H. Tsuruta

744 total citations
31 papers, 594 citations indexed

About

H. Tsuruta is a scholar working on Molecular Biology, Endocrinology, Diabetes and Metabolism and Biotechnology. According to data from OpenAlex, H. Tsuruta has authored 31 papers receiving a total of 594 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 8 papers in Endocrinology, Diabetes and Metabolism and 5 papers in Biotechnology. Recurrent topics in H. Tsuruta's work include Alkaline Phosphatase Research Studies (8 papers), Protein Tyrosine Phosphatases (5 papers) and Enzyme Structure and Function (4 papers). H. Tsuruta is often cited by papers focused on Alkaline Phosphatase Research Studies (8 papers), Protein Tyrosine Phosphatases (5 papers) and Enzyme Structure and Function (4 papers). H. Tsuruta collaborates with scholars based in Japan, United Kingdom and United States. H. Tsuruta's co-authors include David Eliezer, Sebastian Doniach, Yasuo Aizono, Ro Osawa, Peter E. Wright, Patricia A. Jennings, Kiyoshi Yamazaki, Kaori Chiba, Keith O. Hodgson and Hiroshi Kihara and has published in prestigious journals such as Science, Journal of Biological Chemistry and PLANT PHYSIOLOGY.

In The Last Decade

H. Tsuruta

30 papers receiving 588 citations

Peers

H. Tsuruta

BIOTE

Ruiying Wu United States

Teresa Caldas France

Johanna Kallio Finland

Rachel A. North New Zealand

Abderrahim Malki France

Mary K. Phillips‐Jones United Kingdom

Márton Miskei Hungary

Milton H. Saier United States

Helmut Pelzer Germany

Alexandra Tsirigotaki Belgium

Ruiying Wu United States

H. Tsuruta

657 ×2.0

155 ×0.9

48 ×0.6

56 ×0.8

BIOTE

47 ×0.7

Citations per year, relative to H. Tsuruta H. Tsuruta (= 1×) peers Ruiying Wu

Countries citing papers authored by H. Tsuruta

Since Specialization

Citations

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

Fields of papers citing papers by H. Tsuruta

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of H. Tsuruta

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

MANTANI, Youhei, Takuya Omotehara, H. Tsuruta, et al.. (2018). Ultrastructural and Immunohistochemical Study on the Lamina Propria Cells Beneath Paneth Cells in the Rat Ileum. The Anatomical Record. 301(6). 1074–1085. 7 indexed citations

Nabe, Takeshi, et al.. (2017). Analysis of major paralogs encoding the Fra a 1 allergen based on their organ-specificity in Fragaria × ananassa. Plant Cell Reports. 37(3). 411–424. 13 indexed citations

Wang, Bochao, Mitsuhiro Nishimura, Huamin Tang, et al.. (2016). Crystal Structure of Human Herpesvirus 6B Tegument Protein U14. PLoS Pathogens. 12(5). e1005594–e1005594. 10 indexed citations

Okazaki, Fumiyoshi, Chiaki Ogino, Akihiko Kondo, et al.. (2011). Expression, crystallization and preliminary X-ray diffraction studies of thermostable β-1,3-xylanase fromThermotoga neapolitanastrain DSM 4359. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(7). 779–781. 1 indexed citations

Tsuruta, H., et al.. (2010). Crystal Structure of Cold-Active Alkaline Phosphatase from the PsychrophileShewanellasp.. Bioscience Biotechnology and Biochemistry. 74(1). 69–74. 15 indexed citations

Isogai, Emiko, et al.. (2010). Tertiary structure-related activity of tick defensin (persulcatusin) in the taiga tick, Ixodes persulcatus. Experimental and Applied Acarology. 53(1). 71–77. 18 indexed citations

Iguchi, Atsushi, et al.. (2010). Polymorphism and distribution of putative cell-surface adhesin-encoding ORFs among human fecal isolates of Bifidobacterium longum subsp. longum. Antonie van Leeuwenhoek. 99(3). 457–471. 10 indexed citations

Tsuruta, H., et al.. (2010). Functional Analysis of the Cucumisin Propeptide as a Potent Inhibitor of Its Mature Enzyme. Journal of Biological Chemistry. 285(39). 29797–29807. 20 indexed citations

Tsuruta, H., et al.. (2008). Identification and cloning of a gene encoding tannase (tannin acylhydrolase) from Lactobacillus plantarum ATCC 14917T. Systematic and Applied Microbiology. 31(4). 269–277. 82 indexed citations

10.

Tsuruta, H., Bunzo Mikami, Chiaki Yamamoto, & Hiroshi Yamagata. (2008). The role of group bulkiness in the catalytic activity of psychrophile cold‐active protein tyrosine phosphatase. FEBS Journal. 275(17). 4317–4328. 8 indexed citations

11.

Tsuruta, H., et al.. (2007). Characterisitics and Gene Cloning of Phospholipase D of the Psychrophile,Shewanellasp.. Bioscience Biotechnology and Biochemistry. 71(10). 2534–2542. 6 indexed citations

12.

Tsuruta, H.. (2005). Crystal Structure of Cold-Active Protein-Tyrosine Phosphatase from a Psychrophile, Shewanella sp.. The Journal of Biochemistry. 137(1). 69–77. 20 indexed citations

13.

Tsuruta, H., Bunzo Mikami, Chiaki Yamamoto, & Yasuo Aizono. (2002). Crystallization and preliminary X-ray studies of cold-active protein-tyrosine phosphatase ofShewanellasp.. Acta Crystallographica Section D Biological Crystallography. 58(9). 1465–1466. 2 indexed citations

14.

Murakawa, T., Hiroshi Yamagata, H. Tsuruta, & Yasuo Aizono. (2002). Cloning of Cold-active Alkaline Phosphatase Gene of a Psychrophile,Shewanellasp., and Expression of the Recombinant Enzyme. Bioscience Biotechnology and Biochemistry. 66(4). 754–761. 12 indexed citations

15.

Tsuruta, H. & Yasuo Aizono. (2000). Cloning of Phosphatase I Gene from a Psychrophile, Shewanella sp., and Some Properties of the Recombinant Enzyme. The Journal of Biochemistry. 127(1). 143–149. 12 indexed citations

16.

Tsuruta, H. & Yasuo Aizono. (1999). Enzymatical Properties of Psychrophilic Phosphatase I. The Journal of Biochemistry. 125(4). 690–695. 10 indexed citations

17.

Ishida, Yoshihiro, et al.. (1998). Characteristics of Psychrophilic Alkaline Phosphatase. Bioscience Biotechnology and Biochemistry. 62(11). 2246–2250. 21 indexed citations

18.

Eliezer, David, et al.. (1995). The Radius of Gyration of an Apomyoglobin Folding Intermediate. Science. 270(5235). 487–487. 123 indexed citations

19.

Tsuruta, H., et al.. (1994). Transitional Lateral Drag Acting on Ship Moving from Rest : An Experimental Study by Using a Ship's Model. The Journal of Japan Institute of Navigation. 90(0). 273–279. 2 indexed citations

20.

Eliezer, David, Kaori Chiba, H. Tsuruta, et al.. (1993). Evidence of an associative intermediate on the myoglobin refolding pathway. Biophysical Journal. 65(2). 912–917. 76 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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