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Showing 1–9 of 9 results
Advanced filters: Author: Raphael Gasper Clear advanced filters

  • New methods for targeted covalent protein modification at low reactivity aspartates and glutamates are of high interest. Here, the authors report a technique inspired by the HaloTag technology, which employs a covalent conjugation reaction between ligands with a reactive chloroalkane linker and a specific aspartic acid, and use it to covalently modify lipoprotein chaperone PDEδ at a binding site glutamic acid.

    • Ruirui Zhang
    • Jie Liu
    • Herbert Waldmann
    ResearchOpen Access
    Nature Communications
    Volume: 17, P: 1-18

  • 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
    Volume: 18, P: 585-596

  • The dysregulation of the inositol-requiring enzyme 1 alpha (IRE1α) has been associated with multiple human diseases, so IRE1α-targeting small molecules present great therapeutic potential. Here, the authors report a series of substituted indoles as IRE1α inhibitors of good potency and selectivity, and show that the inhibitor IA107 allosterically inhibits IRE1α RNase activity via binding to the IRE1α kinase domain but without inhibiting the IRE1α dimerization.

    • Yang Liu
    • Amrutha K. Avathan Veettil
    • Peng Wu
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • Targeting the interaction between transcription factor TEAD and its co-repressor VGL4 is an attractive strategy to chemically modulate Hippo signaling. Here, the authors develop a proteomimetic with stabilized tertiary structure that inhibits the TEAD:VGL4 interaction in vitro and in cells.

    • Hélène Adihou
    • Ranganath Gopalakrishnan
    • Herbert Waldmann
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-10

  • Bacteriorhodopsin (bR) is a light-driven proton pump. Here the authors combine time-resolved crystallography at a free-electron laser, ultrafast spectroscopy and quantum chemistry to study the structural changes following multiphoton photoexcitation of bR and find that they occur within 300 fs not only in the light-absorbing chromophore but also in the surrounding protein.

    • Gabriela Nass Kovacs
    • Jacques-Philippe Colletier
    • Ilme Schlichting
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-17

  • Guanine nucleotide-binding (G) proteins are regulated by GTPase-activating proteins and guanine nucleotide-exchange factors. Another class of G proteins is emerging that are regulated by homodimerization. The authors propose that juxtaposition of the G domains of two monomers across the GTP-binding sites activates the biological function of these proteins and the GTPase reaction.

    • Raphael Gasper
    • Simon Meyer
    • Alfred Wittinghofer
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 10, P: 423-429

  • Dipali Mhaindarkar et al. examine the functional effects of a salt bridge loss in the active site of glycosyl hydrolase Bg1M-G1, found in the metagenome of a seasonally cold marine habitat. They show that the catalytic efficiency is overall higher with the lost salt bridge, trading off with lower thermal stability.

    • Dipali Mhaindarkar
    • Raphael Gasper
    • Lars I. Leichert
    ResearchOpen Access
    Communications Biology
    Volume: 1, P: 1-11