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Showing 1–4 of 4 results
Advanced filters: Author: Melisa Merdanovic Clear advanced filters

  • Prokaryotic DegP functions as an ATPase-independent protease chaperone complex that is activated by oligomerization. Site-directed mutagenesis, combined with refolding and oligomerization studies of chemically denatured DegP, shows how substrates trigger the conversion of the resting conformation into the active conformation.

    • Melisa Merdanovic
    • Nicolette Mamant
    • Michael Ehrmann
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 837-843

  • The pathophysiology of Amyloid light-chain (AL) amyloidosis remains poorly understood due to the lack of reliable in vivo models. Here, the authors describe a transgenic mouse model that reproduces cardiac AL amyloidosis and provides new information on the formation of AL amyloid fibrils.

    • Gemma Martinez-Rivas
    • Maria Victoria Ayala
    • Christophe Sirac
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-16

  • Rare mutations in the high requirement temperature protein A1 (HTRA1) cause cerebral vasculopathy. Here, authors establish mechanistically distinct protein repair approaches to reverse the deleterious effects of pathogenic mutations interfering with the assembly and protease function of HTRA1.

    • Nathalie Beaufort
    • Linda Ingendahl
    • Martin Dichgans
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-18

  • Current strategies for protein encapsulation in DNA vessels for controlled enzymatic catalysis or therapeutic delivery rely on formation of covalent complexes. Here, the authors design a system that mimics natural reversible non-covalent host–guest interactions between a DNA host and the protein DegP.

    • Andreas Sprengel
    • Pascal Lill
    • Barbara Saccà
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-12