Gerhard Schenk

9.1k total citations
234 papers, 7.2k citations indexed

About

Gerhard Schenk is a scholar working on Molecular Biology, Oncology and Inorganic Chemistry. According to data from OpenAlex, Gerhard Schenk has authored 234 papers receiving a total of 7.2k indexed citations (citations by other indexed papers that have themselves been cited), including 115 papers in Molecular Biology, 80 papers in Oncology and 42 papers in Inorganic Chemistry. Recurrent topics in Gerhard Schenk's work include Metal complexes synthesis and properties (66 papers), Enzyme Catalysis and Immobilization (32 papers) and Metal-Catalyzed Oxygenation Mechanisms (31 papers). Gerhard Schenk is often cited by papers focused on Metal complexes synthesis and properties (66 papers), Enzyme Catalysis and Immobilization (32 papers) and Metal-Catalyzed Oxygenation Mechanisms (31 papers). Gerhard Schenk collaborates with scholars based in Australia, Ireland and Germany. Gerhard Schenk's co-authors include Lawrence R. Gahan, Nataša Mitić, Luke W. Guddat, David L. Ollis, Ross P. McGeary, Ademir Neves, Sarah J. Smith, Graeme R. Hanson, Peter Comba and Peter F. Nixon and has published in prestigious journals such as Nature, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

Gerhard Schenk

225 papers receiving 7.1k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Gerhard Schenk Australia	49	3.0k	2.4k	1.5k	1.2k	926	234	7.2k
Norbert Sträter Germany	40	3.4k 1.1×	1.9k 0.8×	801 0.5×	1.3k 1.1×	1.0k 1.1×	140	7.6k
Lawrence R. Gahan Australia	42	1.5k 0.5×	2.6k 1.1×	1.8k 1.2×	1.6k 1.3×	1.0k 1.1×	205	5.4k
Stefano Mangani Italy	41	2.6k 0.9×	1.2k 0.5×	631 0.4×	1.1k 0.9×	1.0k 1.1×	165	5.9k
Wilfred A. van der Donk United States	73	13.6k 4.5×	1.7k 0.7×	2.4k 1.5×	4.5k 3.8×	1.2k 1.3×	345	19.8k
Mohammad Abdulkader Akbarsha India	38	1.5k 0.5×	2.4k 1.0×	869 0.6×	1.7k 1.4×	553 0.6×	173	5.2k
Wenjie Zheng China	53	1.8k 0.6×	1.6k 0.7×	323 0.2×	1.6k 1.3×	1.8k 1.9×	169	8.2k
David L. Tierney United States	35	1.1k 0.4×	586 0.2×	644 0.4×	469 0.4×	574 0.6×	114	3.5k
Nataša Mitić Australia	29	978 0.3×	858 0.4×	644 0.4×	337 0.3×	336 0.4×	52	2.4k
David L. Ollis Australia	47	5.4k 1.8×	794 0.3×	295 0.2×	570 0.5×	1.2k 1.3×	140	7.9k
H.A. Tajmir‐Riahi Canada	51	5.5k 1.8×	2.0k 0.8×	356 0.2×	1.5k 1.3×	1.1k 1.1×	210	8.6k

Countries citing papers authored by Gerhard Schenk

Since Specialization

Citations

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

Fields of papers citing papers by Gerhard Schenk

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Gerhard Schenk

This figure shows the co-authorship network connecting the top 25 collaborators of Gerhard Schenk. A scholar is included among the top collaborators of Gerhard Schenk 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 Gerhard Schenk. Gerhard Schenk 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

Pérez-Gil, Jordi, et al.. (2025). Iron–Sulfur Cluster Enzymes of the Methylerythritol Phosphate Pathway: IspG and IspH. Biochemistry. 64(12). 2544–2555.

Dinda, Rupam, Monalisa Mohanty, Satabdi Roy, et al.. (2024). Synthesis, characterization, and structures of mononuclear and phenoxo-/acetato-bridged trinuclear zinc(II) complexes from salan ligands: Study of their hydrolytic activity. Journal of Molecular Structure. 1308. 138106–138106. 2 indexed citations

Pedroso, Marcelo Monteiro, et al.. (2023). Structure, function, and evolution of metallo-β-lactamases from the B3 subgroup—emerging targets to combat antibiotic resistance. Frontiers in Chemistry. 11. 1196073–1196073. 8 indexed citations

Liu, Lian, Manuel R. Plan, Bingyin Peng, et al.. (2023). Metabolic flux enhancement from the translational fusion of terpene synthases is linked to terpene synthase accumulation. Metabolic Engineering. 77. 143–151. 31 indexed citations

Zheng, Shan, Adi Goldenzweig, Fengjiang Liu, et al.. (2022). Enhancing the Thermal and Kinetic Stability of Ketol-Acid Reductoisomerase, a Central Catalyst of a Cell-Free Enzyme Cascade for the Manufacture of Platform Chemicals. MDPI (MDPI AG). 1(2). 163–178. 4 indexed citations

Wang, Lijuan, Kun Cao, Marcelo Monteiro Pedroso, et al.. (2021). Sequence- and structure-guided improvement of the catalytic performance of a GH11 family xylanase from Bacillus subtilis. Journal of Biological Chemistry. 297(5). 101262–101262. 20 indexed citations

Pedroso, Marcelo Monteiro, et al.. (2021). Pesticide degradation by immobilised metalloenzymes provides an attractive avenue for bioremediation. SHILAP Revista de lepidopterología. 1. 100015–100015. 20 indexed citations

Lonhienne, Thierry, M.D. Garcia, Tristan I. Croll, et al.. (2020). Structures of fungal and plant acetohydroxyacid synthases. Nature. 586(7828). 317–321. 54 indexed citations

Awad, Dania, et al.. (2020). Towards high-throughput optimization of microbial lipid production: from strain development to process monitoring. Sustainable Energy & Fuels. 4(12). 5958–5969. 8 indexed citations

10.

Mostert, A. Bernardus, Paul Zierep, Graeme R. Hanson, et al.. (2020). Engineering proton conductivity in melanin using metal doping. Journal of Materials Chemistry B. 8(35). 8050–8060. 32 indexed citations

11.

Kan, Meng‐Wei, et al.. (2019). Synthesis, evaluation and structural investigations of potent purple acid phosphatase inhibitors as drug leads for osteoporosis. European Journal of Medicinal Chemistry. 182. 111611–111611. 8 indexed citations

12.

Sharma, Gaurav, et al.. (2019). Investigating coordination flexibility of glycerophosphodiesterase (GpdQ) through interactions with mono-, di-, and triphosphoester (NPP, BNPP, GPE, and paraoxon) substrates. Physical Chemistry Chemical Physics. 21(10). 5499–5509. 14 indexed citations

13.

Baek, Jong‐Min, Raine E. S. Thomson, Dominic J. B. Hunter, et al.. (2018). Engineering highly functional thermostable proteins using ancestral sequence reconstruction. Nature Catalysis. 1(11). 878–888. 138 indexed citations

14.

Hussein, Waleed M., et al.. (2018). Synthesis and evaluation of novel purple acid phosphatase inhibitors. MedChemComm. 10(1). 61–71. 6 indexed citations

15.

Pedroso, Marcelo Monteiro, Jeffrey R. Harmer, Nataša Mitić, et al.. (2017). Characterization of a highly efficient antibiotic-degrading metallo-β-lactamase obtained from an uncultured member of a permafrost community. Metallomics. 9(8). 1157–1168. 15 indexed citations

16.

Neves, Ademir, Rosely A. Peralta, Elene C. Pereira‐Maia, et al.. (2017). Second-Sphere Effects in Dinuclear Fe^IIIZn^II Hydrolase Biomimetics: Tuning Binding and Reactivity Properties. Inorganic Chemistry. 57(1). 187–203. 32 indexed citations

17.

Pedroso, Marcelo Monteiro, Jeffrey R. Harmer, Lawrence R. Gahan, et al.. (2017). Reaction mechanism of the metallohydrolase CpsB from Streptococcus pneumoniae, a promising target for novel antimicrobial agents. Dalton Transactions. 46(39). 13194–13201. 6 indexed citations

18.

Mitić, Nataša, et al.. (2014). Catalytic Mechanisms of Metallohydrolases Containing Two Metal Ions. Advances in protein chemistry and structural biology. 97. 49–81. 60 indexed citations

19.

Gahan, Lawrence R., et al.. (2007). 2. Metalloproteins. JBIC Journal of Biological Inorganic Chemistry. 12(S1). 53–98. 2 indexed citations

20.

Hanson, Graeme R., Gerhard Schenk, & C J Noble. (2000). Modelling strain broadening in the EPR spectra of high spin FE(III) metalloproteins. Queensland's institutional digital repository (The University of Queensland). 42(5). 59–59.

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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