Lenz Steimer

447 total citations
9 papers, 348 citations indexed

About

Lenz Steimer is a scholar working on Molecular Biology, Pollution and Inorganic Chemistry. According to data from OpenAlex, Lenz Steimer has authored 9 papers receiving a total of 348 indexed citations (citations by other indexed papers that have themselves been cited), including 6 papers in Molecular Biology, 4 papers in Pollution and 4 papers in Inorganic Chemistry. Recurrent topics in Lenz Steimer's work include Microbial bioremediation and biosurfactants (4 papers), Metal-Catalyzed Oxygenation Mechanisms (4 papers) and RNA and protein synthesis mechanisms (3 papers). Lenz Steimer is often cited by papers focused on Microbial bioremediation and biosurfactants (4 papers), Metal-Catalyzed Oxygenation Mechanisms (4 papers) and RNA and protein synthesis mechanisms (3 papers). Lenz Steimer collaborates with scholars based in Germany, Italy and Bulgaria. Lenz Steimer's co-authors include Dagmar Klostermeier, Linda Foit, James C.A. Bardwell, Gareth J. Morgan, Sheena E. Radford, Stuart L. Warriner, A. Stolz, Sibylle Bürger, Marta Ferraroni and Fabrizio Briganti and has published in prestigious journals such as Nucleic Acids Research, Molecular Cell and FEBS Journal.

In The Last Decade

Lenz Steimer

8 papers receiving 346 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Lenz Steimer Germany 8 253 73 46 44 34 9 348
T. Kovaĺ Czechia 12 176 0.7× 42 0.6× 52 1.1× 12 0.3× 34 1.0× 35 350
Justin Acheson United States 9 358 1.4× 59 0.8× 30 0.7× 27 0.6× 48 1.4× 13 503
Erin L. Dodd Canada 10 159 0.6× 38 0.5× 38 0.8× 8 0.2× 78 2.3× 18 372
Yuling Sheng China 8 169 0.7× 25 0.3× 49 1.1× 10 0.2× 18 0.5× 15 295
Mahmoud Ghanem United States 13 364 1.4× 21 0.3× 14 0.3× 15 0.3× 80 2.4× 17 507
S. Brokx Canada 10 309 1.2× 32 0.4× 124 2.7× 7 0.2× 58 1.7× 17 482
K. Krishnamurthy Rao India 10 191 0.8× 33 0.5× 85 1.8× 8 0.2× 69 2.0× 22 356
Julia Winkelmann Italy 11 312 1.2× 85 1.2× 16 0.3× 5 0.1× 49 1.4× 19 532
Alberto del Monte‐Martínez Cuba 9 227 0.9× 11 0.2× 34 0.7× 13 0.3× 39 1.1× 29 358
Christine Addy Japan 9 281 1.1× 14 0.2× 62 1.3× 13 0.3× 119 3.5× 12 374

Countries citing papers authored by Lenz Steimer

Since Specialization
Citations

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

Fields of papers citing papers by Lenz Steimer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Lenz Steimer

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

All Works

9 of 9 papers shown
2.
Steimer, Lenz, et al.. (2015). Nickel quercetinase, a “promiscuous” metalloenzyme: metal incorporation and metal ligand substitution studies. BMC Biochemistry. 16(1). 10–10. 35 indexed citations
3.
Ferraroni, Marta, et al.. (2015). Function of different amino acid residues in the reaction mechanism of gentisate 1,2-dioxygenases deduced from the analysis of mutants of the salicylate 1,2-dioxygenase from Pseudaminobacter salicylatoxidans. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854(10). 1425–1437. 16 indexed citations
4.
Ferraroni, Marta, I. Matera, Sibylle Bürger, et al.. (2013). The salicylate 1,2‐dioxygenase as a model for a conventional gentisate 1,2‐dioxygenase: crystal structures of the G106A mutant and its adducts with gentisate and salicylate. FEBS Journal. 280(7). 1643–1652. 26 indexed citations
5.
Steimer, Lenz, et al.. (2013). Recognition of two distinct elements in the RNA substrate by the RNA-binding domain of the T. thermophilus DEAD box helicase Hera. Nucleic Acids Research. 41(12). 6259–6272. 24 indexed citations
7.
Steimer, Lenz & Dagmar Klostermeier. (2012). RNA helicases in infection and disease. RNA Biology. 9(6). 751–771. 81 indexed citations
8.
Ferraroni, Marta, I. Matera, Lenz Steimer, et al.. (2011). Crystal structures of salicylate 1,2-dioxygenase-substrates adducts: A step towards the comprehension of the structural basis for substrate selection in class III ring cleaving dioxygenases. Journal of Structural Biology. 177(2). 431–438. 29 indexed citations
9.
Foit, Linda, Gareth J. Morgan, Lenz Steimer, et al.. (2009). Optimizing Protein Stability In Vivo. Molecular Cell. 36(5). 861–871. 125 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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