Malte Gersch

2.7k total citations
33 papers, 1.6k citations indexed

About

Malte Gersch is a scholar working on Molecular Biology, Oncology and Organic Chemistry. According to data from OpenAlex, Malte Gersch has authored 33 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 14 papers in Oncology and 4 papers in Organic Chemistry. Recurrent topics in Malte Gersch's work include Ubiquitin and proteasome pathways (17 papers), Peptidase Inhibition and Analysis (11 papers) and Glycosylation and Glycoproteins Research (4 papers). Malte Gersch is often cited by papers focused on Ubiquitin and proteasome pathways (17 papers), Peptidase Inhibition and Analysis (11 papers) and Glycosylation and Glycoproteins Research (4 papers). Malte Gersch collaborates with scholars based in Germany, United Kingdom and Netherlands. Malte Gersch's co-authors include Stephan A. Sieber, Johannes Kreuzer, David Komander, Christina Gladkova, Martin A. Michel, M. Groll, Stefan M.V. Freund, Sarah Maslen, Jane L. Wagstaff and Alexander F. Schubert and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Malte Gersch

32 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Malte Gersch Germany 18 1.1k 353 321 291 143 33 1.6k
David T. Barkan United States 12 1.4k 1.3× 206 0.6× 152 0.5× 238 0.8× 161 1.1× 16 1.9k
Remigiusz Serwa Poland 22 1.2k 1.0× 214 0.6× 212 0.7× 539 1.9× 245 1.7× 56 1.8k
I.W. McNae United Kingdom 26 1.1k 1.0× 345 1.0× 234 0.7× 371 1.3× 134 0.9× 46 1.8k
Paul D. Kirchhoff United States 23 1.1k 0.9× 171 0.5× 209 0.7× 257 0.9× 101 0.7× 39 1.7k
P. Sledz Germany 20 1.7k 1.5× 252 0.7× 172 0.5× 317 1.1× 286 2.0× 32 2.1k
A. Cousido-Siah France 23 851 0.7× 202 0.6× 256 0.8× 257 0.9× 256 1.8× 51 1.5k
Steven M. Johnson United States 24 1.2k 1.0× 335 0.9× 161 0.5× 439 1.5× 294 2.1× 49 2.0k
William P. Heal United Kingdom 20 1.0k 0.9× 189 0.5× 170 0.5× 627 2.2× 259 1.8× 24 1.7k
James C. Burnett United States 26 928 0.8× 241 0.7× 104 0.3× 427 1.5× 252 1.8× 57 1.9k
Anders Poulsen Singapore 26 1.2k 1.0× 398 1.1× 154 0.5× 399 1.4× 282 2.0× 56 2.0k

Countries citing papers authored by Malte Gersch

Since Specialization
Citations

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

Fields of papers citing papers by Malte Gersch

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Malte Gersch

This figure shows the co-authorship network connecting the top 25 collaborators of Malte Gersch. A scholar is included among the top collaborators of Malte Gersch 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 Malte Gersch. Malte Gersch 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.
Kaschani, Farnusch, et al.. (2025). Small Molecule‐Induced Alterations of Protein Polyubiquitination Revealed by Mass‐Spectrometric Ubiquitome Analysis. Angewandte Chemie International Edition. 64(32). e202508916–e202508916. 1 indexed citations
2.
Gersch, Malte, et al.. (2025). Chimeric deubiquitinase engineering reveals structural basis for specific inhibition of the mitophagy regulator USP30. Nature Structural & Molecular Biology. 32(9). 1776–1786. 2 indexed citations
3.
Cheng, Xiu‐Fen, Philipp Lampe, Stefano Ugel, et al.. (2025). Design, Synthesis, and Structural Evolution of Pseudo‐Natural Product IDO1 Inhibitors and Degraders. Angewandte Chemie International Edition. 65(3). e18753–e18753.
4.
Gersch, Malte, et al.. (2024). N‐Cyanopiperazines as Specific Covalent Inhibitors of the Deubiquitinating Enzyme UCHL1. Angewandte Chemie International Edition. 63(12). e202318849–e202318849. 6 indexed citations
5.
Fish, Alexander, et al.. (2024). Variety in the USP deubiquitinase catalytic mechanism. Life Science Alliance. 7(4). e202302533–e202302533. 14 indexed citations
6.
Bezstarosti, Karel, et al.. (2024). Discovery and mechanism of K63-linkage-directed deubiquitinase activity in USP53. Nature Chemical Biology. 21(5). 746–757. 8 indexed citations
7.
Boom, Johannes van den, et al.. (2024). Light‐Activatable Ubiquitin for Studying Linkage‐Specific Ubiquitin Chain Formation Kinetics. Advanced Science. 12(6). e2406570–e2406570. 2 indexed citations
8.
Gersch, Malte, Jane L. Wagstaff, Angela V. Toms, et al.. (2019). Distinct USP25 and USP28 Oligomerization States Regulate Deubiquitinating Activity. Molecular Cell. 74(3). 436–451.e7. 56 indexed citations
9.
Stahl, Matthias, Vadim S. Korotkov, Dóra Balogh, et al.. (2018). Selektive Aktivierung der humanen caseinolytischen Protease P (ClpP). Angewandte Chemie. 130(44). 14811–14816. 3 indexed citations
10.
Stahl, Matthias, Vadim S. Korotkov, Dóra Balogh, et al.. (2018). Selective Activation of Human Caseinolytic Protease P (ClpP). Angewandte Chemie International Edition. 57(44). 14602–14607. 47 indexed citations
11.
Gersch, Malte, Christina Gladkova, Alexander F. Schubert, et al.. (2017). Mechanism and regulation of the Lys6-selective deubiquitinase USP30. Nature Structural & Molecular Biology. 24(11). 920–930. 169 indexed citations
12.
Düwel, Stephan, Christian Hundshammer, Malte Gersch, et al.. (2017). Imaging of pH in vivo using hyperpolarized 13C-labelled zymonic acid. Nature Communications. 8(1). 15126–15126. 96 indexed citations
13.
Mevissen, Tycho E.T., Yogesh Kulathu, Monique P. C. Mulder, et al.. (2016). Molecular basis of Lys11-polyubiquitin specificity in the deubiquitinase Cezanne. Nature. 538(7625). 402–405. 117 indexed citations
14.
Gersch, Malte, Mathias W. Hackl, Christian Dubiella, et al.. (2015). A Mass Spectrometry Platform for a Streamlined Investigation of Proteasome Integrity, Posttranslational Modifications, and Inhibitor Binding. Chemistry & Biology. 22(3). 404–411. 13 indexed citations
15.
Gersch, Malte, Christoph Göbl, Imran T. Malik, et al.. (2015). AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control. Nature Communications. 6(1). 6320–6320. 106 indexed citations
16.
Wauer, Tobias, Kirby N. Swatek, Jane L. Wagstaff, et al.. (2014). Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis. The EMBO Journal. 34(3). 307–325. 241 indexed citations
17.
Dubiella, Christian, Haissi Cui, Malte Gersch, et al.. (2014). Selektive Inhibition des Immunoproteasoms durch ligandeninduzierte Vernetzung des katalytischen Zentrums. Angewandte Chemie. 126(44). 12163–12167. 20 indexed citations
18.
Gersch, Malte, Vadim S. Korotkov, Johannes Lehmann, et al.. (2013). The Mechanism of Caseinolytic Protease (ClpP) Inhibition. Angewandte Chemie International Edition. 52(10). 3009–3014. 46 indexed citations
19.
Gersch, Malte, et al.. (2012). Insights into Structural Network Responsible for Oligomerization and Activity of Bacterial Virulence Regulator Caseinolytic Protease P (ClpP) Protein. Journal of Biological Chemistry. 287(12). 9484–9494. 57 indexed citations
20.
Shen, Aimee, Patrick J. Lupardus, Malte Gersch, et al.. (2011). Defining an allosteric circuit in the cysteine protease domain of Clostridium difficile toxins. Nature Structural & Molecular Biology. 18(3). 364–371. 51 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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