N. Kunishima

3.7k total citations · 1 hit paper
90 papers, 2.9k citations indexed

About

N. Kunishima is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, N. Kunishima has authored 90 papers receiving a total of 2.9k indexed citations (citations by other indexed papers that have themselves been cited), including 67 papers in Molecular Biology, 54 papers in Materials Chemistry and 11 papers in Cell Biology. Recurrent topics in N. Kunishima's work include Enzyme Structure and Function (52 papers), Protein Structure and Dynamics (22 papers) and Biochemical and Molecular Research (18 papers). N. Kunishima is often cited by papers focused on Enzyme Structure and Function (52 papers), Protein Structure and Dynamics (22 papers) and Biochemical and Molecular Research (18 papers). N. Kunishima collaborates with scholars based in Japan, India and Colombia. N. Kunishima's co-authors include Hisato Jingami, Masaki Yamamoto, Shigetada Nakanishi, K. Morikawa, Toshihiro Sato, Yuji Tsuji, Kosuke Morikawa, Takashi Kumasaka, Yoshimi Shimada and Narutoshi Kamiya and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Physical Review Letters.

In The Last Decade

N. Kunishima

88 papers receiving 2.8k citations

Hit Papers

Structural basis of glutamate recognition by a dimeric me... 2000 2026 2008 2017 2000 250 500 750
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor
    2000 980 citations N. Kunishima, Masaki Yamamoto et al. profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
N. Kunishima Japan 24 2.1k 869 540 402 259 90 2.9k
Filip Van Petegem Canada 38 3.6k 1.7× 1.1k 1.2× 191 0.4× 158 0.4× 320 1.2× 133 4.4k
Delia Picone Italy 31 2.4k 1.2× 825 0.9× 294 0.5× 352 0.9× 91 0.4× 115 3.6k
Takatsugu Hirokawa Japan 31 2.7k 1.3× 566 0.7× 147 0.3× 333 0.8× 365 1.4× 159 4.6k
Jeff Abramson United States 32 4.0k 2.0× 950 1.1× 446 0.8× 216 0.5× 359 1.4× 65 5.1k
Atsuko Yamashita Japan 25 3.1k 1.5× 1.1k 1.2× 199 0.4× 319 0.8× 663 2.6× 69 5.0k
Tomohiro Nishizawa Japan 35 2.6k 1.3× 792 0.9× 186 0.3× 134 0.3× 236 0.9× 108 4.0k
Irina D. Pogozheva United States 28 3.9k 1.9× 1.3k 1.5× 216 0.4× 356 0.9× 347 1.3× 83 4.9k
Marcin Golczak United States 47 5.5k 2.6× 1.5k 1.7× 392 0.7× 285 0.7× 456 1.8× 118 6.6k
Hideyuki Hayashi Japan 32 1.9k 0.9× 263 0.3× 822 1.5× 270 0.7× 142 0.5× 93 2.9k
Joachim Krebs Switzerland 27 2.3k 1.1× 345 0.4× 303 0.6× 173 0.4× 567 2.2× 63 3.2k

Countries citing papers authored by N. Kunishima

Since Specialization
Citations

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

Fields of papers citing papers by N. Kunishima

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of N. Kunishima

This figure shows the co-authorship network connecting the top 25 collaborators of N. Kunishima. A scholar is included among the top collaborators of N. Kunishima 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 N. Kunishima. N. Kunishima 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.
Kashiwagi, Tatsuki, N. Kunishima, Hisashi Naitow, et al.. (2023). Ambient temperature structure of phosphoketolase from Bifidobacterium longum determined by serial femtosecond X-ray crystallography. Acta Crystallographica Section D Structural Biology. 79(4). 290–303. 3 indexed citations
2.
Yasuda, Satoshi, Keiichi Kojima, Tomohiko Hayashi, et al.. (2022). Development of an Outward Proton Pumping Rhodopsin with a New Record in Thermostability by Means of Amino Acid Mutations. The Journal of Physical Chemistry B. 126(5). 1004–1015. 6 indexed citations
3.
Kumar, S. Madan, M.K. Hema, Karthik Kumara, et al.. (2017). Crystal structure of SAM-dependent methyltransferase from Pyrococcus horikoshii. Acta Crystallographica Section F Structural Biology Communications. 73(12). 706–712. 4 indexed citations
4.
Matsuura, Yoshinori, Yasumasa Joti, Kyoko Ogasahara, et al.. (2015). Thermodynamics of protein denaturation at temperatures over 100 °C: CutA1 mutant proteins substituted with hydrophobic and charged residues. Scientific Reports. 5(1). 15545–15545. 66 indexed citations
5.
Bagautdinov, B., Yoshinori Matsuura, H. Yamamoto, et al.. (2014). Thermodynamic analysis of unusually thermostable CutA1 protein from human brain and its protease susceptibility. The Journal of Biochemistry. 157(3). 169–176. 4 indexed citations
6.
Lokanath, N.K., et al.. (2014). Crystal structure of product-bound complex of UDP-N-acetyl-d-mannosamine dehydrogenase from Pyrococcus horikoshii OT3. Biochemical and Biophysical Research Communications. 453(3). 662–667. 1 indexed citations
7.
Kumar, S. Madan, et al.. (2014). Crystal structure studies of NADP+ dependent isocitrate dehydrogenase from Thermus thermophilus exhibiting a novel terminal domain. Biochemical and Biophysical Research Communications. 449(1). 107–113. 4 indexed citations
8.
Kumar, S. Madan, et al.. (2014). Crystal structures of type IIIH NAD-dependent D-3-phosphoglycerate dehydrogenase from two thermophiles. Biochemical and Biophysical Research Communications. 451(1). 126–130.
9.
Kuroishi, Chizu, et al.. (2010). Dimeric Crystal Structure of Rabbit l-Gulonate 3-Dehydrogenase/λ-Crystallin: Insights into the Catalytic Mechanism. Journal of Molecular Biology. 401(5). 906–920. 5 indexed citations
10.
Endo, Satoshi, et al.. (2008). Biochemical and structural characterization of a short-chain dehydrogenase/reductase of Thermus thermophilus HB8. Chemico-Biological Interactions. 178(1-3). 117–126. 16 indexed citations
11.
Yamamoto, H., Koji Takio, Mitsuaki Sugahara, & N. Kunishima. (2008). Structure of a haloacid dehalogenase superfamily phosphatase PH1421 fromPyrococcus horikoshiiOT3: oligomeric state and thermoadaptation mechanism. Acta Crystallographica Section D Biological Crystallography. 64(10). 1068–1077. 1 indexed citations
12.
Sugahara, Michihiro, Katsumi Shimizu, H. Yamamoto, et al.. (2008). High-throughput crystallization-to-structure pipeline at RIKEN SPring-8 Center. Journal of Structural and Functional Genomics. 9(1-4). 21–28. 23 indexed citations
13.
Lokanath, N.K., et al.. (2007). Purification, crystallization and preliminary X-ray diffraction studies of a putative UDP-N-acetyl-D-mannosamine dehydrogenase fromPyrococcus horikoshiiOT3. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63(5). 412–414. 2 indexed citations
14.
Sugahara, Michihiro, et al.. (2005). Heavy-atom Database System: a tool for the preparation of heavy-atom derivatives of protein crystals based on amino-acid sequence and crystallization conditions. Acta Crystallographica Section D Biological Crystallography. 61(9). 1302–1305. 14 indexed citations
15.
Ogasahara, Kyoko, Jeyaraman Jeyakanthan, N. Kunishima, et al.. (2005). Stabilization Due to Dimer Formation of Phosphoribosyl Anthranilate Isomerase from Thermus thermophilus HB8: X-Ray Analysis and DSC Experiments. The Journal of Biochemistry. 137(5). 569–578. 7 indexed citations
16.
Tsutakawa, Susan E., Takanori Muto, Tomohiko Kawate, et al.. (1999). Crystallographic and Functional Studies of Very Short Patch Repair Endonuclease. Molecular Cell. 3(5). 621–628. 60 indexed citations
17.
Suzuki, Chise, Tatsuki Kashiwagi, Fumihiko Tsuchiya, et al.. (1997). Circular dichroism analysis of the interaction between the alpha and beta subunits in a killer toxin produced by a halotolerant yeast, Pichia farinosa. Protein Engineering Design and Selection. 10(2). 99–101. 8 indexed citations
18.
Kashiwagi, Tatsuki, N. Kunishima, Chise Suzuki, et al.. (1997). The novel acidophilic structure of the killer toxin from halotolerant yeast demonstrates remarkable folding similarity with a fungal killer toxin. Structure. 5(1). 81–94. 29 indexed citations
19.
Ashikari, Toshihiko, Yoshikazu Tanaka, Yasuhiko Asada, et al.. (1995). Cloning, Sequencing, and Heterologous Expression of a Gene Coding forArthromyces ramosusPeroxidase. Bioscience Biotechnology and Biochemistry. 59(7). 1221–1228. 37 indexed citations
20.
Kunishima, N., Keiichi Fukuyama, Hiroshi Matsubara, et al.. (1994). Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1·9 Å resolution. Journal of Molecular Biology. 235(1). 331–344. 167 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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