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  • Periodicals (Báo – Tạp chí)

  • Altered structure and dynamics of pathogenic cytochrome c variants correlate with increased apoptotic activity

    • Authors : Fellner, Matthias (2020)

  • Mutation of cytochrome c in humans causes mild autosomal dominant thrombocytopenia. The role of cytochrome c in platelet formation, and molecular mechanism underlying the association of cytochrome c mutations with thrombocytopenia remains unknown, although a gain-of-function is most likely. Cytochrome c contributes to several cellular processes, with exchange between conformational states proposed to regulate changes in function. Here we use experimental and computational a...
  • Journal article

  • Lanthanide-dependent alcohol dehydrogenases require an essential aspartate residue for metal coordination and function

    • Authors : Good, Nathan M; Fellner, Matthias; Demirer, Kemal (2020)

  • The presence of lanthanide elements (Ln3+) and pyrroloquinoline quinone (PQQ) containing cofactors in XoxF methanol dehydrogenases (MDHs) and ExaF ethanol dehydrogenases (EDHs) has expanded the list of biological elements and opened novel areas of metabolism and ecology. Other MDHs known as MxaFIs are related in sequence and structure to these proteins, yet they instead possess a Ca2+-PQQ cofactor. An important missing piece of the Ln3+ puzzle is definin...
  • Journal article

  • Structural basis for active-site probes targeting Staphylococcus aureus serine hydrolase virulence factors

    • Authors : Fellner, Matthias; Lentz, Christian S; Jamieson, Sam A (2020)

  • Staphylococcus aureus is a major cause of infection in the community and in hospitals. Serine hydrolases play key roles in bacterial homeostasis, in particular biofilms. Activity-based profiling has previously identified a family of serine hydrolases, designated fluorophosphonate-binding hydrolases (Fphs), which contribute to virulence of S. aureus in the biofilm niche. Here we report structures of the putative tributyrin esterase FphF, alone and covalently bound by&#x...