Markus Pietzsch

1.8k total citations
68 papers, 1.4k citations indexed

About

Markus Pietzsch is a scholar working on Molecular Biology, Biotechnology and Pulmonary and Respiratory Medicine. According to data from OpenAlex, Markus Pietzsch has authored 68 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 47 papers in Molecular Biology, 17 papers in Biotechnology and 15 papers in Pulmonary and Respiratory Medicine. Recurrent topics in Markus Pietzsch's work include Enzyme Catalysis and Immobilization (16 papers), Blood properties and coagulation (14 papers) and Enzyme Structure and Function (12 papers). Markus Pietzsch is often cited by papers focused on Enzyme Catalysis and Immobilization (16 papers), Blood properties and coagulation (14 papers) and Enzyme Structure and Function (12 papers). Markus Pietzsch collaborates with scholars based in Germany, Switzerland and South Korea. Markus Pietzsch's co-authors include Thomas C. Hertel, Christoph Syldatk, Christian Marx, Christian Ihling, Anja Buttstedt, Robin F. A. Moritz, Henning Hopf, Ralf Mattes, Jörg Kreßler and Joachim Ulrich and has published in prestigious journals such as Nature, Current Biology and International Journal of Molecular Sciences.

In The Last Decade

Markus Pietzsch

66 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Markus Pietzsch Germany 24 766 296 273 234 227 68 1.4k
Yoh Kodera Japan 23 832 1.1× 195 0.7× 150 0.5× 39 0.2× 158 0.7× 71 1.5k
Jihye Yoo South Korea 19 760 1.0× 105 0.4× 50 0.2× 164 0.7× 233 1.0× 50 1.7k
Yuntao Zhu China 25 1.3k 1.6× 677 2.3× 90 0.3× 86 0.4× 133 0.6× 44 2.0k
Susumu Hama Japan 25 1.0k 1.4× 136 0.5× 111 0.4× 36 0.2× 42 0.2× 55 1.8k
Xiaohua Peng China 28 1.1k 1.4× 740 2.5× 41 0.2× 88 0.4× 348 1.5× 114 2.2k
Haruko Takahashi Japan 25 966 1.3× 691 2.3× 176 0.6× 77 0.3× 123 0.5× 66 2.2k
Sinéad M. Ryan Ireland 21 750 1.0× 447 1.5× 112 0.4× 35 0.1× 133 0.6× 28 1.6k
Haifeng Wang China 23 615 0.8× 134 0.5× 37 0.1× 28 0.1× 121 0.5× 73 1.5k
Pierre Lemieux Canada 18 1.1k 1.4× 215 0.7× 41 0.2× 60 0.3× 92 0.4× 38 1.8k
Weier Bao China 19 706 0.9× 75 0.3× 82 0.3× 326 1.4× 642 2.8× 35 2.1k

Countries citing papers authored by Markus Pietzsch

Since Specialization
Citations

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

Fields of papers citing papers by Markus Pietzsch

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Markus Pietzsch

This figure shows the co-authorship network connecting the top 25 collaborators of Markus Pietzsch. A scholar is included among the top collaborators of Markus Pietzsch 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 Markus Pietzsch. Markus Pietzsch 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.
Pietzsch, Markus, et al.. (2024). Alternative strategies for the recombinant synthesis, DOPA modification and analysis of mussel foot proteins – A case study for Mefp-3 from Mytilus edulis. Protein Expression and Purification. 219. 106483–106483. 5 indexed citations
2.
Steenbock, Heiko, Jürgen Brinckmann, Matthias Menzel, et al.. (2023). Fabrication of Insoluble Elastin by Enzyme‐Free Cross‐Linking. Macromolecular Bioscience. 23(11). e2300203–e2300203. 2 indexed citations
3.
Rexer, Thomas, Marcus Hoffmann, Simon Boecker, et al.. (2020). Synthesis of lipid-linked oligosaccharides by a compartmentalized multi-enzyme cascade for the in vitro N-glycosylation of peptides. Journal of Biotechnology. 322. 54–65. 8 indexed citations
4.
Mäder, Karsten, et al.. (2019). Conjugation of Amine-Functionalized Polyesters With Dimethylcasein Using Microbial Transglutaminase. Journal of Pharmaceutical Sciences. 109(2). 981–991. 11 indexed citations
5.
Moritz, Bodo, J. Wendler, Thomas C. Hertel, et al.. (2019). Enzymatic activity and thermoresistance of improved microbial transglutaminase variants. Amino Acids. 52(2). 313–326. 28 indexed citations
6.
Klapproth, Jan, Thomas Rexer, Steffen Klamt, et al.. (2018). Establishment of a five-enzyme cell-free cascade for the synthesis of uridine diphosphate N-acetylglucosamine. Journal of Biotechnology. 283. 120–129. 33 indexed citations
7.
Buttstedt, Anja, Christian Ihling, Markus Pietzsch, & Robin F. A. Moritz. (2016). Royalactin is not a royal making of a queen. Nature. 537(7621). E10–E12. 76 indexed citations
8.
Malešević, Miroslav, et al.. (2015). A Fluorescence‐Based Array Screen for Transglutaminase Substrates. ChemBioChem. 16(8). 1169–1174. 29 indexed citations
9.
Sommer, Claudia, et al.. (2010). Model based optimization of the fed-batch production of a highly active transglutaminase variant in Escherichia coli. Protein Expression and Purification. 77(1). 9–19. 27 indexed citations
10.
Fuchs, Sebastian, et al.. (2010). Transglutaminase: New insights into gelatin nanoparticle cross-linking. Journal of Microencapsulation. 27(8). 747–754. 31 indexed citations
11.
Besheer, Ahmed, Thomas C. Hertel, Jörg Kreßler, Karsten Mäder, & Markus Pietzsch. (2009). Enzymatically catalyzed HES conjugation using microbial transglutaminase: Proof of feasibility. Journal of Pharmaceutical Sciences. 98(11). 4420–4428. 46 indexed citations
12.
Kreßler, Jörg, et al.. (2008). Cloning, expression, purification, and characterization of a designer protein with repetitive sequences. Protein Expression and Purification. 59(2). 203–214. 5 indexed citations
13.
Pietzsch, Markus, et al.. (2001). Immobilization of the hydantoin cleaving enzymes from Arthrobacter aurescens DSM 3747. Journal of Biotechnology. 92(2). 179–186. 16 indexed citations
14.
15.
Pietzsch, Markus, Anja Wiese, Burkhard Wilms, et al.. (2000). Purification of recombinant hydantoinase and l-N-carbamoylase from Arthrobacter aurescens expressed in Escherichia coli: comparison of wild-type and genetically modified proteins. Journal of Chromatography B Biomedical Sciences and Applications. 737(1-2). 179–186. 20 indexed citations
16.
Wiese, Anja, Markus Pietzsch, Christoph Syldatk, Ralf Mattes, & Josef Altenbuchner. (2000). Hydantoin racemase from Arthrobacter aurescens DSM 3747: heterologous expression, purification and characterization. Journal of Biotechnology. 80(3). 217–230. 32 indexed citations
17.
Hopf, Henning, et al.. (1998). Synthesis of planar-chiral [2.2]paracyclophanes by biotransformations: screening for hydrolase activity for the kinetic resolution of 4-acetoxy-[2.2]paracyclophane. Journal of Molecular Catalysis B Enzymatic. 5(1-4). 317–319. 27 indexed citations
18.
Kroutil, Wolfgang, et al.. (1998). Purification and characterization of a highly selective epoxide hydrolase from Nocardia sp. EH1. Journal of Biotechnology. 61(2). 143–150. 33 indexed citations
19.
May, Oliver, Martin Siemann, Markus Pietzsch, et al.. (1998). Substrate-dependent enantioselectivity of a novel hydantoinase from Arthrobacter aurescens DSM 3745: Purification and characterization as new member of cyclic amidases. Journal of Biotechnology. 61(1). 1–13. 48 indexed citations
20.
Pietzsch, Markus, et al.. (1996). Fast purification and kinetic studies of the glycerol-3-phosphate dehydrogenase from the yeast Saccharomyces cerevisiae. Journal of Biotechnology. 49(1-3). 19–27. 14 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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