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Showing 1–10 of 10 results
Advanced filters: Author: Emma Sierecki Clear advanced filters

  • Single-molecule in vitro assays require dedicated confocal microscopes equipped with fluorescence correlation spectroscopy (FCS) modules. Here the authors present a compact, cheap and open-source 3D-printed confocal microscope for single photon counting and FCS measurements, and use it to detect α-synuclein aggregation.

    • James W. P. Brown
    • Arnaud Bauer
    • Yann Gambin
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-7

  • Here the authors show that a gene-inactivating protein complex packs inactive genes into a dynamic and accessible structure. The study challenges the traditional views that restricted accessibility and low dynamics cause gene repression.

    • Michael Uckelmann
    • Vita Levina
    • Chen Davidovich
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 520-530

  • During SARS-CoV-2 replication, viral and cellular proteases play crucial roles and have been shown to be promising anti-viral targets. Here, Meyer et al. apply mass spectrometry to characterize the proteolytic cleavage profile of viral and cellular proteins in vitro.

    • Bjoern Meyer
    • Jeanne Chiaravalli
    • Edward Emmott
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-16

  • Macrophage-expressed gene 1 (MPEG1) functions within the phagolysosome to damage engulfed microbes, presumably via forming pores in target membranes. In order to provide insights into the mechanism of MPEG1 function and membrane binding, the authors present structures of hexadecameric MPEG1 prepores both in solution and in complex with liposomes.

    • Siew Siew Pang
    • Charles Bayly-Jones
    • James C. Whisstock
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-9

  • MAL and MyD88 are downstream adaptors of Toll-like receptors (TLR) and the MAL TIR domain forms filaments in vitro, which in turn nucleate the assembly of crystalline arrays of the MyD88 TIR domain. Here, the authors present the structure of these MyD88 TIR crystalline arrays solved by both microcrystal electron diffraction and serial femtosecond crystallography, and they show with mutagenesis experiments that MyD88 interface residues are important for TLR4 signaling in vivo.

    • Max T. B. Clabbers
    • Susannah Holmes
    • Thomas Ve
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-14

  • Caveolae are plasma membrane invaginations containing cavin proteins that are disrupted upon stress stimuli, causing cavin release inside the cell. Here, McMahon et al. identify cavin interacting proteins using proteomic analyses and reveal functions in stress signaling that can promote apoptosis.

    • Kerrie-Ann McMahon
    • Yeping Wu
    • Robert G. Parton
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-17

  • Structural insight into TIR-domain interactions, which are essential for the recruitment of signaling adapters to Toll-like receptors during innate immune responses, demonstrates a conserved interaction mode involved in both TLR and IL-1R signaling.

    • Thomas Ve
    • Parimala R Vajjhala
    • Bostjan Kobe
    Research
    Nature Structural & Molecular Biology
    Volume: 24, P: 743-751

  • To better understand the specific cascade of protein interactions that lead to the pathological aggregation of α-synuclein (wild-type and mutant forms), Leitão et al. present a method to measure interactions of monomeric, oligomeric, and fibrillar forms of α-syn with 65 proteins that were previously shown to be components of Lewy bodies. This approach is useful to understand the sequence of protein-binding events that lead to α-syn aggregation.

    • André D. G. Leitão
    • Paulina Rudolffi-Soto
    • Emma Sierecki
    ResearchOpen Access
    Communications Biology
    Volume: 4, P: 1-16