Takaho Terada

7.0k total citations
129 papers, 4.7k citations indexed

About

Takaho Terada is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Takaho Terada has authored 129 papers receiving a total of 4.7k indexed citations (citations by other indexed papers that have themselves been cited), including 112 papers in Molecular Biology, 41 papers in Materials Chemistry and 10 papers in Cell Biology. Recurrent topics in Takaho Terada's work include Enzyme Structure and Function (41 papers), RNA and protein synthesis mechanisms (37 papers) and RNA modifications and cancer (21 papers). Takaho Terada is often cited by papers focused on Enzyme Structure and Function (41 papers), RNA and protein synthesis mechanisms (37 papers) and RNA modifications and cancer (21 papers). Takaho Terada collaborates with scholars based in Japan, United States and Germany. Takaho Terada's co-authors include Shigeyuki Yokoyama, Mikako Shirouzu, T. Kigawa, Seiki Kuramitsu, Akiko Tanaka, Takashi Yabuki, Makoto Inoue, Kazutaka Murayama, Mutsuko Kukimoto‐Niino and Eiko Seki and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Nucleic Acids Research.

In The Last Decade

Takaho Terada

129 papers receiving 4.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Takaho Terada Japan 40 3.7k 679 449 433 329 129 4.7k
Dirk Kostrewa Switzerland 29 3.0k 0.8× 427 0.6× 473 1.1× 372 0.9× 291 0.9× 42 3.9k
Gilles Labesse France 43 3.1k 0.8× 484 0.7× 446 1.0× 562 1.3× 524 1.6× 127 4.9k
B.M. Hallberg Sweden 32 3.2k 0.9× 569 0.8× 374 0.8× 444 1.0× 209 0.6× 63 4.6k
M.S. Nissen United States 24 3.6k 1.0× 442 0.7× 434 1.0× 574 1.3× 253 0.8× 40 4.5k
O. Gileadi United Kingdom 44 4.3k 1.2× 346 0.5× 568 1.3× 272 0.6× 346 1.1× 108 5.5k
Raphaël Guérois France 38 4.7k 1.3× 1.1k 1.6× 509 1.1× 737 1.7× 631 1.9× 117 5.8k
Yuequan Shen China 35 3.0k 0.8× 366 0.5× 636 1.4× 254 0.6× 448 1.4× 101 4.4k
Constance J. Jeffery United States 29 2.6k 0.7× 274 0.4× 316 0.7× 544 1.3× 342 1.0× 73 3.9k
Birgit Eisenhaber Singapore 29 2.7k 0.7× 664 1.0× 281 0.6× 194 0.4× 482 1.5× 77 3.8k
Fritz K. Winkler Switzerland 35 3.2k 0.8× 405 0.6× 506 1.1× 418 1.0× 837 2.5× 60 4.9k

Countries citing papers authored by Takaho Terada

Since Specialization
Citations

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

Fields of papers citing papers by Takaho Terada

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Takaho Terada

This figure shows the co-authorship network connecting the top 25 collaborators of Takaho Terada. A scholar is included among the top collaborators of Takaho Terada 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 Takaho Terada. Takaho Terada 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.
Adachi, Jiro, Kazushige Katsura, Eiko Seki, et al.. (2019). Cell-Free Protein Synthesis Using S30 Extracts from Escherichia coli RFzero Strains for Efficient Incorporation of Non-Natural Amino Acids into Proteins. International Journal of Molecular Sciences. 20(3). 492–492. 22 indexed citations
2.
Katsura, Kazushige, Yuri Tomabechi, Takayoshi Matsuda, et al.. (2018). Phosphorylated and non-phosphorylated HCK kinase domains produced by cell-free protein expression. Protein Expression and Purification. 150. 92–99. 9 indexed citations
3.
Shimizu, Hideaki, Haruko Miyazaki, Noboru Ohsawa, et al.. (2016). Structure-based site-directed photo-crosslinking analyses of multimeric cell-adhesive interactions of voltage-gated sodium channel β subunits. Scientific Reports. 6(1). 26618–26618. 12 indexed citations
4.
Alam, Md. Jahangir, Satoshi Arai, Shinya Saijo, et al.. (2013). Loose Binding of the DF Axis with the A3B3 Complex Stimulates the Initial Activity of Enterococcus hirae V1-ATPase. PLoS ONE. 8(9). e74291–e74291. 6 indexed citations
5.
Terada, Takaho, Takeshi Murata, Mikako Shirouzu, & Shigeyuki Yokoyama. (2013). Cell-Free Expression of Protein Complexes for Structural Biology. Methods in molecular biology. 1091. 151–159. 24 indexed citations
6.
Umehara, Takashi, Kazuki Sasaki, Yoshihiro Nakamura, et al.. (2011). Real-Time Imaging of Histone H4K12–Specific Acetylation Determines the Modes of Action of Histone Deacetylase and Bromodomain Inhibitors. Chemistry & Biology. 18(4). 495–507. 80 indexed citations
7.
Wang, Xiaoying, Ryogo Akasaka, Chie Takemoto, et al.. (2011). Overexpression, purification, crystallization and preliminary crystallographic studies of a hyperthermophilic adenylosuccinate synthetase fromPyrococcus horikoshiiOT3. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(12). 1551–1555. 1 indexed citations
8.
Shimada, Atsushi, Kazunori Takano, Mikako Shirouzu, et al.. (2010). Mapping of the basic amino‐acid residues responsible for tubulation and cellular protrusion by the EFC/F‐BAR domain of pacsin2/Syndapin II. FEBS Letters. 584(6). 1111–1118. 63 indexed citations
9.
Ohnishi, Satoshi, N. Tochio, T. Tomizawa, et al.. (2008). Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily. Protein Science. 17(9). 1531–1541. 8 indexed citations
10.
Kukimoto‐Niino, Mutsuko, Ryogo Akasaka, Marcos Hikari Toyama, et al.. (2008). Crystal structure of the human receptor activity‐modifying protein 1 extracellular domain. Protein Science. 17(11). 1907–1914. 41 indexed citations
11.
Wang, Hongfei, Chie Takemoto, Ryogo Akasaka, et al.. (2008). Novel dimerization mode of the human Bcl-2 family protein Bak, a mitochondrial apoptosis regulator. Journal of Structural Biology. 166(1). 32–37. 39 indexed citations
12.
Tanaka, Hiroaki, Takashi Umehara, Koji Inaka, et al.. (2007). Crystallization of the archaeal transcription termination factor NusA: a significant decrease in twinning under microgravity conditions. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63(2). 69–73. 9 indexed citations
13.
Tochio, N., S. Koshiba, Naohiro Kobayashi, et al.. (2006). Solution structure of the kinase‐associated domain 1 of mouse microtubule‐associated protein/microtubule affinity‐regulating kinase 3. Protein Science. 15(11). 2534–2543. 33 indexed citations
14.
Hattori, Motoyuki, Eiichi Mizohata, Ayako Tatsuguchi, et al.. (2006). Crystal structure of the single‐domain rhodanese homologue TTHA0613 from Thermus thermophilus HB8. Proteins Structure Function and Bioinformatics. 64(1). 284–287. 5 indexed citations
15.
Arai, Ryoichi, Mutsuko Kukimoto‐Niino, Satoshi Morita, et al.. (2005). Crystal structure of an enhancer of rudimentary homolog (ERH) at 2.1 Å resolution. Protein Science. 14(7). 1888–1893. 28 indexed citations
16.
Shigi, Naoki, Tsutomu Suzuki, Takaho Terada, et al.. (2005). Temperature-dependent Biosynthesis of 2-Thioribothymidine of Thermus thermophilus tRNA. Journal of Biological Chemistry. 281(4). 2104–2113. 67 indexed citations
17.
Sakai, Hiroaki, Hongfei Wang, Chie Takemoto‐Hori, et al.. (2004). Crystal structures of the signal transducing protein GlnK from Thermus thermophilus HB8. Journal of Structural Biology. 149(1). 99–110. 33 indexed citations
18.
Murayama, Kazutaka, M. Kato-Murayama, Kazushige Katsura, et al.. (2004). Structure of a putativetrans-editing enzyme for prolyl-tRNA synthetase fromAeropyrum pernixK1 at 1.7 Å resolution. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(1). 26–29. 7 indexed citations
19.
Yamasaki, Kazuhiko, T. Kigawa, Makoto Inoue, et al.. (2004). A Novel Zinc-binding Motif Revealed by Solution Structures of DNA-binding Domains of Arabidopsis SBP-family Transcription Factors. Journal of Molecular Biology. 337(1). 49–63. 236 indexed citations
20.
Someya, Tatsuhiko, Nobukazu Nameki, Haruko Hosoi, et al.. (2002). Solution structure of a tmRNA‐binding protein, SmpB, from Thermus thermophilus. FEBS Letters. 535(1-3). 94–100. 41 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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