T. Arakawa

2.4k total citations
53 papers, 1.6k citations indexed

About

T. Arakawa is a scholar working on Molecular Biology, Biotechnology and Materials Chemistry. According to data from OpenAlex, T. Arakawa has authored 53 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 21 papers in Biotechnology and 19 papers in Materials Chemistry. Recurrent topics in T. Arakawa's work include Enzyme Production and Characterization (20 papers), Enzyme Structure and Function (19 papers) and Glycosylation and Glycoproteins Research (8 papers). T. Arakawa is often cited by papers focused on Enzyme Production and Characterization (20 papers), Enzyme Structure and Function (19 papers) and Glycosylation and Glycoproteins Research (8 papers). T. Arakawa collaborates with scholars based in Japan, Australia and United Kingdom. T. Arakawa's co-authors include Shinya Fushinobu, Tatsuro Shimamura, So Iwata, Masafumi Yohda, Norimichi Nomura, Takuya Kobayashi, Takao Hamakubo, Takeshi Murata, Tomoya Hino and Alexander D. Cameron and has published in prestigious journals such as Nature, Science and Journal of the American Chemical Society.

In The Last Decade

T. Arakawa

51 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
T. Arakawa Japan	21	1.1k	234	213	195	180	53	1.6k
Jamshid Davoodi Iran	19	1.1k 1.0×	222 0.9×	88 0.4×	94 0.5×	200 1.1×	46	1.7k
Yraima Cordeiro Brazil	34	2.5k 2.4×	165 0.7×	454 2.1×	262 1.3×	87 0.5×	97	3.1k
David R Grubb Australia	13	1.2k 1.2×	73 0.3×	93 0.4×	100 0.5×	105 0.6×	22	1.9k
Yijian Rao China	19	750 0.7×	77 0.3×	109 0.5×	126 0.6×	147 0.8×	88	1.5k
Tadao Terao Japan	26	1.1k 1.1×	153 0.7×	139 0.7×	129 0.7×	127 0.7×	96	2.0k
Michael J. McLeish United States	28	1.3k 1.3×	83 0.4×	59 0.3×	224 1.1×	114 0.6×	93	2.4k
Daniel Rettori Brazil	16	978 0.9×	130 0.6×	122 0.6×	88 0.5×	77 0.4×	22	1.8k
Mikael Widersten Sweden	29	2.4k 2.3×	64 0.3×	82 0.4×	151 0.8×	141 0.8×	82	3.1k
Hideyuki Hayashi Japan	32	1.9k 1.8×	139 0.6×	270 1.3×	822 4.2×	47 0.3×	93	2.9k
Jason G. McCoy United States	23	1.1k 1.0×	55 0.2×	82 0.4×	173 0.9×	55 0.3×	41	1.6k

Countries citing papers authored by T. Arakawa

Since Specialization

Citations

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

Fields of papers citing papers by T. Arakawa

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

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

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

All Works

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20 of 20 papers shown

1.

Gerle, Christoph, et al.. (2024). Structural insights into thermophilic chaperonin complexes. Structure. 32(6). 679–689.e4. 2 indexed citations

2.

Doi, Yuki, Shunsuke Masuo, T. Arakawa, et al.. (2023). Protocatechuate hydroxylase is a novel group A flavoprotein monooxygenase with a unique substrate recognition mechanism. Journal of Biological Chemistry. 300(1). 105508–105508. 3 indexed citations

3.

Nakaya, Makoto, Shigeo Takenaka, T. Arakawa, et al.. (2021). Biochemical and structural characterization of a novel 4‐ O ‐α‐ l ‐rhamnosyl‐β‐ d ‐glucuronidase from Fusarium oxysporum. FEBS Journal. 288(16). 4918–4938. 6 indexed citations

4.

McGregor, Nicholas G. S., Marta Artola, Alba Nin‐Hill, et al.. (2021). Cysteine Nucleophiles in Glycosidase Catalysis: Application of a Covalent β‐l‐Arabinofuranosidase Inhibitor. Angewandte Chemie. 133(11). 5818–5822. 4 indexed citations

5.

McGregor, Nicholas G. S., Marta Artola, Alba Nin‐Hill, et al.. (2021). Cysteine Nucleophiles in Glycosidase Catalysis: Application of a Covalent β‐l‐Arabinofuranosidase Inhibitor. Angewandte Chemie International Edition. 60(11). 5754–5758. 20 indexed citations

6.

Nam, Youngwoo, Mamoru Nishimoto, T. Arakawa, Motomitsu Kitaoka, & Shinya Fushinobu. (2019). Structural basis for broad substrate specificity of UDP-glucose 4-epimerase in the human milk oligosaccharide catabolic pathway of Bifidobacterium longum. Scientific Reports. 9(1). 11081–11081. 20 indexed citations

7.

Arakawa, T., Chihaya Yamada, Takashi Kinoshita, et al.. (2019). Structural basis for the specific cleavage of core-fucosylated N-glycans by endo-β-N-acetylglucosaminidase from the fungus Cordyceps militaris. Journal of Biological Chemistry. 294(45). 17143–17154. 14 indexed citations

8.

Arakawa, T., et al.. (2018). Structural features of a bacterial cyclic α-maltosyl-(1→6)-maltose (CMM) hydrolase critical for CMM recognition and hydrolysis. Journal of Biological Chemistry. 293(43). 16874–16888. 7 indexed citations

9.

Liebschner, Dorothée, Yusuke Yamada, Naohiro Matsugaki, et al.. (2017). The first crystal structure of a family 129 glycoside hydrolase from a probiotic bacterium reveals critical residues and metal cofactors. Journal of Biological Chemistry. 292(29). 12126–12138. 20 indexed citations

10.

Abe, Koichi, Masahiro Nakajima, Tetsuro Yamashita, et al.. (2017). Biochemical and structural analyses of a bacterial endo-β-1,2-glucanase reveal a new glycoside hydrolase family. Journal of Biological Chemistry. 292(18). 7487–7506. 34 indexed citations

11.

Arakawa, T., et al.. (2015). Open–close structural change upon ligand binding and two magnesium ions required for the catalysis of N-acetylhexosamine 1-kinase. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854(5). 333–340. 14 indexed citations

12.

Nam, Youngwoo, Takanori Nihira, T. Arakawa, et al.. (2015). Crystal Structure and Substrate Recognition of Cellobionic Acid Phosphorylase, Which Plays a Key Role in Oxidative Cellulose Degradation by Microbes. Journal of Biological Chemistry. 290(30). 18281–18292. 18 indexed citations

13.

Koike‐Takeshita, Ayumi, T. Arakawa, Hideki Taguchi, & Tatsuro Shimamura. (2014). Crystal Structure of a Symmetric Football-Shaped GroEL:GroES2-ATP14 Complex Determined at 3.8 Å Reveals Rearrangement between Two GroEL Rings. Journal of Molecular Biology. 426(21). 3634–3641. 44 indexed citations

14.

Nomura, Yayoi, T. Arakawa, Tomoya Hino, et al.. (2014). Proteoliposome-based Selection of a Recombinant Antibody Fragment Against the Human M2 Muscarinic Acetylcholine Receptor. Monoclonal Antibodies in Immunodiagnosis and Immunotherapy. 33(6). 378–385. 16 indexed citations

15.

Sakamoto, Satoko, Toshimasa Ishizaki, Katsuya Okawa, et al.. (2012). Liprin-α controls stress fiber formation by binding to mDia and regulating its membrane localization. Journal of Cell Science. 125(1). 108–120. 32 indexed citations

16.

Hino, Tomoya, T. Arakawa, Hiroko Iwanari, et al.. (2012). G-protein-coupled receptor inactivation by an allosteric inverse-agonist antibody. Nature. 482(7384). 237–240. 239 indexed citations

17.

Ohtaki, Akashi, Ryo Iizuka, T. Arakawa, et al.. (2007). Structure of aspartate racemase complexed with a dual substrate analogue, citric acid, and implications for the reaction mechanism. Proteins Structure Function and Bioinformatics. 70(4). 1167–1174. 21 indexed citations

18.

Ohtaki, Akashi, Hiroshi Kida, Naoki Ide, et al.. (2007). Structure and Molecular Dynamics Simulation of Archaeal Prefoldin: The Molecular Mechanism for Binding and Recognition of Nonnative Substrate Proteins. Journal of Molecular Biology. 376(4). 1130–1141. 45 indexed citations

19.

Arakawa, T., Yoshiaki Kawano, Yoko Katayama, et al.. (2006). Structure of Thiocyanate Hydrolase: A New Nitrile Hydratase Family Protein with a Novel Five-coordinate Cobalt(III) Center. Journal of Molecular Biology. 366(5). 1497–1509. 63 indexed citations

20.

Arakawa, T., Shota Hori, Yoko Katayama, et al.. (2006). Functional expression of thiocyanate hydrolase is promoted by its activator protein, P15K. FEBS Letters. 580(19). 4667–4672. 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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