K.‐H. van Pée

1.3k total citations
31 papers, 1.0k citations indexed

About

K.‐H. van Pée is a scholar working on Inorganic Chemistry, Plant Science and Molecular Biology. According to data from OpenAlex, K.‐H. van Pée has authored 31 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Inorganic Chemistry, 15 papers in Plant Science and 12 papers in Molecular Biology. Recurrent topics in K.‐H. van Pée's work include Vanadium and Halogenation Chemistry (13 papers), Enzyme-mediated dye degradation (13 papers) and Metal-Catalyzed Oxygenation Mechanisms (11 papers). K.‐H. van Pée is often cited by papers focused on Vanadium and Halogenation Chemistry (13 papers), Enzyme-mediated dye degradation (13 papers) and Metal-Catalyzed Oxygenation Mechanisms (11 papers). K.‐H. van Pée collaborates with scholars based in Germany, United States and Belarus. K.‐H. van Pée's co-authors include Franz Lingens, Josef Altenbuchner, James M. Ligon, Stephen T.S. Lam, Isabelle Pelletier, H.J. Hecht, Philip E. Hammer, D. Steven Hill, Birgit Hofmann and Harald Sobek and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Applied and Environmental Microbiology.

In The Last Decade

K.‐H. van Pée

31 papers receiving 1.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
K.‐H. van Pée Germany 16 529 362 221 137 131 31 1.0k
Eric Eichhorn Switzerland 13 697 1.3× 175 0.5× 273 1.2× 116 0.8× 298 2.3× 22 1.3k
Daniel E. Torres Pazmiño Netherlands 24 1.3k 2.4× 265 0.7× 190 0.9× 143 1.0× 173 1.3× 26 1.7k
Saul L. Neidleman Malaysia 18 355 0.7× 255 0.7× 174 0.8× 64 0.5× 54 0.4× 46 863
John Geigert United States 18 358 0.7× 214 0.6× 154 0.7× 57 0.4× 44 0.3× 47 785
Robin Teufel Germany 21 825 1.6× 228 0.6× 142 0.6× 158 1.2× 226 1.7× 41 1.4k
Michael D. Corbett United States 19 254 0.5× 143 0.4× 149 0.7× 61 0.4× 89 0.7× 62 931
Tobias Wage Germany 8 247 0.5× 109 0.3× 120 0.5× 93 0.7× 82 0.6× 8 572
Jian‐bo Wang China 22 746 1.4× 135 0.4× 97 0.4× 83 0.6× 37 0.3× 47 1.2k
Wolfgang Blodig Switzerland 9 217 0.4× 162 0.4× 557 2.5× 55 0.4× 56 0.4× 10 740
Sumio Kanematsu Japan 20 621 1.2× 196 0.5× 683 3.1× 24 0.2× 62 0.5× 31 1.2k

Countries citing papers authored by K.‐H. van Pée

Since Specialization
Citations

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

Fields of papers citing papers by K.‐H. van Pée

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by K.‐H. van Pée. 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 K.‐H. van Pée. The network helps show where K.‐H. van Pée may publish in the future.

Co-authorship network of co-authors of K.‐H. van Pée

This figure shows the co-authorship network connecting the top 25 collaborators of K.‐H. van Pée. A scholar is included among the top collaborators of K.‐H. van Pée 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 K.‐H. van Pée. K.‐H. van Pée 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.
2.
Pée, K.‐H. van, et al.. (2016). Application and Modification of Flavin-Dependent Halogenases. Methods in enzymology on CD-ROM/Methods in enzymology. 575. 65–92. 9 indexed citations
3.
Muffler, Kai, et al.. (2008). Biologische Halogenierung. Chemie Ingenieur Technik. 80(6). 783–794. 1 indexed citations
4.
Muffler, Kai, et al.. (2006). Regioselektive Bio‐Halogenierung pharmazeutisch bedeutender Precursor. Chemie Ingenieur Technik. 78(9). 1385–1385. 1 indexed citations
5.
Schmid, Christoph, et al.. (2006). Enzymatic Incorporation of Halogen Atoms into Natural Compounds. PubMed. 165–194. 15 indexed citations
6.
Pée, K.‐H. van, et al.. (2003). Halogenating Enzymes in the Biosynthesis of Antibiotics. Biochemistry (Moscow). 68(10). 1132–1135. 4 indexed citations
7.
Pée, K.‐H. van, et al.. (2002). [Oxidation of indole and its derivatives by heme-independent chloroperoxidases].. PubMed. 37(3). 285–8. 1 indexed citations
8.
Pée, K.‐H. van, et al.. (2001). Oxidation of Indole and Indole Derivatives Catalyzed by Nonheme Chloroperoxidases. Applied Biochemistry and Microbiology. 37(3). 248–250. 10 indexed citations
9.
Hofmann, Birgit, et al.. (1998). Structural investigation of the cofactor-free chloroperoxidases. Journal of Molecular Biology. 279(4). 889–900. 142 indexed citations
10.
Nagy, István, Geert Schoofs, Paul Proost, et al.. (1997). Thiocarbamate herbicide-inducible nonheme haloperoxidase of Rhodococcus erythropolis NI86/21. Applied and Environmental Microbiology. 63(5). 1911–1916. 23 indexed citations
11.
Krauss, Susanne, et al.. (1996). The non-haem chloroperoxidase from Pseudomonas fluorescens and its relationship to pyrrolnitrin biosynthesis. Microbiology. 142(8). 2129–2135. 66 indexed citations
12.
Altenbuchner, Josef, et al.. (1994). Chloroperoxidase from Streptomyces lividans: isolation and characterization of the enzyme and the corresponding gene. Journal of Bacteriology. 176(8). 2339–2347. 49 indexed citations
13.
Candidus, Sonja, K.‐H. van Pée, & Franz Lingens. (1994). The catechol 2,3-dioxygenase gene of Rhodococcus rhodochrous CTM: nucleotide sequence, comparison with isofunctional dioxygenases and evidence for an active-site histidine. Microbiology. 140(2). 321–330. 44 indexed citations
14.
Pelletier, Isabelle, et al.. (1992). Molecular cloning and sequencing of a non-haem bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762. Journal of General Microbiology. 138(6). 1123–1131. 56 indexed citations
15.
Sobek, Harald, et al.. (1991). Crystallization and preliminary X-ray data of bromoperoxidase from Streptomyces aureofaciens ATCC 10762. Journal of Molecular Biology. 221(1). 35–37. 10 indexed citations
16.
Pée, K.‐H. van. (1990). Enzymology and Genetics of Halogenating Enzymes from Bacteria. Biocatalysis. 4(1). 1–9. 3 indexed citations
17.
18.
Pée, K.‐H. van. (1988). Molecular cloning and high-level expression of a bromoperoxidase gene from Streptomyces aureofaciens Tü24. Journal of Bacteriology. 170(12). 5890–5894. 17 indexed citations
19.
Pée, K.‐H. van, et al.. (1988). Purification and Partial Characterization of Multiple Bromoperoxidases from Streptomyces griseus. Microbiology. 134(12). 3141–3149. 17 indexed citations
20.
Pée, K.‐H. van & Franz Lingens. (1985). Purification of bromoperoxidase from Pseudomonas aureofaciens. Journal of Bacteriology. 161(3). 1171–1175. 50 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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