Takeshi Tenno

2.0k total citations
44 papers, 1.6k citations indexed

About

Takeshi Tenno is a scholar working on Molecular Biology, Oncology and Materials Chemistry. According to data from OpenAlex, Takeshi Tenno has authored 44 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Molecular Biology, 9 papers in Oncology and 9 papers in Materials Chemistry. Recurrent topics in Takeshi Tenno's work include Protein Structure and Dynamics (10 papers), Enzyme Structure and Function (8 papers) and Ubiquitin and proteasome pathways (7 papers). Takeshi Tenno is often cited by papers focused on Protein Structure and Dynamics (10 papers), Enzyme Structure and Function (8 papers) and Ubiquitin and proteasome pathways (7 papers). Takeshi Tenno collaborates with scholars based in Japan, United States and Italy. Takeshi Tenno's co-authors include Hidekazu Hiroaki, Masahiro Shirakawa, Hidehito Tochio, Natsuko Goda, Yutaka Ito, Ayako Ohno, Shin Isogai, Kohsuke Inomata, Kenichiro Fujiwara and Shiroh Futaki and has published in prestigious journals such as Nature, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Takeshi Tenno

43 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Takeshi Tenno Japan 18 1.2k 294 278 198 178 44 1.6k
Kenji Sugase Japan 19 1.6k 1.3× 514 1.7× 234 0.8× 366 1.8× 88 0.5× 72 2.1k
Oliver Ohlenschläger Germany 29 1.4k 1.2× 323 1.1× 145 0.5× 428 2.2× 127 0.7× 102 2.1k
Daniel Wüstner Denmark 31 2.3k 1.9× 145 0.5× 628 2.3× 164 0.8× 126 0.7× 103 3.1k
Voula Kanelis Canada 20 1.8k 1.5× 265 0.9× 208 0.7× 254 1.3× 90 0.5× 34 2.4k
Shiou‐Ru Tzeng Taiwan 18 1.6k 1.3× 357 1.2× 183 0.7× 203 1.0× 56 0.3× 33 1.9k
Fang Tian United States 23 1.1k 0.9× 322 1.1× 149 0.5× 446 2.3× 82 0.5× 59 1.5k
Woonghee Lee United States 18 1.9k 1.6× 370 1.3× 230 0.8× 320 1.6× 78 0.4× 62 2.4k
Alex U. Singer Canada 18 2.2k 1.9× 505 1.7× 358 1.3× 366 1.8× 82 0.5× 28 3.0k
Till Rudack Germany 22 1.8k 1.5× 402 1.4× 486 1.7× 99 0.5× 163 0.9× 39 2.3k
Arnout P. Kalverda United Kingdom 23 1.6k 1.3× 388 1.3× 208 0.7× 196 1.0× 71 0.4× 54 2.0k

Countries citing papers authored by Takeshi Tenno

Since Specialization
Citations

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

Fields of papers citing papers by Takeshi Tenno

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Takeshi Tenno

This figure shows the co-authorship network connecting the top 25 collaborators of Takeshi Tenno. A scholar is included among the top collaborators of Takeshi Tenno 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 Takeshi Tenno. Takeshi Tenno 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.
Mizoguchi, Takamasa, et al.. (2023). Small-Molecule-Mediated Suppression of BMP Signaling by Selective Inhibition of BMP1-Dependent Chordin Cleavage. International Journal of Molecular Sciences. 24(5). 4313–4313. 3 indexed citations
2.
3.
Goda, Natsuko, et al.. (2022). Direct inhibition of the first PDZ domain of ZO-1 by glycyrrhizin is a possible mechanism of tight junction opening of Caco-2 cells. Food & Function. 13(4). 1953–1964. 4 indexed citations
4.
Tenno, Takeshi, et al.. (2022). Relevance of Amorphous and Amyloid-Like Aggregates of the p53 Core Domain to Loss of its DNA-Binding Activity. Frontiers in Molecular Biosciences. 9. 869851–869851. 4 indexed citations
5.
Matsuo, Naoki, Natsuko Goda, Takeshi Tenno, & Hidekazu Hiroaki. (2021). Cryoprotective activities of FK20, a human genome-derived intrinsically disordered peptide against cryosensitive enzymes without a stereospecific molecular interaction. SHILAP Revista de lepidopterología. 3. e20–e20. 2 indexed citations
6.
Goda, Natsuko, et al.. (2020). High dose of baicalin or baicalein can reduce tight junction integrity by partly targeting the first PDZ domain of zonula occludens-1 (ZO-1). European Journal of Pharmacology. 887. 173436–173436. 15 indexed citations
7.
8.
Goda, Natsuko, et al.. (2020). Opposing Effect of Naringenin and Quercetin on the Junctional Compartment of MDCK II Cells to Modulate the Tight Junction. Nutrients. 12(11). 3285–3285. 21 indexed citations
9.
Goda, Natsuko, Akihiro Narita, Takeshi Tenno, et al.. (2020). Principal component analysis of data from NMR titration experiment of uniformly 15N labeled amyloid beta (1–42) peptide with osmolytes and phenolic compounds. Archives of Biochemistry and Biophysics. 690. 108446–108446. 6 indexed citations
10.
Ohtsuka, Hokuto, et al.. (2017). Ecl1 is a zinc-binding protein involved in the zinc-limitation-dependent extension of chronological life span in fission yeast. Molecular Genetics and Genomics. 292(2). 475–481. 19 indexed citations
11.
Isogai, Shin, Daichi Morimoto, Kyohei Arita, et al.. (2011). Crystal Structure of the Ubiquitin-associated (UBA) Domain of p62 and Its Interaction with Ubiquitin. Journal of Biological Chemistry. 286(36). 31864–31874. 118 indexed citations
12.
Umetsu, Yoshitaka, Takeshi Tenno, Natsuko Goda, et al.. (2011). Structural difference of vasoactive intestinal peptide in two distinct membrane-mimicking environments. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1814(5). 724–730. 35 indexed citations
13.
Fujiwara, Yoshie, Natsuko Goda, Takeshi Tenno, et al.. (2010). A Common Substrate Recognition Mode Conserved between Katanin p60 and VPS4 Governs Microtubule Severing and Membrane Skeleton Reorganization. Journal of Biological Chemistry. 285(22). 16822–16829. 30 indexed citations
14.
Morimoto, Daichi, Shin Isogai, Takeshi Tenno, et al.. (2010). Purification, crystallization and preliminary crystallographic studies of Lys48-linked polyubiquitin chains. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(7). 834–837. 4 indexed citations
15.
Inomata, Kohsuke, Ayako Ohno, Hidehito Tochio, et al.. (2009). High-resolution multi-dimensional NMR spectroscopy of proteins in human cells. Nature. 458(7234). 106–109. 369 indexed citations
16.
Sakai, Tomomi, Hidehito Tochio, Kohsuke Inomata, et al.. (2007). Fluoroscopic assessment of protein leakage during Xenopus oocytes in-cell NMR experiment by co-injected EGFP. Analytical Biochemistry. 371(2). 247–249. 15 indexed citations
17.
Goda, Natsuko, Takeshi Tenno, Kohsuke Inomata, et al.. (2006). LBT/PTD dual tagged vector for purification, cellular protein delivery and visualization in living cells. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1773(2). 141–146. 11 indexed citations
18.
Ohno, Ayako, Jun‐Goo Jee, Kenichiro Fujiwara, et al.. (2005). Structure of the UBA Domain of Dsk2p in Complex with Ubiquitin. Structure. 13(4). 521–532. 115 indexed citations
19.
Goda, Natsuko, et al.. (2004). The PRESAT‐vector: Asymmetric T‐vector for high‐throughput screening of soluble protein domains for structural proteomics. Protein Science. 13(3). 652–658. 31 indexed citations
20.
Nomura, Makoto, Toshiyuki Kohno, Kenichiro Fujiwara, et al.. (2004). Paramagnetic NMR study of Cu2+–IDA complex localization on a protein surface and its application to elucidate long distance information. FEBS Letters. 566(1-3). 157–161. 17 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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