ZMB Member Malte Gersch

ZMB Member
Malte Gersch

Next ZMB-Member
portrait photo of ZMB member Malte Gersch
© UDE/Bettina Engel-Albustin

Prof. Dr. Malte Gersch

Group

Chemical and Structural Biology

Research Center One Health Ruhr
University Alliance Ruhr

Research Professorship for Cell Biology and Human Disease
Faculty of Biology

University of Duisburg-Essen
Universitätsstr. 2
45141 Essen

Research Overview

We are passionate about investigating molecular mechanisms within the Ubiquitin signaling system and their roles in human disease. Our goal? Transforming molecular insights into translational approaches. To this end, we employ a multidisciplinary strategy centered on chemical probes, protein biochemistry, structural biology, and cellular assays. We’re thrilled to join the Essen research community in Summer 2026—stay tuned for updates and reach out if you want to join us!

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Selected Publications

  • Hennes E, Lucas B, Scholes NS, Cheng XF, Scott DC, Bischoff M, Reich K, Gasper R, Lucas M, Xu TT, Pulvermacher LM, Dötsch L, Imrichova H, Brause A, Naredla KR, Sievers S, Kumar K, Janning P, Gersch M, Murray PJ, Schulman BA, Winter GE, Ziegler S, Waldmann H.
    Monovalent Pseudo-Natural Product Degraders Supercharge the Native Degradation of IDO1 by KLHDC3.
    In: Nat Chem. 2026 Mar;18(3):585-596
    DOI
  • Klink N, Urban S, Seier JA, Adhikari B, Schwalm MP, Müller J, Dorsch M, Kaschani F, Koch J, Führer S, Kaiser M, Schulze N, Knapp S, Wolf E, Paschen A, Grüner BM, Gersch M.
    Targeted degradation of USP7 in solid cancer cells reveals disparate effects of deubiquitinase inhibition vs. acute protein depletion.
    In: bioRxiv, 2025
    DOI
  • Führer S, Gallant K, Kaschani F, Kaiser M, Janning P, Waldmann H, Gersch M.
    Cell-type specificity of the human mutation landscape with respect to DNA replication dynamics.
    In: Angew Chem Int Ed 2025, 64 (32), e202508916
    DOI
  • Kazi NH, Klink N, Gallant K, Kipka GM, Gersch M.
    Chimeric deubiquitinase engineering reveals structural basis for specific inhibition of USP30 and a framework for DUB ligandability.
    In: Nat Struct Mol Biol 2025, 32, 1776–1786
    DOI
  • Wendrich K, Gallant K, Recknagel S, Petroulia S, Kazi NH, Hane, JA, Führer S, Bezstarosti K, O’Dea R, Demmers J, Gersch M.
    Discovery and mechanism of K63-linkage-directed deubiquitinase activity in USP53.
    In: Nat Chem Biol 2025, 21, 746–757
    DOI
  • Keijzer N, Priyanka A, Stijf-Bultsma Y, Fish A, Gersch M, Sixma TK.
    Variety in the USP deubiquitinase catalytic mechanism.
    In: Life Sci Alliance 2024, 7(4), e202302533
    DOI
  • Schmidt M, Grethe C, Recknagel S, Kipka GM, Klink N, Gersch M.
    N-Cyanopiperazines as Specific Covalent Inhibitors of the Deubiquitinating Enzyme UCHL1.
    In: Angew. Chem., Int. Ed., 2024, 63(12), e202318849
    DOI
  • Zhao Z, O'Dea R, Wendrich K, Kazi N, Gersch M.
    Native semi-synthesis of isopeptide-linked substrates for specificity analysis of deubiquitinases and Ubl proteases.
    In: J Am Chem Soc, 2023, 145(38), 20801–20812
    DOI
  • O’Dea R, Kazi N, Hoffmann-Benito A, Zhao Z, Recknagel S, Wendrich K, Janning P, Gersch M.
    Molecular basis for Ubiquitin/Fubi cross-reactivity in USP16 and USP36.
    In: Nat Chem Biol, 2023, 19(11), 1394–1405
    DOI
  • Grethe C, Schmidt M, Kipka GM, O'Dea R, Gallant K, Janning P, Gersch M.
    Structural basis for specific inhibition of the deubiquitinase UCHL1.
    In: Nat Commun, 2022, 13(1), 5950
    DOI
  • Gersch M, Wagstaff JL, Toms AV, Graves B, Freund SMV, Komander D.
    Distinct USP25 and USP28 Oligomerization States Regulate Deubiquitinating Activity.
    In: Mol Cell, 2019,74, 436–451
    DOI
  • Gersch M, Gladkova C, Schubert A, Michel M, Maslen S, Komander D.
    Mechanism and regulation of the Lys6-selective deubiquitinase USP30.
    In: Nat Struct Mol Biol, 2017, 24(11), 920–930
    DOI
  • Gersch M, Stahl M, Poreba M, Dahmen M, Dziedzic A, Drag M, Sieber SA.
    Barrel-shaped ClpP proteases display attenuated cleavage specificities.
    In: ACS Chem Biol, 2016, 19(11), 389–399
    DOI
  • Gersch M, Famulla K, Dahmen M, Goebl C, Malik I, Richter K, Korotkov VS, Sass P, Ruebsamen-Schaeff H, Madl T, Broetz-Oesterhelt H, Sieber SA.
    AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control.
    In: Nat Commun, 2015, 19(6), 6320
    DOI
  • Gersch M, Hackl M, Dubiella C, Dobrinevski A, Groll M, Sieber SA.
    A mass spectrometry platform for a streamlined investigation of proteasome integrity, posttranslational modifications, and inhibitor binding.
    In: Chem Biol, 2015, 22(3), 404–411
    DOI
  • Gersch M, Kolb R, Alte F, Groll M, Sieber SA.
    Disruption of oligomerization and dehydroalanine formation as mechanisms for ClpP protease inhibition.
    In: J Am Chem Soc, 2014, 136(4),1360–1366
    DOI
  • Gersch M, Gut F, Korotkov V, Lehmann J, Böttcher T, Rusch M, Hedberg C, Waldmann H, Klebe G, Sieber SA.
    The Mechanism of ClpP Inhibition.
    In: J Am Chem Soc, 2014, 136(4),1360–1366
    DOI
  • Gersch M, Kreuzer J, Sieber SA.
    Electrophilic natural products and their biological targets.
    In: Nat Prod Rep, 2012, 29, 659–682. (Review)
    DOI
  • Gersch M, List A, Groll M, Sieber SA.
    Insights into the structural network responsible for oligomerization and activity of the bacterial virulence regulator caseinolytic protease P (ClpP).
    In: J Biol Chem, 2012, 287(12), 9484–9494
    DOI
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