Edmund Maser

7.5k total citations
194 papers, 6.0k citations indexed

About

Edmund Maser is a scholar working on Molecular Biology, Cell Biology and Endocrinology, Diabetes and Metabolism. According to data from OpenAlex, Edmund Maser has authored 194 papers receiving a total of 6.0k indexed citations (citations by other indexed papers that have themselves been cited), including 86 papers in Molecular Biology, 70 papers in Cell Biology and 48 papers in Endocrinology, Diabetes and Metabolism. Recurrent topics in Edmund Maser's work include Aldose Reductase and Taurine (66 papers), Hormonal Regulation and Hypertension (43 papers) and Pharmacogenetics and Drug Metabolism (38 papers). Edmund Maser is often cited by papers focused on Aldose Reductase and Taurine (66 papers), Hormonal Regulation and Hypertension (43 papers) and Pharmacogenetics and Drug Metabolism (38 papers). Edmund Maser collaborates with scholars based in Germany, Czechia and China. Edmund Maser's co-authors include Hans-Jörg Martin, Udo Oppermann, Guangming Xiong, Vladimı́r Wsól, Michael Kisiela, Jennifer S. Strehse, Frank Hoffmann, Bettina Ebert, Michael Gülden and Hasso Seibert and has published in prestigious journals such as Journal of Biological Chemistry, Environmental Science & Technology and PLoS ONE.

In The Last Decade

Edmund Maser

187 papers receiving 5.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Edmund Maser Germany 44 2.7k 1.5k 1.2k 1.0k 607 194 6.0k
Alex Odermatt Switzerland 53 3.5k 1.3× 626 0.4× 2.6k 2.3× 900 0.9× 929 1.5× 241 9.3k
Giorgio Federici Italy 55 6.8k 2.6× 525 0.3× 445 0.4× 794 0.8× 632 1.0× 308 12.2k
Satish K. Srivastava United States 55 4.6k 1.7× 3.4k 2.2× 638 0.6× 223 0.2× 713 1.2× 247 9.5k
Tommy Andersson Sweden 68 5.1k 1.9× 848 0.6× 465 0.4× 1.9k 1.9× 1.8k 3.0× 284 13.2k
Shmuel Shaltiel Israel 35 3.8k 1.4× 1000 0.7× 447 0.4× 349 0.3× 588 1.0× 109 9.2k
William Bourguet France 41 4.1k 1.5× 704 0.5× 564 0.5× 235 0.2× 1.5k 2.4× 105 7.0k
Colin R. Jefcoate United States 54 4.2k 1.6× 454 0.3× 1.7k 1.5× 3.1k 3.1× 1.6k 2.6× 203 9.6k
Rolf Schulte‐Hermann Austria 57 6.1k 2.3× 560 0.4× 376 0.3× 1.3k 1.3× 1.2k 2.0× 202 12.2k
Russell A. Prough United States 49 2.9k 1.1× 314 0.2× 1.2k 1.0× 2.5k 2.5× 970 1.6× 199 7.7k
Howard G. Shertzer United States 46 3.5k 1.3× 493 0.3× 246 0.2× 864 0.9× 1.6k 2.6× 128 8.1k

Countries citing papers authored by Edmund Maser

Since Specialization
Citations

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

Fields of papers citing papers by Edmund Maser

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Edmund Maser

This figure shows the co-authorship network connecting the top 25 collaborators of Edmund Maser. A scholar is included among the top collaborators of Edmund Maser 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 Edmund Maser. Edmund Maser 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
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Maser, Edmund, et al.. (2024). How contaminated is flatfish living near World Wars’ munition dumping sites with energetic compounds?. Archives of Toxicology. 98(11). 3825–3836. 4 indexed citations
3.
Zhang, Chuanzhi, Yong Huang, Jiaxin He, et al.. (2024). The Mechanism of Aniline Blue Degradation by Short-Chain Dehydrogenase (SDRz) in Comamonas testosteroni. Molecules. 29(22). 5405–5405. 1 indexed citations
4.
Brandt, T., et al.. (2024). Light-switchable diazocines as potential inhibitors of testosterone-synthesizing 17β-hydroxysteroid dehydrogenase 3. Chemico-Biological Interactions. 390. 110872–110872. 2 indexed citations
5.
Maser, Edmund, et al.. (2023). Ecotoxicological Risk of World War Relic Munitions in the Sea after Low- and High-Order Blast-in-Place Operations. Environmental Science & Technology. 57(48). 20169–20181. 5 indexed citations
6.
Xu, Miao, Lei He, Ping Sun, et al.. (2023). Critical Role of Monooxygenase in Biodegradation of 2,4,6-Trinitrotoluene by Buttiauxella sp. S19-1. Molecules. 28(4). 1969–1969. 5 indexed citations
7.
Lentes, Pascal, et al.. (2022). Reduction of photoswitched, nitrogen bridged N-acetyl diazocines limits inhibition of 17βHSD3 activity in transfected human embryonic kidney 293 cells. Chemico-Biological Interactions. 354. 109822–109822. 7 indexed citations
8.
Strehse, Jennifer S., et al.. (2022). Carbonyl reduction of 4-oxonon-2-enal (4-ONE) by Sniffer from D. magna and D. pulex. Chemico-Biological Interactions. 354. 109833–109833. 1 indexed citations
9.
Na, Liu, et al.. (2021). Genomic analysis of Gordonia polyisoprenivorans strain R9, a highly effective 17 beta-estradiol- and steroid-degrading bacterium. Chemico-Biological Interactions. 350. 109685–109685. 7 indexed citations
10.
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Czub, Michał, Jakub Nawała, Stanisław Popiel, et al.. (2020). Acute aquatic toxicity of arsenic-based chemical warfare agents to Daphnia magna. Aquatic Toxicology. 230. 105693–105693. 18 indexed citations
12.
Maser, Edmund, et al.. (2019). Sex‐specificity in lung cancer risk. International Journal of Cancer. 146(9). 2376–2382. 152 indexed citations
13.
Kisiela, Michael, et al.. (2017). Crystal structure and catalytic characterization of the dehydrogenase/reductase SDR family member 4 (DHRS4) from Caenorhabditis elegans. FEBS Journal. 285(2). 275–293. 11 indexed citations
14.
Seibert, Hasso, et al.. (2011). Cytoprotective activity against peroxide-induced oxidative damage and cytotoxicity of flavonoids in C6 rat glioma cells. Food and Chemical Toxicology. 49(9). 2398–2407. 29 indexed citations
15.
Sang, Yingying, Guangming Xiong, & Edmund Maser. (2011). Steroid degradation and two steroid-inducible enzymes in the marine bacterium H5. Chemico-Biological Interactions. 191(1-3). 89–94. 15 indexed citations
16.
Pilka, Ewa S., F. Niesen, Wen‐Hwa Lee, et al.. (2009). Structural Basis for Substrate Specificity in Human Monomeric Carbonyl Reductases. PLoS ONE. 4(10). e7113–e7113. 50 indexed citations
17.
18.
Blum, Andreas, et al.. (2001). Human 11β-hydroxysteroid dehydrogenase 1/carbonyl reductase: additional domains for membrane attachment?. Chemico-Biological Interactions. 130-132(1-3). 749–759. 9 indexed citations
19.
Koch, Lutz, et al.. (2000). Development of daunorubicin resistance in tumour cells by induction of carbonyl reduction. Biochemical Pharmacology. 59(3). 293–300. 109 indexed citations
20.
Oppermann, Udo, K.J. Netter, & Edmund Maser. (1995). Cloning and Primary Structure of Murine 11β‐Hydroxysteroid Dehydrogenase/Microsomal Carbonyl Reductase. European Journal of Biochemistry. 227(1-2). 202–208. 54 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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