Eri Chatani

1.9k total citations
52 papers, 1.5k citations indexed

About

Eri Chatani is a scholar working on Molecular Biology, Physiology and Materials Chemistry. According to data from OpenAlex, Eri Chatani has authored 52 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 40 papers in Molecular Biology, 33 papers in Physiology and 11 papers in Materials Chemistry. Recurrent topics in Eri Chatani's work include Alzheimer's disease research and treatments (32 papers), Protein Structure and Dynamics (25 papers) and Enzyme Structure and Function (10 papers). Eri Chatani is often cited by papers focused on Alzheimer's disease research and treatments (32 papers), Protein Structure and Dynamics (25 papers) and Enzyme Structure and Function (10 papers). Eri Chatani collaborates with scholars based in Japan, Taiwan and Germany. Eri Chatani's co-authors include Yuji Goto, Hironobu Naiki, Naoki Yamamoto, Rikimaru Hayashi, Kazuhiro Hasegawa, Hisashi Yagi, Young‐Ho Lee, Miho Kihara, Kazumasa Sakurai and Miyo Sakai and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

Eri Chatani

52 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Eri Chatani Japan 23 1.1k 805 286 173 149 52 1.5k
Anna I. Sulatskaya Russia 20 848 0.8× 703 0.9× 238 0.8× 129 0.7× 96 0.6× 62 1.5k
Tadato Ban Japan 14 1.0k 0.9× 985 1.2× 196 0.7× 297 1.7× 103 0.7× 16 1.6k
Giorgia Zandomeneghi Switzerland 17 856 0.8× 540 0.7× 202 0.7× 273 1.6× 111 0.7× 31 1.5k
Minna Groenning Denmark 17 1.2k 1.1× 963 1.2× 295 1.0× 306 1.8× 131 0.9× 24 1.9k
Keith A. Oberg United States 13 960 0.9× 458 0.6× 214 0.7× 108 0.6× 99 0.7× 20 1.5k
Vytautas Smirnovas Lithuania 27 1.5k 1.3× 988 1.2× 233 0.8× 232 1.3× 169 1.1× 95 2.2k
Masatomo So Japan 21 935 0.9× 776 1.0× 192 0.7× 194 1.1× 195 1.3× 58 1.4k
Manuela López de la Paz Germany 16 1.5k 1.3× 826 1.0× 301 1.1× 409 2.4× 75 0.5× 24 1.9k
Kazumasa Sakurai Japan 25 1.2k 1.1× 610 0.8× 252 0.9× 169 1.0× 524 3.5× 51 1.9k
Maarten F. M. Engel Netherlands 12 989 0.9× 883 1.1× 110 0.4× 340 2.0× 114 0.8× 18 1.5k

Countries citing papers authored by Eri Chatani

Since Specialization
Citations

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

Fields of papers citing papers by Eri Chatani

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Eri Chatani

This figure shows the co-authorship network connecting the top 25 collaborators of Eri Chatani. A scholar is included among the top collaborators of Eri Chatani 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 Eri Chatani. Eri Chatani 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.
Huang, Chih‐Hao, et al.. (2024). Spatiotemporal formation of a single liquid-like condensate and amyloid fibrils of α-synuclein by optical trapping at solution surface. Proceedings of the National Academy of Sciences. 121(39). e2402162121–e2402162121. 3 indexed citations
2.
Chatani, Eri, et al.. (2024). Oligomerization and aggregation of NAP-22 with several metal ions. Neuroscience Letters. 821. 137623–137623. 1 indexed citations
3.
Imamura, Hiroshi, Yuki Fujii, Ken Morishima, et al.. (2024). Mechanistic Modeling of Amyloid Oligomer and Protofibril Formation in Bovine Insulin. Journal of Molecular Biology. 436(6). 168461–168461. 1 indexed citations
4.
Yamamoto, Naoki & Eri Chatani. (2022). Multistep growth of amyloid intermediates and its inhibition toward exploring therapeutic way: A case study using insulin B chain and fibrinogen. Biophysics and Physicobiology. 19(0). n/a–n/a. 2 indexed citations
5.
Yamaguchi, K., Masatomo So, Eri Chatani, et al.. (2021). Breakdown of supersaturation barrier links protein folding to amyloid formation. Communications Biology. 4(1). 120–120. 47 indexed citations
6.
7.
Ishigaki, Mika, et al.. (2020). Exploration of Insulin Amyloid Polymorphism Using Raman Spectroscopy and Imaging. Biophysical Journal. 118(12). 2997–3007. 19 indexed citations
8.
Yamamoto, Naoki, Seongmin Ha, Yuki Masuda, et al.. (2020). Iodine staining as a useful probe for distinguishing insulin amyloid polymorphs. Scientific Reports. 10(1). 16741–16741. 11 indexed citations
9.
Yamamoto, Naoki, et al.. (2018). A specific form of prefibrillar aggregates that functions as a precursor of amyloid nucleation. Scientific Reports. 8(1). 62–62. 21 indexed citations
10.
Chatani, Eri & Naoki Yamamoto. (2017). Recent progress on understanding the mechanisms of amyloid nucleation. Biophysical Reviews. 10(2). 527–534. 124 indexed citations
11.
12.
Chatani, Eri, Hisashi Yagi, Hironobu Naiki, & Yuji Goto. (2012). Polymorphism of β2-Microglobulin Amyloid Fibrils Manifested by Ultrasonication-enhanced Fibril Formation in Trifluoroethanol. Journal of Biological Chemistry. 287(27). 22827–22837. 37 indexed citations
13.
Chatani, Eri, et al.. (2010). Pre-Steady-State Kinetic Analysis of the Elongation of Amyloid Fibrils of β2-Microglobulin with Tryptophan Mutagenesis. Journal of Molecular Biology. 400(5). 1057–1066. 24 indexed citations
14.
Konuma, Tsuyoshi, Eri Chatani, Masanori Yagi, et al.. (2010). Kinetic Intermediates of β2-Microglobulin Fibril Elongation Probed by Pulse-Labeling H/D Exchange Combined with NMR Analysis. Journal of Molecular Biology. 405(3). 851–862. 17 indexed citations
15.
Goto, Yuji, Hisashi Yagi, K. Yamaguchi, Eri Chatani, & Tadato Ban. (2008). Structure, Formation and Propagation of Amyloid Fibrils. Current Pharmaceutical Design. 14(30). 3205–3218. 27 indexed citations
16.
Lee, Young‐Ho, Eri Chatani, Kenji Sasahara, Hironobu Naiki, & Yuji Goto. (2008). A Comprehensive Model for Packing and Hydration for Amyloid Fibrils of β2-Microglobulin. Journal of Biological Chemistry. 284(4). 2169–2175. 51 indexed citations
17.
Chatani, Eri & Yuji Goto. (2005). Structural stability of amyloid fibrils of β2-microglobulin in comparison with its native fold. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1753(1). 64–75. 29 indexed citations
18.
Kihara, Miho, Eri Chatani, Miyo Sakai, et al.. (2005). Seeding-dependent Maturation of β2-Microglobulin Amyloid Fibrils at Neutral pH. Journal of Biological Chemistry. 280(12). 12012–12018. 60 indexed citations
19.
Sakurai, Kazumasa, Eri Chatani, Masaru Hoshino, et al.. (2004). Conformational stability of amyloid fibrils of β2‐microglobulin probed by guanidine‐hydrochloride‐induced unfolding. FEBS Letters. 576(3). 313–319. 68 indexed citations
20.
Chatani, Eri, Rikimaru Hayashi, Hideaki Moriyama, & Tatzuo Ueki. (2002). Conformational strictness required for maximum activity and stability of bovine pancreatic ribonuclease A as revealed by crystallographic study of three Phe120 mutants at 1.4 Å resolution. Protein Science. 11(1). 72–81. 57 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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