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Showing 1–6 of 6 results
Advanced filters: Author: Blerida Banushi Clear advanced filters
  • Lysine hydroxylation of procollagen precursors by LH3 is required for collagen fibril crosslinking and stabilization. Here the authors show that the trafficking protein VIPAR is required for correct sorting of LH3 into post-Golgi collagen carriers and for correct collagen modification and structure.

    • Blerida Banushi
    • Federico Forneris
    • Paul Gissen
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-14
  • In this Review, Banushi et al. discuss how endocytotic pathways impact many cancer processes including nutrient scavenging, metastasis and therapeutic drug delivery, and how knowledge of these pathways can be used to improve cancer therapy in the clinic.

    • Blerida Banushi
    • Shannon R. Joseph
    • Fiona Simpson
    Reviews
    Nature Reviews Cancer
    Volume: 23, P: 450-473
  • Patients with mutations in the ASL gene present with argininosuccinic aciduria characterised by hyperammonaemia and cognitive impairment. Here, the authors show that cerebral disease involves neuronal nitrosative/oxidative stress that is not induced by hyperammonaemia, and that it can be reversed using AAV-ASL directed to liver and brain in mice.

    • Julien Baruteau
    • Dany P. Perocheau
    • Simon N. Waddington
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-14
  • Lysyl hydroxylase 3 (LH3) catalyzes collagen lysine hydroxylation and their subsequent O-linked glycosylation. Here the authors provide mechanistic insights into the lysyl hydroxylase and glycosyltransferase activities of LH3 by determining the crystal structures of full-length human LH3 bound to cofactors and donor substrates.

    • Luigi Scietti
    • Antonella Chiapparino
    • Federico Forneris
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-11
  • How toxic aggregated forms of α-synuclein lead to neurodegeneration is unclear. Here authors use biophysical and cellular imaging methods to show that specific oligomers of α-synuclein exert effects on mitochondria to induce opening of the permeability transition pore, leading to cell death in Parkinson’s disease.

    • Marthe H. R. Ludtmann
    • Plamena R. Angelova
    • Sonia Gandhi
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-16