T. Harada

650 total citations
19 papers, 450 citations indexed

About

T. Harada is a scholar working on Molecular Biology, Cell Biology and Biotechnology. According to data from OpenAlex, T. Harada has authored 19 papers receiving a total of 450 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 8 papers in Cell Biology and 3 papers in Biotechnology. Recurrent topics in T. Harada's work include Endoplasmic Reticulum Stress and Disease (4 papers), RNA Research and Splicing (4 papers) and Protein Structure and Dynamics (3 papers). T. Harada is often cited by papers focused on Endoplasmic Reticulum Stress and Disease (4 papers), RNA Research and Splicing (4 papers) and Protein Structure and Dynamics (3 papers). T. Harada collaborates with scholars based in Japan and Germany. T. Harada's co-authors include Satoru Watanabe, Shigeyuki Yokoyama, T. Kigawa, Peter Güntert, Naohiro Kobayashi, Y. Muto, Eiji Kurimoto, Fahu He, Akiko Tanaka and Takashi Yabuki and has published in prestigious journals such as Nucleic Acids Research, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

T. Harada

19 papers receiving 450 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
T. Harada Japan 13 351 112 39 38 30 19 450
Kemin Zhou United States 12 398 1.1× 223 2.0× 46 1.2× 35 0.9× 31 1.0× 27 626
Victoria M. Longshaw South Africa 8 399 1.1× 93 0.8× 61 1.6× 24 0.6× 34 1.1× 9 494
Alejandro Carpy Germany 11 443 1.3× 130 1.2× 56 1.4× 24 0.6× 18 0.6× 15 573
Birgitta Tomkinson Sweden 15 536 1.5× 83 0.7× 55 1.4× 37 1.0× 39 1.3× 35 682
Sergei Fedorov United States 6 448 1.3× 101 0.9× 44 1.1× 52 1.4× 19 0.6× 10 637
Lucy S. Chong United States 7 373 1.1× 101 0.9× 14 0.4× 50 1.3× 28 0.9× 7 462
Tsuyoshi Imasaki United States 14 679 1.9× 107 1.0× 44 1.1× 62 1.6× 24 0.8× 23 764
Peter Bandilla Germany 5 495 1.4× 126 1.1× 32 0.8× 47 1.2× 26 0.9× 7 668
Danita G. Ashby United States 5 310 0.9× 105 0.9× 19 0.5× 31 0.8× 12 0.4× 5 388

Countries citing papers authored by T. Harada

Since Specialization
Citations

This map shows the geographic impact of T. Harada'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 T. Harada with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites T. Harada more than expected).

Fields of papers citing papers by T. Harada

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of T. Harada

This figure shows the co-authorship network connecting the top 25 collaborators of T. Harada. A scholar is included among the top collaborators of T. Harada 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 T. Harada. T. Harada is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

19 of 19 papers shown
1.
Nagano, Makoto, Daisuke Hoshino, S. Koshiba, et al.. (2011). ZF21 Protein, a Regulator of the Disassembly of Focal Adhesions and Cancer Metastasis, Contains a Novel Noncanonical Pleckstrin Homology Domain. Journal of Biological Chemistry. 286(36). 31598–31609. 13 indexed citations
2.
Tsuda, Kengo, Tatsuhiko Someya, Kanako Kuwasako, et al.. (2010). Structural basis for the dual RNA-recognition modes of human Tra2-β RRM. Nucleic Acids Research. 39(4). 1538–1553. 55 indexed citations
3.
Goroncy, Alexander K., S. Koshiba, N. Tochio, et al.. (2010). The NMR solution structures of the five constituent cold-shock domains (CSD) of the human UNR (upstream of N-ras) protein. Journal of Structural and Functional Genomics. 11(2). 181–188. 14 indexed citations
4.
He, Fahu, Takashi Umehara, Kohei Saito, et al.. (2010). Structural Insight into the Zinc Finger CW Domain as a Histone Modification Reader. Structure. 18(9). 1127–1139. 91 indexed citations
5.
6.
Nakasako, Masayoshi, Eiji Kurimoto, T. Harada, et al.. (2010). Redox-Dependent Domain Rearrangement of Protein Disulfide Isomerase from a Thermophilic Fungus. Biochemistry. 49(32). 6953–6962. 28 indexed citations
7.
Kamiya, Yukiko, Michiko Nakano, Hiroaki Sasakawa, et al.. (2009). Redox-Dependent Domain Rearrangement of Protein Disulfide Isomerase Coupled with Exposure of Its Substrate-Binding Hydrophobic Surface. Journal of Molecular Biology. 396(2). 361–374. 55 indexed citations
8.
He, Fahu, Kohei Saito, Naohiro Kobayashi, et al.. (2009). Structural and Functional Characterization of the NHR1 Domain of the Drosophila Neuralized E3 Ligase in the Notch Signaling Pathway. Journal of Molecular Biology. 393(2). 478–495. 23 indexed citations
9.
Tochio, N., Shinichi Watanabe, T. Harada, et al.. (2009). Structure of the C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP Reveals a Novel Peptide Binding Mode. Journal of Back and Musculoskeletal Rehabilitation. 1 indexed citations
10.
Li, Hua, S. Koshiba, Fumiaki Hayashi, et al.. (2008). Structure of the C-terminal Phosphotyrosine Interaction Domain of Fe65L1 Complexed with the Cytoplasmic Tail of Amyloid Precursor Protein Reveals a Novel Peptide Binding Mode. Journal of Biological Chemistry. 283(40). 27165–27178. 26 indexed citations
11.
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
12.
Ohnishi, Satoshi, Kimmo Pääkkönen, S. Koshiba, et al.. (2008). Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions. Proteins Structure Function and Bioinformatics. 74(1). 133–144. 13 indexed citations
13.
He, Fahu, Kengo Tsuda, Makoto Inoue, et al.. (2008). Solution structure of the RNA binding domain in the human muscleblind‐like protein 2. Protein Science. 18(1). 80–91. 22 indexed citations
14.
Ohnishi, Satoshi, Peter Güntert, S. Koshiba, et al.. (2007). Solution structure of an atypical WW domain in a novel β‐clam‐like dimeric form. FEBS Letters. 581(3). 462–468. 31 indexed citations
15.
Tochio, N., Takashi Umehara, S. Koshiba, et al.. (2007). Structural and Functional Differences of SWIRM Domain Subtypes. Journal of Molecular Biology. 369(1). 222–238. 39 indexed citations
16.
Kurimoto, Eiji, et al.. (2001). In Vitro Refolding of Porcine Pepsin Immobilized on Agarose Beads. The Journal of Biochemistry. 130(2). 295–297. 17 indexed citations
17.
Harada, T., Eiji Kurimoto, Osamu Asami, et al.. (2001). Disulfide Bond Formation in Refolding of Thermophilic Fungal Protein Disulfide Isomerase.. Journal of Bioscience and Bioengineering. 91(6). 596–598. 1 indexed citations
18.
Harada, T., Eiji Kurimoto, Daisuke Ejima, et al.. (2001). Application of Combined Reagent Solution to the Oxidative Refolding of Recombinant Human Interleukin 6.. Chemical and Pharmaceutical Bulletin. 49(9). 1128–1131. 4 indexed citations
19.
Harada, T., Eiji Kurimoto, Osamu Asami, et al.. (2001). Disulfide bond formation in refolding of thermophilic fungal protein disulfide isomerase. Journal of Bioscience and Bioengineering. 91(6). 596–598. 6 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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