Rudolf K. Allemann

6.1k total citations
167 papers, 5.2k citations indexed

About

Rudolf K. Allemann is a scholar working on Molecular Biology, Materials Chemistry and Pharmacology. According to data from OpenAlex, Rudolf K. Allemann has authored 167 papers receiving a total of 5.2k indexed citations (citations by other indexed papers that have themselves been cited), including 152 papers in Molecular Biology, 53 papers in Materials Chemistry and 44 papers in Pharmacology. Recurrent topics in Rudolf K. Allemann's work include Plant biochemistry and biosynthesis (58 papers), Microbial Natural Products and Biosynthesis (44 papers) and Enzyme Structure and Function (43 papers). Rudolf K. Allemann is often cited by papers focused on Plant biochemistry and biosynthesis (58 papers), Microbial Natural Products and Biosynthesis (44 papers) and Enzyme Structure and Function (43 papers). Rudolf K. Allemann collaborates with scholars based in United Kingdom, Switzerland and United States. Rudolf K. Allemann's co-authors include David J. Miller, E. Joel Loveridge, Robert J. Mart, Juan A. Faraldos, Louis Y. P. Luk, Verónica González, Steven A. Benner, Giovanni Maglia, Thomas Wirth and Kai Johnsson and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Rudolf K. Allemann

167 papers receiving 5.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Rudolf K. Allemann United Kingdom 42 4.3k 1.2k 1.2k 632 431 167 5.2k
Frank Löhr Germany 41 4.3k 1.0× 678 0.5× 405 0.3× 228 0.4× 768 1.8× 150 6.1k
Matthew P. Crump United Kingdom 41 3.5k 0.8× 813 0.7× 1.0k 0.9× 1.9k 2.9× 340 0.8× 142 5.9k
Urszula Derewenda United States 42 4.9k 1.1× 917 0.7× 280 0.2× 463 0.7× 872 2.0× 81 6.5k
Vishal Verma United States 13 2.5k 0.6× 438 0.4× 370 0.3× 1.2k 1.8× 214 0.5× 28 4.4k
Albert M. Berghuis Canada 39 4.5k 1.0× 969 0.8× 242 0.2× 480 0.8× 886 2.1× 116 5.9k
Michael D. Toney United States 40 3.0k 0.7× 1.6k 1.3× 316 0.3× 750 1.2× 135 0.3× 98 4.5k
Gordon V. Louie United States 30 3.2k 0.7× 700 0.6× 262 0.2× 355 0.6× 427 1.0× 44 4.0k
Lars‐Oliver Essen Germany 49 6.1k 1.4× 1.0k 0.8× 721 0.6× 466 0.7× 571 1.3× 174 8.7k
Kenji Monde Japan 42 2.5k 0.6× 282 0.2× 546 0.5× 2.1k 3.3× 248 0.6× 201 5.4k
J. Fernando Dı́az Spain 46 4.4k 1.0× 655 0.5× 729 0.6× 2.1k 3.3× 2.7k 6.3× 171 7.1k

Countries citing papers authored by Rudolf K. Allemann

Since Specialization
Citations

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

Fields of papers citing papers by Rudolf K. Allemann

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Rudolf K. Allemann. 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 Rudolf K. Allemann. The network helps show where Rudolf K. Allemann may publish in the future.

Co-authorship network of co-authors of Rudolf K. Allemann

This figure shows the co-authorship network connecting the top 25 collaborators of Rudolf K. Allemann. A scholar is included among the top collaborators of Rudolf K. Allemann 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 Rudolf K. Allemann. Rudolf K. Allemann 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.
Allemann, Rudolf K., et al.. (2024). Engineering terpene synthases and their substrates for the biocatalytic production of terpene natural products and analogues. Chemical Communications. 61(12). 2468–2483. 5 indexed citations
2.
Owens, Siân E., David J. Miller, Jonathan G.L. Mullins, et al.. (2021). Bisphosphonate inhibitors of squalene synthase protect cells against cholesterol‐dependent cytolysins. The FASEB Journal. 35(6). e21640–e21640. 10 indexed citations
3.
Lloyd‐Evans, Emyr, Robert J. Mart, Ian A. Fallis, et al.. (2020). Targeted cell imaging properties of a deep red luminescent iridium(iii) complex conjugated with a c-Myc signal peptide. Chemical Science. 11(6). 1599–1606. 41 indexed citations
4.
Mart, Robert J. & Rudolf K. Allemann. (2016). Azobenzene photocontrol of peptides and proteins. Chemical Communications. 52(83). 12262–12277. 179 indexed citations
5.
Chen, Mengbin, Verónica González, Stefano Leoni, et al.. (2016). Mechanism of Germacradien-4-ol Synthase-Controlled Water Capture. Biochemistry. 55(14). 2112–2121. 33 indexed citations
6.
Luk, Louis Y. P., E. Joel Loveridge, & Rudolf K. Allemann. (2015). Protein motions and dynamic effects in enzyme catalysis. Physical Chemistry Chemical Physics. 17(46). 30817–30827. 48 indexed citations
7.
Luk, Louis Y. P., J. Javier Ruiz‐Pernía, Aduragbemi S. Adesina, et al.. (2015). Chemical Ligation and Isotope Labeling to Locate Dynamic Effects during Catalysis by Dihydrofolate Reductase. Angewandte Chemie. 127(31). 9144–9148. 3 indexed citations
8.
Luk, Louis Y. P., J. Javier Ruiz‐Pernía, Aduragbemi S. Adesina, et al.. (2015). Chemical Ligation and Isotope Labeling to Locate Dynamic Effects during Catalysis by Dihydrofolate Reductase. Angewandte Chemie International Edition. 54(31). 9016–9020. 33 indexed citations
9.
Behiry, Enas M., et al.. (2014). Role of the Occluded Conformation in Bacterial Dihydrofolate Reductases. Biochemistry. 53(29). 4761–4768. 12 indexed citations
10.
Guo, Jiannan, Louis Y. P. Luk, E. Joel Loveridge, & Rudolf K. Allemann. (2014). Thermal Adaptation of Dihydrofolate Reductase from the Moderate Thermophile Geobacillus stearothermophilus. Biochemistry. 53(17). 2855–2863. 15 indexed citations
11.
Luk, Louis Y. P., J. Javier Ruiz‐Pernía, William Dawson, et al.. (2014). Protein Isotope Effects in Dihydrofolate Reductase From Geobacillus stearothermophilus Show Entropic–Enthalpic Compensatory Effects on the Rate Constant. Journal of the American Chemical Society. 136(49). 17317–17323. 29 indexed citations
12.
Luk, Louis Y. P., J. Javier Ruiz‐Pernía, William Dawson, et al.. (2013). Unraveling the role of protein dynamics in dihydrofolate reductase catalysis. Proceedings of the National Academy of Sciences. 110(41). 16344–16349. 109 indexed citations
13.
Mart, Robert J., Rachel J. Errington, Sally C. Chappell, et al.. (2013). BH3 helix-derived biophotonic nanoswitches regulate cytochrome c release in permeabilised cells. Molecular BioSystems. 9(11). 2597–2603. 11 indexed citations
14.
Loveridge, E. Joel, Christopher Williams, Sara B.‐M. Whittaker, et al.. (2012). Aliphatic 1H, 13C and 15N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP+ and folate. Biomolecular NMR Assignments. 7(1). 61–64. 2 indexed citations
15.
Loveridge, E. Joel, et al.. (2009). Effect of Dimerization on the Stability and Catalytic Activity of Dihydrofolate Reductase from the Hyperthermophile Thermotoga maritima. Biochemistry. 48(25). 5922–5933. 34 indexed citations
16.
Edwards, Wayne R., Kathy Busse, Rudolf K. Allemann, & Rochelle D. Ahmed. (2008). Linking the functions of unrelated proteins using a novel directed evolution domain insertion method. Nucleic Acids Research. 36(13). e78–e78. 69 indexed citations
17.
Miller, David J., et al.. (2007). Probing the reaction mechanism of aristolochene synthase with 12,13-difluorofarnesyl diphosphate. Chemical Communications. 4155–4155. 24 indexed citations
18.
Weston, Chris J., et al.. (2004). A Stable Miniature Protein with Oxaloacetate Decarboxylase Activity. ChemBioChem. 5(8). 1075–1080. 26 indexed citations
19.
Maglia, Giovanni & Rudolf K. Allemann. (2003). Evidence for Environmentally Coupled Hydrogen Tunneling during Dihydrofolate Reductase Catalysis. Journal of the American Chemical Society. 125(44). 13372–13373. 89 indexed citations
20.
Sieber, Martin A., et al.. (1995). DNA Binding Specificity of the Basic-Helix-Loop-Helix Protein MASH-1. Biochemistry. 34(35). 11026–11036. 33 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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