S. Kuramitsu

451 total citations
11 papers, 393 citations indexed

About

S. Kuramitsu is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, S. Kuramitsu has authored 11 papers receiving a total of 393 indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Molecular Biology, 6 papers in Materials Chemistry and 5 papers in Biochemistry. Recurrent topics in S. Kuramitsu's work include Enzyme Structure and Function (6 papers), Amino Acid Enzymes and Metabolism (5 papers) and RNA modifications and cancer (3 papers). S. Kuramitsu is often cited by papers focused on Enzyme Structure and Function (6 papers), Amino Acid Enzymes and Metabolism (5 papers) and RNA modifications and cancer (3 papers). S. Kuramitsu collaborates with scholars based in Japan and Russia. S. Kuramitsu's co-authors include Akihiro Okamoto, Hiroyuki Kagamiyama, Taiichi Higuchi, Ken Hirotsu, Yoshimasa Morino, Yasushi Inoue, Ryuichi Kato, Ryoji Masui, Shinichi Kawaguchi and Akihiko Yamagishi and has published in prestigious journals such as Biochemical and Biophysical Research Communications, European Journal of Biochemistry and Electrophoresis.

In The Last Decade

S. Kuramitsu

11 papers receiving 387 citations

Peers

S. Kuramitsu

BIOCH

GENET

BIOTE

H. Kagamiyama Japan

Yukuo Mukohara Japan

Günter Schumacher Germany

Adelia Razeto Germany

Ridong Chen United States

Annette Baich United States

Hisasi Kikuchi Japan

Christiane LEGRAIN Belgium

N. Zwaig Venezuela

Stephan Umhau Germany

H. Kagamiyama Japan

S. Kuramitsu

439 ×1.3

228 ×1.1

176 ×1.1

BIOCH

62 ×1.5

GENET

19 ×1.0

BIOTE

Citations per year, relative to S. Kuramitsu S. Kuramitsu (= 1×) peers H. Kagamiyama

Countries citing papers authored by S. Kuramitsu

Since Specialization

Citations

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

Fields of papers citing papers by S. Kuramitsu

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of S. Kuramitsu

This figure shows the co-authorship network connecting the top 25 collaborators of S. Kuramitsu. A scholar is included among the top collaborators of S. Kuramitsu 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 S. Kuramitsu. S. Kuramitsu is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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11 of 11 papers shown

Onodera, Takashi, S. Tokishita, R Morita, et al.. (2010). Role of alkyltransferase-like (ATL) protein in repair of methylated DNA lesions in Thermus thermophilus. Mutagenesis. 26(2). 303–308. 5 indexed citations

Dong, Xuesong, Yoshitaka Bessho, Madoka Nishimoto, et al.. (2006). Crystal Structure of the tRNA Pseudouridine Synthase TruA from Thermus Thermophilus HB8. RNA Biology. 3(3). 115–121. 11 indexed citations

Hori, Hiroyuki, Tsutomu Suzuki, Yorinao Inoue, et al.. (2002). Identification and characterization of tRNA (Gm18) methyltransferase from Thermus thermophilus HB8: domain structure and conserved amino acid sequence motifs. Genes to Cells. 7(3). 259–272. 51 indexed citations

Spies, Maria, Yury Kil, Ryoji Masui, et al.. (2000). The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C. European Journal of Biochemistry. 267(4). 1125–1137. 22 indexed citations

Okamoto, Akihiro, Ryuichi Kato, Ryoji Masui, et al.. (1996). An Aspartate Aminotransferase from an Extremely Thermophilic Bacterium, Thermus thermophilus HB8. The Journal of Biochemistry. 119(1). 135–144. 40 indexed citations

Kawaguchi, Shinichi & S. Kuramitsu. (1995). Separation of heat‐stable proteins from Thermus thermophilus HB8 by two‐dimensional electrophoresis. Electrophoresis. 16(1). 1060–1066. 15 indexed citations

Okamoto, Akihiro, Taiichi Higuchi, Ken Hirotsu, S. Kuramitsu, & Hiroyuki Kagamiyama. (1994). X-Ray Crystallographic Study of Pyridoxal 5′-Phosphate-Type Aspartate Aminotransferases from Escherichia coli in Open and Closed Form1. The Journal of Biochemistry. 116(1). 95–107. 132 indexed citations

Miyazawa, Keiji, Shinichi Kawaguchi, Akihiro Okamoto, et al.. (1994). Construction of Aminotransferase Chimeras and Analysis of Their Substrate Specificity1. The Journal of Biochemistry. 115(3). 568–577. 12 indexed citations

Inoue, Yasushi, et al.. (1990). Effects of replacement of tryptophan-140 by phenylalanine or glycine on the function of aspartate aminotransferase. Biochemical and Biophysical Research Communications. 167(2). 407–412. 28 indexed citations

10.

Kuramitsu, S., et al.. (1989). [Arg292 → val] or [Arg292 → leu] mutation enhances the reactivity of Escherichia, coli aspartate aminotransferase with aromatic amino acids. Biochemical and Biophysical Research Communications. 159(1). 337–342. 33 indexed citations

11.

Kamitori, S., K. Hirotsu, Tomoko Higuchi, et al.. (1987). Overproduction and Preliminary X-Ray Characterization of Aspartate Aminotransferase from Escherichia coli. The Journal of Biochemistry. 101(3). 813–816. 44 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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