Yoshimi Yamamoto

1.0k total citations
40 papers, 848 citations indexed

About

Yoshimi Yamamoto is a scholar working on Molecular Biology, Insect Science and Biomaterials. According to data from OpenAlex, Yoshimi Yamamoto has authored 40 papers receiving a total of 848 indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 10 papers in Insect Science and 7 papers in Biomaterials. Recurrent topics in Yoshimi Yamamoto's work include Insect Resistance and Genetics (13 papers), Silk-based biomaterials and applications (7 papers) and Insect Utilization and Effects (7 papers). Yoshimi Yamamoto is often cited by papers focused on Insect Resistance and Genetics (13 papers), Silk-based biomaterials and applications (7 papers) and Insect Utilization and Effects (7 papers). Yoshimi Yamamoto collaborates with scholars based in Japan, Tanzania and Germany. Yoshimi Yamamoto's co-authors include Susumu Takahashi, Shoji Watabe, Takashi Kageyama, Tomoko Hiroi, Nagasumi Yago, Xiao‐Fan Zhao, Susumu Izumi, Ken’ichi Yano, Hiroyuki Hasegawa and Orie Nakamura and has published in prestigious journals such as The Journal of Immunology, Brain Research and FEBS Letters.

In The Last Decade

Yoshimi Yamamoto

40 papers receiving 820 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Yoshimi Yamamoto Japan 16 474 169 123 111 74 40 848
Nina Lukinova United States 11 639 1.3× 196 1.2× 147 1.2× 138 1.2× 65 0.9× 13 1.3k
Ursula Müller Germany 25 733 1.5× 156 0.9× 83 0.7× 123 1.1× 9 0.1× 52 1.5k
James C. Robbins United States 13 302 0.6× 147 0.9× 126 1.0× 36 0.3× 20 0.3× 29 726
Pamela B. Moore United States 15 628 1.3× 54 0.3× 43 0.3× 118 1.1× 15 0.2× 31 921
Stephanie Chu Singapore 12 689 1.5× 101 0.6× 31 0.3× 18 0.2× 69 0.9× 26 1.2k
Shoji Watabe Japan 19 685 1.4× 117 0.7× 111 0.9× 126 1.1× 4 0.1× 42 1.0k
Shanta M. Messerli United States 16 537 1.1× 49 0.3× 106 0.9× 59 0.5× 5 0.1× 31 1.1k
Matthew A. Waller Australia 6 777 1.6× 61 0.4× 59 0.5× 70 0.6× 6 0.1× 6 1.1k
Valery Filippov United States 19 855 1.8× 186 1.1× 48 0.4× 154 1.4× 6 0.1× 34 1.4k
Norma Marchesini United States 16 1.0k 2.2× 135 0.8× 18 0.1× 33 0.3× 11 0.1× 18 1.5k

Countries citing papers authored by Yoshimi Yamamoto

Since Specialization
Citations

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

Fields of papers citing papers by Yoshimi Yamamoto

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Yoshimi Yamamoto

This figure shows the co-authorship network connecting the top 25 collaborators of Yoshimi Yamamoto. A scholar is included among the top collaborators of Yoshimi Yamamoto 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 Yoshimi Yamamoto. Yoshimi Yamamoto 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.
Mbassa, G.K., et al.. (2016). Cathepsin L coexists with Cytotoxic T-lymphocyte Antigen-2 alpha in distinct regions of the mouse brain. Acta Histochemica. 118(7). 704–710. 4 indexed citations
2.
Yamamoto, Misa, et al.. (2014). Identification and characterization of the interactive proteins with cytotoxic T-lymphocyte antigen-2α. Bioscience Biotechnology and Biochemistry. 79(4). 587–597. 2 indexed citations
3.
Sugita, Sunao, Junko Hori, Orie Nakamura, et al.. (2009). Acquisition of T Regulatory Function in Cathepsin L-Inhibited T Cells by Eye-Derived CTLA-2α during Inflammatory Conditions. The Journal of Immunology. 183(8). 5013–5022. 46 indexed citations
4.
Usui, Masaru, et al.. (2009). Identification of essential residues of CTLA-2α for inhibitory potency. The Journal of Biochemistry. 147(3). 393–404. 5 indexed citations
5.
Usui, Masaru, et al.. (2009). Intracellular concentrations of enrofloxacin in quinolone-resistant Salmonella enterica subspecies enterica serovar Choleraesuis. International Journal of Antimicrobial Agents. 34(6). 592–595. 10 indexed citations
6.
Yamamoto, Misa, et al.. (2009). Tranilast, an Anti-Allergic Drug, Down-Regulates the Growth of Cultured Neurofibroma Cells Derived from Neurofibromatosis Type 1. The Tohoku Journal of Experimental Medicine. 217(3). 193–201. 22 indexed citations
7.
Sugita, Sunao, Junko Hori, Orie Nakamura, et al.. (2008). Retinal Pigment Epithelium-Derived CTLA-2α Induces TGFβ-Producing T Regulatory Cells,. The Journal of Immunology. 181(11). 7525–7536. 98 indexed citations
8.
Nakamura, Orie, et al.. (2008). Dendritic and axonal localization of cytotoxic T-lymphocyte antigen-2 alpha protein in mouse brain. Brain Research. 1204. 40–52. 8 indexed citations
9.
Usui, Masaru, et al.. (2007). Gene expression and immunohistochemical localization of megalin in the anterior pituitary gland of helmeted guinea fowl (Numida meleagris). Journal of Molecular Histology. 38(1). 65–77. 4 indexed citations
10.
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
11.
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
12.
Miyake, Masashi, Takahiro Yaguchi, Toshiyuki Ogawa, et al.. (2004). Isolation and Expression of Five-Amino-Acid-Deleted Variant of Feline Hepatocyte Growth Factor (HGF) cDNA. Journal of Veterinary Medical Science. 66(1). 9–14. 1 indexed citations
13.
Miyake, Masashi, et al.. (2003). Canine hepatocyte growth factor: molecular cloning and characterization of the recombinant protein. Veterinary Immunology and Immunopathology. 95(3-4). 135–143. 6 indexed citations
14.
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
15.
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
16.
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
17.
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
18.
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
19.
Katoh, Setsuko, Terumi Sueoka, Yoshimi Yamamoto, & Susumu Takahashi. (1994). Phosphorylation by Ca2+/calmodulin‐dependent protein kinase II and protein kinase C of sepiapterin reductase, the terminal enzyme in the biosynthetic pathway of tetrahydrobiopterin. FEBS Letters. 341(2-3). 227–232. 17 indexed citations
20.

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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