Yoji Arata

2.1k total citations
47 papers, 1.8k citations indexed

About

Yoji Arata is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Immunology. According to data from OpenAlex, Yoji Arata has authored 47 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Molecular Biology, 19 papers in Radiology, Nuclear Medicine and Imaging and 8 papers in Immunology. Recurrent topics in Yoji Arata's work include Glycosylation and Glycoproteins Research (22 papers), Monoclonal and Polyclonal Antibodies Research (19 papers) and Protein purification and stability (9 papers). Yoji Arata is often cited by papers focused on Glycosylation and Glycoproteins Research (22 papers), Monoclonal and Polyclonal Antibodies Research (19 papers) and Protein purification and stability (9 papers). Yoji Arata collaborates with scholars based in Japan, United States and Singapore. Yoji Arata's co-authors include Ichio Shimada, Koichi Kato, Ichio Shimada, Hiroaki Gouda, Hidetaka Torigoe, Moriyuki Sato, Akiko T. Saito, Noriko Takahashi, Keiichiro Kami and HaHyung Kim and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Biochemistry.

In The Last Decade

Yoji Arata

46 papers receiving 1.7k citations

Peers

Yoji Arata

RNMI

IMMUN

SPECT

Claudio Vita France

R.A. Lerner United States

Wojciech Ardelt United States

Kathleen L. Grant United States

Melanie J. Cocco United States

Aaron K. Chamberlain United States

Robert O. Fox United States

Jorge Santoro Spain

Anne Pajon United Kingdom

Jean‐Baptiste Charbonnier France

Claudio Vita France

Yoji Arata

1.6k ×1.2

304 ×0.5

RNMI

480 ×1.3

IMMUN

345 ×1.3

169 ×1.0

SPECT

Citations per year, relative to Yoji Arata Yoji Arata (= 1×) peers Claudio Vita

Countries citing papers authored by Yoji Arata

Since Specialization

Citations

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

Fields of papers citing papers by Yoji Arata

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Yoji Arata

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

Nakasako, Masayoshi, Toshihiko Oka, Hideo Takahashi, et al.. (2005). Conformational Dynamics of Complementarity-determining Region H3 of an Anti-dansyl Fv Fragment in the Presence of its Hapten. Journal of Molecular Biology. 351(3). 627–640. 12 indexed citations

Kami, Keiichiro, et al.. (2000). A novel NMR method for determining the interfaces of large protein-protein complexes.. Nature Structural Biology. 7(3). 220–223. 229 indexed citations

Yamaguchi, Yoshiki, Koichi Kato, Mitsuru Shindo, et al.. (1998). Dynamics of the carbohydrate chains attached to the Fc portion of immunoglobulin G as studied by NMR spectroscopy assisted by selective 13C labeling of the glycans. Journal of Biomolecular NMR. 12(3). 385–394. 51 indexed citations

Su, Song‐Nan, Noriko Takahashi, Hiroaki Nakagawa, et al.. (1996). The Carbohydrate Moiety of the Bermuda Grass Antigen BG60. Journal of Biological Chemistry. 271(43). 26653–26658. 44 indexed citations

Torigoe, Hidetaka, et al.. (1995). The Affinity Maturation of Anti-4-hydroxy-3-nitrophenylacetyl Mouse Monoclonal Antibody. Journal of Biological Chemistry. 270(38). 22218–22222. 43 indexed citations

Kim, Jae Il, Shiro Konishi, Hideo Iwaï, et al.. (1995). Three-dimensional Solution Structure of the Calcium Channel Antagonist ω-Agatoxin IVA: Consensus Molecular Folding of Calcium Channel Blockers. Journal of Molecular Biology. 250(5). 659–671. 56 indexed citations

Arata, Yoji, Koichi Kato, Hideo Takahashi, & Ichio Shimada. (1994). [15] Nuclear magnetic resonance study of antibodies: A multinuclear approach. Methods in enzymology on CD-ROM/Methods in enzymology. 239. 440–464. 24 indexed citations

Ito, Keita, Noriko Takahashi, Akira Takahashi, et al.. (1993). Structural study of the oligosaccharide moieties of sphingolipid activator proteins, saposins A, C and D obtained from the spleen of a Gaucher patient. European Journal of Biochemistry. 215(1). 171–179. 16 indexed citations

Arata, Yoji, et al.. (1993). A multinuclear NMR study of the affinity maturation of anti-NP mouse monoclonal antibodies: Comparison of antibody combining sites of primary response antibody N1G9 and secondary response antibody 3B62. Biochemistry. 32(50). 13961–13968. 6 indexed citations

10.

Takahashi, Noriko, et al.. (1993). A structural study of the asparagine-linked oligosaccharide moiety of duck ovomucoid. Glycoconjugate Journal. 10(6). 425–434. 13 indexed citations

11.

Kato, Koichi, et al.. (1993). ¹³C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G. FEBS Letters. 328(1-2). 49–54. 31 indexed citations

12.

Nishimura, Chiaki, Koji Sakamoto, Hiroshi Suzuki, et al.. (1992). Role of leucine residues in the C‐terminal region of human interleukin‐6 in the biological activity. FEBS Letters. 311(3). 271–275. 14 indexed citations

13.

Mizutani, Ryuta, et al.. (1992). A 1H-NMR study of the solution conformation of cyclo(GRGDSPA): Conformational effects on the physiological activity. Biochemical and Biophysical Research Communications. 182(2). 966–973. 12 indexed citations

14.

Kato, Koichi, et al.. (1991). Carbon-13 NMR study of switch variant anti-dansyl antibodies: antigen binding and domain-domain interactions. Biochemistry. 30(26). 6604–6610. 47 indexed citations

15.

Torigoe, Hidetaka, Ichio Shimada, Markus Waelchli, et al.. (1990). ¹⁵N nuclear magnetic resonance studies of the B domain of Staphylococcal protein A: sequence specific assignments of the imide ¹⁵N resonances of the proline residues and the interaction with human immunoglobulin G. FEBS Letters. 269(1). 174–176. 15 indexed citations

16.

Shimada, Ichio, Koichi Kato, Kazuki Saito, et al.. (1990). A 1H-NMR study of the solution conformation of Icaria chemotactic peptide and its [Lys7] analog: Effects on the physiological activity of a substitution of proline to lysine at position 7. Biochemical and Biophysical Research Communications. 168(2). 596–603. 1 indexed citations

17.

Lund, John, et al.. (1990). A protein structural change in aglycosylated IgG3 correlates with loss of huFcγR1 and hufcγR111 binding and/or activation. Molecular Immunology. 27(11). 1145–1153. 104 indexed citations

18.

Odaka, C, et al.. (1990). Analysis of the molecular requirements for T cell recognition and activation by using la-containing lipid vesicles and stopped-flow fluorometry. International Immunology. 2(6). 509–514.

19.

Kato, Koichi, et al.. (1989). Application of 13C Nuclear Magnetic Resonance Spectroscopy to Molecular Structural Analyses of Antibody Molecules1. The Journal of Biochemistry. 105(6). 867–869. 30 indexed citations

20.

Ito, Wataru, et al.. (1987). A 1H NMR Method for the Analysis of Antigen-Antibody Interactions: Binding of a Peptide Fragment of Lysozyme to Anti-Lysozyme Monoclonal Antibody. The Journal of Biochemistry. 102(3). 643–649. 17 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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