Martina Pohl

9.3k total citations
189 papers, 6.9k citations indexed

About

Martina Pohl is a scholar working on Molecular Biology, Biochemistry and Clinical Biochemistry. According to data from OpenAlex, Martina Pohl has authored 189 papers receiving a total of 6.9k indexed citations (citations by other indexed papers that have themselves been cited), including 114 papers in Molecular Biology, 80 papers in Biochemistry and 34 papers in Clinical Biochemistry. Recurrent topics in Martina Pohl's work include Enzyme Catalysis and Immobilization (71 papers), Biochemical Acid Research Studies (71 papers) and Microbial Metabolic Engineering and Bioproduction (49 papers). Martina Pohl is often cited by papers focused on Enzyme Catalysis and Immobilization (71 papers), Biochemical Acid Research Studies (71 papers) and Microbial Metabolic Engineering and Bioproduction (49 papers). Martina Pohl collaborates with scholars based in Germany, United Kingdom and Switzerland. Martina Pohl's co-authors include Michael Müller, Uwe T. Bornscheuer, Michael Müller, Dörte Rother, Ayhan S. Demir, Petra Siegert, Bettina Lingen, Dörte Gocke, Michael Müller and Georg A. Sprenger and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Martina Pohl

176 papers receiving 6.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Martina Pohl Germany 49 4.3k 1.9k 1.2k 974 800 189 6.9k
Vincenzo Zappia Italy 41 2.6k 0.6× 496 0.3× 702 0.6× 206 0.2× 78 0.1× 124 5.3k
Edith Sim United Kingdom 50 4.5k 1.0× 656 0.4× 437 0.4× 239 0.2× 62 0.1× 184 7.9k
Mark J. Kurth United States 50 4.0k 0.9× 377 0.2× 5.1k 4.1× 351 0.4× 74 0.1× 340 10.1k
Billy W. Day United States 52 3.5k 0.8× 249 0.1× 2.4k 2.0× 227 0.2× 83 0.1× 178 7.5k
Dunyaporn Trachootham Thailand 19 4.6k 1.1× 443 0.2× 912 0.7× 1.4k 1.4× 67 0.1× 52 8.4k
Toru Maruyama Japan 41 3.6k 0.8× 198 0.1× 487 0.4× 357 0.4× 55 0.1× 183 6.0k
Jarkko Rautio Finland 31 2.1k 0.5× 544 0.3× 1.0k 0.8× 525 0.5× 58 0.1× 88 5.0k
F.M. Huennekens United States 44 3.8k 0.9× 537 0.3× 506 0.4× 151 0.2× 56 0.1× 173 6.2k
Danuta S. Kalinowski Australia 51 3.4k 0.8× 157 0.1× 2.3k 1.8× 429 0.4× 134 0.2× 113 8.7k
Ludmil Benov Kuwait 38 1.6k 0.4× 123 0.1× 434 0.3× 762 0.8× 104 0.1× 112 4.4k

Countries citing papers authored by Martina Pohl

Since Specialization
Citations

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

Fields of papers citing papers by Martina Pohl

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Martina Pohl

This figure shows the co-authorship network connecting the top 25 collaborators of Martina Pohl. A scholar is included among the top collaborators of Martina Pohl 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 Martina Pohl. Martina Pohl 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
3.
Pohl, Martina, et al.. (2021). Structural Analysis of a Genetically Encoded FRET Biosensor by SAXS and MD Simulations. Sensors. 21(12). 4144–4144. 8 indexed citations
4.
Kempe, Daryan, Julia Walter, Martina Pohl, et al.. (2019). Impact of Molecular Crowding on Translational Mobility and Conformational Properties of Biological Macromolecules. The Journal of Physical Chemistry B. 123(21). 4477–4486. 34 indexed citations
5.
Cerminara, Michele, et al.. (2018). Single-Molecule Studies on a FRET Biosensor: Lessons from a Comparison of Fluorescent Protein Equipped versus Dye-Labeled Species. Molecules. 23(12). 3105–3105. 2 indexed citations
6.
Richter, Michael, et al.. (2018). Structural and Mutagenesis Studies of the Thiamine‐Dependent, Ketone‐Accepting YerE from Pseudomonas protegens. ChemBioChem. 19(21). 2283–2292. 12 indexed citations
7.
Jäger, Vera D., Alexander Grünberger, Meike Baumgart, et al.. (2018). Tailor-made catalytically active inclusion bodies for different applications in biocatalysis. Catalysis Science & Technology. 8(22). 5816–5826. 26 indexed citations
8.
Mackfeld, Ursula, Friederike Hoffmann, Katharina Nöh, et al.. (2018). Towards a Mechanistic Understanding of Factors Controlling the Stereoselectivity of Transketolase. ChemCatChem. 10(12). 2601–2611. 1 indexed citations
10.
Richter, Michael, Lydia Walter, Georg Fuchs, et al.. (2014). Asymmetric Stetter reactions catalyzed by thiamine diphosphate-dependent enzymes. Applied Microbiology and Biotechnology. 98(23). 9681–9690. 21 indexed citations
11.
Müller, Michael, Georg A. Sprenger, & Martina Pohl. (2013). C C bond formation using ThDP-dependent lyases. Current Opinion in Chemical Biology. 17(2). 261–270. 104 indexed citations
13.
Peper, Stephanie, Selin Kara, Wei Long, et al.. (2010). Influence of the hydrostatic pressure and pH on the asymmetric 2‐hydroxyketone formation catalyzed by Pseudomonas putida benzoylformate decarboxylase and variants thereof. Biotechnology and Bioengineering. 106(1). 18–26. 11 indexed citations
14.
Höcker, Britta, Reinhard Feneberg, Jens Drube, et al.. (2009). Improved growth and cardiovascular risk after late steroid withdrawal: 2-year results of a prospective, randomised trial in paediatric renal transplantation. Nephrology Dialysis Transplantation. 25(2). 617–624. 59 indexed citations
15.
Guterl, Jan‐Karl, Jennifer N. Andexer, Torsten Sehl, et al.. (2009). Uneven twins: Comparison of two enantiocomplementary hydroxynitrile lyases with α/β-hydrolase fold. Journal of Biotechnology. 141(3-4). 166–173. 48 indexed citations
16.
Müller, Michael, Dörte Gocke, & Martina Pohl. (2009). Thiamin diphosphate in biological chemistry: exploitation of diverse thiamin diphosphate‐dependent enzymes for asymmetric chemoenzymatic synthesis. FEBS Journal. 276(11). 2894–2904. 113 indexed citations
17.
Langermann, Jan von, Jan‐Karl Guterl, Martina Pohl, Harald Wajant, & Udo Kragl. (2008). Hydroxynitrile lyase catalyzed cyanohydrin synthesis at high pH-values. Bioprocess and Biosystems Engineering. 31(3). 155–161. 23 indexed citations
18.
Müller, Michael, et al.. (2006). Characterization of benzaldehyde lyase from Pseudomonas fluorescens: A versatile enzyme for asymmetric C–C bond formation. Bioorganic Chemistry. 34(6). 345–361. 70 indexed citations
19.
Rösler, Alexander, et al.. (1998). Time course of chemokines in the cerebrospinal fluid and serum during herpes simplex type 1 encephalitis. Journal of the Neurological Sciences. 157(1). 82–89. 59 indexed citations
20.
Pohl, Martina, et al.. (1995). Stability investigations on on the pyruvate decarboxylases from Zymomonas mobilis. Biotechnology and Applied Biochemistry. 22(1). 95–105. 15 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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