Emi Hifumi

928 total citations
65 papers, 755 citations indexed

About

Emi Hifumi is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Immunology. According to data from OpenAlex, Emi Hifumi has authored 65 papers receiving a total of 755 indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Molecular Biology, 38 papers in Radiology, Nuclear Medicine and Imaging and 13 papers in Immunology. Recurrent topics in Emi Hifumi's work include Monoclonal and Polyclonal Antibodies Research (38 papers), Glycosylation and Glycoproteins Research (27 papers) and Protein purification and stability (10 papers). Emi Hifumi is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (38 papers), Glycosylation and Glycoproteins Research (27 papers) and Protein purification and stability (10 papers). Emi Hifumi collaborates with scholars based in Japan, United States and Czechia. Emi Hifumi's co-authors include Taizo Uda, Yukie Mitsuda, Naoyoshi Egashira, Akira Nishizono, Yoshiharu Mitoma, Yoshiko Okamoto, Ryoji Fujii, Shinichi Morita, Hiroaki Taguchi and Naoki Yamamoto and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Emi Hifumi

65 papers receiving 747 citations

Peers

Emi Hifumi

RNMI

IMMUN

ONCOL

Daniel F. Gaddy United States

Mark B. Jones United States

Masumi Iijima Japan

Martina L. Jones Australia

Susanne Kubetzko Switzerland

Richard Bazin Canada

A. M. J. Buiting Netherlands

Christine Klinguer‐Hamour France

Kim Wals United Kingdom

Igor Fisch Switzerland

Daniel F. Gaddy United States

Emi Hifumi

282 ×0.6

148 ×0.3

RNMI

129 ×0.8

IMMUN

261 ×2.8

158 ×1.9

ONCOL

Citations per year, relative to Emi Hifumi Emi Hifumi (= 1×) peers Daniel F. Gaddy

Countries citing papers authored by Emi Hifumi

Since Specialization

Citations

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

Fields of papers citing papers by Emi Hifumi

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Emi Hifumi

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

Hifumi, Emi, et al.. (2024). Enzymatization of mouse monoclonal antibodies to the corresponding catalytic antibodies. Scientific Reports. 14(1). 12184–12184. 1 indexed citations

Higaki, Yuji, et al.. (2023). Cononsolvency of poly(carboxybetaine methacrylate) in water–ethanol mixed solvents. Polymer Journal. 55(8). 869–876. 5 indexed citations

Hifumi, Emi, et al.. (2023). Direct conversion of a general antibody to its catalytic antibody and corresponding applications —Importance and role of Pro95 in CDR-3—. Proceedings of the Japan Academy Series B. 99(6). 155–172. 2 indexed citations

Hifumi, Emi, et al.. (2022). A new catalytic site functioning in antigen cleavage by H34 catalytic antibody light chain. Scientific Reports. 12(1). 19185–19185. 2 indexed citations

Harada, Takunori, Takanori Inoue, Hiroyasu Nishiguchi, et al.. (2020). Decomposition of amyloid fibrils by NIR-active upconversion nanoparticles. Photochemical & Photobiological Sciences. 19(1). 29–33. 2 indexed citations

Hifumi, Emi, Kyohei Higashi, & Taizo Uda. (2010). Catalytic digestion of human tumor necrosis factor‐α by antibody heavy chain. FEBS Journal. 277(18). 3823–3832. 16 indexed citations

Hifumi, Emi, et al.. (2007). Catalytic Features and Eradication Ability of Antibody Light-chain UA15-L against Helicobacter pylori. Journal of Biological Chemistry. 283(2). 899–907. 50 indexed citations

Hifumi, Emi, Yukiko Yamada, & Taizo Uda. (2005). A catalytic antibody heavy chain HpU-2 degrading its epitope peptide and H. pylori urease. Immunology Letters. 103(1). 68–74. 8 indexed citations

Uda, Taizo & Emi Hifumi. (2004). Super catalytic antibody and antigenase. Journal of Bioscience and Bioengineering. 97(3). 143–152. 19 indexed citations

10.

Fujii, Ryoji, et al.. (2004). Epitope mapping and features of the epitope for monoclonal antibodies inhibiting enzymatic activity of Helicobacter pylori urease. Biotechnology and Bioengineering. 86(4). 434–444. 20 indexed citations

11.

Mitsuda, Yukie, et al.. (2004). Catalytic antibody light chain capable of cleaving a chemokine receptor CCR‐5 peptide with a high reaction rate constant. Biotechnology and Bioengineering. 86(2). 217–225. 40 indexed citations

12.

Hifumi, Emi, et al.. (2003). Endopeptidase character of monoclonal antibody i41-7 subunits. Immunology Letters. 86(3). 249–257. 16 indexed citations

13.

Hifumi, Emi, et al.. (2002). Targeted destruction of the HIV-1 coat protein gp41 by a catalytic antibody light chain. Journal of Immunological Methods. 269(1-2). 283–298. 47 indexed citations

14.

Uda, Taizo, et al.. (2000). Catalytic Activity of Antibody Light Chain to gp41: A Consideration of Refolding in Relation to Activation Mechanism. PubMed. 77. 18–32. 15 indexed citations

15.

Morikawa, Keiko, et al.. (2000). Analysis of the antigen recognition sites of anti-methamphetamine monoclonal antibodies (II): Unique feature of MA-3 antibody. Journal of Bioscience and Bioengineering. 89(5). 492–494. 1 indexed citations

16.

Hifumi, Emi, Yoshiko Okamoto, & Taizo Uda. (2000). How and Why 41S-2 Antibody Subunits Acquire the Ability to Catalyze Decomposition of the Conserved Sequence of gp41 of HIV-1. Applied Biochemistry and Biotechnology. 83(1-3). 209–220. 22 indexed citations

17.

Hifumi, Emi, Yoshiko Okamoto, & Taizo Uda. (1999). Super catalytic antibody [I]: Decomposition of targeted protein by its antibody light chain. Journal of Bioscience and Bioengineering. 88(3). 323–327. 25 indexed citations

18.

Hifumi, Emi, et al.. (1999). Immunochemical Features of Complementarity Determining Region (CDR) Peptide in Anti Hemin Monoclonal Antibody. Journal of Peptide Science. 5(1). 24–31. 2 indexed citations

19.

Uda, Taizo, et al.. (1995). An approach for an immunoaffinity AIDS sensor using the conservative region of the HIV envelope protein (gp41) and its monoclonal antibody. Biosensors and Bioelectronics. 10(5). 477–483. 14 indexed citations

20.

Uda, Taizo, et al.. (1994). Application of Polymer-Protected Ultrafine Platinum Particles to the Immunological Detection of Human Serum Albumin. Analytical Biochemistry. 218(2). 259–264. 6 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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