Yoshitake Maeda

715 total citations
20 papers, 575 citations indexed

About

Yoshitake Maeda is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Immunology. According to data from OpenAlex, Yoshitake Maeda has authored 20 papers receiving a total of 575 indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 7 papers in Radiology, Nuclear Medicine and Imaging and 6 papers in Immunology. Recurrent topics in Yoshitake Maeda's work include Glycosylation and Glycoproteins Research (7 papers), Monoclonal and Polyclonal Antibodies Research (7 papers) and Protein purification and stability (4 papers). Yoshitake Maeda is often cited by papers focused on Glycosylation and Glycoproteins Research (7 papers), Monoclonal and Polyclonal Antibodies Research (7 papers) and Protein purification and stability (4 papers). Yoshitake Maeda collaborates with scholars based in Japan, Germany and Italy. Yoshitake Maeda's co-authors include Tadashi Ueda, Taiji Imoto, Hidenori Yamada, Ryota Kuroki, Taro Tamada, Eijiro Honjo, Masao Tokunaga, Tomoyuki Okamoto, Matsujiro Ishibashi and Hiroshi Koga and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Yoshitake Maeda

19 papers receiving 554 citations

Peers

Yoshitake Maeda
Stephanie M.E. Truhlar United States
Mark K. Boehm United Kingdom
Brian Kraybill United States
Andrew G. Popplewell United Kingdom
M. Randal United States
Thorsten Erpel United States
Gabriele Matschiner Germany
Marie Rose van Schravendijk United States
Tamjeed Saleh United States
Charles Reichman United States
Stephanie M.E. Truhlar United States
Yoshitake Maeda
Citations per year, relative to Yoshitake Maeda Yoshitake Maeda (= 1×) peers Stephanie M.E. Truhlar

Countries citing papers authored by Yoshitake Maeda

Since Specialization
Citations

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

Fields of papers citing papers by Yoshitake Maeda

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Yoshitake Maeda

This figure shows the co-authorship network connecting the top 25 collaborators of Yoshitake Maeda. A scholar is included among the top collaborators of Yoshitake Maeda 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 Yoshitake Maeda. Yoshitake Maeda 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.
Arai, Shigeki, Motoyasu Adachi, Yoshitake Maeda, et al.. (2019). The non‐glycosylated N‐terminal domain of human thrombopoietin is a molten globule under native conditions. FEBS Journal. 286(9). 1717–1733. 1 indexed citations
2.
Arai, Shigeki, Motoyasu Adachi, Eijiro Honjo, et al.. (2016). An insight into the thermodynamic characteristics of human thrombopoietin complexation with TN1 antibody. Protein Science. 25(10). 1786–1796. 3 indexed citations
3.
Suganami, Akiko, et al.. (2013). Affinity maturation of a CDR3-grafted VHH using in silico analysis and surface plasmon resonance. The Journal of Biochemistry. 154(4). 325–332. 7 indexed citations
4.
Takahashi, Hideo, et al.. (2011). Affinity transfer to a human protein by CDR3 grafting of camelid VHH. Protein Science. 20(12). 1971–1981. 8 indexed citations
5.
Kitazoe, Midori, Junichiro Futami, Mitsuo Nishikawa, Hidenori Yamada, & Yoshitake Maeda. (2010). Polyethylenimine‐cationized β‐catenin protein transduction activates the Wnt canonical signaling pathway more effectively than cationic lipid‐based transduction. Biotechnology Journal. 5(4). 385–392. 9 indexed citations
6.
Kofuku, Yutaka, Takumi Ueda, Hiroaki Terasawa, et al.. (2009). Structural Basis of the Interaction between Chemokine Stromal Cell-derived Factor-1/CXCL12 and Its G-protein-coupled Receptor CXCR4. Journal of Biological Chemistry. 284(50). 35240–35250. 129 indexed citations
7.
Nagao, Kenji, Takayuki Ohta, Atsushi Hinohara, et al.. (2008). Expression profile analysis of aorta-gonad-mesonephros region-derived stromal cells reveals genes that regulate hematopoiesis. Biochemical and Biophysical Research Communications. 377(1). 205–209. 3 indexed citations
8.
Tamada, Taro, Eijiro Honjo, Yoshitake Maeda, et al.. (2006). Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex. Proceedings of the National Academy of Sciences. 103(9). 3135–3140. 98 indexed citations
9.
Kitazoe, Midori, Hitoshi Murata, Junichiro Futami, et al.. (2005). Protein Transduction Assisted by Polyethylenimine-Cationized Carrier Proteins. The Journal of Biochemistry. 137(6). 693–701. 25 indexed citations
10.
Honjo, Eijiro, Taro Tamada, Yoshitake Maeda, et al.. (2005). Crystallization of a 2:2 complex of granulocyte-colony stimulating factor (GCSF) with the ligand-binding region of the GCSF receptor. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(8). 788–790. 5 indexed citations
11.
Maeda, Yoshitake, Ryota Kuroki, Winfried Haase, Hartmut Michel, & Helmut Reiländer. (2004). Comparative analysis of high‐affinity ligand binding and G protein coupling of the human CXCR1 chemokine receptor and of a CXCR1–Gi2α fusion protein after heterologous production in baculovirus‐infected insect cells. European Journal of Biochemistry. 271(9). 1677–1689. 5 indexed citations
12.
Mine, Shouhei, Takumi Koshiba, Eijiro Honjo, et al.. (2004). Thermodynamic Analysis of the Activation Mechanism of the GCSF Receptor Induced by Ligand Binding. Biochemistry. 43(9). 2458–2464. 12 indexed citations
13.
Feese, M.D., Taro Tamada, Yoichi Kato, et al.. (2004). Structure of the receptor-binding domain of human thrombopoietin determined by complexation with a neutralizing antibody fragment. Proceedings of the National Academy of Sciences. 101(7). 1816–1821. 66 indexed citations
14.
Kuroki, Ryota, Yoichi Kato, M.D. Feese, et al.. (2002). Crystallization of the functional domain of human thrombopoietin using an antigen-binding fragment derived from neutralizing monoclonal antibody. Acta Crystallographica Section D Biological Crystallography. 58(5). 856–858. 10 indexed citations
15.
Maeda, Yoshitake, et al.. (2000). High-Level Secretion of Biologically Active Recombinant Human Macrophage Inflammatory Protein-1α by the Methylotrophic Yeast Pichia pastoris. Protein Expression and Purification. 18(1). 56–63. 6 indexed citations
16.
Maeda, Yoshitake, Tadashi Ueda, & Taiji Imoto. (1996). Effective renaturation of denatured and reduced immunoglobulin G in vitro without assistance of chaperone. Protein Engineering Design and Selection. 9(1). 95–100. 22 indexed citations
17.
Maeda, Yoshitake, Hidenori Yamada, Tadashi Ueda, & Taiji Imoto. (1996). Effect of additives on the renaturation of reduced lysozyme in the presence of 4 M urea. Protein Engineering Design and Selection. 9(5). 461–465. 63 indexed citations
18.
Maeda, Yoshitake, et al.. (1995). Effective renaturation of reduced lysozyme by gentle removal of urea. Protein Engineering Design and Selection. 8(2). 201–205. 66 indexed citations
19.
Maeda, Yoshitake, Tadashi Ueda, Hidenori Yamada, & Taiji Imoto. (1994). The role of net charge on the renaturation of reduced lysozyme by the sulfhydryl–disulfide interchange reaction. Protein Engineering Design and Selection. 7(10). 1249–1254. 13 indexed citations
20.
Ueda, Tadashi, et al.. (1993). Stabilization of lysozyme by the introduction of Gly-Pro sequence. Protein Engineering Design and Selection. 6(2). 183–187. 24 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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