Junzo Hirose

992 total citations
63 papers, 844 citations indexed

About

Junzo Hirose is a scholar working on Molecular Biology, Oncology and Organic Chemistry. According to data from OpenAlex, Junzo Hirose has authored 63 papers receiving a total of 844 indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 29 papers in Oncology and 20 papers in Organic Chemistry. Recurrent topics in Junzo Hirose's work include Metal complexes synthesis and properties (17 papers), Enzyme function and inhibition (15 papers) and Peptidase Inhibition and Analysis (13 papers). Junzo Hirose is often cited by papers focused on Metal complexes synthesis and properties (17 papers), Enzyme function and inhibition (15 papers) and Peptidase Inhibition and Analysis (13 papers). Junzo Hirose collaborates with scholars based in Japan, Italy and South Korea. Junzo Hirose's co-authors include Yoshinori Kidani, Kayoko M. Fukasawa, Hiroyuki Iwamoto, Katsuhiko Fukasawa, Toshiyuki Hata, Keitarō Hiromi, Minoru Harada, Hisashi Koike, Makoto Kanai and Masayoshi Fukasawa and has published in prestigious journals such as Biochemistry, Biochemical Journal and Biochemical and Biophysical Research Communications.

In The Last Decade

Junzo Hirose

61 papers receiving 818 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Junzo Hirose Japan 18 403 307 164 145 107 63 844
Marcin Dyba United States 17 755 1.9× 378 1.2× 207 1.3× 45 0.3× 169 1.6× 41 1.4k
Adelaide Faljoni‐Alário Brazil 21 582 1.4× 109 0.4× 121 0.7× 56 0.4× 56 0.5× 38 1.1k
Anna Maria Santoro Italy 19 437 1.1× 177 0.6× 142 0.9× 37 0.3× 88 0.8× 45 1.1k
Youichi Fujii Japan 17 1.0k 2.5× 229 0.7× 124 0.8× 37 0.3× 40 0.4× 99 1.7k
F.E. Jacobsen United States 13 391 1.0× 309 1.0× 171 1.0× 27 0.2× 308 2.9× 16 1.2k
Sa-Ouk Kang South Korea 11 273 0.7× 105 0.3× 59 0.4× 48 0.3× 43 0.4× 19 711
Irene Witte Germany 19 298 0.7× 96 0.3× 95 0.6× 30 0.2× 43 0.4× 44 927
Zu D. Liu United Kingdom 14 231 0.6× 281 0.9× 274 1.7× 15 0.1× 265 2.5× 24 1.3k
Isabelle Artaud France 25 544 1.3× 314 1.0× 470 2.9× 27 0.2× 32 0.3× 75 1.6k
Yibin Wei United States 14 228 0.6× 99 0.3× 139 0.8× 25 0.2× 63 0.6× 27 876

Countries citing papers authored by Junzo Hirose

Since Specialization
Citations

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

Fields of papers citing papers by Junzo Hirose

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Junzo Hirose

This figure shows the co-authorship network connecting the top 25 collaborators of Junzo Hirose. A scholar is included among the top collaborators of Junzo Hirose 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 Junzo Hirose. Junzo Hirose 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.
Hata, Toshiyuki, Yu Shibata, Hiroshi Iwamoto, et al.. (2015). Flexibility of the Coordination Geometry at the N-Site of Cu(II)<sub>2</sub> Human Serum-Transferrin Induced by the Different Orientations of Arg124. Biological and Pharmaceutical Bulletin. 38(3). 358–364. 1 indexed citations
2.
Anraku, Makoto, Tominari Choshi, Hisao Tomida, et al.. (2014). Antioxidant effects of the highly-substituted carbazole alkaloids and their related carbazoles. Bioorganic & Medicinal Chemistry Letters. 24(15). 3530–3533. 46 indexed citations
3.
Hirose, Junzo, et al.. (2012). Flexibility of the coordination geometry around the cupric ions in Cu(II)-rat dipeptidyl peptidase III is important for the expression of enzyme activity. Archives of Biochemistry and Biophysics. 525(1). 71–81. 7 indexed citations
4.
Fukasawa, Kayoko M., et al.. (2010). In rat dipeptidyl peptidase III, His568 is essential for catalysis, and Glu507 or Glu512 stabilizes the coordination bond between His455 or His450 and zinc ion. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804(10). 2063–2069. 8 indexed citations
5.
Ikeda, Hiroaki, Hidetoshi Tsukamoto, Kenji Kihira, et al.. (2010). Timolol Activates the Enzyme Activities of Human Carbonic Anhydrase I and II. Biological and Pharmaceutical Bulletin. 33(2). 301–306. 14 indexed citations
6.
Hirose, Junzo, et al.. (2006). Characterization of the Metal-Binding Site in Aminopeptidase B. Biological and Pharmaceutical Bulletin. 29(12). 2378–2382. 16 indexed citations
7.
Hirose, Junzo, et al.. (2004). The metal-binding motif of dipeptidyl peptidase III directly influences the enzyme activity in the copper derivative of dipeptidyl peptidase III. Archives of Biochemistry and Biophysics. 431(1). 1–8. 9 indexed citations
8.
Hirose, Junzo, et al.. (2000). Reaction Mechanism of Electron Transfer from FeII(CN)4−6 or WIV(CN)4−8 to the Cupric Ions in Human Copper, Zinc Superoxide Dismutase. Archives of Biochemistry and Biophysics. 383(2). 246–255.
9.
Messori, Luigi, Giovanni Dal Poggetto, Roberto Monnanni, & Junzo Hirose. (1997). The pH dependent properties of metallotransferrins: a comparative study. BioMetals. 10(4). 303–313. 14 indexed citations
10.
Hirose, Junzo, et al.. (1996). Copper binding selectivity of N- and C-sites in serum (human)- and ovo-transferrin. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1296(1). 103–111. 29 indexed citations
11.
Hirose, Junzo, et al.. (1996). Characterization of Monoclonal Antibodies against (1R,2R)-Cyclohexanediamine Platinum(II)-DNA Adduct.. Biological and Pharmaceutical Bulletin. 19(9). 1220–1222. 1 indexed citations
12.
Iwamoto, Hiroyuki, Masahiro Ohno, Masayuki Ohmori, et al.. (1994). Comparison of the Binding of β2-Cyclodextrin and α- and γ-Cyclodextrins with Pullulanase from Klebsiella pneumoniae as Studied by Equilibrium and Kinetic Fluorometry1. The Journal of Biochemistry. 116(6). 1264–1268. 12 indexed citations
13.
Hirose, Junzo, Takeshi Sakurai, Hideomi Watanabe, et al.. (1994). Characterization of Ascorbate Oxidase from Acremonium sp. HI-25. The Journal of Biochemistry. 115(5). 811–813. 18 indexed citations
14.
Yamashita, Tomoko, et al.. (1993). Cytotoxicity of Platinum(IV) and Platinum(II) Complexes Containing lR,2R-Cyclohexanediamine as a Ligand.. Biological and Pharmaceutical Bulletin. 16(10). 1014–1018. 7 indexed citations
15.
Iwamoto, Hiroyuki, Masayuki Ohmori, Masahiro Ohno, et al.. (1993). Interaction between Pullulanase from Klebsiella pneumoniae and Cyclodextrins1. The Journal of Biochemistry. 113(1). 93–96. 24 indexed citations
16.
Hirose, Junzo, Hiroshi Kano, Yoshinori Kidani, Hiroyuki Iwamoto, & Hiromi Kajiya‐Kanegae. (1992). Zinc Deficient Bovine Erythrocyte Superoxide Dismutase Has Low Specific Activity.. Chemical and Pharmaceutical Bulletin. 40(2). 506–508. 2 indexed citations
17.
Sisido, Masahiko, et al.. (1991). Photoreversible antigen—antibody reactions. FEBS Letters. 286(1-2). 6–8. 24 indexed citations
18.
Yamada, Hiroshi, Taiji Kato, Junzo Hirose, et al.. (1990). Antibodies against (1R,2R)-cyclohexanediamineplatinum(II)-DNA adduct recognize the conformational differences of isomeric analogues of cyclohexanediamine. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1049(3). 298–302. 1 indexed citations
19.
Hirose, Junzo, et al.. (1987). Excess zinc ions are a competitive inhibitor for carboxypeptidase A. Biochemistry. 26(20). 6561–6565. 20 indexed citations
20.
Hirose, Junzo & Yoshinori Kidani. (1980). Coordination chemical studies on metalloenzymes. VIII. Reduction of Co(III)-bovine carbonic anhydrase with L-ascorbic acid.. Chemical and Pharmaceutical Bulletin. 28(11). 3189–3195. 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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