Jun Ishibashi

3.5k total citations
67 papers, 2.7k citations indexed

About

Jun Ishibashi is a scholar working on Molecular Biology, Microbiology and Immunology. According to data from OpenAlex, Jun Ishibashi has authored 67 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 25 papers in Microbiology and 25 papers in Immunology. Recurrent topics in Jun Ishibashi's work include Antimicrobial Peptides and Activities (25 papers), Invertebrate Immune Response Mechanisms (22 papers) and Insect Utilization and Effects (13 papers). Jun Ishibashi is often cited by papers focused on Antimicrobial Peptides and Activities (25 papers), Invertebrate Immune Response Mechanisms (22 papers) and Insect Utilization and Effects (13 papers). Jun Ishibashi collaborates with scholars based in Japan, India and Nepal. Jun Ishibashi's co-authors include Minoru Yamakawa, Hiromitsu Tanaka, Ai Asaoka, Seiichi Furukawa, Aki Sagisaka, Hiroshi Nakazawa, Takashi Iwasaki, Kangayam M. Ponnuvel, Toshitaka Gamo and Yoshiro Nakajima and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Jun Ishibashi

66 papers receiving 2.7k citations

Peers

Jun Ishibashi
Zhi Zhou China
Ulrich Stingl Saudi Arabia
A.T. Marshall Australia
Jun Ishibashi
Citations per year, relative to Jun Ishibashi Jun Ishibashi (= 1×) peers Mengqiang Wang

Countries citing papers authored by Jun Ishibashi

Since Specialization
Citations

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

Fields of papers citing papers by Jun Ishibashi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jun Ishibashi

This figure shows the co-authorship network connecting the top 25 collaborators of Jun Ishibashi. A scholar is included among the top collaborators of Jun Ishibashi 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 Jun Ishibashi. Jun Ishibashi 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.
Ishibashi, Jun. (2019). 昆虫由来抗菌ペプチドの応用に関する研究. KAGAKU TO SEIBUTSU. 57(6). 373–379. 1 indexed citations
2.
Furukawa, Seiichi, Hiromitsu Tanaka, Aki Sagisaka, Jun Ishibashi, & Minoru Yamakawa. (2012). Both κB and C/EBP binding sites are indispensable for full expression of a nitric oxide synthase gene in the silkworm, Bombyx mori. Journal of insect biotechnology and sericology. 81(1). 13–20. 2 indexed citations
3.
Teramoto, Hidetoshi, Katsura Kojima, Hideyuki Kajiwara, & Jun Ishibashi. (2011). Expansion of the Amino Acid Repertoire in Protein Biosynthesis in Silkworm Cells. ChemBioChem. 13(1). 61–65. 7 indexed citations
4.
Grause, Guido, et al.. (2011). TG–MS investigation of brominated products from the degradation of brominated flame retardants in high-impact polystyrene. Chemosphere. 85(3). 368–373. 47 indexed citations
5.
Nakashima, Nobuhiko & Jun Ishibashi. (2010). Identification of the 3C-protease-mediated 2A/2B and 2B/2C cleavage sites in the nonstructural polyprotein precursor of a dicistrovirus lacking the NPGP motif. Archives of Virology. 155(9). 1477–1482. 4 indexed citations
6.
Tanaka, Hiromitsu, Noriko Suzuki, Yoshiro Nakajima, et al.. (2010). Expression profiling of novel bacteria‐induced genes from the silkworm, Bombyx mori. Archives of Insect Biochemistry and Physiology. 73(3). 148–162. 11 indexed citations
7.
Iwasaki, Takashi, et al.. (2009). Multiple Functions of Short Synthetic Enantiomeric Peptides Based on Beetle Defensins. Bioscience Biotechnology and Biochemistry. 73(3). 683–687. 5 indexed citations
8.
Furukawa, Seiichi, Hiromitsu Tanaka, Jun Ishibashi, Shigeo Imanishi, & Minoru Yamakawa. (2009). Functional Characterization of a Cactus Homolog from the SilkwormBombyx mori. Bioscience Biotechnology and Biochemistry. 73(12). 2665–2670. 14 indexed citations
9.
Iwasaki, Takashi, Jun Ishibashi, Hiromitsu Tanaka, et al.. (2008). Selective cancer cell cytotoxicity of enantiomeric 9-mer peptides derived from beetle defensins depends on negatively charged phosphatidylserine on the cell surface. Peptides. 30(4). 660–668. 108 indexed citations
10.
Furukawa, Seiichi, Aki Sagisaka, Hiromitsu Tanaka, et al.. (2007). Molecular Cloning and Characterization of Histone H2A.Z Gene of the Silkworm, Bombyx mori. Journal of insect biotechnology and sericology. 76(3). 121–127. 2 indexed citations
11.
Saido‐Sakanaka, Hisako, Eiichi Momotani, Hiromi Yamada, et al.. (2005). Effect of a Synthetic Peptide Designed on the Basis of the Active Site of Insect Defensins on the Proliferation of Methicillin-resistant Staphylococcus aureus under the Conditions for External Application. Journal of insect biotechnology and sericology. 74(1). 15–20. 3 indexed citations
12.
Kobayashi, Satoe, Ai Asaoka, Mitsuhiro Miyazawa, Jun Ishibashi, & Minoru Yamakawa. (2005). Interactions of an Antimicrobial Peptide Moricin with Lipid Bilayers. 2004. 251–254. 1 indexed citations
13.
Saido‐Sakanaka, Hisako, et al.. (2004). In vitro and in vivo activity of antimicrobial peptides synthesized based on the insect defensin. Peptides. 25(1). 19–27. 44 indexed citations
14.
Nakazawa, Hiroshi, Fumiko Yukuhiro, Seiichi Furukawa, et al.. (2003). Spontaneous Synthesis of an Antibacterial Peptide Linked to Ecdysis in Lepidopteran Insects. Journal of insect biotechnology and sericology. 72(3). 133–137. 2 indexed citations
15.
Ishibashi, Jun, et al.. (2003). Scarabaecin, a novel cysteine-containing antifungal peptide from the rhinoceros beetle, Oryctes rhinoceros. Biochemical and Biophysical Research Communications. 307(2). 261–266. 27 indexed citations
16.
Nakajima, Yoshiro, Jun Ishibashi, Fumiko Yukuhiro, et al.. (2003). Antibacterial activity and mechanism of action of tick defensin against Gram-positive bacteria. Biochimica et Biophysica Acta (BBA) - General Subjects. 1624(1-3). 125–130. 86 indexed citations
17.
18.
Hemmi, Hikaru, Jun Ishibashi, Seiichi Hara, & Minoru Yamakawa. (2002). Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori. FEBS Letters. 518(1-3). 33–38. 44 indexed citations
19.
Mizoguchi, Akira, et al.. (2001). Developmental profile of the changes in the prothoracicotropic hormone titer in hemolymph of the silkworm Bombyx mori: correlation with ecdysteroid secretion. Insect Biochemistry and Molecular Biology. 31(4-5). 349–358. 94 indexed citations
20.
Noguti, Tosiyuki, Takashi Adachi‐Yamada, Atsushi Kawakami, et al.. (1995). Insect prothoracicotropic hormone: a new member of the vertebrate growth factor superfamily. FEBS Letters. 376(3). 251–256. 49 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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