Takatoshi Ohkuri

1.4k total citations
50 papers, 1.1k citations indexed

About

Takatoshi Ohkuri is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Materials Chemistry. According to data from OpenAlex, Takatoshi Ohkuri has authored 50 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 38 papers in Molecular Biology, 16 papers in Radiology, Nuclear Medicine and Imaging and 15 papers in Materials Chemistry. Recurrent topics in Takatoshi Ohkuri's work include Monoclonal and Polyclonal Antibodies Research (16 papers), Protein purification and stability (15 papers) and Enzyme Structure and Function (15 papers). Takatoshi Ohkuri is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (16 papers), Protein purification and stability (15 papers) and Enzyme Structure and Function (15 papers). Takatoshi Ohkuri collaborates with scholars based in Japan, United States and Switzerland. Takatoshi Ohkuri's co-authors include Tadashi Ueda, Yuzo Ninomiya, Keiko Yasumatsu, Johannes le Coutre, Ryusuke Yoshida, C. Cartoni, Noriatsu Shigemura, Sami Damak, Nicolas Godinot and Akihiko Yamagishi and has published in prestigious journals such as Journal of Neuroscience, The Journal of Immunology and Journal of Molecular Biology.

In The Last Decade

Takatoshi Ohkuri

50 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Takatoshi Ohkuri Japan 16 562 306 197 152 140 50 1.1k
Tsukasa Kusakizako Japan 21 878 1.6× 131 0.4× 199 1.0× 83 0.5× 96 0.7× 33 1.3k
JaeHyung Koo South Korea 15 274 0.5× 272 0.9× 320 1.6× 60 0.4× 105 0.8× 37 809
Valeriy G. Ostapchenko Canada 21 943 1.7× 242 0.8× 62 0.3× 346 2.3× 19 0.1× 26 1.2k
Jonathan Kil United States 17 425 0.8× 163 0.5× 998 5.1× 41 0.3× 49 0.3× 24 1.8k
Yuji Tsuji Japan 9 870 1.5× 312 1.0× 146 0.7× 50 0.3× 85 0.6× 32 1.3k
Melissa Vos United States 21 896 1.6× 190 0.6× 139 0.7× 307 2.0× 12 0.1× 29 1.6k
Christopher E. Hopkins United States 13 965 1.7× 52 0.2× 88 0.4× 105 0.7× 62 0.4× 24 1.6k
Alex Perálvarez‐Marín Spain 18 588 1.0× 67 0.2× 234 1.2× 316 2.1× 34 0.2× 56 1.1k
Simon J. Dowell United Kingdom 26 2.1k 3.7× 99 0.3× 37 0.2× 161 1.1× 51 0.4× 39 2.7k
Tetsuya Miyamoto Japan 22 670 1.2× 168 0.5× 90 0.5× 84 0.6× 33 0.2× 80 1.9k

Countries citing papers authored by Takatoshi Ohkuri

Since Specialization
Citations

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

Fields of papers citing papers by Takatoshi Ohkuri

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Takatoshi Ohkuri

This figure shows the co-authorship network connecting the top 25 collaborators of Takatoshi Ohkuri. A scholar is included among the top collaborators of Takatoshi Ohkuri 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 Takatoshi Ohkuri. Takatoshi Ohkuri 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.
Senda, Miki, Hitomi Nakamura, Naoko Oda‐Ueda, et al.. (2024). Stabilization of adalimumab Fab through the introduction of disulfide bonds between the variable and constant domains. Biochemical and Biophysical Research Communications. 700. 149592–149592. 1 indexed citations
2.
Ohkuri, Takatoshi, et al.. (2021). High-level expression of human CH2 domain from the Fc region in Pichia pastoris and preparation of anti-CH2 antibodies. The Journal of Biochemistry. 170(2). 289–297. 5 indexed citations
3.
Nakamura, Hitomi, et al.. (2021). A comprehensive analysis of novel disulfide bond introduction site into the constant domain of human Fab. Scientific Reports. 11(1). 12937–12937. 6 indexed citations
4.
Ohkuri, Takatoshi, et al.. (2021). Abolition of aggregation of CH2 domain of human IgG1 when combining glycosylation and protein stabilization. Biochemical and Biophysical Research Communications. 558. 114–119. 5 indexed citations
5.
Nakamura, Hitomi, Naoko Oda‐Ueda, Tadashi Ueda, & Takatoshi Ohkuri. (2018). Introduction of a glycosylation site in the constant region decreases the aggregation of adalimumab Fab. Biochemical and Biophysical Research Communications. 503(2). 752–756. 17 indexed citations
6.
Abe, Masahiro, Yoshito Abe, Takatoshi Ohkuri, et al.. (2013). Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein. Protein Science. 22(4). 467–474. 37 indexed citations
7.
Ohkuri, Takatoshi, et al.. (2013). Characterization of deamidation at Asn138 in L-chain of recombinant humanized Fab expressed from Pichia pastoris. The Journal of Biochemistry. 154(4). 333–340. 12 indexed citations
8.
Igawa, Takeshi, Shougo Higashi, Yoshito Abe, et al.. (2012). Preparation and characterization of a monoclonal antibody against the refolded and functional extracellular domain of rat P2X4 receptor. The Journal of Biochemistry. 153(3). 275–282. 13 indexed citations
9.
Cartoni, C., Keiko Yasumatsu, Takatoshi Ohkuri, et al.. (2010). Taste Preference for Fatty Acids Is Mediated by GPR40 and GPR120. Journal of Neuroscience. 30(25). 8376–8382. 323 indexed citations
10.
Ohkuri, Takatoshi, et al.. (2009). Effects of His mutations on the fibrillation of amyloidogenic Vλ6 protein Wil under acidic and physiological conditions. Biochemical and Biophysical Research Communications. 391(1). 615–620. 7 indexed citations
11.
Oda, Masayuki, Akikazu Murakami, Miyuki Nishimura, et al.. (2009). Evaluation of the conformational equilibrium of reduced hen egg lysozyme by antibodies to the native form. Archives of Biochemistry and Biophysics. 494(2). 145–150. 12 indexed citations
12.
Goto, Takashi, et al.. (2008). Crystal Structures of K33 Mutant Hen Lysozymes with Enhanced Activities. The Journal of Biochemistry. 144(5). 619–623. 3 indexed citations
13.
Shimizu, Hideaki, Shin‐ichi Yokobori, Takatoshi Ohkuri, et al.. (2007). Extremely Thermophilic Translation System in the Common Ancestor Commonote: Ancestral Mutants of Glycyl-tRNA Synthetase from the Extreme Thermophile Thermus thermophilus. Journal of Molecular Biology. 369(4). 1060–1069. 20 indexed citations
14.
Fujii, T., Takatoshi Ohkuri, Rie Onodera, & Tadashi Ueda. (2007). Stable Supply of Large Amounts of Human Fab from the Inclusion Bodies in E. coli. The Journal of Biochemistry. 141(5). 699–707. 22 indexed citations
15.
Watanabe, Keiko, Takatoshi Ohkuri, Shin‐ichi Yokobori, & Akihiko Yamagishi. (2005). Designing Thermostable Proteins: Ancestral Mutants of 3-Isopropylmalate Dehydrogenase Designed by using a Phylogenetic Tree. Journal of Molecular Biology. 355(4). 664–674. 77 indexed citations
16.
Watanabe, Keiko, et al.. (2005). Thermostability of ancestral mutants ofCaldococcus noboribetusisocitrate dehydrogenase. FEMS Microbiology Letters. 243(2). 393–398. 23 indexed citations
17.
Ohkuri, Takatoshi, Tadashi Ueda, Yuichiro Yoshida, et al.. (2002). A metal binding in the polypeptide chain improves the folding efficiency of a denatured and reduced protein. Biopolymers. 64(2). 106–114. 1 indexed citations
18.
Ohkuri, Takatoshi, et al.. (2001). Evidence for an initiation site for hen lysozyme folding from the reduced form using its dissected peptide fragments. Protein Engineering Design and Selection. 14(11). 829–833. 9 indexed citations
19.
Ueda, Tadashi, Takatoshi Ohkuri, & Taiji Imoto. (1996). Identification of the Peptide Region That Folds Native Conformation in the Early Stage of the Renaturation of Reduced Lysozyme. Biochemical and Biophysical Research Communications. 228(1). 203–208. 10 indexed citations
20.
Ueda, Tadashi, et al.. (1995). Kinetically trapped structure in the renaturation of reduced oxindolealanine 62 lysozyme. Biochemistry. 34(49). 16178–16185. 8 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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