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Showing 1–3 of 3 results
Advanced filters: Author: Umberto Capasso Palmiero Clear advanced filters

  • The underlying mechanism for how heterotypic protein–RNA interactions modulate the liquid to amyloid transition of hnRNPA1A, a protein involved in amyotrophic lateral sclerosis, has so far remained elusive. Now characterization of hnRNPA1A condensate formation and aggregation in vitro reveals that the RNA/protein stoichiometry affects the molecular pathways leading to amyloid formation.

    • Chiara Morelli
    • Lenka Faltova
    • Paolo Arosio
    ResearchOpen Access
    Nature Chemistry
    Volume: 16, P: 1052-1061

  • A proteome-wide thermal profiling study of osmolyte action on E. coli and human proteins within the cellular milieu reveals mechanisms of protein thermal stabilization by osmolytes and in situ behavior of intrinsically disordered proteins.

    • Monika Pepelnjak
    • Britta Velten
    • Paola Picotti
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 20, P: 1053-1065

  • Understanding of the molecular mechanisms underlying the maturation of protein condensates into amyloid fibrils associated with neurodegenerative diseases has so far remained elusive. Now it has been shown that in condensates formed by the low-complexity domain of the amyotrophic lateral sclerosis-associated protein hnRNPA1, fibril formation is promoted at the interface, which provides a potential therapeutic target for counteracting aberrant protein aggregation.

    • Miriam Linsenmeier
    • Lenka Faltova
    • Paolo Arosio
    ResearchOpen Access
    Nature Chemistry
    Volume: 15, P: 1340-1349