Stefan Rahlfs

3.4k total citations
81 papers, 2.6k citations indexed

About

Stefan Rahlfs is a scholar working on Molecular Biology, Public Health, Environmental and Occupational Health and Oncology. According to data from OpenAlex, Stefan Rahlfs has authored 81 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 57 papers in Molecular Biology, 32 papers in Public Health, Environmental and Occupational Health and 11 papers in Oncology. Recurrent topics in Stefan Rahlfs's work include Redox biology and oxidative stress (30 papers), Malaria Research and Control (27 papers) and Mosquito-borne diseases and control (12 papers). Stefan Rahlfs is often cited by papers focused on Redox biology and oxidative stress (30 papers), Malaria Research and Control (27 papers) and Mosquito-borne diseases and control (12 papers). Stefan Rahlfs collaborates with scholars based in Germany, United States and Switzerland. Stefan Rahlfs's co-authors include Katja Becker, R. Heiner Schirmer, Karin Fritz‐Wolf, Marcel Deponte, Sebastian Kehr, Marina Fischer, Esther Jortzik, Volker Müller, Saša Končarević and Jude M. Przyborski and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Stefan Rahlfs

80 papers receiving 2.6k citations

Peers

Stefan Rahlfs

PHEOH

PARAS

IMMUN

Marcel Deponte Germany

Rolf D. Walter Germany

Kevin J. Saliba Australia

Govindarajan Padmanaban India

Mitali Chatterjee India

Mohammad Imran Siddiqi India

José Andrés Morgado‐Díaz Brazil

Sérgio de Albuquerque Brazil

Alan Mellors Canada

Babu L. Tekwani United States

Marcel Deponte Germany

Stefan Rahlfs

1.8k ×1.1

518 ×0.6

PHEOH

180 ×0.6

PARAS

263 ×1.3

159 ×0.8

IMMUN

Citations per year, relative to Stefan Rahlfs Stefan Rahlfs (= 1×) peers Marcel Deponte

Countries citing papers authored by Stefan Rahlfs

Since Specialization

Citations

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

Fields of papers citing papers by Stefan Rahlfs

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Stefan Rahlfs

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

Stumpf, Michaela, et al.. (2023). Structure of Leishmania donovani 6-Phosphogluconate Dehydrogenase and Inhibition by Phosphine Gold(I) Complexes: A Potential Approach to Leishmaniasis Treatment. International Journal of Molecular Sciences. 24(10). 8615–8615. 4 indexed citations

Nietzel, Thomas, Stefan Rahlfs, Jude M. Przyborski, et al.. (2022). Structure and Function of Redox-Sensitive Superfolder Green Fluorescent Protein Variant. Antioxidants and Redox Signaling. 37(1-3). 1–18. 9 indexed citations

Fritz‐Wolf, Karin, et al.. (2018). Characterization of Plasmodium falciparum 6-Phosphogluconate Dehydrogenase as an Antimalarial Drug Target. Journal of Molecular Biology. 430(21). 4049–4067. 17 indexed citations

Fritz‐Wolf, Karin, et al.. (2017). Kinetic characterization of wild‐type and mutant human thioredoxin glutathione reductase defines its reaction and regulatory mechanisms. FEBS Journal. 285(3). 542–558. 20 indexed citations

Rahlfs, Stefan, et al.. (2017). H2O2 dynamics in the malaria parasite Plasmodium falciparum. PLoS ONE. 12(4). e0174837–e0174837. 32 indexed citations

Wang, Lihui, Claire Delahunty, Judith Helena Prieto, et al.. (2013). Protein S -nitrosylation in Plasmodium falciparum. Antioxidants and Redox Signaling. 20(18). 2923–2935. 24 indexed citations

Mohring, Franziska, et al.. (2013). Real-Time Imaging of the Intracellular Glutathione Redox Potential in the Malaria Parasite Plasmodium falciparum. PLoS Pathogens. 9(12). e1003782–e1003782. 49 indexed citations

Preuss, Janina, Eduard Sergienko, Anthony B. Pinkerton, et al.. (2012). High-Throughput Screening for Small-Molecule Inhibitors of Plasmodium falciparum Glucose-6-Phosphate Dehydrogenase 6-Phosphogluconolactonase. SLAS DISCOVERY. 17(6). 738–751. 23 indexed citations

Gromer, Stephan, Heike Adler, Stefan Rahlfs, et al.. (2011). The bacterial redox signaller pyocyanin as an antiplasmodial agent: comparisons with its thioanalog methylene blue. Redox Report. 16(4). 154–165. 37 indexed citations

10.

Austin, Christopher, Ghassan J. Maghzal, Alicia Sánchez‐Pérez, et al.. (2010). Biochemical characteristics and inhibitor selectivity of mouse indoleamine 2,3-dioxygenase-2. Amino Acids. 39(2). 565–578. 56 indexed citations

11.

Gallo, Valentina, Evelin Schwarzer, Stefan Rahlfs, et al.. (2009). Inherited Glutathione Reductase Deficiency and Plasmodium falciparum Malaria—A Case Study. PLoS ONE. 4(10). e7303–e7303. 26 indexed citations

12.

Jortzik, Esther, Saša Končarević, Marcel Deponte, et al.. (2009). Identification of Proteins Targeted by the Thioredoxin Superfamily in Plasmodium falciparum. PLoS Pathogens. 5(4). e1000383–e1000383. 69 indexed citations

13.

Rahlfs, Stefan & Katja Becker. (2006). Interference with Redox-Active Enzymes as a Basis for the Design of Antimalarial Drugs. Mini-Reviews in Medicinal Chemistry. 6(2). 163–176. 17 indexed citations

14.

Iozef, Rimma, Stefan Rahlfs, Marcel Deponte, et al.. (2005). Characterization of the glyoxalases of the malarial parasite Plasmodium falciparum and comparison with their human counterparts. Biological Chemistry. 386(1). 41–52. 40 indexed citations

15.

Sarma, Ganapathy N., et al.. (2004). Crystal Structure of a Novel Plasmodium falciparum 1-Cys Peroxiredoxin. Journal of Molecular Biology. 346(4). 1021–1034. 76 indexed citations

16.

Becker, Katja, Stefan M. Kanzok, Rimma Iozef, et al.. (2003). Plasmoredoxin, a novel redox‐active protein unique for malarial parasites. European Journal of Biochemistry. 270(6). 1057–1064. 38 indexed citations

17.

Iozef, Rimma, Stefan Rahlfs, Tammy T. Chang, Heiner Schirmer, & Katja Becker. (2003). Glyoxalase I of the malarial parasite Plasmodium falciparum: evidence for subunit fusion. FEBS Letters. 554(3). 284–288. 34 indexed citations

18.

Kanzok, Stefan M., Stefan Rahlfs, Katja Becker, & R. Heiner Schirmer. (2002). Thioredoxin, Thioredoxin Reductase, and Thioredoxin Peroxidase of Malaria Parasite Plasmodium falciparum. Methods in enzymology on CD-ROM/Methods in enzymology. 370–381. 34 indexed citations

19.

Rahlfs, Stefan, et al.. (2002). Glutathione S-Transferase of the Malarial Parasite Plasmodium falciparum: Characterization of a Potential Drug Target. Biological Chemistry. 383(5). 821–30. 104 indexed citations

20.

Müller, Volker, et al.. (2001). The Na+ cycle in Acetobacterium woodii: identification and characterization of a Na+ translocating F1F0-ATPase with a mixed oligomer of 8 and 16 kDa proteolipids. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1505(1). 108–120. 53 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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