norheim, Bernd Thiede, et al.. (2015). Irisin – a myth rather than an exercise-inducible myokine. Scientific Reports. 5(1). 8889–8889. 273 indexed citations

Hashimoto, Takao, Tomoo Ohashi, Daisuke Watanabe, et al.. (2013). Usefulness of embolization of the middle meningeal artery for refractory chronic subdural hematomas. Surgical Neurology International. 4(1). 104–104. 101 indexed citations

Schumacher, Maria A., Naga Babu Chinnam, Tomoo Ohashi, Riddhi Shah, & Harold Erickson. (2013). The Structure of Irisin Reveals a Novel Intersubunit β-Sheet Fibronectin Type III (FNIII) Dimer. Journal of Biological Chemistry. 288(47). 33738–33744. 187 indexed citations

Lemmon, Christopher A., Tomoo Ohashi, & Harold Erickson. (2011). Probing the Folded State of Fibronectin Type III Domains in Stretched Fibrils by Measuring Buried Cysteine Accessibility. Journal of Biological Chemistry. 286(30). 26375–26382. 38 indexed citations

Ohashi, Tomoo, et al.. (2010). Development of a semi-quantitative evaluation system for surveillance of bovine spongiform encephalopathy, using the analytic hierarchy process. Revue Scientifique et Technique de l OIE. 29(3). 473–483. 4 indexed citations

10.

Ohashi, Tomoo & Harold Erickson. (2005). Domain Unfolding Plays a Role in Superfibronectin Formation. Journal of Biological Chemistry. 280(47). 39143–39151. 57 indexed citations

11.

Abu‐Lail, Nehal I., Tomoo Ohashi, Robert L. Clark, Harold Erickson, & Stefan Zauscher. (2005). Understanding the elasticity of fibronectin fibrils: Unfolding strengths of FN-III and GFP domains measured by single molecule force spectroscopy. Matrix Biology. 25(3). 175–184. 53 indexed citations

12.

Koyama, Yoh‐ichi, Masashi Kusubata, Atsushi Yoshiki, et al.. (1998). Effect of Tenascin-C Deficiency on Chemically Induced Dermatitis in the Mouse. Journal of Investigative Dermatology. 111(6). 930–935. 45 indexed citations

13.

Ohashi, Tomoo & Harold Erickson. (1998). Oligomeric Structure and Tissue Distribution of Ficolins from Mouse, Pig and Human. Archives of Biochemistry and Biophysics. 360(2). 223–232. 88 indexed citations

14.

Ohashi, Tomoo & Harold Erickson. (1997). Two Oligomeric Forms of Plasma Ficolin Have Differential Lectin Activity. Journal of Biological Chemistry. 272(22). 14220–14226. 59 indexed citations

15.

Ohashi, Tomoo & Seiji KUSUHARA. (1993). Immunoelectron microscopic detection of estrogen target cells in the bone marrow of estrogen-treated male Japanese quail. Bone and Mineral. 20(1). 31–39. 12 indexed citations

16.

Ohashi, Tomoo, Seiji KUSUHARA, & K. Ishida. (1991). Immunoelectron microscopic demonstration of estrogen receptors in osteogenic cells of Japanese quail. Histochemistry and Cell Biology. 96(1). 41–44. 20 indexed citations

17.

Ohashi, Tomoo, Seiji KUSUHARA, & K. Ishida. (1990). Histochemical identification of oestrogen target cells in the medullary bone of laying hens. British Poultry Science. 31(1). 221–224. 5 indexed citations

18.

Ohashi, Tomoo, Seiji KUSUHARA, & K. Ishida. (1987). Effects of oestrogen and anti‐oestrogen on the cells of the endosteal surface of male Japanese quail. British Poultry Science. 28(4). 727–732. 19 indexed citations

19.

Ohashi, Tomoo, et al.. (1977). [The epidermoid and dermoid cysts of the central nervous system--reported of unusual cases (author's transl)].. Munich Personal RePEc Archive (Ludwig Maximilian University of Munich). 5(6). 585–92. 1 indexed citations

20.

Tabak, Joël, et al.. (1975). The effect of butaclamol and of other neuroleptic agents on the apomorphine-elicited inhibition of synaptosomal tyrosine hydroxylase activity.. Munich Personal RePEc Archive (Ludwig Maximilian University of Munich). 1(5). 501–10. 1 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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