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Showing 1–15 of 15 results
Advanced filters: Author: Carsten Sachse Clear advanced filters

  • Selective autophagy helps to degrade aggregated proteins accumulating in neurodegenerative diseases. Here, the authors show that NEMO, a ubiquitin binding protein previously linked to innate immune signaling, is recruited to misfolded proteins and promotes their autophagic clearance by forming condensates with the autophagy receptor p62.

    • Nikolas Furthmann
    • Verian Bader
    • Konstanze F. Winklhofer
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-24

  • A cryogenic scanning transmission electron microscopy (STEM) approach for analyzing thick biological specimens expands the reach of cryo-electron microscopy.

    • Carsten Sachse
    News & Views
    Nature Methods
    Volume: 22, P: 2015-2016

  • In this work, the authors determined the cryo-EM structures of autophagy-related protein 18 organized in helical tubes and provide insights into the molecular framework for the positioning of downstream components of the autophagy machinery.

    • Daniel Mann
    • Simon A. Fromm
    • Carsten Sachse
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-13

  • The authors present structures of endosomal sorting complexes required for transport III family member vesicle-inducing protein in plastids 1, ranging from helical assemblies and stacked rings to flat carpets, providing insights into transitions dependent on membrane tubulation and curvature needed for forming different architectures involved in membrane remodeling.

    • Benedikt Junglas
    • David Kartte
    • Carsten Sachse
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 555-570

  • Using cryo-EM, the authors revealed structures of ESCRT-III superfamily member PspA and the molecular basis of structural plasticity that enables assembly modulations by the addition of nucleotides and targeted mutations.

    • Benedikt Junglas
    • Esther Hudina
    • Carsten Sachse
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 23-34

  • This paper explores the use of scanning transmission electron microscopy (STEM) to vitrified biological samples for biomolecular structure elucidation. Integrated differential phase contrast (iDPC)–STEM imaging of keyhole limpet hemocyanin and tobacco mosaic virus enabled cryo-EM structure determination at 6.5 and 3.5 Å resolution, respectively.

    • Ivan Lazić
    • Maarten Wirix
    • Carsten Sachse
    ResearchOpen Access
    Nature Methods
    Volume: 19, P: 1126-1136

  • RNA polymerase III (Pol III), the largest eukaryote polymerase yet characterized, transcribes structured small non-coding RNAs; here cryo-electron microscopy structures of budding yeast Pol III allow building of an atomic-level model of the complete 17-subunit complex, both unbound and while elongating RNA.

    • Niklas A. Hoffmann
    • Arjen J. Jakobi
    • Christoph W. Müller
    Research
    Nature
    Volume: 528, P: 231-236

  • In eukaryotes, dynamins and dynamin-like proteins (DLPs) are involved in various membrane remodeling processes. Here, the authors present the structure and functional characterization of a DLP of the cyanobacterium Synechocystis sp. PCC 6803.

    • Lucas Gewehr
    • Benedikt Junglas
    • Dirk Schneider
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-17

  • 4D-scanning transmission electron microscopy uses diffractive imaging for structural studies. Here, authors study single particle cryo-EM protein samples at up to 5.8 Å resolution, using 4D-STEM and ptychography data processing.

    • Berk Küçükoğlu
    • Inayathulla Mohammed
    • Henning Stahlberg
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-10

  • PB1-mediated oligomerization of p62/SQSTM1 is essential for its function as a selective autophagy receptor. Here the authors present the cryo-EM structures of human and Arabidopsis PB1 domain helical assemblies and find that a conserved double arginine finger in the PB1 domain is important for p62 polymerisation and lysosomal targeting of p62.

    • Arjen J. Jakobi
    • Stefan T. Huber
    • Carsten Sachse
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-15

  • A hybrid cryo-electron microscopy/tomography approach is used to solve the structure of the immature Mason–Pfizer monkey virus Gag lattice at a resolution of 8 Å, allowing the derivation of a model for the structure of retroviral capsid in the immature Gag shell.

    • Tanmay A. M. Bharat
    • Norman E. Davey
    • John A. G. Briggs
    Research
    Nature
    Volume: 487, P: 385-389

  • Binding of bacterial peptidoglycan muramyl dipeptides induces NOD2 activation and signalling via the downstream adaptor kinase RIP2. Here the authors show that RIP2 forms filaments via its CARD domain, analyse the structure of the CARD filaments and demonstrate the requirement of RIP2 polymerisation for the activation of NF-κB by NOD2.

    • Erika Pellegrini
    • Ambroise Desfosses
    • Stephen Cusack
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-19

  • Schiebel and colleagues use in vitro techniques and yeast genetics to study the role of GTP binding in the microtubule nucleation activity of γ-tubulin.

    • Linda Gombos
    • Annett Neuner
    • Elmar Schiebel
    Research
    Nature Cell Biology
    Volume: 15, P: 1317-1327

  • Structures of actin-like ParM filaments at near-atomic resolution and their arrangements into doublets reveal how subunits and filaments come together to segregate low-copy-number plasmid R1 in Escherichia coli, producing the simplest known mitotic machinery.

    • Tanmay A. M. Bharat
    • Garib N. Murshudov
    • Jan Löwe
    Research
    Nature
    Volume: 523, P: 106-110