Kyoko Suto

939 total citations
19 papers, 760 citations indexed

About

Kyoko Suto is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, Kyoko Suto has authored 19 papers receiving a total of 760 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 4 papers in Materials Chemistry and 3 papers in Organic Chemistry. Recurrent topics in Kyoko Suto's work include Enzyme Structure and Function (4 papers), Porphyrin Metabolism and Disorders (3 papers) and Inorganic and Organometallic Chemistry (3 papers). Kyoko Suto is often cited by papers focused on Enzyme Structure and Function (4 papers), Porphyrin Metabolism and Disorders (3 papers) and Inorganic and Organometallic Chemistry (3 papers). Kyoko Suto collaborates with scholars based in Japan and United States. Kyoko Suto's co-authors include Y. Morimoto, Noritake Yasuoka, Naoki Shibata, Hiroshi Mizuno, Takashi Morita, Yasuo Yamazaki, Tetsuo Toraya, Takamasa Tobimatsu, Jun Masuda and Issei Mabuchi and has published in prestigious journals such as Nature, Journal of Biological Chemistry and The EMBO Journal.

In The Last Decade

Kyoko Suto

19 papers receiving 748 citations

Peers

Kyoko Suto
Craig T. Armstrong United Kingdom
Douglas S. Daniels United States
Anthony P. Duff Australia
Narendra Narayana United States
G.M.T. Cheetham United States
K.A. Weyer Switzerland
Kyoko Suto
Citations per year, relative to Kyoko Suto Kyoko Suto (= 1×) peers Metaxia Vlassi

Countries citing papers authored by Kyoko Suto

Since Specialization
Citations

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

Fields of papers citing papers by Kyoko Suto

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kyoko Suto

This figure shows the co-authorship network connecting the top 25 collaborators of Kyoko Suto. A scholar is included among the top collaborators of Kyoko Suto 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 Kyoko Suto. Kyoko Suto 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.
Watanabe, Hideki, et al.. (2009). Optimizing pH Response of Affinity between Protein G and IgG Fc. Journal of Biological Chemistry. 284(18). 12373–12383. 46 indexed citations
2.
Suto, Kyoko, Hiromi Masuda, Yasuhiro Takenaka, Frederick I. Tsuji, & Hiroshi Mizuno. (2009). Structural basis for red‐shifted emission of a GFP‐like protein from the marine copepod Chiridius poppei. Genes to Cells. 14(6). 727–737. 14 indexed citations
3.
Watanabe, Kazunori, Yukimatsu Toh, Kyoko Suto, et al.. (2007). Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase. Nature. 449(7164). 867–871. 71 indexed citations
4.
Kitamura, Mitsuru, H. Inoue, Tomohiro Hayashida, et al.. (2007). Determination of the Role of the Carboxyl-terminal Leucine-122 in FMN-binding Protein by Mutational and Structural Analysis. The Journal of Biochemistry. 141(4). 459–468. 9 indexed citations
5.
Suto, Kyoko, et al.. (2006). Structure of an RNA duplex r(GGCGBrUGCGCU)2with terminal and internal tandem G·U base pairs. Acta Crystallographica Section D Biological Crystallography. 62(3). 331–338. 6 indexed citations
6.
Suto, Kyoko, Yoshihiro Shimizu, Kazunori Watanabe, et al.. (2006). Crystal structures of leucyl/phenylalanyl‐tRNA‐protein transferase and its complex with an aminoacyl‐tRNA analog. The EMBO Journal. 25(24). 5942–5950. 49 indexed citations
7.
Shikamoto, Yasuo, Kyoko Suto, Yasuo Yamazaki, Takashi Morita, & Hiroshi Mizuno. (2005). Crystal Structure of a CRISP Family Ca2+-channel Blocker Derived from Snake Venom. Journal of Molecular Biology. 350(4). 735–743. 88 indexed citations
8.
Suto, Kyoko, Yasuo Yamazaki, Takashi Morita, & Hiroshi Mizuno. (2004). Crystal Structures of Novel Vascular Endothelial Growth Factors (VEGF) from Snake Venoms. Journal of Biological Chemistry. 280(3). 2126–2131. 79 indexed citations
9.
Hamada, Kensaku, et al.. (2003). Expression, purification, crystallization and preliminary X-ray studies of geranylgeranyl diphosphate synthase fromThermus thermophilusHB8. Acta Crystallographica Section D Biological Crystallography. 60(1). 178–180. 2 indexed citations
10.
Yamanishi, Mamoru, Takamasa Tobimatsu, Hideaki Sato, et al.. (2002). The crystal structure of coenzyme B12‐dependent glycerol dehydratase in complex with cobalamin and propane‐1,2‐diol. European Journal of Biochemistry. 269(18). 4484–4494. 94 indexed citations
11.
Suto, Kyoko, et al.. (2000). How do the X-ray structure and the NMR structure of FMN-binding protein differ?. Acta Crystallographica Section D Biological Crystallography. 56(3). 368–371. 29 indexed citations
12.
Shibata, Naoki, Jun Masuda, Takamasa Tobimatsu, et al.. (1999). A new mode of B12 binding and the direct participation of a potassium ion in enzyme catalysis: X-ray structure of diol dehydratase. Structure. 7(8). 997–1008. 183 indexed citations
13.
Suto, Kyoko, Naoki Shibata, Y. Morimoto, et al.. (1999). Crystallization and preliminary crystallographic studies of FMN-binding protein fromDesulfovibrio vulgarisMiyazaki F. Acta Crystallographica Section D Biological Crystallography. 55(5). 1089–1090. 4 indexed citations
14.
Masuda, Jun, Takamasa Tobimatsu, Tetsuo Toraya, et al.. (1999). Crystallization and preliminary X-ray study of two crystal forms of Klebsiella oxytoca diol dehydratase–cyanocobalamin complex. Acta Crystallographica Section D Biological Crystallography. 55(4). 907–909. 9 indexed citations
15.
Suto, Kyoko & Issei Mabuchi. (1989). End-label fingerprintings show that an N-terminal segment of depactin participates in interaction with actin. Biochemistry. 28(1). 102–106. 40 indexed citations
16.
Iwai, Makoto, Kyoko Suto, Satoru Nakashima, et al.. (1986). Studies on the Valence State of Iron Atoms in the Mixed-Valence Binuclear Ferrocenes by X-Ray Absorption Near Edge Structure (XANES) and by X-Ray Photoelectron Spectroscopy (XPS). Bulletin of the Chemical Society of Japan. 59(9). 2675–2681. 19 indexed citations
17.
Suto, Kyoko, Motomi Katada, Izumi Motoyama, & Hirotoshi Sano. (1985). MÖSSBAUER SPECTROSCOPIC STUDY ON 1′-MONOHALOBIFERROCENES. Chemistry Letters. 14(4). 433–436. 3 indexed citations
18.
Watanabe, Masanobu, Kyoko Suto, Izumi Motoyama, & Hirotoshi Sano. (1984). MÖSSBAUER SPECTROSCOPIC STUDIES OF MERCURY(II) CHLORIDE ADDUCTS OF BIFERROCENE AND BIFERROCENYLENE. Chemistry Letters. 13(8). 1317–1320. 4 indexed citations
19.
Motoyama, Izumi, Kyoko Suto, Motomi Katada, & Hirotoshi Sano. (1983). MÖSSSBAUER SPECTROSCOPIC AND ELECTROCHEMICAL STUDIES ON 1′,1'″-DIHALOBIFERROCENES. Chemistry Letters. 12(8). 1215–1218. 11 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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