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Showing 1–9 of 9 results
Advanced filters: Author: Christian P. R. Hackenberger Clear advanced filters

  • Current photoproximity labelling methods often require metal-based catalysts to map protein interactomes but, owing to their toxicity, they have limited intracellular applicability. A deazaflavin cofactor has now been developed as a biocompatible alternative for diazirine activation inside living cells, offering accurate mapping of protein interactors and dynamics with excellent spatio-temporal control.

    • Leander B. Crocker
    • Jan Vincent V. Arafiles
    • Christian P. R. Hackenberger
    ResearchOpen Access
    Nature Chemistry
    P: 1-13

  • Our understanding of how post-translational modification—protein phosphorylation—impacts the complexity of eukaryotic signalling pathways is continuously expanding. Now, protein oligophosphorylation has been characterized as an additional phosphorylation mode. Structural and mass spectrometry methods revealed that NME1 catalysed its own oligophosphorylation, leading to altered protein–protein interactions.

    • Arif Celik
    • Felix Schöpf
    • Dorothea Fiedler
    ResearchOpen Access
    Nature Chemistry
    Volume: 17, P: 1757-1767

  • Robust delivery of proteins into cells is challenging, but it has now been shown that by conjugating arginine-rich cell-penetrating peptides to the surface of cells, proteins containing a cell-penetrating peptide can be delivered efficiently into them. Using a thiol-reactive cell-penetrating peptide enables thiol-containing proteins to be delivered by simple co-incubation.

    • Anselm F. L. Schneider
    • Marina Kithil
    • Christian P. R. Hackenberger
    Research
    Nature Chemistry
    Volume: 13, P: 530-539

  • Protein phosphorylation mediates signalling and other important cellular processes, but the specific effect of cysteine phosphorylation is unclear. Here, the authors present a chemical strategy to selectively phosphorylate cysteine residues and a mass spectrometry approach to detect and characterize endogenous pCys sites.

    • Jordi Bertran-Vicente
    • Martin Penkert
    • Christian P. R. Hackenberger
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-9

  • Delivery of antibodies into living cells enables the labelling and manipulation of intracellular antigens; however, transporting antibodies into the cytosol in a functional state is difficult. Now, a modular strategy for creating cell-permeable nanobodies capable of targeting intracellular antigens has been developed. The cell-permeable nanobodies are formed by site-specific attachment of cyclic arginine-rich cell-penetrating peptides to camelid-derived single-chain antibody fragments.

    • Henry D. Herce
    • Dominik Schumacher
    • Christian P. R. Hackenberger
    Research
    Nature Chemistry
    Volume: 9, P: 762-771

  • Meshworks of claudin polymers control the paracellular transport and barrier properties of epithelial tight junctions. Here, the authors show different claudin nanoscale organization principles, finding that claudin segregation enables barrier formation and paracellular ion flux across tight junctions.

    • Hannes Gonschior
    • Christopher Schmied
    • Martin Lehmann
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-20