Shoji Watabe

1.2k total citations
42 papers, 1.0k citations indexed

About

Shoji Watabe is a scholar working on Molecular Biology, Insect Science and Biomaterials. According to data from OpenAlex, Shoji Watabe has authored 42 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Molecular Biology, 9 papers in Insect Science and 7 papers in Biomaterials. Recurrent topics in Shoji Watabe's work include Insect Resistance and Genetics (13 papers), Mitochondrial Function and Pathology (8 papers) and Silk-based biomaterials and applications (7 papers). Shoji Watabe is often cited by papers focused on Insect Resistance and Genetics (13 papers), Mitochondrial Function and Pathology (8 papers) and Silk-based biomaterials and applications (7 papers). Shoji Watabe collaborates with scholars based in Japan, China and Armenia. Shoji Watabe's co-authors include Susumu Takahashi, Yoshimi Yamamoto, Nagasumi Yago, Tomoko Hiroi, Tokuji Kimura, Hiroyuki Hasegawa, Takashi Kageyama, T. NAKAZAWA, Hiroyuki Kohno and Shiro Tomino and has published in prestigious journals such as Journal of Biological Chemistry, Biochemical and Biophysical Research Communications and FEBS Letters.

In The Last Decade

Shoji Watabe

41 papers receiving 977 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Shoji Watabe Japan 19 685 126 117 111 89 42 1.0k
Yoshimi Yamamoto Japan 16 474 0.7× 111 0.9× 169 1.4× 123 1.1× 41 0.5× 40 848
Carmen G. Vallejo Spain 21 893 1.3× 94 0.7× 80 0.7× 69 0.6× 80 0.9× 43 1.4k
Ursula Müller Germany 25 733 1.1× 123 1.0× 156 1.3× 83 0.7× 139 1.6× 52 1.5k
Claire-Lise Rosenfield United States 15 572 0.8× 211 1.7× 72 0.6× 206 1.9× 50 0.6× 27 1.1k
Ivor D. Bowen United Kingdom 13 490 0.7× 118 0.9× 123 1.1× 297 2.7× 51 0.6× 21 1.1k
Pamela B. Moore United States 15 628 0.9× 118 0.9× 54 0.5× 43 0.4× 114 1.3× 31 921
Shiro Matsuura Japan 19 641 0.9× 183 1.5× 246 2.1× 226 2.0× 152 1.7× 56 1.5k
Ralph SCHALOSKE Germany 11 592 0.9× 83 0.7× 86 0.7× 39 0.4× 235 2.6× 14 967
Mathieu Miron Canada 9 1.1k 1.6× 182 1.4× 211 1.8× 45 0.4× 144 1.6× 9 1.4k
Valery Filippov United States 19 855 1.2× 154 1.2× 186 1.6× 48 0.4× 76 0.9× 34 1.4k

Countries citing papers authored by Shoji Watabe

Since Specialization
Citations

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

Fields of papers citing papers by Shoji Watabe

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Shoji Watabe

This figure shows the co-authorship network connecting the top 25 collaborators of Shoji Watabe. A scholar is included among the top collaborators of Shoji Watabe 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 Shoji Watabe. Shoji Watabe 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.
Watabe, Shoji, et al.. (2007). Drosophila CTLA-2-like Protein (D/CTLA-2) Inhibits Cysteine Proteinase 1 (CP1), a Cathepsin L-like Enzyme. ZOOLOGICAL SCIENCE. 24(1). 21–30. 13 indexed citations
2.
Yamamoto, Misa, Tomoko Hiroi, Hiroyuki Kohno, et al.. (2005). Nucleotide sequence for cDNA of bovine mitochondrial ATP-dependent protease and determination of N-terminus of the mature enzyme from the adrenal cortex. DNA sequence. 16(6). 474–478. 1 indexed citations
3.
Fujii, Akiko, Toshika Okumiya, Shoji Watabe, et al.. (2004). The study of cytopathological aspects induced by human cytomegalovirus infection. Diagnostic Cytopathology. 31(5). 289–293. 4 indexed citations
4.
Tamotsu, Satoshi, et al.. (2003). In vivo activation of pro-form Bombyx cysteine protease (BCP) in silkmoth eggs: localization of yolk proteins and BCP, and acidification of yolk granules. Journal of Insect Physiology. 49(2). 131–140. 37 indexed citations
5.
Yamamoto, Yoshimi, Shoji Watabe, Takashi Kageyama, & Susumu Takahashi. (1999). Proregion of Bombyx mori cysteine proteinase functions as an intramolecular chaperone to promote proper folding of the mature enzyme. Archives of Insect Biochemistry and Physiology. 42(3). 167–178. 1 indexed citations
6.
Yamamoto, Yoshimi, Shoji Watabe, Takashi Kageyama, & Susumu Takahashi. (1999). A novel inhibitor protein for Bombyx cysteine proteinase is homologous to propeptide regions of cysteine proteinases. FEBS Letters. 448(2-3). 257–260. 24 indexed citations
7.
Takahashi, Susumu, Yoshimi Yamamoto, Shoji Watabe, & Takashi Kageyama. (1997). Autolytic activation mechanism of Bombyx acid cysteine protease (BCP). IUBMB Life. 42(3). 591–600. 10 indexed citations
8.
Watabe, Shoji, et al.. (1997). SP‐22 is a Thioredoxin‐Dependent Peroxide Reductase in Mitochondria. European Journal of Biochemistry. 249(1). 52–60. 134 indexed citations
9.
Hiroi, Tomoko, Shoji Watabe, Koichi Takimoto, et al.. (1996). The cDNA sequence encoding bovine SP-22, a new defence system against reactive oxygen species in mitochondria. DNA sequence. 6(4). 239–242. 10 indexed citations
10.
11.
Watabe, Shoji, et al.. (1996). Activation of cathepsin D by polyanionic compounds. IUBMB Life. 39(4). 703–710. 4 indexed citations
12.
Hasegawa, Hiroyuki, et al.. (1995). Rapid Turnover of Tryptophan Hydoxylase : Demonstration of Proteolytic Process in Cell-free System. Pteridines. 6(3). 138–140. 2 indexed citations
13.
Suzuki, Takashi, Masahiro Sato, Ikuo Shoji, et al.. (1995). In vivo and in vitro trans-cleavage activity of hepatitis C virus serine proteinase expressed by recombinant baculoviruses. Journal of General Virology. 76(12). 3021–3029. 29 indexed citations
14.
Watabe, Shoji, Hiroyuki Hasegawa, Koichi Takimoto, Yoshio Yamamoto, & Susumu Takahashi. (1995). Possible Function of SP-22, a Substrate of Mitochondrial ATP-Dependent Protease, as a Radical Scavenger. Biochemical and Biophysical Research Communications. 213(3). 1010–1016. 58 indexed citations
15.
Watabe, Shoji, et al.. (1994). Purification and Characterization of a Substrate Protein for Mitochondrial ATP-Dependent Protease in Bovine Adrenal Cortex. The Journal of Biochemistry. 115(4). 648–654. 96 indexed citations
16.
Watabe, Shoji, Takayuki Hara, Hiroyuki Kohno, et al.. (1993). In Vitro Degradation of Mitochondrial Proteins by ATP-Dependent Protease in Bovine Adrenal Cortex. The Journal of Biochemistry. 113(6). 672–676. 18 indexed citations
17.
Watabe, Shoji & Tokuji Kimura. (1985). ATP-dependent protease in bovine adrenal cortex. Tissue specificity, subcellular localization, and partial characterization.. Journal of Biological Chemistry. 260(9). 5511–5517. 52 indexed citations
18.
Taguchi, Shigeru, et al.. (1981). Isopycnic density values for lysosomes and mitochondria in rat adrenal cortex.. Endocrinologia Japonica. 28(2). 245–248. 2 indexed citations
19.
Watabe, Shoji, et al.. (1979). Polyphosphate anions increase the activity of bovine spleen cathepsin D. Biochemical and Biophysical Research Communications. 89(4). 1161–1167. 23 indexed citations
20.
Watabe, Shoji & Miki Akino. (1977). Biosynthesis of Drosopterins in the Swordtail Fish,Xiphophorus helleri. 日本動物学彙報. 50(1). 1–11. 1 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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