Alexandra Lerchner

431 total citations
12 papers, 371 citations indexed

About

Alexandra Lerchner is a scholar working on Molecular Biology, Biochemistry and Materials Chemistry. According to data from OpenAlex, Alexandra Lerchner has authored 12 papers receiving a total of 371 indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 4 papers in Biochemistry and 3 papers in Materials Chemistry. Recurrent topics in Alexandra Lerchner's work include Enzyme Catalysis and Immobilization (6 papers), Biochemical and Molecular Research (4 papers) and Amino Acid Enzymes and Metabolism (3 papers). Alexandra Lerchner is often cited by papers focused on Enzyme Catalysis and Immobilization (6 papers), Biochemical and Molecular Research (4 papers) and Amino Acid Enzymes and Metabolism (3 papers). Alexandra Lerchner collaborates with scholars based in Germany, Netherlands and United States. Alexandra Lerchner's co-authors include Arne Skerra, Renate Ulbrich‐Hofmann, Lýdia Bezáková, Marek Obložinský, A. Jarasch, Christian Rausch, A. Schiefner, Francesco G. Mutti, Christine Fuchs and Desiree Pressnitz and has published in prestigious journals such as Journal of Biological Chemistry, Proteins Structure Function and Bioinformatics and Biotechnology and Bioengineering.

In The Last Decade

Alexandra Lerchner

12 papers receiving 371 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Alexandra Lerchner Germany 11 317 71 70 45 32 12 371
Marleen Otzen Netherlands 12 562 1.8× 42 0.6× 57 0.8× 47 1.0× 46 1.4× 17 614
Mohammed Khysar Pasha Canada 15 277 0.9× 157 2.2× 67 1.0× 28 0.6× 30 0.9× 38 522
Sigrid Egger Austria 10 242 0.8× 39 0.5× 30 0.4× 70 1.6× 35 1.1× 11 330
Yuji Kado Japan 11 266 0.8× 46 0.6× 57 0.8× 40 0.9× 37 1.2× 23 460
Zhengmao Guo United States 8 183 0.6× 111 1.6× 57 0.8× 23 0.5× 24 0.8× 9 338
Kristin K. Brown United States 9 461 1.5× 72 1.0× 32 0.5× 20 0.4× 27 0.8× 11 545
John N. Barlow Belgium 9 225 0.7× 89 1.3× 45 0.6× 74 1.6× 6 0.2× 12 340
Jacques Mauger Japan 8 434 1.4× 91 1.3× 89 1.3× 51 1.1× 24 0.8× 10 537
Mary Ortmayer United Kingdom 7 236 0.7× 69 1.0× 12 0.2× 26 0.6× 29 0.9× 10 339
Zachary D. Parsons United States 9 299 0.9× 69 1.0× 54 0.8× 18 0.4× 9 0.3× 12 400

Countries citing papers authored by Alexandra Lerchner

Since Specialization
Citations

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

Fields of papers citing papers by Alexandra Lerchner

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Alexandra Lerchner

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

All Works

12 of 12 papers shown
1.
Powers, Nicholas E., Benjamin J. Swartzwelter, Carlo Marchetti, et al.. (2020). PASylation of IL-1 receptor antagonist (IL-1Ra) retains IL-1 blockade and extends its duration in mouse urate crystal-induced peritonitis. Journal of Biological Chemistry. 295(3). 868–882. 24 indexed citations
2.
Powers, Nicholas E., Benjamin J. Swartzwelter, Carlo Marchetti, et al.. (2019). PASylation of IL-1 receptor antagonist (IL-1Ra) retains IL-1 blockade and extends its duration in mouse urate crystal-induced peritonitis. Journal of Biological Chemistry. 295(3). 868–882. 15 indexed citations
3.
Lerchner, Alexandra, et al.. (2016). Fusion of an alcohol dehydrogenase with an aminotransferase using a PAS linker to improve coupled enzymatic alcohol-to-amine conversion. Protein Engineering Design and Selection. 29(12). 557–562. 24 indexed citations
4.
Lerchner, Alexandra, A. Jarasch, & Arne Skerra. (2015). Engineering of alanine dehydrogenase from Bacillus subtilis for novel cofactor specificity. Biotechnology and Applied Biochemistry. 63(5). 616–624. 17 indexed citations
5.
Rausch, Christian, Alexandra Lerchner, A. Schiefner, & Arne Skerra. (2013). Crystal structure of the ω‐aminotransferase from Paracoccus denitrificans and its phylogenetic relationship with other class III amino‐ transferases that have biotechnological potential. Proteins Structure Function and Bioinformatics. 81(5). 774–787. 38 indexed citations
6.
Lerchner, Alexandra, A. Jarasch, Winfried Meining, A. Schiefner, & Arne Skerra. (2013). Crystallographic analysis and structure‐guided engineering of NADPH‐dependent Ralstonia sp. Alcohol dehydrogenase toward NADH cosubstrate specificity. Biotechnology and Bioengineering. 110(11). 2803–2814. 26 indexed citations
7.
Lerchner, Alexandra, et al.. (2013). Coupled Enzymatic Alcohol‐to‐Amine Conversion of Isosorbide using Engineered Transaminases and Dehydrogenases. ChemCatChem. 5(11). 3374–3383. 30 indexed citations
8.
Mutti, Francesco G., Christine Fuchs, Desiree Pressnitz, et al.. (2011). Amination of Ketones by Employing Two New (S)‐Selective ω‐Transaminases and the His‐Tagged ω‐TA from Vibrio fluvialis. European Journal of Organic Chemistry. 2012(5). 1003–1007. 75 indexed citations
9.
Lerchner, Alexandra. (2006). Probing conserved amino acids in phospholipase D (Brassica oleracea var. capitata) for their importance in hydrolysis and transphosphatidylation activity. Protein Engineering Design and Selection. 19(10). 443–452. 21 indexed citations
10.
Ulbrich‐Hofmann, Renate, Alexandra Lerchner, Marek Obložinský, & Lýdia Bezáková. (2005). Phospholipase D and its application in biocatalysis. Biotechnology Letters. 27(8). 535–544. 68 indexed citations
11.
Lerchner, Alexandra, et al.. (2005). Two highly homologous phospholipase D isoenzymes from Papaver somniferum L. with different transphosphatidylation potential. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1737(2-3). 94–101. 24 indexed citations
12.
Younus, Hina, Regina Schöps, Alexandra Lerchner, et al.. (2003). Proteolytic Sensitivity of a Recombinant Phospholipase D from Cabbage: Identification of Loop Regions and Conformational Changes. Journal of Protein Chemistry. 22(6). 499–508. 9 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.

Explore authors with similar magnitude of impact

Rankless by CCL
2026