David E. Heppner

4.6k total citations · 2 hit papers
50 papers, 3.3k citations indexed

About

David E. Heppner is a scholar working on Molecular Biology, Oncology and Immunology. According to data from OpenAlex, David E. Heppner has authored 50 papers receiving a total of 3.3k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 16 papers in Oncology and 15 papers in Immunology. Recurrent topics in David E. Heppner's work include Lung Cancer Treatments and Mutations (13 papers), Cancer therapeutics and mechanisms (12 papers) and Neutrophil, Myeloperoxidase and Oxidative Mechanisms (11 papers). David E. Heppner is often cited by papers focused on Lung Cancer Treatments and Mutations (13 papers), Cancer therapeutics and mechanisms (12 papers) and Neutrophil, Myeloperoxidase and Oxidative Mechanisms (11 papers). David E. Heppner collaborates with scholars based in United States, Germany and Hungary. David E. Heppner's co-authors include Edward I. Solomon, Christian H. Kjaergaard, Matthew T. Kieber‐Emmons, Jake W. Ginsbach, Li Tian, Jordi Cirera, Munzarin F. Qayyum, Ryan G. Hadt, Esther M. Johnston and Albert van der Vliet and has published in prestigious journals such as Cell, Chemical Reviews and Journal of the American Chemical Society.

In The Last Decade

David E. Heppner

45 papers receiving 3.3k citations

Hit Papers

Copper Active Sites in Biology 2014 2026 2018 2022 2014 2020 400 800 1.2k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
David E. Heppner United States 26 1.4k 1.1k 933 631 611 50 3.3k
Júlio S. Rebouças Brazil 33 976 0.7× 928 0.9× 325 0.3× 1.2k 1.9× 611 1.0× 91 2.9k
Hong‐Ke Liu China 28 765 0.6× 1.0k 1.0× 1.2k 1.3× 778 1.2× 1.1k 1.8× 87 3.2k
Seungwoo Hong South Korea 31 696 0.5× 1.7k 1.6× 794 0.9× 1.1k 1.8× 678 1.1× 91 2.9k
Takafumi Ueno Japan 38 2.5k 1.8× 955 0.9× 652 0.7× 1.3k 2.1× 1.1k 1.8× 144 4.9k
Nicolai Burzlaff Germany 28 641 0.5× 936 0.9× 787 0.8× 367 0.6× 1.0k 1.7× 98 2.5k
Hong Liang China 38 1.7k 1.3× 545 0.5× 1.6k 1.7× 1.3k 2.0× 1.1k 1.8× 158 4.3k
Patric J. Jansson Australia 42 2.6k 1.9× 417 0.4× 2.4k 2.5× 320 0.5× 981 1.6× 85 5.5k
Christian R. Kowol Austria 37 1.3k 1.0× 839 0.8× 3.1k 3.4× 693 1.1× 2.2k 3.5× 109 4.8k
Yong Qian China 29 685 0.5× 236 0.2× 423 0.5× 730 1.2× 841 1.4× 89 3.1k
Robert F. Anderson New Zealand 36 1.6k 1.2× 243 0.2× 439 0.5× 297 0.5× 997 1.6× 150 3.6k

Countries citing papers authored by David E. Heppner

Since Specialization
Citations

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

Fields of papers citing papers by David E. Heppner

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by David E. Heppner. 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 David E. Heppner. The network helps show where David E. Heppner may publish in the future.

Co-authorship network of co-authors of David E. Heppner

This figure shows the co-authorship network connecting the top 25 collaborators of David E. Heppner. A scholar is included among the top collaborators of David E. Heppner 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 David E. Heppner. David E. Heppner 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.
Möllers, Mareike, Torbjörn Hartman, Marcel Günther, et al.. (2025). Structure–Activity Relationships of Inactive‐Conformation Binding EGFR Inhibitors: Linking the ATP and Allosteric Pockets. Archiv der Pharmazie. 358(7). e70027–e70027.
2.
Lin, Kui, et al.. (2025). Profiling and Optimizing Targeted Covalent Inhibitors through EGFR-Guided Studies. Journal of Medicinal Chemistry. 68(16). 17917–17932. 1 indexed citations
3.
Reis, Joana, Miao-chong J. Lin, Qing Lin, et al.. (2025). Enhancing Selectivity and Potency of SNAr Covalent Inhibitors of NADPH Oxidase Enzymes. Journal of Medicinal Chemistry. 68(13). 14072–14084.
4.
Heppner, David E., et al.. (2025). Lazertinib: breaking the mold of third-generation EGFR inhibitors. RSC Medicinal Chemistry. 16(3). 1049–1066. 8 indexed citations
5.
Heppner, David E., et al.. (2024). Design and characterization of NOX-targeting compounds for improved understanding of covalent inhibitors. Free Radical Biology and Medicine. 218. 5–5.
6.
Damayanti, Nur P., et al.. (2024). TFE3-Splicing Factor Fusions Represent Functional Drivers and Druggable Targets in Translocation Renal Cell Carcinoma. Cancer Research. 84(8). 1286–1302. 5 indexed citations
7.
Lacy, David C., et al.. (2024). Twelve CO molecules for the price of one. A simple water-soluble organometallic CORM, [Mn(CO)3(µ3-OH)]4. Polyhedron. 251. 116859–116859. 2 indexed citations
8.
Sausville, Erin L., et al.. (2023). Inhibition of a lower potency target drives the anticancer activity of a clinical p38 inhibitor. Cell chemical biology. 30(10). 1211–1222.e5. 9 indexed citations
9.
Beyett, Tyler S., et al.. (2023). Structural elements that enable specificity for mutant EGFR kinase domains with next-generation small-molecule inhibitors. Methods in enzymology on CD-ROM/Methods in enzymology. 685. 171–198. 4 indexed citations
10.
Beyett, Tyler S., Ciric To, David E. Heppner, et al.. (2022). Molecular basis for cooperative binding and synergy of ATP-site and allosteric EGFR inhibitors. Nature Communications. 13(1). 2530–2530. 56 indexed citations
11.
Vliet, Albert van der, et al.. (2022). Architecture of the NADPH oxidase family of enzymes. Redox Biology. 52. 102298–102298. 51 indexed citations
12.
Dustin, Christopher M., Aida Habibovic, Milena Hristova, et al.. (2021). Oxidation–Dependent Activation of Src Kinase Mediates Epithelial IL-33 Production and Signaling during Acute Airway Allergen Challenge. The Journal of Immunology. 206(12). 2989–2999. 9 indexed citations
13.
Xiao, Haopeng, Mark P. Jedrychowski, Devin K. Schweppe, et al.. (2020). A Quantitative Tissue-Specific Landscape of Protein Redox Regulation during Aging. Cell. 180(5). 968–983.e24. 260 indexed citations breakdown →
14.
To, Ciric, Jaebong Jang, Ting Chen, et al.. (2019). Single and Dual Targeting of Mutant EGFR with an Allosteric Inhibitor. Cancer Discovery. 9(7). 926–943. 250 indexed citations
15.
Dustin, Christopher M., David E. Heppner, Miao-chong J. Lin, & Albert van der Vliet. (2019). Redox regulation of tyrosine kinase signalling: more than meets the eye. The Journal of Biochemistry. 167(2). 151–163. 47 indexed citations
16.
Heppner, David E., Christopher M. Dustin, Chenyi Liao, et al.. (2018). Direct cysteine sulfenylation drives activation of the Src kinase. Nature Communications. 9(1). 4522–4522. 97 indexed citations
17.
Heppner, David E., Yvonne Janssen‐Heininger, & Albert van der Vliet. (2017). The role of sulfenic acids in cellular redox signaling: Reconciling chemical kinetics and molecular detection strategies. Archives of Biochemistry and Biophysics. 616. 40–46. 42 indexed citations
18.
Little, Andrew C., Milena Hristova, Karamatullah Danyal, et al.. (2016). DUOX1 silencing in lung cancer promotes EMT, cancer stem cell characteristics and invasive properties. Oncogenesis. 5(10). e261–e261. 52 indexed citations
19.
Heppner, David E., et al.. (2007). Validation of density functional modeling protocols on experimental bis(μ-oxo)/μ-η2:η2-peroxo dicopper equilibria. JBIC Journal of Biological Inorganic Chemistry. 12(8). 1221–1234. 36 indexed citations
20.
Gherman, Benjamin F., David E. Heppner, William B. Tolman, & Christopher J. Cramer. (2005). Models for dioxygen activation by the CuB site of dopamine β-monooxygenase and peptidylglycine α-hydroxylating monooxygenase. JBIC Journal of Biological Inorganic Chemistry. 11(2). 197–205. 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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