Takeshi Baba

1.6k total citations
28 papers, 1.3k citations indexed

About

Takeshi Baba is a scholar working on Molecular Biology, Cell Biology and Physiology. According to data from OpenAlex, Takeshi Baba has authored 28 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 10 papers in Cell Biology and 9 papers in Physiology. Recurrent topics in Takeshi Baba's work include Erythrocyte Function and Pathophysiology (8 papers), Lipid Membrane Structure and Behavior (8 papers) and Blood properties and coagulation (4 papers). Takeshi Baba is often cited by papers focused on Erythrocyte Function and Pathophysiology (8 papers), Lipid Membrane Structure and Behavior (8 papers) and Blood properties and coagulation (4 papers). Takeshi Baba collaborates with scholars based in Japan, France and United States. Takeshi Baba's co-authors include Shinichi Ohno, Christophe Lamaze, Annick Dujeancourt, Alexandre Benmerah, Charles G. Lo, Alice Dautry‐Varsat, Sandra L. Schmid, Nobuo Terada, Hideho Ueda and Asami Makino and has published in prestigious journals such as Journal of Biological Chemistry, Molecular Cell and Nature Structural & Molecular Biology.

In The Last Decade

Takeshi Baba

28 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Takeshi Baba Japan 16 923 592 306 158 101 28 1.3k
Pranav Sharma United States 13 1.5k 1.6× 725 1.2× 274 0.9× 180 1.1× 119 1.2× 18 2.0k
Eva M. Wenzel Norway 23 1.2k 1.3× 1.1k 1.8× 341 1.1× 174 1.1× 163 1.6× 42 2.2k
Masaya Yamamoto Japan 15 1.1k 1.2× 676 1.1× 145 0.5× 113 0.7× 81 0.8× 24 1.6k
Gillian Howard United Kingdom 13 941 1.0× 1.1k 1.8× 313 1.0× 70 0.4× 91 0.9× 16 1.5k
Oleksiy Kovtun Australia 17 1.1k 1.2× 780 1.3× 282 0.9× 66 0.4× 91 0.9× 24 1.6k
Marko Jović United States 17 744 0.8× 682 1.2× 166 0.5× 98 0.6× 60 0.6× 24 1.2k
Alex H. Hutagalung United States 12 1.4k 1.6× 1.1k 1.8× 197 0.6× 125 0.8× 179 1.8× 13 2.0k
Ginette Guay Canada 10 695 0.8× 438 0.7× 156 0.5× 222 1.4× 76 0.8× 12 1.2k
James R. Edgar United Kingdom 23 991 1.1× 583 1.0× 299 1.0× 150 0.9× 243 2.4× 37 1.7k
Marina Vietri Norway 11 1.2k 1.3× 822 1.4× 216 0.7× 132 0.8× 84 0.8× 13 1.7k

Countries citing papers authored by Takeshi Baba

Since Specialization
Citations

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

Fields of papers citing papers by Takeshi Baba

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Takeshi Baba

This figure shows the co-authorship network connecting the top 25 collaborators of Takeshi Baba. A scholar is included among the top collaborators of Takeshi Baba 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 Takeshi Baba. Takeshi Baba 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.
Sakuragi, Takaharu, R. Kanai, Akihisa Tsutsumi, et al.. (2021). The tertiary structure of the human Xkr8–Basigin complex that scrambles phospholipids at plasma membranes. Nature Structural & Molecular Biology. 28(10). 825–834. 31 indexed citations
2.
Terada, Nobuo, Nobuhiko Ohno, Yasuhisa Fujii, Takeshi Baba, & Shinichi Ohno. (2006). Dynamic study of intramembranous particles in human fresh erythrocytes using an “in vitro cryotechnique”. Microscopy Research and Technique. 69(4). 291–295. 3 indexed citations
3.
Terada, Nobuo, Nobuhiko Ohno, Hisashi Yamakawa, et al.. (2005). Immunohistochemical study of a membrane skeletal molecule, protein 4.1G, in mouse seminiferous tubules. Histochemistry and Cell Biology. 124(3-4). 303–311. 19 indexed citations
4.
Terada, Nobuo, Nobuhiko Ohno, Zilong Li, et al.. (2005). Detection of injected fluorescence‐conjugated IgG in living mouse organs using “in vivo cryotechnique” with freeze‐substitution. Microscopy Research and Technique. 66(4). 173–178. 22 indexed citations
5.
Ohno, Nobuhiko, Nobuo Terada, Junya Tanaka, et al.. (2005). Protein 4.1 G localizes in rodent microglia. Histochemistry and Cell Biology. 124(6). 477–486. 16 indexed citations
6.
Terada, Nobuo, Nobuhiko Ohno, Yasuhisa Fujii, et al.. (2004). Replica immunoelectron microscopic study of the upper surface layer in rat mandibular condylar cartilage by a quick-freezing method. Histochemistry and Cell Biology. 121(3). 255–259. 17 indexed citations
7.
Terada, Nobuo, Nobuhiko Ohno, Hisashi Yamakawa, et al.. (2004). Protein 4.1B localizes on unmyelinated axonal membranes in the mouse enteric nervous system. Neuroscience Letters. 366(1). 15–17. 5 indexed citations
8.
Ohno, Nobuhiko, Hisashi Yamakawa, George Seki, et al.. (2004). Immunoelectron microscopic localization of protein 4.1B in proximal S1 and S2 tubules of rodent kidneys. PubMed. 37(1). 45–51. 16 indexed citations
9.
Terada, Nobuo, Nobuhiko Ohno, Hisashi Yamakawa, et al.. (2004). Immunohistochemical Study of Protein 4.1B in the Normal and W/Wv Mouse Seminiferous Epithelium. Journal of Histochemistry & Cytochemistry. 52(6). 769–777. 22 indexed citations
10.
Baba, Takeshi, Nobuo Terada, Yasuhisa Fujii, et al.. (2004). Ultrastructural study of echinocytes induced by poly (ethylene glycol)-cholesterol. Histochemistry and Cell Biology. 122(6). 587–592. 12 indexed citations
11.
Terada, Nobuo, Nobuhiko Ohno, Hisashi Yamakawa, et al.. (2004). Immunolocalization of Protein 4.1B in the Rat Digestive System. Journal of Molecular Histology. 35(4). 347–353. 10 indexed citations
12.
Yagi, Takashi, Nobuo Terada, Takeshi Baba, & Shinichi Ohno. (2003). Immunolocalization of laminin-α1-like antigens around synapses in mouse cerebellar perineuronal nets. The Histochemical Journal. 34(11-12). 559–565. 2 indexed citations
13.
Makino, Asami, Takeshi Baba, Kazushi Fujimoto, et al.. (2003). Cinnamycin (Ro 09-0198) Promotes Cell Binding and Toxicity by Inducing Transbilayer Lipid Movement. Journal of Biological Chemistry. 278(5). 3204–3209. 64 indexed citations
14.
Yamaji‐Hasegawa, Akiko, Asami Makino, Takeshi Baba, et al.. (2003). Oligomerization and Pore Formation of a Sphingomyelin-specific Toxin, Lysenin. Journal of Biological Chemistry. 278(25). 22762–22770. 108 indexed citations
15.
Yagi, Takashi, Nobuo Terada, Takeshi Baba, & Shinichi Ohno. (2003). Localization of Endogenous Biotin-Containing Proteins in Mouse Bergmann Glial Cells. The Histochemical Journal. 34(11-12). 567–572. 11 indexed citations
16.
Lamaze, Christophe, Annick Dujeancourt, Takeshi Baba, et al.. (2001). Interleukin 2 Receptors and Detergent-Resistant Membrane Domains Define a Clathrin-Independent Endocytic Pathway. Molecular Cell. 7(3). 661–671. 424 indexed citations
17.
Damke, Hanna, Derk D. Binns, Hideho Ueda, Sandra L. Schmid, & Takeshi Baba. (2001). Dynamin GTPase Domain Mutants Block Endocytic Vesicle Formation at Morphologically Distinct Stages. Molecular Biology of the Cell. 12(9). 2578–2589. 147 indexed citations
18.
Ueda, Hideho, Takeshi Baba, Nobuo Terada, et al.. (1998). Immunolocalization of myotonic dystrophy protein kinase in corbular and junctional sarcoplasmic reticulum of human cardiac muscle. The Histochemical Journal. 30(4). 245–251. 6 indexed citations
19.
20.
Xue, Mei, et al.. (1998). Morphological study by an ‘in vivo cryotechnique’ of the shape of erythrocytes circulating in large blood vessels. Journal of Anatomy. 193(1). 73–79. 12 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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