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Showing 1–17 of 17 results
Advanced filters: Author: Ivo A. Hendriks Clear advanced filters

  • Tryptic digestion of SUMOylated proteins generates large peptides, rendering proteomic characterisation of this post-translational modification particularly challenging unless mutant SUMO is used. Hendriks et al.present a method that allows the quantitative identification of wild-type SUMO sites.

    • Ivo A. Hendriks
    • Rochelle C. D’Souza
    • Alfred C. O. Vertegaal
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-16

  • The authors uncover the roles and regulations of DNA polymerase κ (Polκ) during DNA damage bypass. In addition to a catalytic function across minor groove DNA lesions, Polκ stimulates Polζ-mediated extension past various DNA lesions.

    • Selene Sellés-Baiget
    • Sara M. Ambjørn
    • Julien P. Duxin
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 300-314

  • The authors identify a DNA-protein crosslink (DPC) repair pathway orchestrated by poly-ADP-ribosylation. In this process, PARP1 PARylates the DPC, marking it for removal by proteolysis. Consequently, PARP1 facilitates the repair of DPCs located next to DNA breaks, such as topoisomerase 1-DPCs.

    • Zita Fábián
    • Ellen S. Kakulidis
    • Julien P. Duxin
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-18

  • ADP-ribosylation is regulated by HPF1 and ARH3, but the cellular target spectrum of these enzymes is not fully understood. Here, the authors use quantitative proteomics to define the HPF1- and ARH3-dependent ADP-ribosylome, providing evidence that mono-ADP-ribosylation of serine predominates in cells.

    • Ivo A. Hendriks
    • Sara C. Buch-Larsen
    • Michael L. Nielsen
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-16

  • Zorya uses a membrane-anchored H+-driven rotary motor ZorAB to sense phage invasion and to recruit the intracellular effectors ZorC and ZorD that execute anti-phage defence.

    • Haidai Hu
    • Philipp F. Popp
    • Nicholas M. I. Taylor
    ResearchOpen Access
    Nature
    Volume: 639, P: 1093-1101

  • Liu et al. reveal that human TOPORS is a SUMO1-selective SUMO-targeted ubiquitin ligase (STUbL). The parallel action of TOPORS and the STUbL RNF4 defines a general mechanistic principle governing pathways driven by direct SUMO–ubiquitin crosstalk.

    • Julio C. Y. Liu
    • Leena Ackermann
    • Niels Mailand
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 31, P: 1355-1367

  • p97/VCP, a nexus of the ubiquitin system, recognizes and unfolds ubiquitylated substrates via multiple cofactors. Here, the authors identify VCF1, a nuclear cofactor promoting p97 recruitment to, and proteasomal degradation of, ubiquitylated targets.

    • Ann Schirin Mirsanaye
    • Saskia Hoffmann
    • Niels Mailand
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-16

  • Here the authors leverage state-of-the-art quantitative proteomics to provide a comprehensive overview of the human citrullinome. Supporting evidence from peptide microarrays hints at the potential clinical relevance of some of the identified sites.

    • Alexandra S. Rebak
    • Ivo A. Hendriks
    • Michael L. Nielsen
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 31, P: 977-995

  • Using Xenopus egg extracts, the authors developed a mass spectrometry method (UBIMAX) to identify proteins ubiquitylated in response to defined DNA lesions. Highlighting UBIMAX’s versatility, they describe the ubiquitylation of the actin regulator Dbn1 in response to DNA double-strand breaks.

    • Camilla S. Colding-Christensen
    • Ellen S. Kakulidis
    • Michael L. Nielsen
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-19

  • Hertz et al. use CRISPR screening to identify genetic vulnerabilities to inhibition of SUMOylation in human cells. They show that SUMO exerts its essential role in cell proliferation via NIP45- and BTRR-PICH-mediated DNA catenane resolution pathways.

    • Emil P. T. Hertz
    • Ignacio Alonso-de Vega
    • Niels Mailand
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 30, P: 1303-1313

  • Proteomics is a powerful method to study protein SUMOylation, but system-wide insights into endogenous SUMO2/3 modification events are still sparse. Here, the authors develop a more sensitive SUMO proteomics approach, providing detailed maps of endogenous SUMO2/3 sites in human cells and mouse tissues.

    • Ivo A. Hendriks
    • David Lyon
    • Michael L. Nielsen
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-17

  • Analysis of the available human small ubiquitin-like modifier (SUMO) proteomics data provided evidence for the sumoylation of thousands of proteins and residues, and clustered the sumoylated proteins into functional networks. Sumoylation is a frequent modification, occurring mostly on nuclear proteins, with functions including transcription, mRNA processing and the DNA-damage response.

    • Ivo A. Hendriks
    • Alfred C. O. Vertegaal
    Research
    Nature Reviews Molecular Cell Biology
    Volume: 17, P: 581-595

  • High-resolution MS identifies >4,300 SUMOylation sites in >1,600 proteins in human cells under standard growth conditions and after proteasome inhibition or heat shock. The data reveal cross-talk between SUMO and other post-translational modifications.

    • Ivo A Hendriks
    • Rochelle C J D'Souza
    • Alfred C O Vertegaal
    Research
    Nature Structural & Molecular Biology
    Volume: 21, P: 927-936

  • A comprehensive analysis of the human SUMO proteome, in HeLa and U2OS cell lines and under different conditions, identifies new SUMOylated sites and reveals cross-talk between SUMO and other post-translational modifications, such as phosphorylation.

    • Ivo A Hendriks
    • David Lyon
    • Michael L Nielsen
    Research
    Nature Structural & Molecular Biology
    Volume: 24, P: 325-336