Hajo Kries

2.0k total citations
40 papers, 1.5k citations indexed

About

Hajo Kries is a scholar working on Molecular Biology, Pharmacology and Organic Chemistry. According to data from OpenAlex, Hajo Kries has authored 40 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 17 papers in Pharmacology and 11 papers in Organic Chemistry. Recurrent topics in Hajo Kries's work include Microbial Natural Products and Biosynthesis (17 papers), Biochemical and Structural Characterization (11 papers) and Chemical Synthesis and Analysis (8 papers). Hajo Kries is often cited by papers focused on Microbial Natural Products and Biosynthesis (17 papers), Biochemical and Structural Characterization (11 papers) and Chemical Synthesis and Analysis (8 papers). Hajo Kries collaborates with scholars based in Germany, Switzerland and United Kingdom. Hajo Kries's co-authors include Donald Hilvert, Rebecca Blomberg, David L. Niquille, Sarah E. O’Connor, Peer R. E. Mittl, Daniel M. Pinkas, Stephen L. Mayo, Markus G. Grütter, Heidi K. Privett and Benedikt M. Wanner and has published in prestigious journals such as Nature, Journal of the American Chemical Society and Advanced Materials.

In The Last Decade

Hajo Kries

38 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Hajo Kries Germany	21	1.2k	505	274	169	141	40	1.5k
Mark C. Walker United States	16	908 0.8×	588 1.2×	251 0.9×	33 0.2×	116 0.8×	19	1.4k
Christopher J. Thibodeaux Canada	17	1.1k 1.0×	481 1.0×	685 2.5×	216 1.3×	123 0.9×	44	1.7k
Jaclyn M. Winter United States	18	707 0.6×	780 1.5×	504 1.8×	82 0.5×	138 1.0×	38	1.7k
Fanglu Huang United Kingdom	18	743 0.6×	422 0.8×	325 1.2×	247 1.5×	51 0.4×	31	1.2k
Akimasa Miyanaga Japan	24	1.2k 1.0×	776 1.5×	535 2.0×	197 1.2×	244 1.7×	80	2.0k
Alessandra S. Eustáquio United States	27	1.3k 1.1×	1.1k 2.2×	521 1.9×	106 0.6×	164 1.2×	58	2.2k
Lars Herfindal Norway	23	572 0.5×	274 0.5×	175 0.6×	52 0.3×	58 0.4×	76	1.4k
Moshe Goldsmith Israel	22	1.4k 1.3×	172 0.3×	178 0.6×	232 1.4×	516 3.7×	35	2.2k
Youli Xiao China	25	976 0.8×	364 0.7×	375 1.4×	83 0.5×	288 2.0×	57	1.9k
Andrew M. Piggott Australia	28	1.0k 0.9×	1.2k 2.3×	664 2.4×	73 0.4×	165 1.2×	93	2.3k

Countries citing papers authored by Hajo Kries

Since Specialization

Citations

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

Fields of papers citing papers by Hajo Kries

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Hajo Kries

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

1.

Little, Rory F., Hideki Hashizume, Ryûichi Sawa, et al.. (2024). Analysis of the Valgamicin Biosynthetic Pathway Reveals a General Mechanism for Cyclopropanol Formation across Diverse Natural Product Scaffolds. ACS Chemical Biology. 19(3). 660–668. 5 indexed citations

2.

Kries, Hajo, et al.. (2023). Novel Biocatalysts from Specialized Metabolism. Angewandte Chemie International Edition. 63(4). e202309284–e202309284. 6 indexed citations

3.

Kries, Hajo, et al.. (2023). Novel Biocatalysts from Specialized Metabolism. Angewandte Chemie. 136(4). 2 indexed citations

4.

Vilotijević, Ivan, et al.. (2023). Biosynthetic incorporation of fluorinated amino acids into the nonribosomal peptide gramicidin S. RSC Chemical Biology. 4(9). 692–697. 4 indexed citations

5.

Hoernke, Maria, et al.. (2023). Analysing Megasynthetase Mutants at High Throughput Using Droplet Microfluidics**. ChemBioChem. 24(24). e202300680–e202300680. 2 indexed citations

6.

Ishida, Keishi, et al.. (2022). Pathogenic bacteria remodel central metabolic enzyme to build a cyclopropanol warhead. Nature Chemistry. 14(8). 884–890. 21 indexed citations

7.

Fischer, Dagmar, et al.. (2020). Bacterial-Like Nonribosomal Peptide Synthetases Produce Cyclopeptides in the Zygomycetous Fungus Mortierella alpina. Applied and Environmental Microbiology. 87(3). 12 indexed citations

8.

Ishida, Keishi, et al.. (2020). Sulfonium Acids Loaded onto an Unusual Thiotemplate Assembly Line Construct the Cyclopropanol Warhead of a Burkholderia Virulence Factor. Angewandte Chemie. 132(32). 13613–13617. 3 indexed citations

9.

Kries, Hajo, Joël S. Bloch, H. Adrian Bunzel, Daniel M. Pinkas, & Donald Hilvert. (2020). Contribution of Oxyanion Stabilization to Kemp Eliminase Efficiency. ACS Catalysis. 10(8). 4460–4464. 19 indexed citations

10.

Ishida, Keishi, et al.. (2020). Sulfonium Acids Loaded onto an Unusual Thiotemplate Assembly Line Construct the Cyclopropanol Warhead of a Burkholderia Virulence Factor. Angewandte Chemie International Edition. 59(32). 13511–13515. 24 indexed citations

11.

Bunzel, H. Adrian, Hajo Kries, Cathleen Zeymer, et al.. (2019). Emergence of a Negative Activation Heat Capacity during Evolution of a Designed Enzyme. Journal of the American Chemical Society. 141(30). 11745–11748. 45 indexed citations

12.

Götze, Sebastian, Gerald Lackner, Shuai‐Bing Zhang, et al.. (2019). Structure elucidation of the syringafactin lipopeptides provides insight in the evolution of nonribosomal peptide synthetases. Chemical Science. 10(48). 10979–10990. 23 indexed citations

13.

Niquille, David L., et al.. (2017). Nonribosomal biosynthesis of backbone-modified peptides. Nature Chemistry. 10(3). 282–287. 90 indexed citations

14.

Kries, Hajo & Sarah E. O’Connor. (2016). Biocatalysts from alkaloid producing plants. Current Opinion in Chemical Biology. 31. 22–30. 26 indexed citations

15.

Kries, Hajo, David L. Niquille, & Donald Hilvert. (2015). A Subdomain Swap Strategy for Reengineering Nonribosomal Peptides. Chemistry & Biology. 22(5). 640–648. 86 indexed citations

16.

Schulz, Jessica D., Sophie Basler, Hajo Kries, et al.. (2015). Site‐Specific Polymer Conjugation Stabilizes Therapeutic Enzymes in the Gastrointestinal Tract. Advanced Materials. 28(7). 1455–1460. 38 indexed citations

17.

Alagna, Fiammetta, Fernando Geu‐Flores, Hajo Kries, et al.. (2015). Identification and Characterization of the Iridoid Synthase Involved in Oleuropein Biosynthesis in Olive (Olea europaea) Fruits. Journal of Biological Chemistry. 291(11). 5542–5554. 72 indexed citations

18.

Kries, Hajo, et al.. (2014). Reprogramming Nonribosomal Peptide Synthetases for “Clickable” Amino Acids. Angewandte Chemie International Edition. 53(38). 10105–10108. 98 indexed citations

19.

Blomberg, Rebecca, Hajo Kries, Daniel M. Pinkas, et al.. (2013). Precision is essential for efficient catalysis in an evolved Kemp eliminase. Nature. 503(7476). 418–421. 261 indexed citations

20.

Kries, Hajo, Rebecca Blomberg, & Donald Hilvert. (2013). De novo enzymes by computational design. Current Opinion in Chemical Biology. 17(2). 221–228. 191 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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