Tadashi Hatanaka

1.9k total citations
95 papers, 1.6k citations indexed

About

Tadashi Hatanaka is a scholar working on Molecular Biology, Oncology and Biotechnology. According to data from OpenAlex, Tadashi Hatanaka has authored 95 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 63 papers in Molecular Biology, 29 papers in Oncology and 21 papers in Biotechnology. Recurrent topics in Tadashi Hatanaka's work include Peptidase Inhibition and Analysis (28 papers), Enzyme Production and Characterization (17 papers) and Chemical Synthesis and Analysis (12 papers). Tadashi Hatanaka is often cited by papers focused on Peptidase Inhibition and Analysis (28 papers), Enzyme Production and Characterization (17 papers) and Chemical Synthesis and Analysis (12 papers). Tadashi Hatanaka collaborates with scholars based in Japan, Canada and China. Tadashi Hatanaka's co-authors include Jiro Arima, Yoshiko Uesugi, Masaki Iwabuchi, Misugi Uraji, Hirokazu Usuki, Kayoko Kawakami, Yuya Kumagai, Takafumi Mukaihara, Tomofumi Negishi and Y. Yamamoto and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Journal of Applied Physics.

In The Last Decade

Tadashi Hatanaka

95 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Tadashi Hatanaka Japan 23 1.1k 363 339 237 181 95 1.6k
Jiro Arima Japan 18 703 0.6× 287 0.8× 219 0.6× 117 0.5× 102 0.6× 72 1.1k
Mikio Fujii Japan 23 1.1k 0.9× 118 0.3× 233 0.7× 197 0.8× 82 0.5× 73 1.7k
Marcos D. Pereira Brazil 26 839 0.7× 265 0.7× 69 0.2× 318 1.3× 113 0.6× 75 2.0k
Wen-Hwei Hsu Taiwan 23 1.1k 1.0× 139 0.4× 381 1.1× 164 0.7× 210 1.2× 78 1.5k
Ping Zhu China 24 1.1k 0.9× 108 0.3× 341 1.0× 275 1.2× 139 0.8× 110 1.8k
Shun‐ichi Wada Japan 28 1.3k 1.2× 143 0.4× 142 0.4× 245 1.0× 67 0.4× 101 2.2k
R.D. Seidel United States 21 1.1k 0.9× 68 0.2× 197 0.6× 132 0.6× 188 1.0× 35 1.4k
Long‐Liu Lin Taiwan 25 1.2k 1.1× 244 0.7× 779 2.3× 417 1.8× 354 2.0× 120 1.9k
R. Natesh United Kingdom 12 1.1k 1.0× 178 0.5× 87 0.3× 59 0.2× 64 0.4× 21 1.5k
Kuo‐Chiang Hsu Taiwan 29 1.4k 1.3× 263 0.7× 318 0.9× 151 0.6× 70 0.4× 73 2.5k

Countries citing papers authored by Tadashi Hatanaka

Since Specialization
Citations

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

Fields of papers citing papers by Tadashi Hatanaka

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Tadashi Hatanaka

This figure shows the co-authorship network connecting the top 25 collaborators of Tadashi Hatanaka. A scholar is included among the top collaborators of Tadashi Hatanaka 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 Tadashi Hatanaka. Tadashi Hatanaka 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.
Yang, Lingli & Tadashi Hatanaka. (2023). Enhanced overexpression of secreted enzymes by discrete repeat promoters in Streptomyces lividans. Bioscience Biotechnology and Biochemistry. 87(11). 1420–1426. 2 indexed citations
2.
Kawakami, Kayoko, et al.. (2022). Isolation of the hemeoxygenase-1 inducer from rice-derived peptide. Journal of Clinical Biochemistry and Nutrition. 71(1). 41–47. 1 indexed citations
3.
Uraji, Misugi, et al.. (2019). Molecular insights into the mechanism of substrate recognition of Streptomyces transglutaminases. Bioscience Biotechnology and Biochemistry. 84(3). 575–582. 7 indexed citations
4.
Bito, Tomohiro, et al.. (2018). Active site pocket of Streptomyces d-stereospecific amidohydrolase has functional roles in aminolysis activity. Journal of Bioscience and Bioengineering. 126(3). 293–300. 3 indexed citations
5.
Uraji, Misugi, H. Tamura, Eiichi Mizohata, et al.. (2017). Loop of Streptomyces Feruloyl Esterase Plays an Important Role in the Enzyme's Catalyzing the Release of Ferulic Acid from Biomass. Applied and Environmental Microbiology. 84(3). 20 indexed citations
6.
7.
Kumagai, Yuya, Kayoko Kawakami, Misugi Uraji, & Tadashi Hatanaka. (2012). Binding of bivalent ions to actinomycete mannanase is accompanied by conformational change and is a key factor in its thermal stability. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1834(1). 301–307. 14 indexed citations
8.
Kumagai, Yuya, et al.. (2012). The structural analysis and the role of calcium binding site for thermal stability in mannanase. Biochimie. 94(12). 2783–2790. 24 indexed citations
9.
Hatanaka, Tadashi, Akihiro Yamasato, Jiro Arima, et al.. (2011). Extracellular Production and Characterization of Streptomyces X-prolyl Dipeptidyl Aminopeptidase. Applied Biochemistry and Biotechnology. 164(4). 475–486. 9 indexed citations
10.
Hatanaka, Tadashi, Hirokazu Usuki, Jiro Arima, et al.. (2010). Extracellular Production and Characterization of Two Streptomyces l-Asparaginases. Applied Biochemistry and Biotechnology. 163(7). 836–844. 31 indexed citations
11.
Arima, Jiro, Yoshiko Uesugi, & Tadashi Hatanaka. (2009). Bacillus d-stereospecific metallo-amidohydrolase: Active-site metal-ion substitution changes substrate specificity. Biochimie. 91(4). 568–576. 9 indexed citations
12.
Uesugi, Yoshiko & Tadashi Hatanaka. (2009). Phospholipase D mechanism using Streptomyces PLD. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1791(9). 962–969. 52 indexed citations
13.
Uraji, Misugi, Jiro Arima, Yoshiko Uesugi, Masaki Iwabuchi, & Tadashi Hatanaka. (2007). Effect of salt on the activity of Streptomyces prolyl aminopeptidase. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1774(11). 1462–1469. 23 indexed citations
14.
Arima, Jiro, Yoshiko Uesugi, Masaki Iwabuchi, & Tadashi Hatanaka. (2006). Change in Substrate Preference ofStreptomycesAminopeptidase through Modification of the Environment around the Substrate Binding Site. Applied and Environmental Microbiology. 72(12). 7962–7967. 3 indexed citations
15.
Uesugi, Yoshiko, Jiro Arima, Masaki Iwabuchi, & Tadashi Hatanaka. (2006). C‐terminal loop of Streptomyces phospholipase D has multiple functional roles. Protein Science. 16(2). 197–207. 20 indexed citations
16.
Uesugi, Yoshiko, Kōichi Mori, Jiro Arima, Masaki Iwabuchi, & Tadashi Hatanaka. (2005). Recognition of Phospholipids in Streptomyces Phospholipase D. Journal of Biological Chemistry. 280(28). 26143–26151. 20 indexed citations
17.
Arima, Jiro, Yoshiko Uesugi, Misugi Uraji, et al.. (2005). Modulation of Streptomyces Leucine Aminopeptidase by Calcium. Journal of Biological Chemistry. 281(9). 5885–5894. 25 indexed citations
18.
Takei, Satoshi, et al.. (2004). Thin film and high-etch-rate type 248-nm bottom antireflective coatings. Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE. 5376. 689–689. 1 indexed citations
19.
Tsuboi, Seiji, Kenichi Ogawa, Tadashi Hatanaka, et al.. (2002). An Intramolecular Disulfide Bridge as a Catalytic Switch for Serotonin N-Acetyltransferase. Journal of Biological Chemistry. 277(46). 44229–44235. 9 indexed citations
20.
Nishikawa, Masanobu, et al.. (2000). Primary structure and expression of peroxisomal acetylspermidine oxidase in the methylotrophic yeast Candida boidinii. FEBS Letters. 476(3). 150–154. 20 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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