Masaru Hoshino

4.2k total citations
86 papers, 3.7k citations indexed

About

Masaru Hoshino is a scholar working on Molecular Biology, Materials Chemistry and Physiology. According to data from OpenAlex, Masaru Hoshino has authored 86 papers receiving a total of 3.7k indexed citations (citations by other indexed papers that have themselves been cited), including 62 papers in Molecular Biology, 22 papers in Materials Chemistry and 20 papers in Physiology. Recurrent topics in Masaru Hoshino's work include Protein Structure and Dynamics (36 papers), Enzyme Structure and Function (20 papers) and Alzheimer's disease research and treatments (20 papers). Masaru Hoshino is often cited by papers focused on Protein Structure and Dynamics (36 papers), Enzyme Structure and Function (20 papers) and Alzheimer's disease research and treatments (20 papers). Masaru Hoshino collaborates with scholars based in Japan, United States and Iran. Masaru Hoshino's co-authors include Yuji Goto, Hironobu Naiki, Kazuhiro Hasegawa, Yoshihisa Hagihara, Hidenori Katou, Katsumi Matsuzaki, Dong-Pyo Hong, Ryoichi Kuboi, Daizo Hamada and Carl A. Batt and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Masaru Hoshino

84 papers receiving 3.6k 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 Hoshino Japan 34 2.5k 1.2k 716 446 372 86 3.7k
Irina М. Kuznetsova Russia 40 3.8k 1.5× 1.3k 1.1× 1.1k 1.6× 271 0.6× 568 1.5× 200 5.8k
Daizo Hamada Japan 24 1.9k 0.8× 623 0.5× 644 0.9× 465 1.0× 194 0.5× 52 2.7k
Boris I. Kurganov Russia 35 3.3k 1.3× 661 0.5× 1.1k 1.6× 307 0.7× 268 0.7× 266 4.4k
Melinda Balbirnie United States 8 3.5k 1.4× 2.4k 1.9× 787 1.1× 203 0.5× 352 0.9× 11 4.6k
Ian S. Millett United States 26 2.9k 1.2× 769 0.6× 1.0k 1.4× 134 0.3× 332 0.9× 29 4.0k
Rebecca A. Nelson United States 14 3.8k 1.5× 2.6k 2.1× 775 1.1× 224 0.5× 359 1.0× 37 5.2k
Jochen Balbach Germany 33 2.6k 1.0× 325 0.3× 989 1.4× 161 0.4× 412 1.1× 127 3.4k
Samrat Mukhopadhyay India 30 2.1k 0.8× 562 0.5× 607 0.8× 184 0.4× 182 0.5× 84 3.1k
Jayant B. Udgaonkar India 41 4.4k 1.8× 792 0.6× 2.3k 3.1× 337 0.8× 532 1.4× 171 5.2k
Robert Grothe United States 10 2.4k 0.9× 1.2k 1.0× 457 0.6× 129 0.3× 459 1.2× 13 3.1k

Countries citing papers authored by Masaru Hoshino

Since Specialization
Citations

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

Fields of papers citing papers by Masaru Hoshino

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Masaru Hoshino

This figure shows the co-authorship network connecting the top 25 collaborators of Masaru Hoshino. A scholar is included among the top collaborators of Masaru Hoshino 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 Hoshino. Masaru Hoshino 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.
Kobayashi, Yuka, Tomoshi Kameda, Masaru Hoshino, et al.. (2017). Fe(ii)-Complexation of tripodal hexapeptide ligands with three bidentate triazolylpyridines: induction of metal-centred chirality by peptide macrocyclization. Dalton Transactions. 46(40). 13673–13676. 5 indexed citations
3.
Itoh, Naoya, Yoshiaki Yano, Masaru Hoshino, et al.. (2017). Not Oligomers but Amyloids are Cytotoxic in the Membrane‐Mediated Amyloidogenesis of Amyloid‐β Peptides. ChemBioChem. 19(5). 430–433. 23 indexed citations
4.
5.
Morimoto, Daichi, Erik Walinda, Harumi Fukada, et al.. (2015). The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates. Nature Communications. 6(1). 6116–6116. 70 indexed citations
6.
Kawata, Yasushi, et al.. (2014). Evaluation of the stability of an SR398/GroES chaperonin complex. The Journal of Biochemistry. 155(5). 295–300. 1 indexed citations
7.
Ogawa, Mariko, Takahiro Yamaguchi, Keisuke Ikeda, et al.. (2010). Ganglioside‐mediated aggregation of amyloid β‐proteins (Aβ): comparison between Aβ‐(1–42) and Aβ‐(1–40). Journal of Neurochemistry. 116(5). 851–857. 41 indexed citations
8.
Hoshino, Masaru, Hidenori Katou, K. Yamaguchi, & Yuji Goto. (2007). Dimethylsulfoxide-quenched hydrogen/deuterium exchange method to study amyloid fibril structure. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1768(8). 1886–1899. 45 indexed citations
9.
Lee, Young‐Ho, Masahiro Maeda, Masaru Hoshino, et al.. (2006). Cores and pH-dependent Dynamics of Ferredoxin-NADP+ Reductase Revealed by Hydrogen/Deuterium Exchange. Journal of Biological Chemistry. 282(8). 5959–5967. 22 indexed citations
10.
Hoshino, Masaru, et al.. (2005). Measurement of shape and velocity of snow particles using two cameras. 29(34). 21–24. 3 indexed citations
11.
Ban, Tadato, Masaru Hoshino, Satoshi Takahashi, et al.. (2004). Direct Observation of Aβ Amyloid Fibril Growth and Inhibition. Journal of Molecular Biology. 344(3). 757–767. 199 indexed citations
12.
Hoshino, Masaru, Hidenori Katou, Yoshihisa Hagihara, et al.. (2002). Mapping the core of the β2-microglobulin amyloid fibril by H/D exchange. Nature Structural Biology. 9(5). 332–336. 287 indexed citations
13.
Hoshino, Masaru, et al.. (2002). The interaction of β2‐glycoprotein I domain V with chaperonin GroEL: The similarity with the domain V and membrane interaction. Protein Science. 11(12). 2792–2803. 3 indexed citations
14.
Nishiguchi, Miyuki, Misako Matsumoto, Toshifumi Takao, et al.. (2001). Mycoplasma fermentans Lipoprotein M161Ag-Induced Cell Activation Is Mediated by Toll-Like Receptor 2: Role of N-Terminal Hydrophobic Portion in its Multiple Functions. The Journal of Immunology. 166(4). 2610–2616. 106 indexed citations
15.
Katou, Hidenori, Masaru Hoshino, Hironari Kamikubo, Carl A. Batt, & Yuji Goto. (2001). Native-like β-hairpin retained in the cold-denatured state of bovine β-lactoglobulin. Journal of Molecular Biology. 310(2). 471–484. 26 indexed citations
16.
Forge, Vincent, Masaru Hoshino, Kazuo Kuwata, et al.. (2000). Is folding of β-lactoglobulin non-hierarchic? intermediate with native-like β-sheet and non-native α-helix. Journal of Molecular Biology. 296(4). 1039–1051. 90 indexed citations
17.
Hoshino, Masaru, et al.. (1999). Single molecular observation of the interaction of GroEL with substrate proteins. Seibutsu Butsuri. 39(supplement). S131–S131. 1 indexed citations
18.
Yamasaki, Ryo, Masaru Hoshino, Tetsuichi Wazawa, et al.. (1999). Single molecular observation of the interaction of GroEL with substrate proteins. Journal of Molecular Biology. 292(5). 965–972. 34 indexed citations
19.
Hagihara, Yoshihisa, Masaru Hoshino, Daizo Hamada, Mikio Kataoka, & Yuji Goto. (1998). Chain-like conformation of heat-denatured ribonuclease A and cytochromec as evidenced by solution X-ray scattering. PubMed. 3(3). 195–201. 29 indexed citations
20.
Yanaihara, Noboru, Chizuko Yanaihara, Takashi Inoue, et al.. (1989). Demonstration of two distinct insulin-binding components in solubilized human placental membranes by radioimmunoassay using synthetic peptide and anti-synthetic peptide antibody. Diabetes Research and Clinical Practice. 7. S109–S113. 3 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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