Ryoko Maesaki

823 total citations
18 papers, 679 citations indexed

About

Ryoko Maesaki is a scholar working on Molecular Biology, Cell Biology and Immunology and Allergy. According to data from OpenAlex, Ryoko Maesaki has authored 18 papers receiving a total of 679 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 10 papers in Cell Biology and 5 papers in Immunology and Allergy. Recurrent topics in Ryoko Maesaki's work include Protein Kinase Regulation and GTPase Signaling (6 papers), Cell Adhesion Molecules Research (5 papers) and Enzyme Structure and Function (5 papers). Ryoko Maesaki is often cited by papers focused on Protein Kinase Regulation and GTPase Signaling (6 papers), Cell Adhesion Molecules Research (5 papers) and Enzyme Structure and Function (5 papers). Ryoko Maesaki collaborates with scholars based in Japan, United States and Czechia. Ryoko Maesaki's co-authors include Toshio Hakoshima, Shin‐ichi Terawaki, Kozo Kaibuchi, Toshiyuki Shimizu, Kentaro Ihara, Ken Kitano, Shinya Kuroda, Tomoyuki Mori, Takashi Watanabe and Masaki Fukata and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Ryoko Maesaki

18 papers receiving 672 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ryoko Maesaki Japan 11 495 335 85 81 68 18 679
Véronique Pizon France 16 814 1.6× 354 1.1× 81 1.0× 118 1.5× 42 0.6× 19 1.1k
Saara Hämälistö Finland 8 382 0.8× 302 0.9× 69 0.8× 76 0.9× 23 0.3× 11 805
Paul A. Bromann United States 9 453 0.9× 224 0.7× 102 1.2× 145 1.8× 16 0.2× 10 734
Haiqing Yi United States 19 533 1.1× 154 0.5× 44 0.5× 81 1.0× 50 0.7× 34 851
Stavroula Mili United States 17 1.4k 2.7× 258 0.8× 23 0.3× 90 1.1× 138 2.0× 23 1.6k
Vadym Sulimenko Czechia 19 638 1.3× 505 1.5× 41 0.5× 53 0.7× 14 0.2× 41 930
Antonio Ferreira United Kingdom 5 438 0.9× 381 1.1× 39 0.5× 54 0.7× 13 0.2× 7 676
William T. Wong United States 12 461 0.9× 168 0.5× 46 0.5× 70 0.9× 8 0.1× 12 657
Diego Pulido Spain 12 555 1.1× 113 0.3× 35 0.4× 95 1.2× 19 0.3× 20 791
Aie Kawajiri Japan 11 1.1k 2.3× 1.0k 3.1× 58 0.7× 257 3.2× 43 0.6× 12 1.4k

Countries citing papers authored by Ryoko Maesaki

Since Specialization
Citations

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

Fields of papers citing papers by Ryoko Maesaki

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ryoko Maesaki

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

All Works

18 of 18 papers shown
1.
Murase, Kohji, Yoshitaka Moriwaki, Tomoyuki Mori, et al.. (2020). Mechanism of self/nonself-discrimination in Brassica self-incompatibility. Nature Communications. 11(1). 4916–4916. 29 indexed citations
2.
Maesaki, Ryoko, Ryosuke Satoh, Masato Taoka, et al.. (2014). Efficient and cost effective production of active-form human PKB using silkworm larvae. Scientific Reports. 4(1). 6016–6016. 9 indexed citations
3.
Takizawa, Naoki, et al.. (2013). Structural Insights into the Recruitment of SMRT by the Corepressor SHARP under Phosphorylative Regulation. Structure. 22(1). 35–46. 22 indexed citations
4.
Maesaki, Ryoko, et al.. (2012). Microtubule-binding sites of the CH domain of EB1 and its autoinhibition revealed by NMR. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1834(2). 499–507. 10 indexed citations
5.
Mori, Tomoyuki, et al.. (2008). Structural basis for CD44 recognition by ERM proteins. Acta Crystallographica Section A Foundations of Crystallography. 64(a1). C233–C234. 1 indexed citations
6.
Mori, Tomoyuki, et al.. (2008). Structural Basis for CD44 Recognition by ERM Proteins. Journal of Biological Chemistry. 283(43). 29602–29612. 107 indexed citations
7.
Kitano, Ken, et al.. (2008). Structural Basis of the Cytoplasmic Tail of Adhesion Molecule CD43 and Its Binding to ERM Proteins. Journal of Molecular Biology. 381(3). 634–644. 28 indexed citations
8.
Kitano, Ken, et al.. (2007). Structural basis of PSGL‐1 binding to ERM proteins. Genes to Cells. 12(12). 1329–1338. 34 indexed citations
9.
Mori, Tomoyuki, Ken Kitano, Shin‐ichi Terawaki, Ryoko Maesaki, & Toshio Hakoshima. (2007). Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of adhesion molecule CD44. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63(10). 844–847. 10 indexed citations
10.
Maesaki, Ryoko, et al.. (2007). Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition. Proceedings of the National Academy of Sciences. 104(25). 10346–10351. 95 indexed citations
11.
Terawaki, Shin‐ichi, Ryoko Maesaki, & Toshio Hakoshima. (2006). Structural Basis for NHERF Recognition by ERM Proteins. Structure. 14(4). 777–789. 82 indexed citations
12.
Kitano, Ken, et al.. (2006). Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63(1). 49–51. 7 indexed citations
13.
Shimizu, Toshiyuki, Kentaro Ihara, Ryoko Maesaki, et al.. (2003). Parallel Coiled-coil Association of the RhoA-binding Domain in Rho-kinase. Journal of Biological Chemistry. 278(46). 46046–46051. 47 indexed citations
14.
Terawaki, Shin‐ichi, Ryoko Maesaki, Kengo Okada, & Toshio Hakoshima. (2002). Crystallographic characterization of the radixin FERM domain bound to the C-terminal region of the human Na+/H+-exchanger regulatory factor (NHERF). Acta Crystallographica Section D Biological Crystallography. 59(1). 177–179. 12 indexed citations
15.
Ihara, Kentaro, Toshiyuki Shimizu, Ryoko Maesaki, et al.. (2000). Crystallization and preliminary crystallographic analysis of the Rho-binding domain of bovine Rho-kinase. Acta Crystallographica Section D Biological Crystallography. 56(8). 1042–1044. 1 indexed citations
16.
Shimizu, Toshiyuki, Kentaro Ihara, Ryoko Maesaki, et al.. (2000). An Open Conformation of Switch I Revealed by the Crystal Structure of a Mg2+-free Form of RHOA Complexed with GDP. Journal of Biological Chemistry. 275(24). 18311–18317. 50 indexed citations
17.
Maesaki, Ryoko, Toshiyuki Shimizu, Kentaro Ihara, et al.. (1999). Biochemical and Crystallographic Characterization of a Rho Effector Domain of the Protein Serine/Threonine Kinase N in a Complex with RhoA. Journal of Structural Biology. 126(2). 166–170. 7 indexed citations
18.
Maesaki, Ryoko, Kentaro Ihara, Toshiyuki Shimizu, et al.. (1999). The Structural Basis of Rho Effector Recognition Revealed by the Crystal Structure of Human RhoA Complexed with the Effector Domain of PKN/PRK1. Molecular Cell. 4(5). 793–803. 128 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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