Terukazu Nogi

2.1k total citations
43 papers, 1.6k citations indexed

About

Terukazu Nogi is a scholar working on Molecular Biology, Cell Biology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Terukazu Nogi has authored 43 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Molecular Biology, 9 papers in Cell Biology and 8 papers in Cellular and Molecular Neuroscience. Recurrent topics in Terukazu Nogi's work include Metalloenzymes and iron-sulfur proteins (8 papers), Glycosylation and Glycoproteins Research (6 papers) and Cellular transport and secretion (6 papers). Terukazu Nogi is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (8 papers), Glycosylation and Glycoproteins Research (6 papers) and Cellular transport and secretion (6 papers). Terukazu Nogi collaborates with scholars based in Japan, United States and Spain. Terukazu Nogi's co-authors include Junichi Takagi, N. Yasui, Emiko Mihara, Kunio Miki, Masamichi Nagae, Tsunenori Nozawa, Masayuki Kobayashi, Yukinari Kato, Mika K. Kaneko and Yuji Sugita and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and The Journal of Cell Biology.

In The Last Decade

Terukazu Nogi

42 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Terukazu Nogi Japan 20 1.0k 470 327 156 147 43 1.6k
Noboru Ishiyama Canada 26 1.7k 1.7× 821 1.7× 206 0.6× 148 0.9× 156 1.1× 48 2.4k
Jean Paul Olivier Canada 8 1.3k 1.2× 280 0.6× 307 0.9× 52 0.3× 145 1.0× 11 1.5k
Iris Rapoport United States 17 1.1k 1.1× 1.0k 2.1× 287 0.9× 122 0.8× 428 2.9× 30 2.0k
Brigitte Ritter Canada 24 1.2k 1.2× 1.0k 2.2× 276 0.8× 98 0.6× 95 0.6× 29 1.7k
Thomas P. Stauffer Switzerland 11 1.7k 1.6× 847 1.8× 396 1.2× 160 1.0× 188 1.3× 17 2.2k
Janelle Lauer United States 20 983 1.0× 216 0.5× 161 0.5× 102 0.7× 378 2.6× 33 1.9k
Karin Ridderstråle Sweden 6 1.9k 1.8× 448 1.0× 189 0.6× 108 0.7× 217 1.5× 6 2.5k
Samuel Bouyain United States 18 731 0.7× 249 0.5× 159 0.5× 68 0.4× 168 1.1× 34 1.1k
Ralf Heilker Germany 23 1.2k 1.1× 275 0.6× 318 1.0× 111 0.7× 525 3.6× 47 2.1k
Reina E. Itoh Japan 9 1.1k 1.1× 887 1.9× 186 0.6× 194 1.2× 82 0.6× 10 1.7k

Countries citing papers authored by Terukazu Nogi

Since Specialization
Citations

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

Fields of papers citing papers by Terukazu Nogi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Terukazu Nogi

This figure shows the co-authorship network connecting the top 25 collaborators of Terukazu Nogi. A scholar is included among the top collaborators of Terukazu Nogi 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 Terukazu Nogi. Terukazu Nogi 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.
Asahi, Katsuhiko, Mika Hirose, Michiko Tajiri, et al.. (2025). Cryo-EM structure of the bacterial intramembrane metalloprotease RseP in the substrate-bound state. Science Advances. 11(9). eadu0925–eadu0925. 1 indexed citations
2.
3.
Ekimoto, Toru, Tsutomu Yamane, Emiko Mihara, et al.. (2022). Hybrid in vitro/in silico analysis of low‐affinity protein–protein interactions that regulate signal transduction by Sema6D. Protein Science. 31(11). e4452–e4452. 5 indexed citations
4.
Hirose, Mika, Toru Ekimoto, T. Miyake, et al.. (2021). Moving toward generalizable NZ-1 labeling for 3D structure determination with optimized epitope-tag insertion. Acta Crystallographica Section D Structural Biology. 77(5). 645–662. 15 indexed citations
5.
6.
Hirai, Hidenori & Terukazu Nogi. (2018). Structural Basis for Ligand Capture and Release by the Endocytic Receptor ApoER2. Seibutsu Butsuri. 58(4). 200–203. 1 indexed citations
7.
8.
Nagae, Masamichi, Sushil K. Mishra, Akemi Ikeda, et al.. (2017). 3D structural analysis of protein O‐mannosyl kinase, POMK, a causative gene product of dystroglycanopathy. Genes to Cells. 22(4). 348–359. 21 indexed citations
9.
Fujii, Yuki, et al.. (2014). PA tag: A versatile protein tagging system using a super high affinity antibody against a dodecapeptide derived from human podoplanin. Protein Expression and Purification. 95. 240–247. 164 indexed citations
10.
Nagae, Masamichi, et al.. (2010). Crystallization and preliminary crystallographic analysis of human LR11 Vps10p domain. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(1). 129–132. 5 indexed citations
11.
Yasui, N., Terukazu Nogi, & Junichi Takagi. (2010). Structural Basis for Specific Recognition of Reelin by Its Receptors. Structure. 18(3). 320–331. 67 indexed citations
12.
Nogi, Terukazu, et al.. (2008). A Murine Monoclonal Antibody That Binds N-Terminal Extracellular Segment of Human Protease-Activated Receptor-4. Hybridoma. 27(5). 331–335. 7 indexed citations
13.
Nogi, Terukazu, Masamichi Nagae, Keiko Tamura‐Kawakami, et al.. (2008). Novel affinity tag system using structurally defined antibody‐tag interaction: Application to single‐step protein purification. Protein Science. 17(12). 2120–2126. 23 indexed citations
14.
Nogi, Terukazu, N. Yasui, Mitsuharu Hattori, Kenji Iwasaki, & Junichi Takagi. (2006). Structure of a signaling‐competent reelin fragment revealed by X‐ray crystallography and electron tomography. The EMBO Journal. 25(15). 3675–3683. 32 indexed citations
15.
Nogi, Terukazu, et al.. (2005). Eye regeneration assay reveals an invariant functional left-right asymmetry in the early bilaterian, Dugesia japonica.. Laterality Asymmetries of Body Brain and Cognition. 10(2). 193–205. 22 indexed citations
16.
Nogi, Terukazu, Yoko Shiba, Masato Kawasaki, et al.. (2002). Structural basis for the accessory protein recruitment by the γ-adaptin ear domain. Nature Structural Biology. 56 indexed citations
17.
Liu, Lijun, Terukazu Nogi, Masayuki Kobayashi, Tsunenori Nozawa, & Kunio Miki. (2002). Ultrahigh-resolution structure of high-potential iron–sulfur protein fromThermochromatium tepidum. Acta Crystallographica Section D Biological Crystallography. 58(7). 1085–1091. 32 indexed citations
18.
Nogi, Terukazu, Masayuki Kobayashi, Tsunenori Nozawa, & Kunio Miki. (2000). Crystallization and preliminary crystallographic analysis of the high-potential iron–sulfur protein fromThermochromatium tepidum. Acta Crystallographica Section D Biological Crystallography. 56(5). 656–658. 6 indexed citations
19.
Nogi, Terukazu, et al.. (2000). Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum : Thermostability and electron transfer. Proceedings of the National Academy of Sciences. 97(25). 13561–13566. 135 indexed citations
20.
Nogi, Terukazu, Takaaki A. Fukami, Masami Ishida, Masasuke Yoshida, & Kunio Miki. (1999). Purification, Crystallization, and Preliminary X-ray Crystallographic Analysis of Thermus thermophilus V1-ATPase B Subunit. Journal of Structural Biology. 127(1). 79–82. 5 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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