Yoshiko Kikuchi

3.2k total citations
52 papers, 2.7k citations indexed

About

Yoshiko Kikuchi is a scholar working on Molecular Biology, Cell Biology and Genetics. According to data from OpenAlex, Yoshiko Kikuchi has authored 52 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 47 papers in Molecular Biology, 7 papers in Cell Biology and 6 papers in Genetics. Recurrent topics in Yoshiko Kikuchi's work include Fungal and yeast genetics research (19 papers), Ubiquitin and proteasome pathways (12 papers) and RNA and protein synthesis mechanisms (10 papers). Yoshiko Kikuchi is often cited by papers focused on Fungal and yeast genetics research (19 papers), Ubiquitin and proteasome pathways (12 papers) and RNA and protein synthesis mechanisms (10 papers). Yoshiko Kikuchi collaborates with scholars based in Japan, United States and Cameroon. Yoshiko Kikuchi's co-authors include Akio Toh‐e, Jonathan King, Yoshimitsu Takahashi, Hideki Yashiroda, Yukifumi Uesono, Keiji Tanaka, Yasushi Saeki, Daisuke Kaida, Toshiaki Katada and S. Hoshino and has published in prestigious journals such as Cell, Journal of Biological Chemistry and The EMBO Journal.

In The Last Decade

Yoshiko Kikuchi

52 papers receiving 2.6k citations

Peers

Yoshiko Kikuchi
Steven G. Sedgwick United Kingdom
Shirley McCready United Kingdom
Jean D. Beggs United Kingdom
Michel Duguet France
John L. Woolford United States
William K. Holloman United States
Paul A. Fisher United States
Pascal Chartrand Canada
Heinz‐Peter Nasheuer Ireland
Vincent Géli France
Steven G. Sedgwick United Kingdom
Yoshiko Kikuchi
Citations per year, relative to Yoshiko Kikuchi Yoshiko Kikuchi (= 1×) peers Steven G. Sedgwick

Countries citing papers authored by Yoshiko Kikuchi

Since Specialization
Citations

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

Fields of papers citing papers by Yoshiko Kikuchi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Yoshiko Kikuchi

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

All Works

20 of 20 papers shown
1.
2.
Toh‐e, Akio, Yoshiko Kikuchi, Takushi Hachiya, et al.. (2014). Tetracaine, a local anesthetic, preferentially induces translational inhibition with processing body formation rather than phosphorylation of eIF2α in yeast. Current Genetics. 61(1). 43–53. 5 indexed citations
3.
Sasaki, Takeshi, et al.. (2013). Nuclear PP2A-Cdc55 prevents APC-Cdc20 activation during the spindle assembly checkpoint. Journal of Cell Science. 126(19). 4396–4405. 13 indexed citations
4.
Saeki, Yasushi, Tai Kudo, Yoshiko Kikuchi, et al.. (2009). Lysine 63‐linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome. The EMBO Journal. 28(4). 359–371. 211 indexed citations
5.
Takahashi, Yoshimitsu & Yoshiko Kikuchi. (2008). Cytoplasmic sumoylation by PIAS-type Siz1-SUMO ligase. Cell Cycle. 7(12). 1738–1744. 20 indexed citations
6.
Suzuki, Rintaro, et al.. (2008). Solution structures and DNA binding properties of the N‐terminal SAP domains of SUMO E3 ligases from Saccharomyces cerevisiae and Oryza sativa. Proteins Structure Function and Bioinformatics. 75(2). 336–347. 34 indexed citations
7.
Ohkuni, Kentaro, et al.. (2005). Suppressor analysis of the mpt5/htr1/uth4/puf5 deletion in Saccharomyces cerevisiae. Molecular Genetics and Genomics. 275(1). 81–88. 10 indexed citations
8.
Takahashi, Yoshimitsu & Yoshiko Kikuchi. (2005). Yeast PIAS-type Ull1/Siz1 Is Composed of SUMO Ligase and Regulatory Domains. Journal of Biological Chemistry. 280(43). 35822–35828. 42 indexed citations
9.
Hosoda, Nao, Tetsuo Kobayashi, Naoyuki Uchida, et al.. (2003). Translation Termination Factor eRF3 Mediates mRNA Decay through the Regulation of Deadenylation. Journal of Biological Chemistry. 278(40). 38287–38291. 129 indexed citations
10.
Kaida, Daisuke, Hideki Yashiroda, Akio Toh‐e, & Yoshiko Kikuchi. (2002). Yeast Whi2 and Psr1‐phosphatase form a complex and regulate STRE‐mediated gene expression. Genes to Cells. 7(6). 543–552. 76 indexed citations
11.
Takahashi, Yoshimitsu, Tomoaki Kahyo, Akio Toh‐e, Hideyo Yasuda, & Yoshiko Kikuchi. (2001). Yeast Ull1/Siz1 Is a Novel SUMO1/Smt3 Ligase for Septin Components and Functions as an Adaptor between Conjugating Enzyme and Substrates. Journal of Biological Chemistry. 276(52). 48973–48977. 157 indexed citations
12.
Miyajima, Atsuko, Masayuki Seki, Fumitoshi Onoda, et al.. (2000). Sgs1 Helicase Activity Is Required for Mitotic but Apparently Not for Meiotic Functions. Molecular and Cellular Biology. 20(17). 6399–6409. 41 indexed citations
13.
Toh‐e, Akio, et al.. (2000). Yeast Pdr13p and Zuo1p molecular chaperones are new functional Hsp70 and Hsp40 partners. Gene. 257(1). 131–137. 15 indexed citations
14.
Hoshino, S., et al.. (1998). Molecular Cloning of a Novel Member of the Eukaryotic Polypeptide Chain-Releasing Factors (eRF). Journal of Biological Chemistry. 273(35). 22254–22259. 100 indexed citations
15.
Yashiroda, Hideki, Daisuke Kaida, Akio Toh‐e, & Yoshiko Kikuchi. (1998). The PY-motif of Bul1 protein is essential for growth of Saccharomyces cerevisiae under various stress conditions. Gene. 225(1-2). 39–46. 49 indexed citations
16.
Uesono, Yukifumi, Akio Toh‐e, & Yoshiko Kikuchi. (1997). Ssd1p of Saccharomyces cerevisiae Associates with RNA. Journal of Biological Chemistry. 272(26). 16103–16109. 91 indexed citations
17.
Yashiroda, Hideki, Tomoko Oguchi, Yuko Yasuda, Akio Toh‐e, & Yoshiko Kikuchi. (1996). Bul1, a New Protein That Binds to the Rsp5 Ubiquitin Ligase in Saccharomyces cerevisiae. Molecular and Cellular Biology. 16(7). 3255–3263. 92 indexed citations
18.
Takeuchi, Jun, Mitsumasa Okada, Akio Toh‐e, & Yoshiko Kikuchi. (1995). The SMS1 gene encoding a serine-rich transmembrane protein suppresses the temperature sensitivity of the htr1 disruptant in Saccharomyces cerevisiae. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1260(1). 94–96. 16 indexed citations
19.
Kikuchi, Yoshiko, Yoshio Oka, Mariko Kobayashi, et al.. (1994). A new yeast gene, HTR1, required for growth at high temperature, is needed for recovery from mating pheromone-induced G1 arrest. Molecular and General Genetics MGG. 245(1). 107–116. 33 indexed citations
20.
Kikuchi, Yoshiko, et al.. (1988). The primary structure of the leul + gene of Schizosaccharomyces pombe. Current Genetics. 14(4). 375–379. 51 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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