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Showing 1–12 of 12 results
Advanced filters: Author: Malte Gersch Clear advanced filters

  • In targeted protein degradation, a degrader molecule brings a neosubstrate protein proximal to a hijacked E3 ligase for its ubiquitination. Here, pseudo-natural products derived from (−)-myrtanol—iDegs—are identified to inhibit and induce degradation of the immunomodulatory enzyme indoleamine-2,3-dioxygenase 1 (IDO1) by a distinct mechanism. iDegs prime apo-IDO1 ubiquitination and subsequent degradation using its native proteolytic pathway.

    • Elisabeth Hennes
    • Belén Lucas
    • Herbert Waldmann
    ResearchOpen Access
    Nature Chemistry
    P: 1-12

  • Acyldepsipeptides are natural antibiotics that function by activating the ClpP protease and deregulating proteolysis. Here, Gersch et al.show that acyldepsipeptides not only increase access to the active sites but also exert conformational control, thereby allosterically stimulating ClpP catalysis.

    • Malte Gersch
    • Kirsten Famulla
    • Stephan A. Sieber
    Research
    Nature Communications
    Volume: 6, P: 1-12

  • Kazi et al. report the crystal structure of the mitochondrial deubiquitinase USP30, a clinical stage Parkinson’s disease drug target, in complex with a specific inhibitor. The authors delineate a framework for specific deubiquitinase inhibition.

    • Nafizul Haque Kazi
    • Nikolas Klink
    • Malte Gersch
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 1776-1786

  • MARUbylation is a hybrid post-translational protein modification in which mono-ADP-ribosylation acts as a scaffold for sequential mono- and polyubiquitylation. Recent studies illuminate its substrates, molecular recognition, and emerging roles in DNA repair.

    • Katarzyna W. Kliza
    • Malte Gersch
    News & Views
    Nature Chemical Biology
    Volume: 21, P: 1648-1649

  • A probe for the ubiquitin-like protein Fubi led to the discovery of dual ubiquitin/Fubi C-terminal hydrolase activity in the deubiquitinase USP16 in addition to USP36, enabling structural characterization of this distinctive Ub/Ubl specificity, and revealed a synergistic role of USP16 in ribosomal protein maturation.

    • Rachel O’Dea
    • Nafizul Kazi
    • Malte Gersch
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 19, P: 1394-1405

  • The deubiquitinase UCHL1 has been linked to cancer invasiveness and neurodegeneration yet its molecular roles have remained poorly defined. Here the authors reveal the structural basis for how UCHL1 can be specifically inhibited and how chemogenomic probes can be used to dissect its functions in living cells.

    • Christian Grethe
    • Mirko Schmidt
    • Malte Gersch
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-17

  • Wendrich, Gallant and colleagues find that USP53 and USP54 are active deubiquitinases, with USP53 removing ubiquitin chains from substrate proteins in a chain-linkage-directed manner, and provide biochemical and structural insights into their mechanism, cellular substrates and disease implications.

    • Kim Wendrich
    • Kai Gallant
    • Malte Gersch
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 21, P: 746-757

  • Local pH alterations can be manifestations of pathologies such as cancer, inflammation and ischaemia. Here Düwelet al. show hyperpolarized 13C-labelled zymonic acid can be used as a non-invasive probe to map and measure pH in vivo, suggesting it as a candidate for clinical imaging and a diagnostic tool.

    • Stephan Düwel
    • Christian Hundshammer
    • Franz Schilling
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-9

  • Structural and biochemical analyses of human USP30 explain the basis of Lys6-linkage preference and regulation by PINK1 and Parkin, shedding light onto how USP30 can act as a brake on mitophagy.

    • Malte Gersch
    • Christina Gladkova
    • David Komander
    Research
    Nature Structural & Molecular Biology
    Volume: 24, P: 920-930

  • Small molecules are identified that inhibit the ubiquitin-specific protease USP7 with high affinity and specificity as explained by co-crystal structures, and are shown to reduce tumour growth in mice.

    • Andrew P. Turnbull
    • Stephanos Ioannidis
    • David Komander
    Research
    Nature
    Volume: 550, P: 481-486

  • Knowledge of the molecular mechanisms of activation of Clostridium difficile toxins will significantly enhance the ability to design specific anti-virulence therapies. Using activity-based chemical probes in combination with other techniques, this study reveals mechanistic insights into how inositol hexakisphosphate binding at the active site of the cysteine protease domain shifts the conformational equilibrium towards an active conformer.

    • Aimee Shen
    • Patrick J Lupardus
    • Matthew Bogyo
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 364-371