Masahiko Nanami

562 total citations
17 papers, 432 citations indexed

About

Masahiko Nanami is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Immunology. According to data from OpenAlex, Masahiko Nanami has authored 17 papers receiving a total of 432 indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 10 papers in Radiology, Nuclear Medicine and Imaging and 4 papers in Immunology. Recurrent topics in Masahiko Nanami's work include Monoclonal and Polyclonal Antibodies Research (10 papers), Glycosylation and Glycoproteins Research (8 papers) and Protein purification and stability (3 papers). Masahiko Nanami is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (10 papers), Glycosylation and Glycoproteins Research (8 papers) and Protein purification and stability (3 papers). Masahiko Nanami collaborates with scholars based in Japan and United States. Masahiko Nanami's co-authors include Tatsuhiko Tachibana, Hiroyuki Tsunoda, Tomoyuki Igawa, Kunihiro Hattori, Yoshinori Aso, Yasuo Sekimori, Chifumi Moriyama, Atsuhiko Maeda, Yoshiaki Nabuchi and Futa Mimoto and has published in prestigious journals such as Blood, Clinical Cancer Research and Drug Metabolism and Disposition.

In The Last Decade

Masahiko Nanami

17 papers receiving 396 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Masahiko Nanami Japan 9 267 266 106 55 38 17 432
S. Maloney Canada 12 111 0.4× 193 0.7× 114 1.1× 26 0.5× 10 0.3× 32 528
Marie-Pierre Gras France 8 88 0.3× 207 0.8× 258 2.4× 102 1.9× 19 0.5× 12 525
Patrick H. van Berkel United Kingdom 9 181 0.7× 112 0.4× 96 0.9× 26 0.5× 13 0.3× 35 496
Johanna Stéen Sweden 11 188 0.7× 192 0.7× 165 1.6× 17 0.3× 2 0.1× 24 520
Gadi Gazit Bornstein United States 6 189 0.7× 151 0.6× 104 1.0× 21 0.4× 2 0.1× 9 335
Juha Pekka Turunen Finland 14 78 0.3× 300 1.1× 238 2.2× 31 0.6× 11 0.3× 20 573
Inna Vainshtein United States 13 211 0.8× 210 0.8× 221 2.1× 21 0.4× 2 0.1× 26 510
Mei Su United States 13 25 0.1× 143 0.5× 143 1.3× 23 0.4× 14 0.4× 28 403
Christie Fanton United States 11 38 0.1× 198 0.7× 267 2.5× 17 0.3× 13 0.3× 26 587
Alexander Buffone United States 13 50 0.2× 319 1.2× 222 2.1× 52 0.9× 3 0.1× 17 565

Countries citing papers authored by Masahiko Nanami

Since Specialization
Citations

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

Fields of papers citing papers by Masahiko Nanami

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Masahiko Nanami

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

All Works

17 of 17 papers shown
1.
Hori, Yuji, Hitoshi Katada, Yuki Noguchi, et al.. (2022). Elimination of plasma soluble antigen in cynomolgus monkeys by combining pH-dependent antigen binding and novel Fc engineering. mAbs. 14(1). 2068213–2068213. 6 indexed citations
2.
Kitamura, Hidetomo, Taichi Kuramochi, Yoshinobu Higuchi, et al.. (2016). Cynomolgus monkey model of interleukin‐31‐induced scratching depicts blockade of human interleukin‐31 receptor A by a humanized monoclonal antibody. Experimental Dermatology. 27(1). 14–21. 41 indexed citations
3.
Shimizu, Masaru, Hiroshi Noda, Chie Nakagawa, et al.. (2016). The Optimal Duration of PTH(1–34) Infusion Is One Hour per Day to Increase Bone Mass in Rats. Biological and Pharmaceutical Bulletin. 39(4). 625–630. 12 indexed citations
4.
Haraya, Kenta, Tatsuhiko Tachibana, Masahiko Nanami, & Masaki Ishigai. (2014). Application of human FcRn transgenic mice as a pharmacokinetic screening tool of monoclonal antibody. Xenobiotica. 44(12). 1127–1134. 22 indexed citations
5.
Igawa, Tomoyuki, Hiroyuki Tsunoda, Tatsuhiko Tachibana, et al.. (2010). Reduced elimination of IgG antibodies by engineering the variable region. Protein Engineering Design and Selection. 23(5). 385–392. 204 indexed citations
6.
TAKAI, H., Atsuhiko Kato, Teruo Nakamura, et al.. (2010). The importance of characterization of FITC-labeled antibodies used in tissue cross-reactivity studies. Acta Histochemica. 113(4). 472–476. 11 indexed citations
7.
Amano, Jun, et al.. (2010). Antigen-Dependent Internalization Is Related to Rapid Elimination from Plasma of Humanized Anti-HM1.24 Monoclonal Antibody. Drug Metabolism and Disposition. 38(12). 2339–2346. 13 indexed citations
8.
Yoshikubo, T, Yoshihiro Matsumoto, Masahiko Nanami, et al.. (2008). Humanized Sc(Fv)2 Minibody against C-Mpl Successfully Increased Platelet Number in Monkey and Increased Engraftment of Human Umbilical Cord Blood Cells in NOD/SCID Mouse.. Blood. 112(11). 2322–2322. 1 indexed citations
9.
Azuma, Yumiko, Yuji Ishikawa, Shigeto Kawai, et al.. (2007). Recombinant Human Hexamer-Dominant IgM Monoclonal Antibody to Ganglioside GM3 for Treatment of Melanoma. Clinical Cancer Research. 13(9). 2745–2750. 27 indexed citations
10.
Kikuchi, Yasufumi, Masahiko Nanami, Yasushi Yoshimura, et al.. (2005). Determination of concentration and binding affinity of antibody fragments by use of surface plasmon resonance. Journal of Bioscience and Bioengineering. 100(3). 311–317. 28 indexed citations
11.
Orita, Tetsuro, Hiroyuki Tsunoda, Kiyotaka Nakano, et al.. (2004). A novel therapeutic approach for thrombocytopenia by minibody agonist of the thrombopoietin receptor. Blood. 105(2). 562–566. 54 indexed citations
12.
Nanami, Masahiko, Kiyoshi Zaitsu, & Yosuke Ohkura. (1993). Preparation of Fluorescence Labeled Insulins, Sulfobenzoxadiazolyl-insulins, for Fluorescence Immunoassay.. Biological and Pharmaceutical Bulletin. 16(2). 99–102. 2 indexed citations
13.
Nanami, Masahiko, Kiyoshi Zaitsu, & Yosuke Ohkura. (1993). Effect of Spacer Groups Connecting Insulin with Fluorophore in Gly(A1)-sulfobenzoxadiazole-Labeled Insulins on the Immunoreactivity toward Anti-insulin Antibody.. Biological and Pharmaceutical Bulletin. 16(5). 516–517. 2 indexed citations
14.
Nanami, Masahiko, Kiyoshi Zaitsu, & Yosuke Ohkura. (1993). Solid-Phase Fluoroimmunoassay of Insulin Using Two Insulins Labeled with a Fluorescent Sulfobenzoxadiazolyl Group. Analytical Sciences. 9(2). 213–216. 1 indexed citations
15.
Nanami, Masahiko, Kiyoshi Zaitsu, & Yosuke Ohkura. (1992). Preparation of S-acetylthioglycoloyl Insulins Based on Separation by Anion-Exchange High-Performance Liquid Chromatography.. Chemical and Pharmaceutical Bulletin. 40(4). 957–960. 2 indexed citations
16.
Zaitsu, Kiyoshi, et al.. (1992). Evaluation of the Numbers of Functional Groups Introduced into Horseradish Peroxidase in Reactions with Four Heterobifunctional Reagents.. Chemical and Pharmaceutical Bulletin. 40(8). 2205–2207. 2 indexed citations
17.
Zaitsu, Kiyoshi, Masafumi Nakayama, Masahiko Nanami, & Yosuke Ohkura. (1991). Solid-phase enzyme-immunoassay of anti-insulin antibodies: Effect of labeling site in insulin and of labeled number of horseradish peroxidase on the assay sensitivity.. Chemical and Pharmaceutical Bulletin. 39(2). 499–500. 4 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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