Max Nanao

4.6k total citations · 1 hit paper
63 papers, 3.1k citations indexed

About

Max Nanao is a scholar working on Molecular Biology, Materials Chemistry and Plant Science. According to data from OpenAlex, Max Nanao has authored 63 papers receiving a total of 3.1k indexed citations (citations by other indexed papers that have themselves been cited), including 41 papers in Molecular Biology, 25 papers in Materials Chemistry and 14 papers in Plant Science. Recurrent topics in Max Nanao's work include Enzyme Structure and Function (21 papers), Plant Molecular Biology Research (14 papers) and Protein Structure and Dynamics (11 papers). Max Nanao is often cited by papers focused on Enzyme Structure and Function (21 papers), Plant Molecular Biology Research (14 papers) and Protein Structure and Dynamics (11 papers). Max Nanao collaborates with scholars based in France, United States and Germany. Max Nanao's co-authors include Renaud Dumas, Chloé Zubieta, Raimond B. G. Ravelli, Joseph M. Jez, Corey S. Westfall, Senyon Choe, S. Cusack, François Parcy, Rob W. H. Ruigrok and Darren J. Hart and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Max Nanao

61 papers receiving 3.1k citations

Hit Papers

align trajectories sort by overperformance

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Structural insight into cap-snatching and RNA synthesis by influenza polymerase

2014 354 citations Max Nanao, Rob W. H. Ruigrok et al. profile →

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author						Papers	Cites
Max Nanao	2.0k	1.0k	505	324	277	63	3.1k
Adam Round	2.5k 1.3×	625 0.6×	759 1.5×	278 0.9×	122 0.4×	80	3.9k
Robert P. Rambo	4.3k 2.2×	520 0.5×	960 1.9×	232 0.7×	160 0.6×	63	5.4k
Robert L. Shoeman	2.5k 1.3×	552 0.5×	812 1.6×	192 0.6×	332 1.2×	98	4.0k
Eugene Palovcak	4.1k 2.1×	330 0.3×	496 1.0×	342 1.1×	534 1.9×	13	5.9k
Dari Kimanius	4.1k 2.1×	255 0.3×	562 1.1×	333 1.0×	527 1.9×	22	5.8k
Kliment A. Verba	4.3k 2.2×	301 0.3×	544 1.1×	338 1.0×	531 1.9×	19	5.9k
Dominika Borek	2.0k 1.0×	231 0.2×	360 0.7×	373 1.2×	688 2.5×	70	3.9k
Carsten Sachse	3.0k 1.5×	214 0.2×	350 0.7×	750 2.3×	260 0.9×	79	4.5k
Oleg V. Sobolev	2.7k 1.4×	178 0.2×	860 1.7×	244 0.8×	314 1.1×	60	4.4k
Barry Stoddard	5.9k 3.0×	793 0.8×	572 1.1×	128 0.4×	101 0.4×	109	7.0k

Countries citing papers authored by Max Nanao

Since Specialization

Citations

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

Fields of papers citing papers by Max Nanao

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Max Nanao

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

Nanao, Max, Gerd Schluckebier, Mathias Norrman, et al.. (2025). Exploring humidity effects on polycrystalline human insulin–ligand complexes: preliminary crystallographic insights. Journal of Applied Crystallography. 58(6). 1920–1935.

Rieu, Philippe, Francesca Caselli, Emmanuel Thévenon, et al.. (2024). The ALOG domain defines a family of plant-specific transcription factors acting during Arabidopsis flower development. Proceedings of the National Academy of Sciences. 121(10). e2310464121–e2310464121. 11 indexed citations

Hugouvieux, Véronique, Romain Blanc‐Mathieu, Jérémy Lucas, et al.. (2024). SEPALLATA-driven MADS transcription factor tetramerization is required for inner whorl floral organ development. The Plant Cell. 36(9). 3435–3450. 11 indexed citations

Felisaz, Franck, Antonia Beteva, Matthew W. Bowler, et al.. (2024). In situ serial crystallography facilitates 96-well plate structural analysis at low symmetry. IUCrJ. 11(5). 780–791. 1 indexed citations

Rieu, Philippe, Laura Turchi, Emmanuel Thévenon, et al.. (2023). The F-box protein UFO controls flower development by redirecting the master transcription factor LEAFY to new cis-elements. Nature Plants. 9(2). 315–329. 24 indexed citations

Hutin, Stephanie, Janet R. Kumita, Vivien I. Strotmann, et al.. (2023). Phase separation and molecular ordering of the prion-like domain of the Arabidopsis thermosensory protein EARLY FLOWERING 3. Proceedings of the National Academy of Sciences. 120(28). e2304714120–e2304714120. 30 indexed citations

Bessa, Luiza M., Serafima Guseva, Aldo R. Camacho‐Zarco, et al.. (2022). The intrinsically disordered SARS-CoV-2 nucleoprotein in dynamic complex with its viral partner nsp3a. Science Advances. 8(3). eabm4034–eabm4034. 59 indexed citations

Lai, Xuelei, Véronique Hugouvieux, Romain Blanc‐Mathieu, et al.. (2021). The intervening domain is required for DNA-binding and functional identity of plant MADS transcription factors. Nature Communications. 12(1). 4760–4760. 44 indexed citations

Silva, Catarina S., Xuelei Lai, Stephanie Hutin, et al.. (2020). Molecular mechanisms of Evening Complex activity in Arabidopsis. Proceedings of the National Academy of Sciences. 117(12). 6901–6909. 113 indexed citations

10.

Fellows, Rachel, Christopher M. Russo, Catarina S. Silva, et al.. (2018). A multisubstrate reductase from Plantago major: structure-function in the short chain reductase superfamily. Scientific Reports. 8(1). 14796–14796. 11 indexed citations

11.

Martín-Arevalillo, Raquel, Max Nanao, Antoine Larrieu, et al.. (2017). Structure of the Arabidopsis TOPLESS corepressor provides insight into the evolution of transcriptional repression. Proceedings of the National Academy of Sciences. 114(30). 8107–8112. 68 indexed citations

12.

Vito, Alyssa, Nancy Janzen, Max Nanao, et al.. (2016). Preparation of an ¹⁸F‐Labeled Hydrocyanine Dye as a Multimodal Probe for Reactive Oxygen Species. Chemistry - A European Journal. 23(2). 254–258. 44 indexed citations

13.

Sanctis, Daniele de, Chloé Zubieta, Franck Felisaz, Hugo Caserotto, & Max Nanao. (2016). Radiation-damage-induced phasing: a case study using UV irradiation with light-emitting diodes. Acta Crystallographica Section D Structural Biology. 72(3). 395–402. 6 indexed citations

14.

Sayou, Camille, Marie Monniaux, Max Nanao, et al.. (2014). A Promiscuous Intermediate Underlies the Evolution of LEAFY DNA Binding Specificity. Science. 343(6171). 645–648. 97 indexed citations

15.

Korasick, David A., Corey S. Westfall, Soon Goo Lee, et al.. (2014). Molecular basis for AUXIN RESPONSE FACTOR protein interaction and the control of auxin response repression. Proceedings of the National Academy of Sciences. 111(14). 5427–5432. 229 indexed citations

16.

Larabi, Amédé, Juliette M. Devos, Sze‐Ling Ng, et al.. (2013). Crystal Structure and Mechanism of Activation of TANK-Binding Kinase 1. Cell Reports. 3(3). 734–746. 186 indexed citations

17.

Sanctis, Daniele de & Max Nanao. (2012). Segmenting data sets for RIP. Acta Crystallographica Section D Biological Crystallography. 68(9). 1152–1162. 14 indexed citations

18.

Rudiño-Piñera, E., Raimond B. G. Ravelli, George M. Sheldrick, et al.. (2007). The Solution and Crystal Structures of a Module Pair from the Staphylococcus aureus-Binding Site of Human Fibronectin—A Tale with a Twist. Journal of Molecular Biology. 368(3). 833–844. 31 indexed citations

19.

Zhang, Yihong, Naushaba Nayeem, Max Nanao, & T.C. Green. (2006). Interface Interactions Modulating Desensitization of the Kainate-Selective Ionotropic Glutamate Receptor Subunit GluR6. Journal of Neuroscience. 26(39). 10033–10042. 24 indexed citations

20.

Nanao, Max, Tim Green, Yael Stern-Bach, Stephen F. Heinemann, & Senyon Choe. (2005). Structure of the kainate receptor subunit GluR6 agonist-binding domain complexed with domoic acid. Proceedings of the National Academy of Sciences. 102(5). 1708–1713. 101 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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