Kenji Inaba

4.6k total citations
95 papers, 3.1k citations indexed

About

Kenji Inaba is a scholar working on Cell Biology, Molecular Biology and Nutrition and Dietetics. According to data from OpenAlex, Kenji Inaba has authored 95 papers receiving a total of 3.1k indexed citations (citations by other indexed papers that have themselves been cited), including 59 papers in Cell Biology, 55 papers in Molecular Biology and 12 papers in Nutrition and Dietetics. Recurrent topics in Kenji Inaba's work include Endoplasmic Reticulum Stress and Disease (49 papers), Redox biology and oxidative stress (11 papers) and Cellular transport and secretion (11 papers). Kenji Inaba is often cited by papers focused on Endoplasmic Reticulum Stress and Disease (49 papers), Redox biology and oxidative stress (11 papers) and Cellular transport and secretion (11 papers). Kenji Inaba collaborates with scholars based in Japan, United States and Italy. Kenji Inaba's co-authors include Koreaki Ito, Masaki Okumura, Mamoru Suzuki, Shoji Masui, Shingo Kanemura, Hiroshi Kadokura, Roberto Sitia, Kazutaka Araki, Satoshi Watanabe and Yoshimi Sato and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Kenji Inaba

93 papers receiving 3.1k citations

Peers

Kenji Inaba

EPIDE

IMMUN

Jakob R. Winther Denmark

Carolyn S. Sevier United States

Akira Matsuura Japan

Frank Rusnak United States

Patricia M. Kane United States

André Trouet Belgium

Jean de Gunzburg France

Maria Monti Italy

E.D. Lowe United Kingdom

Hans Jörnvall Sweden

Jakob R. Winther Denmark

Kenji Inaba

3.3k ×1.8

1.3k ×0.9

230 ×0.7

EPIDE

478 ×1.6

225 ×0.9

IMMUN

Citations per year, relative to Kenji Inaba Kenji Inaba (= 1×) peers Jakob R. Winther

Countries citing papers authored by Kenji Inaba

Since Specialization

Citations

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

Fields of papers citing papers by Kenji Inaba

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kenji Inaba

This figure shows the co-authorship network connecting the top 25 collaborators of Kenji Inaba. A scholar is included among the top collaborators of Kenji Inaba 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 Kenji Inaba. Kenji Inaba is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Inaba, Kenji, et al.. (2024). Structures, Mechanisms, and Physiological Functions of Zinc Transporters in Different Biological Kingdoms. International Journal of Molecular Sciences. 25(5). 3045–3045. 8 indexed citations

Watanabe, Satoshi, Yoshiaki Kise, Kento Yonezawa, et al.. (2024). Structure of full-length ERGIC-53 in complex with MCFD2 for cargo transport. Nature Communications. 15(1). 2404–2404. 4 indexed citations

Watanabe, Satoshi, Norimichi Nomura, Kehong Liu, et al.. (2023). Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn2+ uptake into the Golgi apparatus. Nature Communications. 14(1). 4770–4770. 21 indexed citations

Levantino, Matteo, et al.. (2023). Tracking the structural dynamics of SERCA regulation in real time. Biophysical Journal. 122(3). 58a–58a. 2 indexed citations

Machida, Kodai, Kentaro Noi, Masaki Okumura, et al.. (2021). Distinct roles and actions of protein disulfide isomerase family enzymes in catalysis of nascent-chain disulfide bond formation. iScience. 24(4). 102296–102296. 10 indexed citations

Kanemura, Shingo, Yuxi Lin, Kimiko Kuroki, et al.. (2021). Ca2+ Regulates ERp57-Calnexin Complex Formation. Molecules. 26(10). 2853–2853. 7 indexed citations

Okada, Rina, Shingo Kanemura, Yuxi Lin, et al.. (2021). Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding. Biology. 10(11). 1112–1112. 5 indexed citations

Watanabe, Satoshi, et al.. (2021). Cryo‐EM analysis provides new mechanistic insight into ATP binding to Ca ²⁺ ‐ATPase SERCA2b. The EMBO Journal. 40(19). e108482–e108482. 13 indexed citations

Ninagawa, Satoshi, Masaki Okumura, Misaki Kinoshita, et al.. (2020). Antipsychotic olanzapine-induced misfolding of proinsulin in the endoplasmic reticulum accounts for atypical development of diabetes. eLife. 9. 23 indexed citations

10.

Kanemura, Shingo, et al.. (2020). PDI Family Members as Guides for Client Folding and Assembly. International Journal of Molecular Sciences. 21(24). 9351–9351. 25 indexed citations

11.

Arai, Kenta, et al.. (2018). Coupling effects of thiol and urea-type groups for promotion of oxidative protein folding. Chemical Communications. 55(6). 759–762. 24 indexed citations

12.

Ushioda, Ryo, Akitoshi Miyamoto, M. Inoue, et al.. (2016). Redox-assisted regulation of Ca ²⁺ homeostasis in the endoplasmic reticulum by disulfide reductase ERdj5. Proceedings of the National Academy of Sciences. 113(41). E6055–E6063. 77 indexed citations

13.

Watanabe, Satoshi, Tamotsu Kanai, Takehiko Wada, et al.. (2015). Structural basis of a Ni acquisition cycle for [NiFe] hydrogenase by Ni-metallochaperone HypA and its enhancer. Proceedings of the National Academy of Sciences. 112(25). 7701–7706. 43 indexed citations

14.

Ramming, Thomas, Masaki Okumura, Shingo Kanemura, et al.. (2015). A PDI-catalyzed thiol–disulfide switch regulates the production of hydrogen peroxide by human Ero1. Free Radical Biology and Medicine. 83. 361–372. 62 indexed citations

15.

Appenzeller‐Herzog, Christian, Kenji Inaba, & A Delaunay. (2014). Cell Biology of Cysteine-Based Molecular Switches. International Journal of Cell Biology. 2014. 1–2. 1 indexed citations

16.

Sannino, Sara, Tiziana Anelli, Margherita Cortini, et al.. (2014). Progressive quality control of secretory proteins in the early secretory compartment by ERp44. Journal of Cell Science. 127(Pt 19). 4260–9. 36 indexed citations

17.

Hagiwara, Masatoshi, Mamoru Suzuki, Ryo Ushioda, et al.. (2011). Structural Basis of an ERAD Pathway Mediated by the ER-Resident Protein Disulfide Reductase ERdj5. Molecular Cell. 41(4). 432–444. 114 indexed citations

18.

Kamiya, Yukiko, Michiko Nakano, Hiroaki Sasakawa, et al.. (2009). Redox-Dependent Domain Rearrangement of Protein Disulfide Isomerase Coupled with Exposure of Its Substrate-Binding Hydrophobic Surface. Journal of Molecular Biology. 396(2). 361–374. 55 indexed citations

19.

Inaba, Kenji & Koreaki Ito. (2007). Structure and mechanisms of the DsbB–DsbA disulfide bond generation machine. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1783(4). 520–529. 74 indexed citations

20.

Shirai, Tsuyoshi, et al.. (1998). Design, construction, crystallization, and preliminary X-ray studies of a fine-tuning mutant (F133V) of module-substituted chimera hemoglobin. Proteins Structure Function and Bioinformatics. 32(3). 263–267. 2 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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