Hermann Schindelin

10.6k total citations
140 papers, 8.4k citations indexed

About

Hermann Schindelin is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Hermann Schindelin has authored 140 papers receiving a total of 8.4k indexed citations (citations by other indexed papers that have themselves been cited), including 101 papers in Molecular Biology, 39 papers in Materials Chemistry and 36 papers in Cell Biology. Recurrent topics in Hermann Schindelin's work include Enzyme Structure and Function (29 papers), Metalloenzymes and iron-sulfur proteins (25 papers) and Endoplasmic Reticulum Stress and Disease (24 papers). Hermann Schindelin is often cited by papers focused on Enzyme Structure and Function (29 papers), Metalloenzymes and iron-sulfur proteins (25 papers) and Endoplasmic Reticulum Stress and Disease (24 papers). Hermann Schindelin collaborates with scholars based in Germany, United States and United Kingdom. Hermann Schindelin's co-authors include Caroline Kisker, Petra Hänzelmann, Douglas C. Rees, K.V. Rajagopalan, Udo Heinemann, William J. Lennarz, Margot M. Wuebbens, Song Xiang, Alexander Buchberger and James B. Howard and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Hermann Schindelin

138 papers receiving 8.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Hermann Schindelin Germany 49 5.7k 2.4k 1.5k 1.2k 1.1k 140 8.4k
Judy Hirst United Kingdom 57 8.3k 1.5× 2.2k 0.9× 444 0.3× 635 0.5× 492 0.5× 133 12.1k
Ulrich Mühlenhoff Germany 53 6.1k 1.1× 3.9k 1.6× 681 0.5× 606 0.5× 1.0k 1.0× 96 8.8k
Günter Schwarz Germany 50 3.4k 0.6× 2.5k 1.0× 502 0.3× 562 0.5× 1.1k 1.0× 155 6.5k
Brian R. Crane United States 57 5.1k 0.9× 710 0.3× 1.2k 0.8× 1.0k 0.8× 1.7k 1.6× 166 9.7k
Matti Saraste Germany 55 9.5k 1.7× 493 0.2× 2.5k 1.6× 1.4k 1.2× 1.0k 1.0× 99 12.4k
T.M. Iverson United States 32 4.3k 0.8× 1.3k 0.5× 206 0.1× 1.1k 0.9× 1.1k 1.0× 89 6.2k
M C Kennedy United States 36 3.0k 0.5× 1.3k 0.5× 471 0.3× 718 0.6× 497 0.5× 68 5.9k
Kristina Djinović‐Carugo Austria 42 3.3k 0.6× 367 0.2× 1.3k 0.9× 715 0.6× 367 0.3× 144 5.9k
Shinya Yoshikawa Japan 42 6.9k 1.2× 528 0.2× 1.4k 0.9× 1.1k 0.9× 2.2k 2.0× 165 8.9k
Israel Pecht Israel 50 5.3k 0.9× 499 0.2× 941 0.6× 1.1k 0.9× 871 0.8× 368 10.6k

Countries citing papers authored by Hermann Schindelin

Since Specialization
Citations

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

Fields of papers citing papers by Hermann Schindelin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Hermann Schindelin

This figure shows the co-authorship network connecting the top 25 collaborators of Hermann Schindelin. A scholar is included among the top collaborators of Hermann Schindelin 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 Hermann Schindelin. Hermann Schindelin 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.
Schulte, Clemens, Katherina Hemmen, Thomas-Otavio Peulen, et al.. (2025). eSylites: Synthetic Probes for Visualization and Topographic Mapping of Single Excitatory Synapses. Journal of the American Chemical Society. 147(18). 15261–15280.
3.
Hänzelmann, Petra, Christoph Wiedemann, Ute A. Hellmich, et al.. (2022). Fragment screening using biolayer interferometry reveals ligands targeting the SHP-motif binding site of the AAA+ ATPase p97. Communications Chemistry. 5(1). 169–169. 5 indexed citations
4.
Kasaragod, Vikram Babu, Natascha Schaefer, Fang Zheng, et al.. (2020). Pyridoxal kinase inhibition by artemisinins down-regulates inhibitory neurotransmission. Proceedings of the National Academy of Sciences. 117(52). 33235–33245. 20 indexed citations
5.
Wagner, Annika, Hermann Schindelin, Till Opatz, et al.. (2020). Predicting 19F NMR Chemical Shifts: A Combined Computational and Experimental Study of a Trypanosomal Oxidoreductase–Inhibitor Complex. Angewandte Chemie International Edition. 59(31). 12669–12673. 15 indexed citations
6.
Wagner, Annika, Hermann Schindelin, Till Opatz, et al.. (2020). Predicting 19F NMR Chemical Shifts: A Combined Computational and Experimental Study of a Trypanosomal Oxidoreductase–Inhibitor Complex. Angewandte Chemie. 132(31). 12769–12773. 2 indexed citations
7.
Schaefer, Natascha, et al.. (2019). The P429L loss of function mutation of the human glycine transporter 2 associated with hyperekplexia. European Journal of Neuroscience. 50(12). 3906–3920. 8 indexed citations
8.
Wagner, Annika, Martha Brennich, Natalie Dirdjaja, et al.. (2019). Inhibitor‐Induced Dimerization of an Essential Oxidoreductase from African Trypanosomes. Angewandte Chemie International Edition. 58(11). 3640–3644. 17 indexed citations
9.
Wagner, Annika, Martha Brennich, Natalie Dirdjaja, et al.. (2019). Inhibitor‐induzierte Dimerisierung einer essentiellen Oxidoreduktase aus afrikanischen Trypanosomen. Angewandte Chemie. 131(11). 3679–3683. 2 indexed citations
10.
Kasaragod, Vikram Babu & Hermann Schindelin. (2018). Structure–Function Relationships of Glycine and GABAA Receptors and Their Interplay With the Scaffolding Protein Gephyrin. Frontiers in Molecular Neuroscience. 11. 317–317. 38 indexed citations
11.
Misra, Mohit, Maximilian Kühn, Heeseon An, et al.. (2017). Dissecting the Specificity of Adenosyl Sulfamate Inhibitors Targeting the Ubiquitin-Activating Enzyme. Structure. 25(7). 1120–1129.e3. 25 indexed citations
12.
Hänzelmann, Petra & Hermann Schindelin. (2015). Characterization of an Additional Binding Surface on the p97 N-Terminal Domain Involved in Bipartite Cofactor Interactions. Structure. 24(1). 140–147. 33 indexed citations
13.
Hänzelmann, Petra & Hermann Schindelin. (2015). Structural Basis of ATP Hydrolysis and Intersubunit Signaling in the AAA+ ATPase p97. Structure. 24(1). 127–139. 61 indexed citations
14.
Li, Hua, et al.. (2008). Structure of the Oligosaccharyl Transferase Complex at 12 Å Resolution. Structure. 16(3). 432–440. 39 indexed citations
15.
Zhao, Guoping, Xiang Zhou, Yukishige Ito, et al.. (2008). Structural and mutational studies on the importance of oligosaccharide binding for the activity of yeast PNGase. Glycobiology. 19(2). 118–125. 25 indexed citations
16.
Hänzelmann, Petra & Hermann Schindelin. (2006). Binding of 5′-GTP to the C-terminal FeS cluster of the radical S -adenosylmethionine enzyme MoaA provides insights into its mechanism. Proceedings of the National Academy of Sciences. 103(18). 6829–6834. 133 indexed citations
17.
Geng, Tian, et al.. (2006). The Crystal Structure of Yeast Protein Disulfide Isomerase Suggests Cooperativity between Its Active Sites. Cell. 124(5). 1085–1088. 9 indexed citations
18.
Wuebbens, Margot M., et al.. (2001). Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB–MoaD complex. Nature. 414(6861). 325–329. 202 indexed citations
19.
Stowell, Michael H. B., S. Michael Soltis, Caroline Kisker, et al.. (1996). A simple device for studying macromolecular crystals under moderate gas pressures (0.1–10 MPa). Journal of Applied Crystallography. 29(5). 608–613. 21 indexed citations
20.
Schindelin, Hermann, Michael Herrler, Gerald Willimsky, Mohamed A. Marahiel, & Udo Heinemann. (1992). Overproduction, crystallization, and preliminary X‐ray diffraction studies of the major cold shock protein from Bacillus subtilis, CspB. Proteins Structure Function and Bioinformatics. 14(1). 120–124. 43 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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