Clemens Peterbauer

4.3k total citations
91 papers, 3.5k citations indexed

About

Clemens Peterbauer is a scholar working on Molecular Biology, Plant Science and Biotechnology. According to data from OpenAlex, Clemens Peterbauer has authored 91 papers receiving a total of 3.5k indexed citations (citations by other indexed papers that have themselves been cited), including 58 papers in Molecular Biology, 46 papers in Plant Science and 26 papers in Biotechnology. Recurrent topics in Clemens Peterbauer's work include Enzyme-mediated dye degradation (39 papers), Enzyme Catalysis and Immobilization (25 papers) and Electrochemical sensors and biosensors (20 papers). Clemens Peterbauer is often cited by papers focused on Enzyme-mediated dye degradation (39 papers), Enzyme Catalysis and Immobilization (25 papers) and Electrochemical sensors and biosensors (20 papers). Clemens Peterbauer collaborates with scholars based in Austria, Sweden and Thailand. Clemens Peterbauer's co-authors include Dietmar Haltrich, Matteo Lorito, Roland Ludwig, Christian P. Kubicek, Joseph Strauss, Robert L. Mach, Sabine Goller, Christiane Galhaup, Christina Divne and Christoph Sygmund and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

Clemens Peterbauer

90 papers receiving 3.4k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Clemens Peterbauer Austria	36	1.8k	1.6k	856	707	632	91	3.5k
Masahiro Samejima Japan	42	2.1k 1.2×	2.0k 1.3×	1.8k 2.0×	368 0.5×	2.9k 4.5×	145	5.0k
Mukund V. Deshpande India	32	1.8k 1.0×	1.2k 0.8×	690 0.8×	123 0.2×	842 1.3×	98	4.1k
Debbie Yaver United States	19	1.3k 0.7×	1.2k 0.8×	692 0.8×	147 0.2×	226 0.4×	24	2.9k
Yazhong Xiao China	29	884 0.5×	1.1k 0.7×	1.1k 1.2×	162 0.2×	521 0.8×	124	2.3k
Xiulan Sun China	33	1.4k 0.8×	658 0.4×	128 0.1×	324 0.5×	1.0k 1.6×	99	2.9k
Zheng Han China	32	754 0.4×	1.5k 1.0×	104 0.1×	227 0.3×	372 0.6×	109	2.6k
Peiji Gao China	24	914 0.5×	550 0.4×	514 0.6×	285 0.4×	696 1.1×	83	2.0k
Xiuyun Ye China	24	768 0.4×	1.0k 0.7×	648 0.8×	197 0.3×	236 0.4×	76	2.1k
Markku Saloheimo Finland	45	3.8k 2.1×	2.1k 1.4×	2.4k 2.8×	137 0.2×	2.7k 4.2×	110	6.0k
Martin Schülein Denmark	31	1.6k 0.9×	795 0.5×	1.6k 1.8×	120 0.2×	1.5k 2.4×	61	3.0k

Countries citing papers authored by Clemens Peterbauer

Since Specialization

Citations

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

Fields of papers citing papers by Clemens Peterbauer

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Clemens Peterbauer

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

All Works

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20 of 20 papers shown

Bennett, Alexandra, Daniel Maresch, Roland Ludwig, et al.. (2024). Dye-Decolorizing Peroxidases Maintain High Stability and Turnover on Kraft Lignin and Lignocellulose Substrates. ACS Omega. 9(45). 45025–45034. 1 indexed citations

Rodrigues, Carolina F., et al.. (2024). Engineering A‐type Dye‐Decolorizing Peroxidases by Modification of a Conserved Glutamate Residue. ChemBioChem. 25(9). e202300872–e202300872. 3 indexed citations

Erven, Gijs van, et al.. (2024). Characterization of Amycolatopsis 75iv2 dye-decolorizing peroxidase on O -glycosides. Applied and Environmental Microbiology. 90(5). e0020524–e0020524. 5 indexed citations

Takenaka, Shinji, Clemens Peterbauer, Dietmar Haltrich, et al.. (2023). Functional modification of thermostable alkaline protease from Bacillus halodurans SE5 for efficient production of antioxidative and ACE-inhibitory peptides from sericin. Biocatalysis and Agricultural Biotechnology. 54. 102943–102943. 5 indexed citations

Peterbauer, Clemens, et al.. (2023). Localization of Pyranose 2-Oxidase from Kitasatospora aureofaciens: A Step Closer to Elucidate a Biological Role. International Journal of Molecular Sciences. 24(3). 1975–1975. 6 indexed citations

Chang, Lee Sin, Abdul Salam Babji, Nurul Aqilah Mohd Zaini, et al.. (2023). A review on proteolytic fermentation of dietary protein using lactic acid bacteria for the development of novel proteolytically fermented foods. International Journal of Food Science & Technology. 59(3). 1213–1236. 13 indexed citations

Peterbauer, Clemens, et al.. (2023). Double-Labeling Method for Visualization and Quantification of Membrane-Associated Proteins in Lactococcus lactis. International Journal of Molecular Sciences. 24(13). 10586–10586.

Herzog, Peter L., E. Borghi, Michael W. Traxlmayr, et al.. (2020). Developing a cell-bound detection system for the screening of oxidase activity using the fluorescent peroxide sensor roGFP2-Orp1. Protein Engineering Design and Selection. 33. 2 indexed citations

Mathiesen, Geir, Alasdair Mackenzie, Jane W. Agger, et al.. (2016). Display of a β-mannanase and a chitosanase on the cell surface of Lactobacillus plantarum towards the development of whole-cell biocatalysts. Microbial Cell Factories. 15(1). 169–169. 28 indexed citations

10.

Kittl, Roman, et al.. (2015). Transcription analysis of pyranose dehydrogenase from the basidiomycete Agaricus bisporus and characterization of the recombinantly expressed enzyme. Protein Expression and Purification. 119. 36–44. 6 indexed citations

11.

Spadiut, Oliver, Thanyaporn Wongnate, Jeerus Sucharitakul, et al.. (2013). The 1.6 Å Crystal Structure of Pyranose Dehydrogenase from Agaricus meleagris Rationalizes Substrate Specificity and Reveals a Flavin Intermediate. PLoS ONE. 8(1). e53567–e53567. 47 indexed citations

12.

Krondorfer, Iris, et al.. (2013). Convenient microtiter plate‐based, oxygen‐independent activity assays for flavin‐dependent oxidoreductases based on different redox dyes. Biotechnology Journal. 9(4). 474–482. 22 indexed citations

13.

Zafar, Muhammad Nadeem, Magnus Falk, Roland Ludwig, et al.. (2013). Optimization of a Membraneless Glucose/Oxygen Enzymatic Fuel Cell Based on a Bioanode with High Coulombic Efficiency and Current Density. ChemPhysChem. 14(10). 2260–2269. 44 indexed citations

14.

Peterbauer, Clemens, et al.. (2012). EFFECT OF ENZYME DEGLYCOSYLATION ON THE AMPEROMETRIC DETECTION OF GLUCOSE AT PDH-MODIFIED ELECTRODE. Studia Universitatis Babeș-Bolyai Chemia. 57(4). 87–99. 3 indexed citations

15.

Nguyen, Tien‐Thanh, Thu‐Ha Nguyen, Thomas Maischberger, et al.. (2011). Quantitative transcript analysis of the inducible expression system pSIP: comparison of the overexpression of Lactobacillus spp. β-galactosidases in Lactobacillus plantarum. Microbial Cell Factories. 10(1). 46–46. 8 indexed citations

16.

Takakura, Yoshimitsu, Masako Tsunashima, Oliver Spadiut, et al.. (2010). Characterisation of recombinant pyranose oxidase from the cultivated mycorrhizal basidiomycete Lyophyllum shimeji (hon-shimeji). Microbial Cell Factories. 9(1). 57–57. 12 indexed citations

17.

Kujawa, Magdalena, Oliver Spadiut, Roman Kittl, et al.. (2009). Pyranose 2-oxidase from Phanerochaete chrysosporium—Expression in E. coli and biochemical characterization. Journal of Biotechnology. 142(2). 97–106. 32 indexed citations

18.

Kittl, Roman, Christoph Sygmund, Petr Halada, et al.. (2007). Molecular cloning of three pyranose dehydrogenase-encoding genes from Agaricus meleagris and analysis of their expression by real-time RT-PCR. Current Genetics. 53(2). 117–127. 29 indexed citations

19.

Brunner, Kurt, Manuel Montero, Robert L. Mach, Clemens Peterbauer, & Christian P. Kubicek. (2003). Expression of theech42(endochitinase) gene ofTrichoderma atrovirideunder carbon starvation is antagonized via a BrlA-likecis-acting element. FEMS Microbiology Letters. 218(2). 259–264. 15 indexed citations

20.

Peterbauer, Clemens, et al.. (2002). Identification of the N-acetyl-D-glucosamine-inducible element in the promoter of the Trichoderma atroviride nag1 gene encoding N-acetyl-glucosaminidase. Molecular Genetics and Genomics. 267(2). 162–170. 18 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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