Masaru Yamanaka

459 total citations
32 papers, 360 citations indexed

About

Masaru Yamanaka is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Masaru Yamanaka has authored 32 papers receiving a total of 360 indexed citations (citations by other indexed papers that have themselves been cited), including 28 papers in Molecular Biology, 14 papers in Materials Chemistry and 12 papers in Cell Biology. Recurrent topics in Masaru Yamanaka's work include Photosynthetic Processes and Mechanisms (16 papers), Protein Structure and Dynamics (15 papers) and Enzyme Structure and Function (13 papers). Masaru Yamanaka is often cited by papers focused on Photosynthetic Processes and Mechanisms (16 papers), Protein Structure and Dynamics (15 papers) and Enzyme Structure and Function (13 papers). Masaru Yamanaka collaborates with scholars based in Japan, India and Indonesia. Masaru Yamanaka's co-authors include Yoshihiro Sambongi, Shun Hirota, Satoshi Nagao, Yoshiki Higuchi, Shigetoshi Aono, Hirofumi Komori, Hitomi Sawai, Hiroshi Sugimoto, Yoshitsugu Shiro and Satoshi Wakai and has published in prestigious journals such as Journal of Biological Chemistry, The Journal of Chemical Physics and PLoS ONE.

In The Last Decade

Masaru Yamanaka

32 papers receiving 359 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Masaru Yamanaka Japan 13 312 106 106 39 27 32 360
Alexander Christiansen Sweden 8 349 1.1× 69 0.7× 163 1.5× 16 0.4× 30 1.1× 11 423
Michael K. Helms United States 10 290 0.9× 115 1.1× 80 0.8× 12 0.3× 31 1.1× 17 378
Elles Steensma Netherlands 11 353 1.1× 64 0.6× 168 1.6× 15 0.4× 14 0.5× 15 417
Andrzej Szczepaniak Poland 13 512 1.6× 92 0.9× 80 0.8× 20 0.5× 61 2.3× 29 570
Sivashankar G. Sivakolundu United States 8 455 1.5× 106 1.0× 147 1.4× 20 0.5× 12 0.4× 9 543
Christina L. Vizcarra United States 14 382 1.2× 180 1.7× 80 0.8× 8 0.2× 35 1.3× 20 578
Stefan Ganscha Switzerland 5 277 0.9× 33 0.3× 115 1.1× 19 0.5× 12 0.4× 6 415
Jang-Su Park South Korea 13 306 1.0× 64 0.6× 26 0.2× 22 0.6× 43 1.6× 31 477
Nelli Erwin Germany 12 244 0.8× 44 0.4× 46 0.4× 12 0.3× 30 1.1× 19 313
Roshan Mammen Regy United States 9 732 2.3× 33 0.3× 97 0.9× 21 0.5× 11 0.4× 10 802

Countries citing papers authored by Masaru Yamanaka

Since Specialization
Citations

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

Fields of papers citing papers by Masaru Yamanaka

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Masaru Yamanaka

This figure shows the co-authorship network connecting the top 25 collaborators of Masaru Yamanaka. A scholar is included among the top collaborators of Masaru Yamanaka 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 Masaru Yamanaka. Masaru Yamanaka 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.
Yamanaka, Masaru, et al.. (2024). Construction of ligand-binding controlled hemoprotein assemblies utilizing 3D domain swapping. Chemical Communications. 60(70). 9440–9443. 1 indexed citations
2.
Zhang, Mohan, Hulin Tai, Sachiko Yanagisawa, et al.. (2023). Resonance Raman Studies on Heme Ligand Stretching Modes in Methionine80-Depleted Cytochrome c: Fe–His, Fe–O2, and O–O Stretching Modes. The Journal of Physical Chemistry B. 127(11). 2441–2449. 8 indexed citations
3.
Fujiyoshi, So, et al.. (2021). Thermal destabilization mechanism of cytochrome c′ from psychrophilic Shewanella violacea. Bioscience Biotechnology and Biochemistry. 85(5). 1121–1127. 2 indexed citations
4.
Yamanaka, Masaru, et al.. (2021). Construction of ferritin hydrogels utilizing subunit–subunit interactions. PLoS ONE. 16(11). e0259052–e0259052. 3 indexed citations
5.
Yamanaka, Masaru, et al.. (2020). 3D domain swapping of azurin fromAlcaligenes xylosoxidans. Metallomics. 12(3). 337–345. 9 indexed citations
6.
Yamanaka, Masaru, Satoshi Nagao, Kazuma Yasuhara, et al.. (2019). Protein surface charge effect on 3D domain swapping in cells for c-type cytochromes. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1867(11). 140265–140265. 7 indexed citations
7.
Nagao, Satoshi, Masaru Yamanaka, Hiroki Watanabe, et al.. (2018). Construction of a Triangle‐Shaped Trimer and a Tetrahedron Using an α‐Helix‐Inserted Circular Permutant of Cytochrome c555. Chemistry - An Asian Journal. 13(8). 964–967. 8 indexed citations
8.
Ren, Chunguang, et al.. (2018). Oxidative modification of methionine80 in cytochrome c by reaction with peroxides. Journal of Inorganic Biochemistry. 182. 200–207. 15 indexed citations
9.
Yamanaka, Masaru, et al.. (2017). Difference in NaCl tolerance of membrane-bound 5′-nucleotidases purified from deep-sea and brackish water Shewanella species. Extremophiles. 21(2). 357–368. 8 indexed citations
10.
Yamanaka, Masaru, et al.. (2016). Formation and carbon monoxide‐dependent dissociation of Allochromatium vinosum cytochrome c′ oligomers using domain‐swapped dimers. Protein Science. 26(3). 464–474. 12 indexed citations
11.
Yamanaka, Masaru, et al.. (2016). Domain swapping oligomerization of thermostable c-type cytochrome in E. coli cells. Scientific Reports. 6(1). 19334–19334. 13 indexed citations
12.
Ren, Chunguang, Satoshi Nagao, Masaru Yamanaka, et al.. (2015). Oligomerization enhancement and two domain swapping mode detection for thermostable cytochrome c 552 via the elongation of the major hinge loop. Molecular BioSystems. 11(12). 3218–3221. 13 indexed citations
13.
Yamanaka, Masaru, Satoshi Nagao, Hirofumi Komori, Yoshiki Higuchi, & Shun Hirota. (2015). Change in structure and ligand binding properties of hyperstable cytochrome c555 from Aquifex aeolicus by domain swapping. Protein Science. 24(3). 366–375. 17 indexed citations
14.
Matsuo, Takashi, et al.. (2015). Effect of a Procaspase-Activating Compound on the Catalytic Activity of Mature Caspase-3. Bulletin of the Chemical Society of Japan. 88(9). 1221–1229. 1 indexed citations
15.
Inoue, Hiroki, et al.. (2013). High Thermal Stability and Unique Trimer Formation of Cytochromec′ from ThermophilicHydrogenophilus thermoluteolus. Bioscience Biotechnology and Biochemistry. 77(8). 1677–1681. 12 indexed citations
16.
Sawai, Hitomi, Masaru Yamanaka, Hiroshi Sugimoto, Yoshitsugu Shiro, & Shigetoshi Aono. (2012). Structural Basis for the Transcriptional Regulation of Heme Homeostasis in Lactococcus lactis. Journal of Biological Chemistry. 287(36). 30755–30768. 51 indexed citations
17.
Oda, Koji, et al.. (2011). Effects of heme on the thermal stability of mesophilic and thermophilic cytochromes c: Comparison between experimental and theoretical results. The Journal of Chemical Physics. 134(2). 25101–25101. 34 indexed citations
18.
Yamanaka, Masaru, Hajime Mita, Yasuhiko Yamamoto, & Yoshihiro Sambongi. (2009). Heme Is Not Required forAquifex aeolicusCytochromec555Polypeptide Folding. Bioscience Biotechnology and Biochemistry. 73(9). 2022–2025. 13 indexed citations
19.
Kawahara, Kazuki, Daisuke Motooka, Shota Nakamura, et al.. (2009). Hyperstability and crystal structure of cytochromec555from hyperthermophilicAquifex aeolicus. Acta Crystallographica Section D Biological Crystallography. 65(8). 804–813. 19 indexed citations
20.
Yamanaka, Masaru, et al.. (2005). Unexpected Elevated Production ofAquifex aeolicusCytochromec555inEscherichia coliCells Lacking Disulfide Oxidoreductases. Bioscience Biotechnology and Biochemistry. 69(7). 1418–1421. 8 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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