Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–6 of 6 results
Advanced filters: Author: Henry D. Herce Clear advanced filters
  • Screens for protein–protein interactions and for drugs that disrupt them typically use in vitro assays which fail to capture the complexity of the cell’s interior. By fixing proteins to distinct cellular locations, Herce et al.demonstrate a fluorescent-three-hybrid approach to probe such interactions in their cellular contexts.

    • Henry D. Herce
    • Wen Deng
    • M. Cristina Cardoso
    ResearchOpen Access
    Nature Communications
    Volume: 4, P: 1-8
  • Cell-penetrating peptides can deliver molecular cargoes into living cells, and cross biological membranes by transduction—a non-endocytic mechanism. Here, the transduction efficiency of cyclic arginine-rich peptides is shown to be higher than that of more flexible linear peptides.

    • Gisela Lättig-Tünnemann
    • Manuel Prinz
    • M. Cristina Cardoso
    ResearchOpen Access
    Nature Communications
    Volume: 2, P: 1-6
  • 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
  • Prew et al. uncovered a structural basis for human VLCAD deficiency that arises from point mutations within the enzyme’s membrane-binding region, which was shown to fold as a putative α-helical hairpin. Helix-breaking mutations selectively disrupt membrane interaction and thus homeostatic function.

    • Michelle S. Prew
    • Christina M. Camara
    • Loren D. Walensky
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-12