N. Nishida

4.2k total citations · 1 hit paper
74 papers, 3.3k citations indexed

About

N. Nishida is a scholar working on Molecular Biology, Atomic and Molecular Physics, and Optics and Condensed Matter Physics. According to data from OpenAlex, N. Nishida has authored 74 papers receiving a total of 3.3k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 22 papers in Atomic and Molecular Physics, and Optics and 16 papers in Condensed Matter Physics. Recurrent topics in N. Nishida's work include Advanced NMR Techniques and Applications (11 papers), Quantum, superfluid, helium dynamics (10 papers) and Protein Structure and Dynamics (9 papers). N. Nishida is often cited by papers focused on Advanced NMR Techniques and Applications (11 papers), Quantum, superfluid, helium dynamics (10 papers) and Protein Structure and Dynamics (9 papers). N. Nishida collaborates with scholars based in Japan, Canada and United States. N. Nishida's co-authors include Timothy A. Springer, R. Hayano, Toshitsugu Yamazaki, J. Imazato, Thomas Walz, Y. J. Uemura, Ichio Shimada, Ryogo Kubo, Jianghai Zhu and Can Xie and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Physical Review Letters.

In The Last Decade

N. Nishida

73 papers receiving 3.2k citations

Hit Papers

Zero-and low-field spin relaxation studied by positive muons 1979 2026 1994 2010 1979 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
N. Nishida Japan 28 1.0k 802 759 513 467 74 3.3k
Georgina Lang United Kingdom 30 2.0k 2.0× 235 0.3× 141 0.2× 289 0.6× 925 2.0× 62 4.4k
D. Norman United Kingdom 53 5.1k 5.0× 161 0.2× 185 0.2× 1.3k 2.6× 286 0.6× 175 8.9k
Jizhong Lou China 34 1.9k 1.9× 587 0.7× 222 0.3× 753 1.5× 947 2.0× 107 3.8k
M.F. Garcia Parajo Spain 49 2.9k 2.9× 222 0.3× 100 0.1× 1.6k 3.1× 535 1.1× 137 7.0k
Takeshi Kambara Japan 34 650 0.6× 173 0.2× 129 0.2× 196 0.4× 90 0.2× 174 3.3k
Albert J. Jin United States 39 2.1k 2.0× 69 0.1× 282 0.4× 487 0.9× 707 1.5× 71 5.0k
Hitoshi Yamazaki Japan 31 1.2k 1.2× 62 0.1× 433 0.6× 323 0.6× 107 0.2× 201 3.4k
Andrew J. Lindsay Ireland 31 883 0.9× 178 0.2× 900 1.2× 1.6k 3.1× 905 1.9× 82 3.3k
Anirban Mitra India 31 1.5k 1.4× 224 0.3× 87 0.1× 208 0.4× 284 0.6× 126 3.9k
Matthew J. Lang United States 40 1.8k 1.7× 198 0.2× 153 0.2× 2.4k 4.7× 1.4k 3.0× 100 5.5k

Countries citing papers authored by N. Nishida

Since Specialization
Citations

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

Fields of papers citing papers by N. Nishida

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of N. Nishida

This figure shows the co-authorship network connecting the top 25 collaborators of N. Nishida. A scholar is included among the top collaborators of N. Nishida 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 N. Nishida. N. Nishida 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.
Nishida, N., et al.. (2025). Bioreactor in-cell NMR: A powerful tool for observing intracellular biological events. Current Opinion in Structural Biology. 93. 103086–103086. 2 indexed citations
2.
Lim, Keesiang, M. Tamura, Akiko Kobayashi, et al.. (2023). Nanoscopic Elucidation of Spontaneous Self-Assembly of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Open Reading Frame 6 (ORF6) Protein. The Journal of Physical Chemistry Letters. 14(38). 8385–8396. 11 indexed citations
3.
Shimada, Ichio, et al.. (2023). Real-time monitoring of the reaction of KRAS G12C mutant specific covalent inhibitor by in vitro and in-cell NMR spectroscopy. Scientific Reports. 13(1). 19253–19253. 4 indexed citations
4.
Nishida, N., et al.. (2020). Structural basis for two-way communication between dynein and microtubules. Nature Communications. 11(1). 1038–1038. 17 indexed citations
5.
Nishida, N., Yutaka Ito, & Ichio Shimada. (2019). In situ structural biology using in-cell NMR. Biochimica et Biophysica Acta (BBA) - General Subjects. 1864(2). 129364–129364. 22 indexed citations
6.
Huang, Shuxian, Yuki Tamura, Yutaka Kofuku, et al.. (2016). Utilization of paramagnetic relaxation enhancements for structural analysis of actin-binding proteins in complex with actin. Scientific Reports. 6(1). 33690–33690. 9 indexed citations
7.
Ueda, Takumi, Koh Takeuchi, N. Nishida, et al.. (2014). Cross-saturation and transferred cross-saturation experiments. Quarterly Reviews of Biophysics. 47(2). 143–187. 19 indexed citations
8.
Nishida, N., Maho Yagi‐Utsumi, Fumihiro Motojima, et al.. (2013). Nuclear magnetic resonance approaches for characterizing interactions between the bacterial chaperonin GroEL and unstructured proteins. Journal of Bioscience and Bioengineering. 116(2). 160–164. 18 indexed citations
10.
Nishida, N., Masanori Osawa, Koh Takeuchi, et al.. (2013). Functional dynamics of cell surface membrane proteins. Journal of Magnetic Resonance. 241. 86–96. 9 indexed citations
11.
Osawa, Masanori, Koh Takeuchi, Takumi Ueda, N. Nishida, & Ichio Shimada. (2012). Functional dynamics of proteins revealed by solution NMR. Current Opinion in Structural Biology. 22(5). 660–669. 30 indexed citations
12.
Kubo, S., et al.. (2012). A Gel‐Encapsulated Bioreactor System for NMR Studies of Protein–Protein Interactions in Living Mammalian Cells. Angewandte Chemie International Edition. 52(4). 1208–1211. 95 indexed citations
13.
Nishida, N. & Ichio Shimada. (2011). An NMR Method to Study Protein–Protein Interactions. Methods in molecular biology. 757. 129–137. 9 indexed citations
14.
Mi, Li-Zhi, Chafen Lu, Zongli Li, et al.. (2011). Simultaneous visualization of the extracellular and cytoplasmic domains of the epidermal growth factor receptor. Nature Structural & Molecular Biology. 18(9). 984–989. 101 indexed citations
15.
Eng, Edward T., et al.. (2011). A pH‐regulated dimeric bouquet in the structure of von Willebrand factor. The EMBO Journal. 30(19). 4098–4111. 95 indexed citations
16.
Nishida, N., et al.. (2010). NMR structure of the calponin homology domain of human IQGAP1 and its implications for the actin recognition mode. Journal of Biomolecular NMR. 48(1). 59–64. 15 indexed citations
17.
Xie, Can, Jianghai Zhu, Xing Chen, et al.. (2009). Structure of an integrin with an αI domain, complement receptor type 4. The EMBO Journal. 29(3). 666–679. 149 indexed citations
18.
Zhu, Jianghai, Bing‐Hao Luo, Tsan Sam Xiao, et al.. (2008). Structure of a Complete Integrin Ectodomain in a Physiologic Resting State and Activation and Deactivation by Applied Forces. Molecular Cell. 32(6). 849–861. 390 indexed citations
19.
Nishida, N., Fumihiro Motojima, Hiroshi Fujikawa, et al.. (2006). Probing Dynamics and Conformational Change of the GroEL-GroES Complex by 13C NMR Spectroscopy. The Journal of Biochemistry. 140(4). 591–598. 22 indexed citations
20.
Kimata, Mitsuyοshi & N. Nishida. (1987). THE CRYSTAL-STRUCTURE OF CO-MONTICELLITE CA1.255CO0.745SIO4 AND ITS SIGNIFICANCE AS A SOLID-SOLUTION CRYSTAL. 160–170. 1 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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