Nathan R. Rose

5.6k total citations · 1 hit paper
32 papers, 4.1k citations indexed

About

Nathan R. Rose is a scholar working on Molecular Biology, Cancer Research and Oncology. According to data from OpenAlex, Nathan R. Rose has authored 32 papers receiving a total of 4.1k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 6 papers in Cancer Research and 4 papers in Oncology. Recurrent topics in Nathan R. Rose's work include Epigenetics and DNA Methylation (23 papers), Histone Deacetylase Inhibitors Research (13 papers) and Cancer-related gene regulation (13 papers). Nathan R. Rose is often cited by papers focused on Epigenetics and DNA Methylation (23 papers), Histone Deacetylase Inhibitors Research (13 papers) and Cancer-related gene regulation (13 papers). Nathan R. Rose collaborates with scholars based in United Kingdom, United States and Singapore. Nathan R. Rose's co-authors include Robert J. Klose, Christopher J. Schofield, M.A. McDonough, Oliver N. F. King, Akane Kawamura, Neil P. Blackledge, Udo Oppermann, Stanley S. Ng, Esther C. Y. Woon and Peter J. Ratcliffe and has published in prestigious journals such as Nature, Chemical Society Reviews and Journal of Biological Chemistry.

In The Last Decade

Nathan R. Rose

32 papers receiving 4.0k citations

Hit Papers

The oncometabolite 2‐hydroxyglutarate inhibits histone ly... 2011 2026 2016 2021 2011 250 500 750

Peers

Nathan R. Rose
Christoph Loenarz United Kingdom
Oliver N. F. King United Kingdom
Punit P. Seth United States
Jinyun Liu United States
Jordan M. Cummins United States
Sonia Franco United States
Michael R. Schlabach United States
Aurelio Lorico United States
Christoph Loenarz United Kingdom
Nathan R. Rose
Citations per year, relative to Nathan R. Rose Nathan R. Rose (= 1×) peers Christoph Loenarz

Countries citing papers authored by Nathan R. Rose

Since Specialization
Citations

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

Fields of papers citing papers by Nathan R. Rose

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Nathan R. Rose. 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 Nathan R. Rose. The network helps show where Nathan R. Rose may publish in the future.

Co-authorship network of co-authors of Nathan R. Rose

This figure shows the co-authorship network connecting the top 25 collaborators of Nathan R. Rose. A scholar is included among the top collaborators of Nathan R. Rose 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 Nathan R. Rose. Nathan R. Rose 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.
Long, Hannah K., Nathan R. Rose, Neil P. Blackledge, & Robert J. Klose. (2018). Biochemical Identification of Nonmethylated DNA by BioCAP-Seq. Methods in molecular biology. 1766. 15–29. 1 indexed citations
2.
Hopkinson, Richard J., Ivanhoe K. H. Leung, Nathan R. Rose, et al.. (2015). Studies on the Glutathione-Dependent Formaldehyde-Activating Enzyme from Paracoccus denitrificans. PLoS ONE. 10(12). e0145085–e0145085. 10 indexed citations
3.
Blackledge, Neil P., Nathan R. Rose, & Robert J. Klose. (2015). Targeting Polycomb systems to regulate gene expression: modifications to a complex story. Nature Reviews Molecular Cell Biology. 16(11). 643–649. 266 indexed citations
4.
Hopkinson, Richard J., Louise J. Walport, Martin Münzel, et al.. (2013). Is JmjC Oxygenase Catalysis Limited to Demethylation?. Angewandte Chemie. 125(30). 7863–7867. 4 indexed citations
5.
Hopkinson, Richard J., Louise J. Walport, Martin Münzel, et al.. (2013). Is JmjC Oxygenase Catalysis Limited to Demethylation?. Angewandte Chemie International Edition. 52(30). 7709–7713. 34 indexed citations
6.
Rai, Ganesha, Akane Kawamura, Anthony Tumber, et al.. (2013). Discovery of ML324, a JMJD2 demethylase inhibitor with demonstrated antiviral activity. 25 indexed citations
7.
Woon, Esther C. Y., Anthony Tumber, Akane Kawamura, et al.. (2012). Linking of 2‐Oxoglutarate and Substrate Binding Sites Enables Potent and Highly Selective Inhibition of JmjC Histone Demethylases. Angewandte Chemie International Edition. 51(7). 1631–1634. 55 indexed citations
8.
Chang, Kai‐Hsuan, Oliver N. F. King, Anthony Tumber, et al.. (2011). Inhibition of Histone Demethylases by 4‐Carboxy‐2,2′‐Bipyridyl Compounds. ChemMedChem. 6(5). 759–764. 61 indexed citations
9.
Hillringhaus, Lars, Wyatt W. Yue, Nathan R. Rose, et al.. (2011). Structural and Evolutionary Basis for the Dual Substrate Selectivity of Human KDM4 Histone Demethylase Family. Journal of Biological Chemistry. 286(48). 41616–41625. 140 indexed citations
10.
Chowdhury, Rasheduzzaman, Kar Kheng Yeoh, Ya‐Min Tian, et al.. (2011). The oncometabolite 2‐hydroxyglutarate inhibits histone lysine demethylases. EMBO Reports. 12(5). 463–469. 762 indexed citations breakdown →
11.
Rose, Nathan R., M.A. McDonough, Oliver N. F. King, Akane Kawamura, & Christopher J. Schofield. (2011). Inhibition of 2-oxoglutarate dependent oxygenases. Chemical Society Reviews. 40(8). 4364–4364. 304 indexed citations
12.
Thalhammer, Armin, Jasmin Mecinović, Christoph Loenarz, et al.. (2010). Inhibition of the histone demethylase JMJD2E by 3-substituted pyridine 2,4-dicarboxylates. Organic & Biomolecular Chemistry. 9(1). 127–135. 48 indexed citations
13.
Kawamura, Akane, Anthony Tumber, Nathan R. Rose, et al.. (2010). Development of homogeneous luminescence assays for histone demethylase catalysis and binding. Analytical Biochemistry. 404(1). 86–93. 51 indexed citations
14.
Hopkinson, Richard J., Refaat B. Hamed, Nathan R. Rose, Timothy D. W. Claridge, & Christopher J. Schofield. (2010). Monitoring the Activity of 2‐Oxoglutarate Dependent Histone Demethylases by NMR Spectroscopy: Direct Observation of Formaldehyde. ChemBioChem. 11(4). 506–510. 53 indexed citations
15.
King, Oliver N. F., Masaaki Sakurai, Akane Kawamura, et al.. (2010). Quantitative High-Throughput Screening Identifies 8-Hydroxyquinolines as Cell-Active Histone Demethylase Inhibitors. PLoS ONE. 5(11). e15535–e15535. 173 indexed citations
16.
Sekirnik, Rok, Nathan R. Rose, Jasmin Mecinović, & Christopher J. Schofield. (2010). 2-Oxoglutarate oxygenases are inhibited by a range of transition metals. Metallomics. 2(6). 397–397. 28 indexed citations
17.
Sakurai, Masaaki, Nathan R. Rose, Lena Schultz, et al.. (2009). A miniaturized screen for inhibitors of Jumonji histonedemethylases. Molecular BioSystems. 6(2). 357–364. 76 indexed citations
18.
Sekirnik, Rok, Nathan R. Rose, Armin Thalhammer, et al.. (2009). Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(ii). Chemical Communications. 6376–6376. 72 indexed citations
19.
Loenarz, Christoph, Wei Ge, Mathew L. Coleman, et al.. (2009). PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an Nε-dimethyl lysine demethylase. Human Molecular Genetics. 19(2). 217–222. 136 indexed citations
20.
Ng, Stanley S., K.L. Kavanagh, M.A. McDonough, et al.. (2007). Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Nature. 448(7149). 87–91. 263 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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