Masatoshi Saiki

411 total citations
12 papers, 324 citations indexed

About

Masatoshi Saiki is a scholar working on Molecular Biology, Physiology and Materials Chemistry. According to data from OpenAlex, Masatoshi Saiki has authored 12 papers receiving a total of 324 indexed citations (citations by other indexed papers that have themselves been cited), including 11 papers in Molecular Biology, 5 papers in Physiology and 4 papers in Materials Chemistry. Recurrent topics in Masatoshi Saiki's work include Protein Structure and Dynamics (7 papers), Alzheimer's disease research and treatments (5 papers) and Enzyme Structure and Function (4 papers). Masatoshi Saiki is often cited by papers focused on Protein Structure and Dynamics (7 papers), Alzheimer's disease research and treatments (5 papers) and Enzyme Structure and Function (4 papers). Masatoshi Saiki collaborates with scholars based in Japan. Masatoshi Saiki's co-authors include Masaki Okumura, Yuji Hidaka, Mamoru Suzuki, Rieko Kojima, Hiroshi Yamaguchi, Shoji Masui, Kenji Inaba, Hisayuki Morii, Takeo Konakahara and Yoshimi Sato and has published in prestigious journals such as Journal of Molecular Biology, Biochemistry and Scientific Reports.

In The Last Decade

Masatoshi Saiki

12 papers receiving 323 citations

Peers

Masatoshi Saiki

MB

CB

PHYSI

IMMUN

EPIDE

Anush Bakunts Italy

Young Ah Kim United States

Maike Thamsen United States

Joanna Bottomley United Kingdom

Bianca Schrul Germany

Akihiko Takasaki Japan

Ritu Kanwar India

Aljona Gutschmidt Germany

Gabriela Ondrovičová Slovakia

Anja Schütz Germany

Anush Bakunts Italy

Masatoshi Saiki

270 ×1.3

MB

141 ×0.9

CB

27 ×0.4

PHYSI

27 ×0.6

IMMUN

68 ×2.2

EPIDE

Citations per year, relative to Masatoshi Saiki Masatoshi Saiki (= 1×) peers Anush Bakunts

Countries citing papers authored by Masatoshi Saiki

Since Specialization

Citations

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

Fields of papers citing papers by Masatoshi Saiki

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Masatoshi Saiki

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

All Works

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12 of 12 papers shown

1.

Kawasaki, Takayasu, Yuusuke Yamaguchi, Toshiaki Ohta, et al.. (2020). Irradiation effect of a submillimeter wave from 420 GHz gyrotron on amyloid peptides in vitro. Biomedical Optics Express. 11(9). 5341–5341. 2 indexed citations

2.

Saiki, Masatoshi, et al.. (2015). Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross‐β region. FEBS Letters. 589(23). 3541–3547. 9 indexed citations

3.

Saiki, Masatoshi, et al.. (2015). Evaluation of the structural stability of amyloid fibrils by dynamic light scattering. 29(1). 24–27. 1 indexed citations

4.

Kojima, Rieko, Masaki Okumura, Shoji Masui, et al.. (2014). Radically Different Thioredoxin Domain Arrangement of ERp46, an Efficient Disulfide Bond Introducer of the Mammalian PDI Family. Structure. 22(3). 431–443. 52 indexed citations

5.

Sato, Yoshimi, Rieko Kojima, Masaki Okumura, et al.. (2013). Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding. Scientific Reports. 3(1). 2456–2456. 122 indexed citations

6.

Saiki, Masatoshi, Yuji Hidaka, Masayuki Nara, & Hisayuki Morii. (2012). Stem-Forming Regions That Are Essential for the Amyloidogenesis of Prion Proteins. Biochemistry. 51(8). 1566–1576. 7 indexed citations

7.

Okumura, Masaki, Masatoshi Saiki, Hiroshi Yamaguchi, & Yuji Hidaka. (2011). Acceleration of disulfide‐coupled protein folding using glutathione derivatives. FEBS Journal. 278(7). 1137–1144. 46 indexed citations

8.

Hidaka, Yuji, et al.. (2010). Fiber formation of a synthetic spider peptide derived from Nephila clavata. Biopolymers. 96(2). 222–227. 3 indexed citations

9.

Saiki, Masatoshi, et al.. (2009). Recognition of the N-Terminal Histone H2A and H3 Peptides by Peptidylarginine Deiminase IV. Protein and Peptide Letters. 16(9). 1012–1016. 16 indexed citations

10.

Saiki, Masatoshi, Takeo Konakahara, & Hisayuki Morii. (2006). Interaction-based evaluation of the propensity for amyloid formation with cross-β structure. Biochemical and Biophysical Research Communications. 343(4). 1262–1271. 15 indexed citations

11.

Morii, Hisayuki, Masatoshi Saiki, Takeo Konakahara, & Miyuki Ishimura. (2006). Peripheral region for core cross-β plays important role in amyloidogenicity. Biochemical and Biophysical Research Communications. 342(3). 808–816. 3 indexed citations

12.

Saiki, Masatoshi, Shinya Honda, Kazunori Kawasaki, et al.. (2005). Higher-order Molecular Packing in Amyloid-like Fibrils Constructed with Linear Arrangements of Hydrophobic and Hydrogen-bonding Side-chains. Journal of Molecular Biology. 348(4). 983–998. 48 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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