Takashi Nirasawa

1.6k total citations
38 papers, 1.3k citations indexed

About

Takashi Nirasawa is a scholar working on Molecular Biology, Spectroscopy and Physiology. According to data from OpenAlex, Takashi Nirasawa has authored 38 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 11 papers in Spectroscopy and 6 papers in Physiology. Recurrent topics in Takashi Nirasawa's work include Metabolomics and Mass Spectrometry Studies (9 papers), Mass Spectrometry Techniques and Applications (6 papers) and Advanced Proteomics Techniques and Applications (6 papers). Takashi Nirasawa is often cited by papers focused on Metabolomics and Mass Spectrometry Studies (9 papers), Mass Spectrometry Techniques and Applications (6 papers) and Advanced Proteomics Techniques and Applications (6 papers). Takashi Nirasawa collaborates with scholars based in Japan, United States and Germany. Takashi Nirasawa's co-authors include Kazuyuki Tohji, Balachandran Jeyadevan, Kōzō Shinoda, Toshiji Kudo, A. Kasuya, Rodion V. Belosludov, V. Sundararajan, Vijay Kumar, Osamu Terasaki and Igor Dmitruk and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Materials.

In The Last Decade

Takashi Nirasawa

35 papers receiving 1.2k citations

Peers

Takashi Nirasawa
Takashi Nirasawa
Citations per year, relative to Takashi Nirasawa Takashi Nirasawa (= 1×) peers Seiichi Tanaka

Countries citing papers authored by Takashi Nirasawa

Since Specialization
Citations

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

Fields of papers citing papers by Takashi Nirasawa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Takashi Nirasawa

This figure shows the co-authorship network connecting the top 25 collaborators of Takashi Nirasawa. A scholar is included among the top collaborators of Takashi Nirasawa 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 Takashi Nirasawa. Takashi Nirasawa 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.
Ikegawa, Masaya, Takashi Nirasawa, Yuichi Tokuda, et al.. (2025). Comprehensive identification of dysregulated extracellular matrix molecules in the corneal endothelium of patients with Fuchs endothelial corneal dystrophy. Scientific Reports. 15(1). 14654–14654. 1 indexed citations
2.
Nirasawa, Takashi, et al.. (2024). Integrated Spatial Multi-Omics Study of Postmortem Brains of Alzheimer’s Disease. ACTA HISTOCHEMICA ET CYTOCHEMICA. 57(3). 119–130. 4 indexed citations
3.
Sugiyama, Eiji, Kenji Yamashita, Yoshiteru Iinuma, et al.. (2023). Charged chiral derivatization for enantioselective imaging of d-,l -2-hydroxyglutaric acid using ion mobility spectrometry/mass spectrometry. Chemical Communications. 59(73). 10916–10919. 3 indexed citations
4.
Ikegawa, Masaya, Nobuto Kakuda, Tomohiro Miyasaka, et al.. (2023). Mass Spectrometry Imaging in Alzheimer's Disease. Brain Connectivity. 13(6). 319–333. 16 indexed citations
6.
Okumura, Naoki, Masaya Ikegawa, Takashi Nirasawa, et al.. (2023). Shotgun proteomics identification of proteins expressed in the Descemet’s membrane of patients with Fuchs endothelial corneal dystrophy. Scientific Reports. 13(1). 10401–10401. 9 indexed citations
7.
Park, Hong-Sun, Tomoyuki Yamanaka, Atsushi Fujita, et al.. (2022). Hornerin deposits in neuronal intranuclear inclusion disease: direct identification of proteins with compositionally biased regions in inclusions. Acta Neuropathologica Communications. 10(1). 28–28. 7 indexed citations
8.
Zhao, Chao, Ting Yong, Yinbin Zhang, et al.. (2021). Breast cancer proliferation and deterioration-associated metabolic heterogeneity changes induced by exposure of bisphenol S, a widespread replacement of bisphenol A. Journal of Hazardous Materials. 414. 125391–125391. 37 indexed citations
9.
Ikegawa, Masaya, Takashi Nirasawa, Nobuto Kakuda, et al.. (2019). Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry. Journal of Visualized Experiments. 17 indexed citations
10.
Tanaka, Mitsuru, Shinya Dohgu, Fuyuko Takata, et al.. (2019). Brain-transportable dipeptides across the blood-brain barrier in mice. Scientific Reports. 9(1). 5769–5769. 56 indexed citations
11.
Ikegawa, Masaya, Takashi Nirasawa, Nobuto Kakuda, et al.. (2019). Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry. Journal of Visualized Experiments. 1 indexed citations
12.
Nagahara, Noriyuki, Shin Koike, Takashi Nirasawa, Hideo Kimura, & Yuki Ogasawara. (2018). Alternative pathway of H2S and polysulfides production from sulfurated catalytic-cysteine of reaction intermediates of 3-mercaptopyruvate sulfurtransferase. Biochemical and Biophysical Research Communications. 496(2). 648–653. 47 indexed citations
13.
Kakuda, Nobuto, Tomohiro Miyasaka, Takashi Nirasawa, et al.. (2017). Distinct deposition of amyloid-β species in brains with Alzheimer’s disease pathology visualized with MALDI imaging mass spectrometry. Acta Neuropathologica Communications. 5(1). 73–73. 101 indexed citations
14.
Nakanishi, Toyofumi, Takashi Nirasawa, & Takayuki Takubo. (2014). Quantitative Mass Barcode-Like Image of Nicotine in Single Longitudinally Sliced Hair Sections from Long-Term Smokers by Matrix-Assisted Laser Desorption Time-of-Flight Mass Spectrometry Imaging. Journal of Analytical Toxicology. 38(6). 349–353. 18 indexed citations
15.
Hayashi, Hironori, Nobutoki Takamune, Takashi Nirasawa, et al.. (2014). Dimerization of HIV-1 protease occurs through two steps relating to the mechanism of protease dimerization inhibition by darunavir. Proceedings of the National Academy of Sciences. 111(33). 12234–12239. 57 indexed citations
17.
Ishigami, Noriko, Takahiko Tokuda, Masaya Ikegawa, et al.. (2012). Cerebrospinal fluid proteomic patterns discriminate Parkinson's disease and multiple system atrophy. Movement Disorders. 27(7). 851–857. 25 indexed citations
18.
Kasuya, A., R. Sivamohan, Igor Dmitruk, et al.. (2004). Ultra-stable nanoparticles of CdSe revealed from mass spectrometry. Nature Materials. 3(2). 99–102. 455 indexed citations
19.
Nirasawa, Takashi. (1996). MALDI-TOF-MS.. KAGAKU TO SEIBUTSU. 34(4). 255–259. 11 indexed citations
20.
Sugimoto, Yasushi, Takahiro Kusakabe, Sumiharu Nagaoka, et al.. (1996). A proteinase inhibitor from egg yolk of hen is an ovoinhibitor analog. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1295(1). 96–102. 9 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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