Yoshiro Saimi

4.1k total citations
78 papers, 3.2k citations indexed

About

Yoshiro Saimi is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Plant Science. According to data from OpenAlex, Yoshiro Saimi has authored 78 papers receiving a total of 3.2k indexed citations (citations by other indexed papers that have themselves been cited), including 66 papers in Molecular Biology, 32 papers in Cellular and Molecular Neuroscience and 27 papers in Plant Science. Recurrent topics in Yoshiro Saimi's work include Protist diversity and phylogeny (33 papers), Ion channel regulation and function (27 papers) and Photoreceptor and optogenetics research (22 papers). Yoshiro Saimi is often cited by papers focused on Protist diversity and phylogeny (33 papers), Ion channel regulation and function (27 papers) and Photoreceptor and optogenetics research (22 papers). Yoshiro Saimi collaborates with scholars based in United States, Japan and United Kingdom. Yoshiro Saimi's co-authors include Ching Kung, Stephen H. Loukin, C Kung, Xinliang Zhou, Robin R. Preston, Boris Martinac, W. John Haynes, Robert D. Hinrichsen, Kit‐Yin Ling and Zhenwei Su and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Yoshiro Saimi

78 papers receiving 3.1k citations

Peers

Yoshiro Saimi

CMN

Michael Whitaker United Kingdom

Joachim E. Schultz Germany

William B. Busa United States

L. F. Jaffe United States

Luigia Santella Italy

Pedro Labarca Chile

Clifford L. Slayman United States

Donner F. Babcock United States

Laurinda A. Jaffe United States

Naoyuki Iwabe Japan

Michael Whitaker United Kingdom

Yoshiro Saimi

2.9k ×1.2

1.1k ×1.0

CMN

707 ×0.9

280 ×0.6

1.3k ×3.9

Citations per year, relative to Yoshiro Saimi Yoshiro Saimi (= 1×) peers Michael Whitaker

Countries citing papers authored by Yoshiro Saimi

Since Specialization

Citations

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

Fields of papers citing papers by Yoshiro Saimi

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Yoshiro Saimi

This figure shows the co-authorship network connecting the top 25 collaborators of Yoshiro Saimi. A scholar is included among the top collaborators of Yoshiro Saimi 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 Yoshiro Saimi. Yoshiro Saimi 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

Su, Zhenwei, Andriy Anishkin, Ching Kung, & Yoshiro Saimi. (2011). The core domain as the force sensor of the yeast mechanosensitive TRP channel. The Journal of General Physiology. 138(6). 627–640. 15 indexed citations

Su, Zhenwei, Ching Kung, & Yoshiro Saimi. (2010). Dissecting the Molecular Mechanism of How Force Activates Yeast TRP Channel TRPY1. Biophysical Journal. 98(3). 324a–324a. 1 indexed citations

Su, Zhenwei, Xinliang Zhou, Stephen H. Loukin, et al.. (2009). The use of yeast to understand TRP-channel mechanosensitivity. Pflügers Archiv - European Journal of Physiology. 458(5). 861–867. 24 indexed citations

Su, Zhenwei, Xinliang Zhou, Stephen H. Loukin, Yoshiro Saimi, & Ching Kung. (2009). Mechanical Force and Cytoplasmic Ca2+ Activate Yeast TRPY1 in Parallel. The Journal of Membrane Biology. 227(3). 141–150. 30 indexed citations

Haynes, W. John, Xinliang Zhou, Zhenwei Su, et al.. (2008). Indole and other aromatic compounds activate the yeast TRPY1 channel. FEBS Letters. 582(10). 1514–1518. 17 indexed citations

Martinac, Boris, Yoshiro Saimi, & Ching Kung. (2008). Ion Channels in Microbes. Physiological Reviews. 88(4). 1449–1490. 160 indexed citations

Kuo, Mario Meng-Chiang, Yoshiro Saimi, Ching Kung, & Senyon Choe. (2007). Patch Clamp and Phenotypic Analyses of a Prokaryotic Cyclic Nucleotide-gated K+ Channel Using Escherichia coli as a Host. Journal of Biological Chemistry. 282(33). 24294–24301. 23 indexed citations

Kuo, Mario Meng-Chiang, W. John Haynes, Stephen H. Loukin, Ching Kung, & Yoshiro Saimi. (2005). Prokaryotic K⁺channels: From crystal structures to diversity. FEMS Microbiology Reviews. 29(5). 961–985. 98 indexed citations

Kung, Ching, Yoshiro Saimi, W. John Haynes, Kit‐Yin Ling, & Roland Kissmehl. (2000). Recent Advances in the Molecular Genetics of Paramecium¹. Journal of Eukaryotic Microbiology. 47(1). 11–14. 10 indexed citations

10.

Chan, Catherine W. M., Yoshiro Saimi, & Ching Kung. (1999). A new multigene family encoding calcium-dependent calmodulin-binding membrane proteins of Paramecium tetraurelia. Gene. 231(1-2). 21–32. 21 indexed citations

11.

Vaillant, Brian, et al.. (1995). YKC1 encodes the depolarization‐activated K⁺ channel in the plasma membrane of yeast. FEBS Letters. 373(2). 170–176. 83 indexed citations

12.

Haynes, W. John, Kit‐Yin Ling, Yoshiro Saimi, & Ching Kung. (1995). Induction of Antibiotic Resistance in Paramecium tetraurelia by the Bacterial Gene APH‐3'‐II. Journal of Eukaryotic Microbiology. 42(1). 83–91. 38 indexed citations

13.

Saimi, Yoshiro & Ching Kung. (1994). Ion channel regulation by calmodulin binding. FEBS Letters. 350(2-3). 155–158. 62 indexed citations

14.

Ling, Kit‐Yin, Robin R. Preston, Robert Burns, et al.. (1992). Primary mutations in calmodulin prevent activation of the Ca^{+ +}‐dependent Na⁺ channel in Paramecium. Proteins Structure Function and Bioinformatics. 12(4). 365–371. 6 indexed citations

15.

Preston, Robin R., Yoshiro Saimi, & C Kung. (1992). Calcium current activated upon hyperpolarization of Paramecium tetraurelia.. The Journal of General Physiology. 100(2). 233–251. 54 indexed citations

16.

Kung, C, et al.. (1992). In vivo Paramecium mutants show that calmodulin orchestrates membrane responses to stimuli. Cell Calcium. 13(6-7). 413–425. 48 indexed citations

17.

Kink, John A., et al.. (1990). Mutations in paramecium calmodulin indicate functional differences between the C-terminal and N-terminal lobes in vivo. Cell. 62(1). 165–174. 120 indexed citations

18.

Kubalski, Andrzej, Boris Martinac, & Yoshiro Saimi. (1989). Proteolytic activation of a hyperpolarization- and calcium-dependent potassium channel inParamecium. The Journal of Membrane Biology. 112(1). 91–96. 17 indexed citations

19.

Saimi, Yoshiro & Boris Martinac. (1989). Calcium-dependent potassium channel inParamecium studied under patch clamp. The Journal of Membrane Biology. 112(1). 79–89. 31 indexed citations

20.

Suzuki, Tatsuo, et al.. (1974). Studies on cephalopod rhodopsin. Conformational changes in chromophore and protein during the photoregeneration process. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 333(1). 149–160. 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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