Satoru Tuzi

2.5k total citations
81 papers, 1.9k citations indexed

About

Satoru Tuzi is a scholar working on Cellular and Molecular Neuroscience, Spectroscopy and Molecular Biology. According to data from OpenAlex, Satoru Tuzi has authored 81 papers receiving a total of 1.9k indexed citations (citations by other indexed papers that have themselves been cited), including 47 papers in Cellular and Molecular Neuroscience, 43 papers in Spectroscopy and 29 papers in Molecular Biology. Recurrent topics in Satoru Tuzi's work include Photoreceptor and optogenetics research (44 papers), Neuroscience and Neuropharmacology Research (42 papers) and Advanced NMR Techniques and Applications (35 papers). Satoru Tuzi is often cited by papers focused on Photoreceptor and optogenetics research (44 papers), Neuroscience and Neuropharmacology Research (42 papers) and Advanced NMR Techniques and Applications (35 papers). Satoru Tuzi collaborates with scholars based in Japan, United States and Italy. Satoru Tuzi's co-authors include Hazime Saitô, Akira Naito, Michikazu Tanio, Satoru Yamaguchi, Janos Κ. Lanyi, Richard Needleman, Katsuyuki Nishimura, Miya Kamihira, Akira Naito and Atsuko Y. Nosaka and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Journal of Applied Physics.

In The Last Decade

Satoru Tuzi

81 papers receiving 1.9k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Satoru Tuzi Japan	25	876	821	789	298	160	81	1.9k
Izuru Kawamura Japan	21	562 0.6×	299 0.4×	590 0.7×	364 1.2×	196 1.2×	100	1.5k
Martin Engelhard Germany	25	1.2k 1.4×	337 0.4×	334 0.4×	282 0.9×	54 0.3×	52	1.8k
Manuel Etzkorn Germany	23	1.3k 1.5×	219 0.3×	892 1.1×	415 1.4×	69 0.4×	50	2.1k
Lena Mäler Sweden	26	1.4k 1.6×	150 0.2×	417 0.5×	211 0.7×	126 0.8×	83	2.0k
Gemma Comellas United States	13	810 0.9×	166 0.2×	499 0.6×	296 1.0×	137 0.9×	14	2.1k
Jean‐Michel Neumann France	25	1.9k 2.1×	334 0.4×	292 0.4×	152 0.5×	50 0.3×	89	2.2k
Dror E. Warschawski France	23	1.3k 1.4×	108 0.1×	539 0.7×	176 0.6×	142 0.9×	53	1.8k
Denise V. Greathouse United States	31	3.0k 3.4×	528 0.6×	415 0.5×	107 0.4×	319 2.0×	81	3.3k
Alessandro Cembran United States	26	1.0k 1.1×	711 0.9×	280 0.4×	817 2.7×	61 0.4×	44	2.3k
Sorin Luca Germany	16	871 1.0×	133 0.2×	800 1.0×	430 1.4×	158 1.0×	19	1.6k

Countries citing papers authored by Satoru Tuzi

Since Specialization

Citations

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

Fields of papers citing papers by Satoru Tuzi

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Satoru Tuzi

This figure shows the co-authorship network connecting the top 25 collaborators of Satoru Tuzi. A scholar is included among the top collaborators of Satoru Tuzi 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 Satoru Tuzi. Satoru Tuzi 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

Nakai, Toshiharu, Yasushi Sugano, Makoto Shoda, et al.. (2012). Formation of Highly Twisted Ribbons in a Carboxymethylcellulase Gene-Disrupted Strain of a Cellulose-Producing Bacterium. Journal of Bacteriology. 195(5). 958–964. 65 indexed citations

Kawamura, Izuru, Yoichi Ikeda, Satoru Yamaguchi, et al.. (2008). Dynamics Change of Phoborhodopsin and Transducer by Activation: Study Using D75N Mutant of the Receptor by Site‐directed Solid‐state ¹³C NMR^†. Photochemistry and Photobiology. 84(4). 921–930. 6 indexed citations

Kawamura, Izuru, et al.. (2007). Dynamic aspects of extracellular loop region as a proton release pathway of bacteriorhodopsin studied by relaxation time measurements by solid state NMR. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1768(12). 3090–3097. 14 indexed citations

Saitô, Hazime, Kazutoshi Yamamoto, Michikazu Tanio, et al.. (2007). Surface and Dynamic Structures of Bacteriorhodopsin in a 2D Crystal, a Distorted or Disrupted Lattice, as Revealed by Site-directed Solid-state 13C NMR†. Photochemistry and Photobiology. 83(2). 253–262. 13 indexed citations

Yamamoto, Kazutoshi, Satoru Tuzi, Hazime Saitô, Izuru Kawamura, & Akira Naito. (2006). Conformation and dynamics changes of bacteriorhodopsin and its D85N mutant in the absence of 2D crystalline lattice as revealed by site-directed 13C NMR. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1758(2). 181–189. 9 indexed citations

Hirai, Manabu, et al.. (2004). Tolerance to freezing stress in cyanobacteria, Nostoc commune and some cyanobacteria with various tolerances to drying stress. Institutional Repository National Institute of Polar Research (National Institute of Polar Research (Japan)). 17. 56–68. 9 indexed citations

Saitô, Hazime, Satoru Yamaguchi, Keiji OGAWA, et al.. (2004). Glutamic Acid Residues of Bacteriorhodopsin at the Extracellular Surface as Determinants for Conformation and Dynamics as Revealed by Site-Directed Solid-State 13C NMR. Biophysical Journal. 86(3). 1673–1681. 17 indexed citations

Saitô, Hazime, et al.. (2004). Site‐directed ¹³C solid‐state NMR studies on membrane proteins: strategy and goals toward revealing conformation and dynamics as illustrated for bacteriorhodopsin labeled with [1‐¹³C]amino acid residues. Magnetic Resonance in Chemistry. 42(2). 218–230. 20 indexed citations

Yamaguchi, Satoru, Kazumi Shimono, Yuki Sudo, et al.. (2003). Conformation and Dynamics of Cytoplasmic Domain of Truncated pharaonis Transducer, pHtr II (1-159) as Revealed by Solid-state NMR. Seibutsu Butsuri. 43(supplement). S193–S193. 1 indexed citations

10.

Saitô, Hazime, et al.. (2002). Residue-specific millisecond to microsecond fluctuations in bacteriorhodopsin induced by disrupted or disorganized two-dimensional crystalline lattice, through modified lipid–helix and helix–helix interactions, as revealed by 13C NMR. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1565(1). 97–106. 26 indexed citations

11.

Naito, Akira, Takashi M. Nagao, Manabu Okamoto, et al.. (2002). Dynorphin induced magnetic ordering in lipid bilayers as studied by 31P NMR spectroscopy. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1558(1). 34–44. 31 indexed citations

12.

Yamaguchi, Satoru, et al.. (2000). Cation-induced alterations on the cytoplasic surface structure and dynamics of bacteriorhodopsin, as viewed by solid state <13>^C NMR. Seibutsu Butsuri. 40(supplement). S130–S130. 1 indexed citations

13.

Kamihira, Miya, Akira Naito, Satoru Tuzi, & Hazime Saitô. (1999). Phenyl Ring Dynamics of Enkephalin Molecules and Behavior of Bound Solvents in the Crystalline States by ²H NMR Spectroscopy. The Journal of Physical Chemistry A. 103(18). 3356–3363. 24 indexed citations

14.

Nagao, Takashi M., Akira Naito, Satoru Tuzi, & Hazime Saitô. (1998). Conformation and Orientation of Biologically Active Peptide Alamethicin in Phospholipid Bilayer by High-Resolution Solid-State NMR Spectroscopy. 1998. 341–344. 1 indexed citations

15.

Nishimura, Katsuyuki, et al.. (1998). Determination of the Three-Dimensional Structure of Crystalline Leu-Enkephalin Dihydrate Based on Six Sets of Accurately Determined Interatomic Distances from ¹³C-REDOR NMR and the Conformation-Dependent ¹³C Chemical Shifts. The Journal of Physical Chemistry B. 102(38). 7476–7483. 24 indexed citations

16.

Naito, Akira, et al.. (1998). Backbone dynamics of polycrystalline peptides studied by measurements of 15N NMR lineshapes and 13C transverse relaxation times. Journal of Molecular Structure. 441(2-3). 231–241. 29 indexed citations

17.

Yamazaki, Yoichi, Satoru Tuzi, Hazime Saitô, et al.. (1996). Hydrogen Bonds of Water and CO Groups Coordinate Long-Range Structural Changes in the L Photointermediate of Bacteriorhodopsin. Biochemistry. 35(13). 4063–4068. 35 indexed citations

18.

Tuzi, Satoru, Akira Naito, & Hazime Saitô. (1996). Temperature‐Dependent Conformational Change of Bacteriorhodopsin as Studied by Solid‐State ¹³C NMR. European Journal of Biochemistry. 239(2). 294–301. 33 indexed citations

19.

Naito, Akira, Katsuyuki Nishimura, Satoru Tuzi, & Hazime Saitô. (1994). Inter- and intra-molecular contributions of neighboring dipolar pairs to the precise determination of interatomic distances in a simple [13C, 15N]-peptide by 13C, 15N-REDOR NMR spectroscopy. Chemical Physics Letters. 229(4-5). 506–511. 60 indexed citations

20.

Naito, Akira, Satoru Tuzi, & Hazime Saitô. (1994). A High‐resolution ¹⁵N Solid‐state NMR Study of Collagen and Related Polypeptides. European Journal of Biochemistry. 224(2). 729–734. 41 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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