Sumio Tanase

3.9k total citations
91 papers, 3.2k citations indexed

About

Sumio Tanase is a scholar working on Molecular Biology, Biochemistry and Materials Chemistry. According to data from OpenAlex, Sumio Tanase has authored 91 papers receiving a total of 3.2k indexed citations (citations by other indexed papers that have themselves been cited), including 54 papers in Molecular Biology, 23 papers in Biochemistry and 18 papers in Materials Chemistry. Recurrent topics in Sumio Tanase's work include Amino Acid Enzymes and Metabolism (22 papers), Enzyme Structure and Function (18 papers) and Metabolism and Genetic Disorders (15 papers). Sumio Tanase is often cited by papers focused on Amino Acid Enzymes and Metabolism (22 papers), Enzyme Structure and Function (18 papers) and Metabolism and Genetic Disorders (15 papers). Sumio Tanase collaborates with scholars based in Japan, United States and Poland. Sumio Tanase's co-authors include Yoshimasa Morino, Hiroyuki Kagamiyama, Hiroshi Watanabe, Masaki Otagiri, Takahisa Imamura, Ulrich Kragh‐Hansen, James Travis, Jan Potempa, Keisuke Nakajou and Takaya Ogawa and has published in prestigious journals such as Journal of Biological Chemistry, The Journal of Experimental Medicine and Hepatology.

In The Last Decade

Sumio Tanase

90 papers receiving 3.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Sumio Tanase Japan 35 1.7k 515 510 468 430 91 3.2k
Richard J. Reece United Kingdom 45 2.9k 1.7× 662 1.3× 370 0.7× 175 0.4× 365 0.8× 81 5.5k
Atsushi Nakazawa Japan 42 2.6k 1.5× 1.1k 2.1× 313 0.6× 180 0.4× 311 0.7× 120 4.9k
Graham J. Hughes Switzerland 31 2.2k 1.3× 325 0.6× 327 0.6× 137 0.3× 238 0.6× 60 3.8k
N Brot United States 31 2.2k 1.3× 475 0.9× 136 0.3× 377 0.8× 226 0.5× 61 3.2k
Masatomo Maeda Japan 40 3.9k 2.3× 185 0.4× 527 1.0× 246 0.5× 237 0.6× 143 4.8k
G A Keller United States 29 4.4k 2.6× 237 0.5× 412 0.8× 299 0.6× 150 0.3× 34 5.6k
K.L. Kavanagh United Kingdom 32 2.8k 1.6× 167 0.3× 889 1.7× 282 0.6× 492 1.1× 56 4.7k
Daniel Wellner United States 25 1.3k 0.8× 562 1.1× 239 0.5× 368 0.8× 107 0.2× 59 2.7k
Lukas C. Kühn Switzerland 47 4.4k 2.6× 522 1.0× 457 0.9× 729 1.6× 120 0.3× 90 8.0k
Carmelo B. Bruni Italy 42 3.5k 2.0× 715 1.4× 317 0.6× 111 0.2× 302 0.7× 127 5.4k

Countries citing papers authored by Sumio Tanase

Since Specialization
Citations

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

Fields of papers citing papers by Sumio Tanase

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Sumio Tanase

This figure shows the co-authorship network connecting the top 25 collaborators of Sumio Tanase. A scholar is included among the top collaborators of Sumio Tanase 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 Sumio Tanase. Sumio Tanase 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.
Nishiura, Hiroshi, Sumio Tanase, Kenichi Tsujita, et al.. (2011). Maintenance of ribosomal protein S19 in plasma by complex formation with prothrombin. European Journal Of Haematology. 86(5). 436–441. 8 indexed citations
2.
Chuang, Victor Tuan Giam, Sumio Tanase, Keiichi Kawai, et al.. (2006). Recombinant Human Serum Albumin Dimer has High Blood Circulation Activity and Low Vascular Permeability in Comparison with Native Human Serum Albumin. Pharmaceutical Research. 23(5). 882–891. 43 indexed citations
3.
Imamura, Takahisa, et al.. (2005). Induction of vascular leakage through release of bradykinin and a novel kinin by cysteine proteinases from Staphylococcus aureus . The Journal of Experimental Medicine. 201(10). 1669–1676. 89 indexed citations
4.
Shibuya, Yoko, et al.. (2004). Primary structures of guinea pig high- and low-molecular-weight kininogens. International Immunopharmacology. 4(10-11). 1391–1400. 2 indexed citations
5.
Nomiyama, Hisayuki, Sumio Tanase, Retsu Miura, et al.. (2003). Comparative DNA Sequence Analysis of Mouse and Human CC Chemokine Gene Clusters. Journal of Interferon & Cytokine Research. 23(1). 37–45. 18 indexed citations
6.
Imamura, Takahisa, Sumio Tanase, Izumi Hayashi, et al.. (2002). Release of a new vascular permeability enhancing peptide from kininogens by human neutrophil elastase. Biochemical and Biophysical Research Communications. 294(2). 423–428. 24 indexed citations
7.
Imamura, Takahisa, Sumio Tanase, Takayoshi Hamamoto, Jan Potempa, & James Travis. (2001). Activation of blood coagulation factor IX by gingipains R, arginine-specific cysteine proteinases from Porphyromonas gingivalis. Biochemical Journal. 353(2). 325–325. 25 indexed citations
8.
Watanabe, Hiroshi, Ulrich Kragh‐Hansen, Sumio Tanase, et al.. (2001). Conformational stability and warfarin-binding properties of human serum albumin studied by recombinant mutants. Biochemical Journal. 357(1). 269–269. 54 indexed citations
9.
Nishimura, Tomohiro, Kei Horino, Hiroshi Nishiura, et al.. (2001). Apoptotic Cells of an Epithelial Cell Line, AsPC-1, Release Monocyte Chemotactic S19 Ribosomal Protein Dimer. The Journal of Biochemistry. 129(3). 445–454. 50 indexed citations
10.
Shibuya, Yoko, et al.. (1999). Primary structure of guinea pig plasma prekallikrein. Immunopharmacology. 45(1-3). 127–134. 4 indexed citations
11.
Fujii, T., Kiminori Nakamura, Kazunori Shibuya, et al.. (1997). Structural characterization of the gene and corresponding cDNA for the cytochrome P450rm from Rhodotorula minuta which catalyzes formation of isobutene and 4-hydroxylation of benzoate. Molecular and General Genetics MGG. 256(2). 115–120. 24 indexed citations
12.
Imamura, Takahisa, Jan Potempa, Sumio Tanase, & James Travis. (1997). Activation of Blood Coagulation Factor X by Arginine-specific Cysteine Proteinases (Gingipain-Rs) from Porphyromonas gingivalis. Journal of Biological Chemistry. 272(25). 16062–16067. 92 indexed citations
13.
Sohocki, Melanie M., Lori S. Sullivan, Wilbur R. Harrison, et al.. (1997). Human Glutamate Pyruvate Transaminase (GPT): Localization to 8q24.3, cDNA and Genomic Sequences, and Polymorphic Sites. Genomics. 40(2). 247–252. 44 indexed citations
14.
15.
Fukuda, H., Takaya Ogawa, & Sumio Tanase. (1993). Ethylene Production by Micro-organisms. Advances in microbial physiology. 35. 275–306. 87 indexed citations
16.
Murakami, T., T Atsumi, Shuichiro Maeda, et al.. (1992). A novel transthyretin mutation at position 30 (Leu for Val) associated with familial amyloidotic polyneuropathy. Biochemical and Biophysical Research Communications. 187(1). 397–403. 17 indexed citations
17.
18.
Molla, Akhteruzzaman, Sumio Tanase, Yeong-Man Hong, & Hiroshi Maeda. (1988). Interdomain cleavage of plasma fibronectin by zinc-metalloproteinase from Serratia marcescens. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 955(1). 77–85. 20 indexed citations
19.
20.
Morino, Yoshimasa & Sumio Tanase. (1978). Chemical structure of the active site of pig heart mitochondrial aspartate aminotransferase labeled with beta-chloro-l-alanine.. Journal of Biological Chemistry. 253(1). 252–256. 24 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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