Takashi Tonozuka

2.4k total citations
103 papers, 1.9k citations indexed

About

Takashi Tonozuka is a scholar working on Biotechnology, Nutrition and Dietetics and Molecular Biology. According to data from OpenAlex, Takashi Tonozuka has authored 103 papers receiving a total of 1.9k indexed citations (citations by other indexed papers that have themselves been cited), including 77 papers in Biotechnology, 41 papers in Nutrition and Dietetics and 40 papers in Molecular Biology. Recurrent topics in Takashi Tonozuka's work include Enzyme Production and Characterization (77 papers), Microbial Metabolites in Food Biotechnology (39 papers) and Biofuel production and bioconversion (25 papers). Takashi Tonozuka is often cited by papers focused on Enzyme Production and Characterization (77 papers), Microbial Metabolites in Food Biotechnology (39 papers) and Biofuel production and bioconversion (25 papers). Takashi Tonozuka collaborates with scholars based in Japan, United States and Netherlands. Takashi Tonozuka's co-authors include Yoshiyuki Sakano, Atsushi Nishikawa, S. Kamitori, Jennifer L. Stamos, Nam‐Chul Ha, William I. Weis, Hee‐Jung Choi, Takatsugu Miyazaki, Yoichiro Shimura and Masahiro Mizuno and has published in prestigious journals such as Journal of Biological Chemistry, Genes & Development and Molecular Cell.

In The Last Decade

Takashi Tonozuka

101 papers receiving 1.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Takashi Tonozuka Japan 25 1.0k 986 536 406 294 103 1.9k
Yoshiyuki Sakano Japan 23 1.1k 1.0× 616 0.6× 430 0.8× 528 1.3× 273 0.9× 103 1.5k
Tomoyuki Nishimoto Japan 29 765 0.7× 1.1k 1.1× 515 1.0× 284 0.7× 291 1.0× 123 2.2k
Noshi Minamiura Japan 19 522 0.5× 592 0.6× 379 0.7× 234 0.6× 161 0.5× 81 1.2k
Valery Belakhov Israel 31 424 0.4× 1.6k 1.6× 132 0.2× 183 0.5× 341 1.2× 108 2.5k
Eui‐Jeon Woo South Korea 24 442 0.4× 1.4k 1.4× 244 0.5× 549 1.4× 244 0.8× 75 2.0k
Henrik Dalbøge Denmark 24 598 0.6× 875 0.9× 129 0.2× 727 1.8× 339 1.2× 39 2.0k
Alberto Barbiroli Italy 26 120 0.1× 975 1.0× 405 0.8× 365 0.9× 95 0.3× 99 2.0k
Koji Ikura Japan 25 313 0.3× 661 0.7× 101 0.2× 130 0.3× 46 0.2× 89 1.9k
Karl Peter Rücknagel Germany 19 247 0.2× 1.1k 1.1× 110 0.2× 113 0.3× 245 0.8× 24 1.5k
Hajime Taniguchi Japan 25 830 0.8× 685 0.7× 658 1.2× 454 1.1× 351 1.2× 118 1.8k

Countries citing papers authored by Takashi Tonozuka

Since Specialization
Citations

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

Fields of papers citing papers by Takashi Tonozuka

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Takashi Tonozuka

This figure shows the co-authorship network connecting the top 25 collaborators of Takashi Tonozuka. A scholar is included among the top collaborators of Takashi Tonozuka 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 Takashi Tonozuka. Takashi Tonozuka 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.
Ragab, Rokaia F., et al.. (2024). Crystal structure of exfoliative toxin D from Staphylococcus aureus. Biochemical and Biophysical Research Communications. 733. 150689–150689.
2.
Sato, Hiroyuki, et al.. (2023). Cleavage of the Jaw1 C-terminal region enhances its augmentative effect on the Ca2+ release via IP3 receptors. Journal of Cell Science. 136(4). 2 indexed citations
3.
Li, Ding, Yuki Miyasaka, Yoshikazu Kitano, et al.. (2023). Characterization and alteration of product specificity of Beijerinckia indica subsp. indica β-fructosyltransferase. Bioscience Biotechnology and Biochemistry. 87(9). 981–990. 1 indexed citations
4.
Sato, Hiroyuki, et al.. (2022). Jaw1/LRMP increases Ca2+ influx upon GPCR stimulation with heterogeneous effect on the activity of each ITPR subtype. Scientific Reports. 12(1). 9476–9476. 6 indexed citations
5.
Li, Ding, Nobumitsu Sasaki, Atsushi Nishikawa, et al.. (2022). Enzymatic and structural characterization of β-fructofuranosidase from the honeybee gut bacterium Frischella perrara. Applied Microbiology and Biotechnology. 106(7). 2455–2470. 8 indexed citations
6.
7.
Miyazaki, Takatsugu, et al.. (2015). Crystal structure and substrate-binding mode of GH63 mannosylglycerate hydrolase from Thermus thermophilus HB8. Journal of Structural Biology. 190(1). 21–30. 8 indexed citations
8.
9.
Tonozuka, Takashi, Takatsugu Miyazaki, & Atsushi Nishikawa. (2011). Structural Similarity between a Starch-hydrolyzing Enzyme and an N-Glycan-Hydrolyzing Enzyme: Exohydrolases Cleaving α-1,X-Glucosidic Linkages to Produce β-Glucose. Trends in Glycoscience and Glycotechnology. 23(130). 93–102. 1 indexed citations
10.
Fujita, Naonobu, et al.. (2008). The relative contribution of mannose salvage pathways to glycosylation in PMI‐deficient mouse embryonic fibroblast cells. FEBS Journal. 275(4). 788–798. 15 indexed citations
11.
Nakamura, Toshio, et al.. (2007). Sugar-binding Sites of the HA1 Subcomponent of Clostridium botulinum Type C Progenitor Toxin. Journal of Molecular Biology. 376(3). 854–867. 42 indexed citations
12.
Kobayashi, Atsushi, Takashi Tonozuka, Kimihiko Sato, et al.. (2006). Molecular Cloning and Characterization of an Enzyme Hydrolyzingp-Nitrophenyl α-D-Glucoside fromBacillus stearothermophilusSA0301. Bioscience Biotechnology and Biochemistry. 70(2). 495–499. 4 indexed citations
13.
Ichikawa, Kazuhiro, Takashi Tonozuka, Masahiro Mizuno, et al.. (2005). Crystallization and preliminary X-ray analysis ofThermoactinomyces vulgarisR-47 maltooligosaccharide-metabolizing enzyme homologous to glucoamylase. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(3). 302–304. 1 indexed citations
14.
Uotsu, Nobuo, Atsushi Nishikawa, Toshihiro Watanabe, et al.. (2005). Cell internalization and traffic pathway of Clostridium botulinum type C neurotoxin in HT-29 cells. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1763(1). 120–128. 27 indexed citations
15.
16.
Tonozuka, Takashi, et al.. (2004). Heterologous Production and Characterization of Arthrobacter globiformis T6 Isomalto-dextranase. Journal of Applied Glycoscience. 51(1). 27–32. 5 indexed citations
17.
Akita, M., Masahiro Mizuno, Takashi Tonozuka, et al.. (2004). Crystallization and preliminary X-ray study of isomaltodextranase fromArthrobacter globiformis. Acta Crystallographica Section D Biological Crystallography. 60(3). 572–573. 1 indexed citations
18.
Tonozuka, Takashi, et al.. (2004). Crystallization and preliminary X-ray analysis ofEscherichia coliK12 YgjK protein, a member of glycosyl hydrolase family 63. Acta Crystallographica Section D Biological Crystallography. 60(7). 1284–1285. 4 indexed citations
19.
Yokota, Takehiro, Takashi Tonozuka, S. Kamitori, & Yoshiyuki Sakano. (2001). The Deletion of Amino-Terminal Domain in Thermoactinomyces vulgaris R-47 α-Amylases: Effects of domain N on Activity, Specificity, Stability and Dimerization. Bioscience Biotechnology and Biochemistry. 65(2). 401–408. 20 indexed citations
20.
Tonozuka, Takashi, Yoichiro Shimura, Akiko Shimizu‐Ibuka, et al.. (1995). Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing α-amylases, TVA I and TVA II, from Thermoactinomyces vulgaris R-47. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1252(1). 35–42. 51 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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