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Showing 1–9 of 9 results
Advanced filters: Author: Andrea Sottini Clear advanced filters

  • The interaction between the polyelectrolytic IDP ProTα and a highly charged folded protein domain is investigated by integrating NMR, single-molecule FRET and MD simulations. Net charge and charge distribution are implicated in binding and selectivity.

    • Katrine Bugge
    • Andrea Sottini
    • Birthe B. Kragelund
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-18

  • Studies on protein–protein interactions using proteins containing d- or l-amino acids show that stereoselectivity of binding varies with the degree of disorder within the complex.

    • Estella A. Newcombe
    • Amanda D. Due
    • Birthe B. Kragelund
    ResearchOpen Access
    Nature
    Volume: 636, P: 762-768

  • Histone H1 binds to nucleosomes with ultrahigh affinity, implying residence times incompatible with efficient biological regulation. Now it has been shown that the disordered regions of H1 retain their large-amplitude dynamics on the nucleosome, which enables a charged disordered histone chaperone to invade the H1–nucleosome complex and vastly accelerate H1 dissociation.

    • Pétur O. Heidarsson
    • Davide Mercadante
    • Benjamin Schuler
    Research
    Nature Chemistry
    Volume: 14, P: 224-231

  • Transcriptomic, proteomic and immune repertoire profiling reveals distinct peripheral features of MIS-C and pediatric COVID-19, including elevated soluble spike protein levels, more pronounced type II IFN-dependent gene expression and a higher B cell mutation rate in patients with MIS-C.

    • Keith Sacco
    • Riccardo Castagnoli
    • Luigi D. Notarangelo
    Research
    Nature Medicine
    Volume: 28, P: 1050-1062

  • A high-affinity complex of histone H1 and prothymosin-α reveals an unexpected interaction mechanism, where the large opposite net charge enables the two proteins to remain highly disordered even in the complex.

    • Alessandro Borgia
    • Madeleine B. Borgia
    • Benjamin Schuler
    Research
    Nature
    Volume: 555, P: 61-66

  • Two highly charged disordered human proteins phase-separate into viscous complex coacervates while retaining their rapid conformational dynamics through pico- to nanosecond exchange of short-lived side-chain interactions.

    • Nicola Galvanetto
    • Miloš T. Ivanović
    • Benjamin Schuler
    Research
    Nature
    Volume: 619, P: 876-883

  • The intrinsically disordered linker histone H1.0 and prothymosin α form a complex which exhibits slow exchange between bound and unbound populations at low protein concentrations and fast exchange at high concentrations. Here authors explain this observation by the formation of transient ternary complexes favored at high protein concentrations that accelerate the exchange.

    • Andrea Sottini
    • Alessandro Borgia
    • Benjamin Schuler
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-14

  • Droplet-based microfluidics enable rapid mixing with millisecond dead times and allow single-molecule measurements of non-equilibrium binding kinetics on even challenging, strongly adsorptive samples, such as intrinsically disordered proteins.

    • Tianjin Yang
    • Karin J. Buholzer
    • Benjamin Schuler
    Research
    Nature Methods
    Volume: 20, P: 1479-1482