Masatake Ohnishi

1.7k total citations
86 papers, 1.5k citations indexed

About

Masatake Ohnishi is a scholar working on Biotechnology, Molecular Biology and Materials Chemistry. According to data from OpenAlex, Masatake Ohnishi has authored 86 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 50 papers in Biotechnology, 47 papers in Molecular Biology and 17 papers in Materials Chemistry. Recurrent topics in Masatake Ohnishi's work include Enzyme Production and Characterization (50 papers), Enzyme Catalysis and Immobilization (21 papers) and Enzyme Structure and Function (17 papers). Masatake Ohnishi is often cited by papers focused on Enzyme Production and Characterization (50 papers), Enzyme Catalysis and Immobilization (21 papers) and Enzyme Structure and Function (17 papers). Masatake Ohnishi collaborates with scholars based in Japan, United States and China. Masatake Ohnishi's co-authors include Keitarō Hiromi, Akiyoshi Tanaka, Toshihiko Suganuma, Ben’ichiro Tonomura, Hiroshi Nakatani, Sumio Ishijima, Ryuichi Matsuno, Masayuki Oda, Hiroki Takagi and Takashi Yamashita and has published in prestigious journals such as Biochemistry, Analytical Biochemistry and Biochemical and Biophysical Research Communications.

In The Last Decade

Masatake Ohnishi

83 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Masatake Ohnishi Japan 20 703 677 383 369 229 86 1.5k
G. Zeikus United States 5 1.3k 1.9× 759 1.1× 285 0.7× 140 0.4× 379 1.7× 8 1.8k
Shigeo Aibara Japan 21 561 0.8× 210 0.3× 409 1.1× 137 0.4× 78 0.3× 75 1.2k
Zümrüt B. Ögel Türkiye 17 635 0.9× 288 0.4× 347 0.9× 153 0.4× 310 1.4× 39 1.4k
Marc Beauregard Canada 23 922 1.3× 326 0.5× 364 1.0× 50 0.1× 328 1.4× 72 1.5k
T. Arakawa Japan 21 1.1k 1.5× 234 0.3× 154 0.4× 213 0.6× 180 0.8× 53 1.6k
Akimasa Miyanaga Japan 24 1.2k 1.7× 515 0.8× 244 0.6× 164 0.4× 220 1.0× 80 2.0k
Jesper Vind Denmark 23 1.3k 1.9× 337 0.5× 337 0.9× 77 0.2× 300 1.3× 45 1.9k
Nham T. Nguyen Canada 13 529 0.8× 271 0.4× 92 0.2× 90 0.2× 112 0.5× 15 963
Roberta Chiaraluce Italy 22 1.1k 1.6× 192 0.3× 168 0.4× 126 0.3× 60 0.3× 64 1.7k
Yehuda Levin Israel 16 1.3k 1.9× 200 0.3× 72 0.2× 124 0.3× 139 0.6× 25 2.0k

Countries citing papers authored by Masatake Ohnishi

Since Specialization
Citations

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

Fields of papers citing papers by Masatake Ohnishi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Masatake Ohnishi

This figure shows the co-authorship network connecting the top 25 collaborators of Masatake Ohnishi. A scholar is included among the top collaborators of Masatake Ohnishi 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 Masatake Ohnishi. Masatake Ohnishi 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.
Maoka, Takashi, et al.. (2005). Structure of β-Glucan Oligomer from Laminarin and Its Effect on Human Monocytes to Inhibit the Proliferation of U937 Cells. Bioscience Biotechnology and Biochemistry. 69(3). 553–558. 77 indexed citations
2.
Ueda, Shigeru, Masayuki Oda, Shigeyuki Imamura, & Masatake Ohnishi. (2004). Kinetic study of the enzymatic cycling reaction conducted with 3α-hydroxysteroid dehydrogenase in the presence of excessive thio-NAD+ and NADH. Analytical Biochemistry. 332(1). 84–89. 17 indexed citations
3.
Ishijima, Sumio, et al.. (2004). Effects of Alkalinization and ATPase Inhibition on Stromal Free Mg2+Concentration in Spinach Chloroplasts. Bioscience Biotechnology and Biochemistry. 68(11). 2411–2414. 1 indexed citations
4.
Kishimoto, Keiko, Sumio Ishijima, & Masatake Ohnishi. (2003). ATP-binding proteins of spinach chloroplast membranes. 3(2). 69–74. 1 indexed citations
5.
Ishijima, Sumio, et al.. (2003). Light-induced increase in free Mg2+ concentration in spinach chloroplasts: Measurement of free Mg2+ by using a fluorescent probe and necessity of stromal alkalinization. Archives of Biochemistry and Biophysics. 412(1). 126–132. 92 indexed citations
6.
Matsumoto, Kenji, Noriko Hiraiwa, Atsushi Yoshiki, Masatake Ohnishi, & Moriaki Kusakabe. (2002). PDGF Receptor-α Deficiency in Glomerular Mesangial Cells of Tenascin-C Knockout Mice. Biochemical and Biophysical Research Communications. 290(4). 1220–1227. 30 indexed citations
7.
Matsumoto, Kenji, Noriko Hiraiwa, Atsushi Yoshiki, Masatake Ohnishi, & Moriaki Kusakabe. (2002). Tenascin-C Expression and Splice Variant in Habu Snake Venom-Induced Glomerulonephritis. Experimental and Molecular Pathology. 72(3). 186–195. 14 indexed citations
8.
Ohnishi, Masatake, et al.. (1997). Subsite structure of the β-glucosidase from Aspergillus niger, evaluated by steady-state kinetics with cello-oligosaccharides as substrates. Carbohydrate Research. 298(1-2). 51–57. 23 indexed citations
9.
10.
Ohnishi, Masatake. (1990). Is There a “Double-Headed Eagle”?. Trends in Glycoscience and Glycotechnology. 2(7). 343–352. 1 indexed citations
11.
12.
Ohnishi, Masatake & Dexter French. (1988). Iodine binding to amylodextrin fractions studied by difference spectrophotometry and potentiometry. Carbohydrate Research. 172(1). 164–169. 2 indexed citations
13.
Ohnishi, Masatake. (1983). . KAGAKU TO SEIBUTSU. 21(8). 502–512. 1 indexed citations
14.
Ohnishi, Masatake & Keitarō Hiromi. (1978). Kinetics studies on the interactin of rhizopus glucoamylase with maltodextrin and maltotriose, utilizing the absorbance change near 300 nm. Carbohydrate Research. 61(1). 335–344. 19 indexed citations
15.
Hiromi, Keitarō, et al.. (1977). Kinetic Studies on the Chemical Modification of Lysozyme by N-Bromosuccinimide and Its Protection by Substrates and Analogs1. The Journal of Biochemistry. 81(6). 1583–1586. 12 indexed citations
16.
Nakatani, Hiroshi, et al.. (1977). A KINETIC METHOD FOR THE DETERMINATION OF ASCORBIC ACID WITH 2,6-DICHLOROPHENOLINDOPHENOL. Chemistry Letters. 6(11). 1333–1336. 6 indexed citations
17.
Ohnishi, Masatake & Keitarō Hiromi. (1976). Studies on the Subsite Structure of Amylases IV. Tryptophan Residues of Glucoamylase1 from Rhizopus niveus Studied by Chemical Modification with N-Bromosuccinimide2. The Journal of Biochemistry. 79(1). 11–16. 17 indexed citations
18.
Hiromi, Keitarō, Masatake Ohnishi, & Takashi Yamashita. (1974). Transient Kinetics of Gloucoamylase1-catalyzed Hydrolysis of Maltodextrin Studied by the Fluorescence Stopped-flow Method2. The Journal of Biochemistry. 76(6). 1365–1367. 11 indexed citations
19.
Ohnishi, Masatake, Hiroyuki Hatano, & Keitarō Hiromi. (1973). Difference-spectrophotometry of the Interaction of Cycloheptaamylose with Saccharifying α-Amylase from Bacillus subtilis*. The Journal of Biochemistry. 74(3). 519–524. 6 indexed citations
20.
Ohnishi, Masatake. (1970). Difference Spectrophotometric Study of Interaction between Maltose and Saccharifying α-Amylase from Bacillus subtilis*. The Journal of Biochemistry. 68(6). 933–936. 5 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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