Rudi Glockshuber

14.7k total citations · 3 hit papers
171 papers, 11.9k citations indexed

About

Rudi Glockshuber is a scholar working on Molecular Biology, Cell Biology and Materials Chemistry. According to data from OpenAlex, Rudi Glockshuber has authored 171 papers receiving a total of 11.9k indexed citations (citations by other indexed papers that have themselves been cited), including 129 papers in Molecular Biology, 34 papers in Cell Biology and 31 papers in Materials Chemistry. Recurrent topics in Rudi Glockshuber's work include Protein Structure and Dynamics (35 papers), Enzyme Structure and Function (31 papers) and Endoplasmic Reticulum Stress and Disease (28 papers). Rudi Glockshuber is often cited by papers focused on Protein Structure and Dynamics (35 papers), Enzyme Structure and Function (31 papers) and Endoplasmic Reticulum Stress and Disease (28 papers). Rudi Glockshuber collaborates with scholars based in Switzerland, Germany and Russia. Rudi Glockshuber's co-authors include Simone Hornemann, Kurt Wüthrich, Roland Riek, Gerhard Wider, Martin Billeter, Martina Wunderlich, Martina Huber‐Wunderlich, Susanne Liemann, A. Plueckthun and Jens Hennecke and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Rudi Glockshuber

170 papers receiving 11.6k citations

Hit Papers

NMR structure of the mouse prion protein domain PrP(121–231) 1996 2026 2006 2016 1996 1997 1997 250 500 750 1000

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Rudi Glockshuber Switzerland 59 9.3k 2.1k 2.0k 1.5k 1.5k 171 11.9k
Reed B. Wickner United States 73 13.1k 1.4× 2.5k 1.2× 3.1k 1.6× 806 0.5× 1.2k 0.8× 277 16.0k
Mick F. Tuite United Kingdom 54 9.4k 1.0× 971 0.5× 1.3k 0.7× 675 0.5× 1.2k 0.8× 196 10.7k
Charles Weissmann Switzerland 81 22.5k 2.4× 5.4k 2.6× 6.5k 3.3× 493 0.3× 999 0.7× 216 28.5k
Osamu Nureki Japan 74 19.5k 2.1× 615 0.3× 306 0.2× 1.2k 0.8× 947 0.6× 367 23.8k
Joël Vandekerckhove Belgium 80 13.6k 1.5× 691 0.3× 225 0.1× 717 0.5× 4.3k 2.9× 307 21.5k
Frédéric Rousseau Belgium 54 8.2k 0.9× 427 0.2× 460 0.2× 1.4k 0.9× 977 0.7× 197 11.6k
Detlev Riesner Germany 49 5.4k 0.6× 1.0k 0.5× 1.3k 0.7× 382 0.3× 181 0.1× 174 7.6k
Elizabeth A. Craig United States 80 22.0k 2.4× 763 0.4× 256 0.1× 2.2k 1.5× 4.3k 3.0× 232 24.6k
Fred Sherman United States 75 27.6k 3.0× 675 0.3× 282 0.1× 1.4k 0.9× 4.6k 3.1× 251 32.7k
Dick Hoekstra Netherlands 64 11.9k 1.3× 257 0.1× 425 0.2× 897 0.6× 2.1k 1.4× 257 16.5k

Countries citing papers authored by Rudi Glockshuber

Since Specialization
Citations

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

Fields of papers citing papers by Rudi Glockshuber

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Rudi Glockshuber

This figure shows the co-authorship network connecting the top 25 collaborators of Rudi Glockshuber. A scholar is included among the top collaborators of Rudi Glockshuber 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 Rudi Glockshuber. Rudi Glockshuber 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.
Afanasyev, Pavel, et al.. (2025). Substrates bind to residues lining the ring of asymmetrically engaged bacterial proteasome activator Bpa. Nature Communications. 16(1). 3042–3042. 1 indexed citations
2.
Rabl, Julius, et al.. (2025). Single-stranded DNA binding to the transcription factor PafBC triggers the mycobacterial DNA damage response. Science Advances. 11(6). eadq9054–eadq9054. 4 indexed citations
3.
Bachmann, P., Pavel Afanasyev, Daniel Boehringer, & Rudi Glockshuber. (2025). Structures of the Escherichia coli type 1 pilus during pilus rod assembly and after assembly termination. Nature Communications. 16(1). 4988–4988. 1 indexed citations
4.
Giese, Christoph, et al.. (2024). Dimerization of a 5-kDa domain defines the architecture of the 5-MDa gammaproteobacterial pyruvate dehydrogenase complex. Science Advances. 10(6). eadj6358–eadj6358. 4 indexed citations
5.
Zyla, Dawid, Thomas Wiegand, P. Bachmann, et al.. (2024). The assembly platform FimD is required to obtain the most stable quaternary structure of type 1 pili. Nature Communications. 15(1). 3032–3032. 7 indexed citations
6.
Boudet, Julien, et al.. (2023). Elongated Bacterial Pili as a Versatile Alignment Medium for NMR Spectroscopy. Angewandte Chemie International Edition. 62(37). e202305120–e202305120. 1 indexed citations
7.
Weiß, Richard, Christoph Giese, Chia‐Wei Lin, et al.. (2021). Glycan–protein interactions determine kinetics of N -glycan remodeling. RSC Chemical Biology. 2(3). 917–931. 19 indexed citations
8.
Weiss, Gregor L., Maximilian M. Sauer, Chia‐Wei Lin, et al.. (2020). Architecture and function of human uromodulin filaments in urinary tract infections. Science. 369(6506). 1005–1010. 84 indexed citations
9.
Matteï, Simone, et al.. (2020). Structure of native glycolipoprotein filaments in honeybee royal jelly. Nature Communications. 11(1). 6267–6267. 18 indexed citations
10.
Zyla, Dawid, Pavel Afanasyev, Jingwei Xu, et al.. (2020). The cryo-EM structure of the human uromodulin filament core reveals a unique assembly mechanism. eLife. 9. 30 indexed citations
11.
Zyla, Dawid, et al.. (2020). Donor strand sequence, rather than donor strand orientation, determines the stability and non-equilibrium folding of the type 1 pilus subunit FimA. Journal of Biological Chemistry. 295(35). 12437–12448. 7 indexed citations
12.
Zyla, Dawid, et al.. (2020). A metabolite binding protein moonlights as a bile‐responsive chaperone. The EMBO Journal. 39(20). e104231–e104231. 10 indexed citations
13.
Zyla, Dawid, A.E. Prota, Guido Capitani, & Rudi Glockshuber. (2019). Alternative folding to a monomer or homopolymer is a common feature of the type 1 pilus subunit FimA from enteroinvasive bacteria. Journal of Biological Chemistry. 294(27). 10553–10563. 9 indexed citations
14.
Klose, Daniel, Raphael Ledermann, Maximilian M. Sauer, et al.. (2019). Structural basis and mechanism for metallochaperone-assisted assembly of the Cu A center in cytochrome oxidase. Science Advances. 5(7). eaaw8478–eaaw8478. 24 indexed citations
15.
Roderer, Daniel & Rudi Glockshuber. (2017). Assembly mechanism of the α-pore–forming toxin cytolysin A from Escherichia coli. Philosophical Transactions of the Royal Society B Biological Sciences. 372(1726). 20160211–20160211. 29 indexed citations
16.
Nishiyama, Mireille, et al.. (2008). Reconstitution of Pilus Assembly Reveals a Bacterial Outer Membrane Catalyst. Science. 320(5874). 376–379. 99 indexed citations
17.
Stirnimann, Christian U., Markus G. Grütter, Rudi Glockshuber, & Guido Capitani. (2006). nDsbD: a redox interaction hub in the Escherichia coli periplasm. Cellular and Molecular Life Sciences. 63(14). 1642–1648. 39 indexed citations
18.
Heuberger, Manfred, et al.. (2004). Protein-mediated boundary lubrication in arthroplasty. Biomaterials. 26(10). 1165–1173. 141 indexed citations
19.
Rossmann, Reinhild, D Stern, Hannes Loferer, et al.. (1997). Replacement of Pro109 by His in TlpA, a thioredoxin‐like protein from Bradyrhizobium japonicum, alters its redox properties but not its in vivo functions. FEBS Letters. 406(3). 249–254. 26 indexed citations
20.
Strobl, Stefan, Ronald Wiltscheck, K. Maskos, et al.. (1995). Determination of the Three-Dimensional Structure of the Bifunctional .alpha.-Amylase/Trypsin Inhibitor from Ragi Seeds by NMR Spectroscopy. Biochemistry. 34(26). 8281–8293. 72 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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