Steffen Brünle

1.4k total citations
11 papers, 159 citations indexed

About

Steffen Brünle is a scholar working on Molecular Biology, Materials Chemistry and Nutrition and Dietetics. According to data from OpenAlex, Steffen Brünle has authored 11 papers receiving a total of 159 indexed citations (citations by other indexed papers that have themselves been cited), including 5 papers in Molecular Biology, 5 papers in Materials Chemistry and 3 papers in Nutrition and Dietetics. Recurrent topics in Steffen Brünle's work include Metalloenzymes and iron-sulfur proteins (3 papers), Enzyme Structure and Function (3 papers) and Photoreceptor and optogenetics research (2 papers). Steffen Brünle is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (3 papers), Enzyme Structure and Function (3 papers) and Photoreceptor and optogenetics research (2 papers). Steffen Brünle collaborates with scholars based in Netherlands, Germany and Switzerland. Steffen Brünle's co-authors include D. Ozerov, Tobias Weinert, Demet Kekilli, Florian Dworkowski, Przemysław Nogły, Ezequiel Panepucci, Petr Skopintsev, Sandra Mous, Meitian Wang and Daniel James and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Steffen Brünle

11 papers receiving 159 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Steffen Brünle Netherlands	6	85	63	53	21	11	11	159
Naomine Yano Japan	10	170 2.0×	62 1.0×	36 0.7×	10 0.5×	7 0.6×	21	216
Egor Marin Russia	7	132 1.6×	52 0.8×	139 2.6×	23 1.1×	6 0.5×	14	252
Emma K. Livingstone Australia	4	225 2.6×	74 1.2×	20 0.4×	15 0.7×	3 0.3×	6	272
Cecilia Wickstrand Sweden	4	113 1.3×	37 0.6×	112 2.1×	28 1.3×	8 0.7×	5	166
Robert Dods United Kingdom	6	119 1.4×	20 0.3×	68 1.3×	20 1.0×	6 0.5×	6	182
Sandra Mous Russia	4	86 1.0×	45 0.7×	54 1.0×	21 1.0×	12 1.1×	5	152
Hossein Batebi Germany	8	178 2.1×	15 0.2×	72 1.4×	31 1.5×	10 0.9×	9	235
Suliman Adam Israel	10	141 1.7×	40 0.6×	145 2.7×	22 1.0×	2 0.2×	16	281
Vicente Rey‐Bakaikoa France	4	120 1.4×	77 1.2×	16 0.3×	9 0.4×	5 0.5×	5	179
Richard Van United States	7	144 1.7×	133 2.1×	22 0.4×	26 1.2×	2 0.2×	16	269

Countries citing papers authored by Steffen Brünle

Since Specialization

Citations

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

Fields of papers citing papers by Steffen Brünle

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Steffen Brünle

This figure shows the co-authorship network connecting the top 25 collaborators of Steffen Brünle. A scholar is included among the top collaborators of Steffen Brünle 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 Steffen Brünle. Steffen Brünle is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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11 of 11 papers shown

Brünle, Steffen, et al.. (2024). Menaquinone-specific oxidation by M. tuberculosis cytochrome bd is redox regulated by the Q-loop disulfide bond. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1865. 149457–149457. 1 indexed citations

Boyle, Aimee L., et al.. (2024). A low-barrier proton shared between two aspartates acts as a conformational switch that changes the substrate specificity of the β-lactamase BlaC. International Journal of Biological Macromolecules. 278(Pt 2). 134665–134665. 2 indexed citations

Brünle, Steffen, et al.. (2024). Menaquinone-specific turnover by Mycobacterium tuberculosis cytochrome bd is redox regulated by the Q-loop disulfide bond. Journal of Biological Chemistry. 301(2). 108094–108094. 2 indexed citations

Mulder, M.H.V., Matthias Broser, Steffen Brünle, et al.. (2024). Structural Insights Into the Opening Mechanism of C1C2 Channelrhodopsin. Journal of the American Chemical Society. 147(1). 1282–1290. 2 indexed citations

Zhou, Yangli, et al.. (2024). Structural perspectives on chemokine receptors. Biochemical Society Transactions. 52(3). 1011–1024. 1 indexed citations

Timmer, Monika, et al.. (2023). Asp179 in the class A β‐lactamase from Mycobacterium tuberculosis is a conserved yet not essential residue due to epistasis. FEBS Journal. 290(20). 4933–4949. 7 indexed citations

Weinert, Tobias, Petr Skopintsev, Daniel James, et al.. (2019). Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography. Science. 365(6448). 61–65. 105 indexed citations

Brünle, Steffen, et al.. (2019). Molybdate pumping into the molybdenum storage protein via an ATP-powered piercing mechanism. Proceedings of the National Academy of Sciences. 116(52). 26497–26504. 8 indexed citations

Brünle, Steffen, et al.. (2018). The Molybdenum Storage Protein: A soluble ATP hydrolysis‐dependent molybdate pump. FEBS Journal. 285(24). 4602–4616. 9 indexed citations

10.

Brünle, Steffen, et al.. (2018). The molybdenum storage protein — A bionanolab for creating experimentally alterable polyoxomolybdate clusters. Journal of Inorganic Biochemistry. 189. 172–179. 6 indexed citations

11.

Brünle, Steffen, et al.. (2016). The Crystal Structure of RosB: Insights into the Reaction Mechanism of the First Member of a Family of Flavodoxin‐like Enzymes. Angewandte Chemie International Edition. 56(4). 1146–1151. 16 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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