Daizo Hamada

3.1k total citations
52 papers, 2.7k citations indexed

About

Daizo Hamada is a scholar working on Molecular Biology, Physiology and Materials Chemistry. According to data from OpenAlex, Daizo Hamada has authored 52 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 38 papers in Molecular Biology, 11 papers in Physiology and 11 papers in Materials Chemistry. Recurrent topics in Daizo Hamada's work include Protein Structure and Dynamics (21 papers), Enzyme Structure and Function (10 papers) and Alzheimer's disease research and treatments (9 papers). Daizo Hamada is often cited by papers focused on Protein Structure and Dynamics (21 papers), Enzyme Structure and Function (10 papers) and Alzheimer's disease research and treatments (9 papers). Daizo Hamada collaborates with scholars based in Japan, United Kingdom and Italy. Daizo Hamada's co-authors include Yuji Goto, Christopher M. Dobson, Tadato Ban, Hironobu Naiki, Kazuhiro Hasegawa, Masaru Hoshino, Shin-ichi Segawa, Yutaka Kuroda, Toshiki Tanaka and Mikio Kataoka and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Daizo Hamada

51 papers receiving 2.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Daizo Hamada Japan 24 1.9k 644 623 465 269 52 2.7k
Masaru Hoshino Japan 34 2.5k 1.3× 716 1.1× 1.2k 2.0× 446 1.0× 325 1.2× 86 3.7k
Vincent Forge France 31 1.8k 1.0× 626 1.0× 296 0.5× 373 0.8× 222 0.8× 46 2.5k
J. Iñaki Guijarro France 22 2.0k 1.1× 582 0.9× 829 1.3× 188 0.4× 236 0.9× 43 2.8k
Arturo Muga Spain 34 3.1k 1.6× 634 1.0× 234 0.4× 227 0.5× 329 1.2× 107 3.9k
Jochen Balbach Germany 33 2.6k 1.3× 989 1.5× 325 0.5× 161 0.3× 293 1.1× 127 3.4k
Véronique Receveur‐Brechot France 27 2.5k 1.3× 976 1.5× 288 0.5× 151 0.3× 291 1.1× 52 3.5k
José Luis R. Arrondo Spain 22 1.8k 1.0× 314 0.5× 194 0.3× 199 0.4× 216 0.8× 44 2.7k
Aaron K. Chamberlain United States 19 1.7k 0.9× 448 0.7× 354 0.6× 134 0.3× 135 0.5× 22 2.2k
Ann H. Kwan Australia 31 1.9k 1.0× 293 0.5× 271 0.4× 202 0.4× 256 1.0× 93 2.8k
Valentina E. Bychkova Russia 19 1.8k 0.9× 979 1.5× 166 0.3× 442 1.0× 336 1.2× 50 2.6k

Countries citing papers authored by Daizo Hamada

Since Specialization
Citations

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

Fields of papers citing papers by Daizo Hamada

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Daizo Hamada

This figure shows the co-authorship network connecting the top 25 collaborators of Daizo Hamada. A scholar is included among the top collaborators of Daizo Hamada 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 Daizo Hamada. Daizo Hamada 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.
Adachi, Naoko, Hideyuki Takahashi, Takahiro Seki, et al.. (2018). Pharmacological induction of heat shock proteins ameliorates toxicity of mutant PKCγ in spinocerebellar ataxia type 14. Journal of Biological Chemistry. 293(38). 14758–14774. 14 indexed citations
2.
Takahashi, Hideyuki, Naoko Adachi, Takehiko Ueyama, et al.. (2014). Identification and characterization of PKCγ, a kinase associated with SCA14, as an amyloidogenic protein. Human Molecular Genetics. 24(2). 525–539. 21 indexed citations
3.
Goda, Natsuko, et al.. (2013). MIT domain of Vps4 is a Ca2+-dependent phosphoinositide-binding domain. The Journal of Biochemistry. 153(5). 473–481. 11 indexed citations
4.
Goda, Natsuko, Takeshi Tenno, Yoshie Fujiwara, et al.. (2012). Effect of Ca2+ on the microtubule‐severing enzyme p60‐katanin. Insight into the substrate‐dependent activation mechanism. FEBS Journal. 279(7). 1339–1352. 11 indexed citations
5.
Hiragami-Hamada, Kyoko, Kaori Shinmyozu, Daizo Hamada, et al.. (2011). N-Terminal Phosphorylation of HP1α Promotes Its Chromatin Binding. Molecular and Cellular Biology. 31(6). 1186–1200. 76 indexed citations
6.
Hamada, Daizo, Toshiki Tanaka, Gian Gaetano Tartaglia, et al.. (2008). Competition between Folding, Native-State Dimerisation and Amyloid Aggregation in β-Lactoglobulin. Journal of Molecular Biology. 386(3). 878–890. 70 indexed citations
7.
Tabata, Atsushi, Fumihiko Namba, Minoru Yamada, et al.. (2006). Expression and purification of recombinant human annexin A2 in Pichia pastoris and utility of expression product for detecting annexin A2 antibody. Journal of Bioscience and Bioengineering. 101(2). 190–197. 4 indexed citations
8.
Kato, Tomoaki, Daizo Hamada, Takashi Fukui, et al.. (2005). A pH‐dependent conformational change in EspA, a component of the Escherichia coli O157:H7 type III secretion system. FEBS Journal. 272(11). 2773–2783. 8 indexed citations
9.
Hamada, Daizo, Tomoaki Kato, Takahisa Ikegami, et al.. (2005). EspB from enterohaemorrhagic Escherichia coli is a natively partially folded protein. FEBS Journal. 272(3). 756–768. 16 indexed citations
10.
Hamada, Daizo, Itaru Yanagihara, & Kouhei Tsumoto. (2004). Engineering amyloidogenicity towards the development of nanofibrillar materials. Trends in biotechnology. 22(2). 93–97. 81 indexed citations
11.
Yamada, Minoru, Koji Inui, Daizo Hamada, et al.. (2004). Analysis of recombinant human saposin A expressed by Pichia pastoris. Biochemical and Biophysical Research Communications. 318(2). 588–593. 8 indexed citations
12.
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
13.
Maeda, Masahiro, Daizo Hamada, Masaru Hoshino, et al.. (2002). Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain. Journal of Biological Chemistry. 277(19). 17101–17107. 14 indexed citations
14.
Dobson, Christopher M., et al.. (2000). Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol.. Nature Structural Biology. 7(1). 58–61. 64 indexed citations
15.
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
16.
Hamada, Daizo, Yutaka Kuroda, Mikio Kataoka, et al.. (1996). Role of Heme Axial Ligands in the Conformational Stability of the Native and Molten Globule States of Horse Cytochrome. Journal of Molecular Biology. 256(1). 172–186. 79 indexed citations
17.
Hamada, Daizo, Shin-ichi Segawa, & Yuji Goto. (1996). Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nature Structural & Molecular Biology. 3(10). 868–873. 230 indexed citations
18.
Kuroda, Yutaka, Daizo Hamada, Toshiki Tanaka, & Yuji Goto. (1996). High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy. PubMed. 1(4). 255–263. 69 indexed citations
19.
Hamada, Daizo, Yutaka Kuroda, Toshiki Tanaka, & Yuji Goto. (1995). High Helical Propensity of the Peptide Fragments Derived from β-Lactoglobulin, a Predominantly β-sheet Protein. Journal of Molecular Biology. 254(4). 737–746. 153 indexed citations
20.
Goto, Yuji, Yoshihisa Hagihara, Daizo Hamada, Masaru Hoshino, & Ichiro Nishii. (1993). Acid-induced unfolding and refolding transitions of cytochrome c: A three-state mechanism in water and deuterium oxide. Biochemistry. 32(44). 11878–11885. 102 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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