Nobutada Tanaka

2.2k total citations
90 papers, 1.8k citations indexed

About

Nobutada Tanaka is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, Nobutada Tanaka has authored 90 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 54 papers in Molecular Biology, 24 papers in Materials Chemistry and 14 papers in Oncology. Recurrent topics in Nobutada Tanaka's work include Enzyme Structure and Function (18 papers), Biochemical and Molecular Research (13 papers) and Peptidase Inhibition and Analysis (12 papers). Nobutada Tanaka is often cited by papers focused on Enzyme Structure and Function (18 papers), Biochemical and Molecular Research (13 papers) and Peptidase Inhibition and Analysis (12 papers). Nobutada Tanaka collaborates with scholars based in Japan, United States and Germany. Nobutada Tanaka's co-authors include Takamasa Nonaka, Masayuki Nakanishi, Akira Hara, Yukio Mitsui, Kazuo Nakamura, Tadashi Yoshimoto, Yoshio Kusakabe, Kazuo Nakamura, Yukio Kitade and Yoshihiro Deyashiki and has published in prestigious journals such as Nucleic Acids Research, Journal of Biological Chemistry and The EMBO Journal.

In The Last Decade

Nobutada Tanaka

86 papers receiving 1.8k citations

Peers

Nobutada Tanaka
Xiaoqiu Wu China
Katsuhiko Yamamoto Japan
Mark Ensor United States
Chi‐Yuan Chou Taiwan
Qing‐Chuan Zheng China
E.J. Levin Canada
Megan L. O’Mara Australia
Dominic J. Campopiano United Kingdom
Xiaoling Yuan China
Xiaoqiu Wu China
Nobutada Tanaka
Citations per year, relative to Nobutada Tanaka Nobutada Tanaka (= 1×) peers Xiaoqiu Wu

Countries citing papers authored by Nobutada Tanaka

Since Specialization
Citations

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

Fields of papers citing papers by Nobutada Tanaka

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Nobutada Tanaka

This figure shows the co-authorship network connecting the top 25 collaborators of Nobutada Tanaka. A scholar is included among the top collaborators of Nobutada Tanaka 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 Nobutada Tanaka. Nobutada Tanaka 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.
Illarionov, Boris, Laís Pessanha de Carvalho, Klaus Pfeffer, et al.. (2024). Reverse N-Substituted Hydroxamic Acid Derivatives of Fosmidomycin Target a Previously Unknown Subpocket of 1-Deoxy-d-xylulose 5-Phosphate Reductoisomerase (DXR). ACS Infectious Diseases. 10(5). 1739–1752. 2 indexed citations
2.
Illarionov, Boris, Laís Pessanha de Carvalho, Adelbert Bacher, et al.. (2024). Expanding the Chemical Space of Reverse Fosmidomycin Analogs. ACS Medicinal Chemistry Letters. 16(1). 136–143.
3.
Okuwaki, Mitsuru, et al.. (2023). The stability of NPM1 oligomers regulated by acidic disordered regions controls the quality of liquid droplets. The Journal of Biochemistry. 174(5). 461–476. 3 indexed citations
4.
Kato, Atsushi, Izumi Nakagome, Nobutada Tanaka, et al.. (2023). Design and Pharmacological Chaperone Effects of N-(4′-Phenylbutyl)-DAB Derivatives Targeting the Lipophilic Pocket of Lysosomal Acid α-Glucosidase. Journal of Medicinal Chemistry. 66(13). 9023–9039. 5 indexed citations
5.
Kato, Atsushi, Izumi Nakagome, Tiantian Lu, et al.. (2022). Introduction of C-alkyl branches to l-iminosugars changes their active site binding orientation. Organic & Biomolecular Chemistry. 20(36). 7250–7260. 2 indexed citations
6.
Kato, Atsushi, Izumi Nakagome, Tiantian Lu, et al.. (2022). 5-C-Branched Deoxynojirimycin: Strategy for Designing a 1-Deoxynojirimycin-Based Pharmacological Chaperone with a Nanomolar Affinity for Pompe Disease. Journal of Medicinal Chemistry. 65(3). 2329–2341. 14 indexed citations
7.
Nakamura, Akihiro, Yoshiyuki Suzuki, Yosuke Shida, et al.. (2021). Structural basis for an exceptionally strong preference for asparagine residue at the S2 subsite of Stenotrophomonas maltophilia dipeptidyl peptidase 7. Scientific Reports. 11(1). 7929–7929. 4 indexed citations
8.
Suzuki, Yoshiyuki, Akihiro Nakamura, Yosuke Shida, et al.. (2018). Crystal structures of a bacterial dipeptidyl peptidase IV reveal a novel substrate recognition mechanism distinct from that of mammalian orthologues. Scientific Reports. 8(1). 2714–2714. 18 indexed citations
9.
Nakamura, Akihiro, Yoshiyuki Suzuki, Yosuke Shida, et al.. (2017). Periplasmic form of dipeptidyl aminopeptidase IV fromPseudoxanthomonas mexicanaWO24: purification, kinetic characterization, crystallization and X-ray crystallographic analysis. Acta Crystallographica Section F Structural Biology Communications. 73(11). 601–606. 1 indexed citations
10.
Suzuki, Yoshiyuki, Hirofumi Okada, Takamasa Nonaka, et al.. (2014). Crystallization and preliminary X-ray crystallographic studies of dipeptidyl aminopeptidase BII from Pseudoxanthomonas mexicana WO24. Acta Crystallographica Section F Structural Biology Communications. 70(2). 221–224. 3 indexed citations
11.
Tanaka, Nobutada, Yoshio Kusakabe, Arayo Haga, et al.. (2010). Crystallization and preliminary X-ray crystallographic study of phosphoglucose isomerase fromPlasmodium falciparum. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(3). 333–336. 3 indexed citations
12.
Tanaka, Nobutada, Masayuki Nakanishi, Yoshio Kusakabe, et al.. (2005). Crystallization of the N-Terminal Ankyrin Repeat Domain of the 2-5ADependent Endoribonuclease, RNase L. Protein and Peptide Letters. 12(4). 387–389. 3 indexed citations
13.
Tanaka, Nobutada, Yoshio Kusakabe, Tatsuyoshi Funasaka, et al.. (2004). Crystallization and preliminary X-ray crystallographic studies of mouse autocrine motility factor. Acta Crystallographica Section D Biological Crystallography. 60(11). 2084–2086. 2 indexed citations
14.
Tanaka, Nobutada, Masayuki Nakanishi, Yoshio Kusakabe, et al.. (2004). Structural basis for recognition of 2′,5′‐linked oligoadenylates by human ribonuclease L. The EMBO Journal. 23(20). 3929–3938. 75 indexed citations
15.
Tanaka, Nobutada, Masayuki Nakanishi, Yoshio Kusakabe, et al.. (2004). Crystal Structure of S-Adenosyl-l-Homocysteine Hydrolase from the Human Malaria Parasite Plasmodium falciparum. Journal of Molecular Biology. 343(4). 1007–1017. 54 indexed citations
16.
Ito, Kiyoshi, et al.. (2003). Novel inhibitor for prolyl aminopeptidase from Serratia marcescens and studies on the mechanism of substrate recognition of the enzyme using the inhibitor. Archives of Biochemistry and Biophysics. 416(2). 147–154. 17 indexed citations
17.
Tsutsumi, Soichi, Suresh K. Gupta, Victor Hogan, et al.. (2002). The enzymatic activity of phosphoglucose isomerase is not required for its cytokine function. FEBS Letters. 534(1-3). 49–53. 24 indexed citations
18.
Ito, Kiyoshi, Tomoyuki Takahashi, Hua‐Shan Huang, et al.. (2001). The Mechanism of Substrate Recognition of Pyroglutamyl-peptidase I from Bacillus amyloliquefaciens as Determined by X-ray Crystallography and Site-directed Mutagenesis. Journal of Biological Chemistry. 276(21). 18557–18562. 12 indexed citations
19.
Tanaka, Nobutada, et al.. (1996). Crystallization and preliminary X-ray crystallographic studies of 7α-hydroxysteroid dehydrogenase from Escherichia coli. Acta Crystallographica Section D Biological Crystallography. 52(1). 215–217. 4 indexed citations
20.
Tanaka, Nobutada, Takamasa Nonaka, Mahito Nakanishi, et al.. (1995). Crystallization of Mouse Lung Carbonyl Reductase Complexed with NADPH and Analysis of Symmetry of Its Tetrameric Molecule. The Journal of Biochemistry. 118(5). 871–873. 10 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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