Advanced search

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 1–13 of 13 results
Advanced filters: Author: Geert van den Bogaart Clear advanced filters

  • Mutations in genes critical for proper intra-Golgi transport can cause human syndromes due to defects in glycosylation of proteins. Here, the authors identify a human variant of Syntaxin-5 that causes fatal multisystem disease and mislocalization of glycosyltransferases due to altered Golgi transport.

    • Peter T. A. Linders
    • Eveline C. F. Gerretsen
    • Geert van den Bogaart
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-15

  • Interactions between synaptotagmin-1 and the SNARE syntaxin-1 are known to mediate synaptic-vesicle exocytosis. Fusion experiments with artificial lipid membranes combined with the crystal structure of synaptotagmin's C2B domain bound to phosphoserine indicate that PIP2 clusters, organized by syntaxin, act as molecular beacons for vesicle docking and direct Ca2+-dependent membrane fusion.

    • Alf Honigmann
    • Geert van den Bogaart
    • Reinhard Jahn
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 679-686

  • The intracellular localization of the karyopherin KAP104 determines where dissociation of the mRNA binding proteins Nab2 and Nab4 from translation competent mRNAs takes place, thus controlling local protein synthesis.

    • Geert van den Bogaart
    • Anne C. Meinema
    • Bert Poolman
    Research
    Nature Cell Biology
    Volume: 11, P: 350-356

  • Cholesterol efflux is mediated by specific transporters in T cells. Here the authors show that when the ABCA1/ABCG1 cholesterol transporters are absent, peripheral T cell numbers are reduced but activation increased with a premature aging phenotype of T cell senescence and apoptosis in middle aged Ldlr−/− mice.

    • Venetia Bazioti
    • Anouk M. La Rose
    • Marit Westerterp
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-23

  • Synaptotagmin promotes SNARE-mediated membrane fusion in a Ca2+-dependent manner, but the mechanism by which it acts is still unclear. In vitro studies have shown that synaptotagmin can make interactions with its own vesicle membrane, inhibiting its ability to stimulate fusion with target membranes. New data now suggest that ATP and other polybasic anions may have a role in directing synaptotagmin to its target membrane in vivo.

    • Yongsoo Park
    • Javier M Hernandez
    • Reinhard Jahn
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 991-997

  • Synaptotagmin-1 is known to accelerate membrane fusion during neuronal exocytosis in response to Ca2+, but how it does this is unclear. By probing the activity of synaptotagmin-1 under conditions of low ionic strength, it is now shown that SNARE-mediated fusion is dependent on synaptotagmin-1, which tethers liposomes together but at distances too far for fusion. Ca2+ then induces synaptotagmin-1 to bring the liposomes closer together, allowing fusion to proceed.

    • Geert van den Bogaart
    • Shashi Thutupalli
    • Reinhard Jahn
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 805-812

  • Most intracellular membrane fusion reactions in eukaryotes are mediated by SNARE proteins present in both fusing membranes. It has been unclear how many SNARE complexes are needed for fusion. FRET studies now show that liposomes with a single SNARE molecule are able to fuse with other liposomes or with purified synaptic vesicles.

    • Geert van den Bogaart
    • Matthew G Holt
    • Reinhard Jahn
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 358-364

  • Clustering of proteins in the plasma membrane plays an important role in the regulation of both cellular signalling and membrane remodelling. Milovanovic et al.demonstrate that mismatch between transmembrane domain length and the lipid bilayer thickness is sufficient to drive clustering of SNARE proteins.

    • Dragomir Milovanovic
    • Alf Honigmann
    • Reinhard Jahn
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-10