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Showing 1–17 of 17 results
Advanced filters: Author: Jean-Paul Armache Clear advanced filters

  • Cryo-electron microscopy and biochemical studies elucidate the read–write mechanisms of non-canonical PRC1-containing RYBP in histone H2A lysine 119 monoubiquitination and their roles in maintaining epigenetic inheritance.

    • Victoria Godínez López
    • Marco Igor Valencia-Sánchez
    • Karim-Jean Armache
    Research
    Nature
    Volume: 636, P: 755-761

  • Previous studies argued that nascent polypeptide chains can form secondary structure in the ribosome exit tunnel despite spatial constraints. Using single-particle cryo-EM reconstructions of eukaryotic ribosomes carrying nascent chains with high helical propensity, density consistent with helix formation is now observed in the exit tunnel as are interactions with tunnel proteins.

    • Shashi Bhushan
    • Marco Gartmann
    • Roland Beckmann
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 313-317

  • Nodelman, Folkwein et al. define a regulatory region in Chd1 containing adjacent inhibitor and activator elements that compete for binding to the remodeler ATPase. The competition between these elements shows how remodeler regulation is integrated into the nucleosome sliding cycle.

    • Ilana M. Nodelman
    • Heather J. Folkwein
    • Gregory D. Bowman
    Research
    Nature Structural & Molecular Biology
    Volume: 32, P: 1445-1455

  • High-resolution cryo-EM density maps are used to present the structures of Drosophila and human 80S ribosomes in complex with eEF2, E-site transfer RNA and Stm1-like proteins, and reveal the presence of two additional structural layers in the ribosomes of metazoan eukaryotes.

    • Andreas M. Anger
    • Jean-Paul Armache
    • Roland Beckmann
    Research
    Nature
    Volume: 497, P: 80-85

  • The high-resolution electron cryo-microscopy structure of the full-length human TRPA1 ion channel is presented; the structure reveals a unique ankyrin repeat domain arrangement, a tetrameric coiled-coil in the centre of the channel that acts as a binding site for inositol hexakisphosphate, an outer poor domain with two pore helices, and a new drug binding site, findings that collectively provide mechanistic insight into TRPA1 regulation.

    • Candice E. Paulsen
    • Jean-Paul Armache
    • David Julius
    Research
    Nature
    Volume: 520, P: 511-517

  • Nucleosome-protein complexes stick to the air-water interface and denature upon plunge freezing for cryoEM. Here, authors Chio and Palovcak et al. develop EM grids that protect such complexes and use these grids to study the ATP-dependent chromatin remodeler SNF2h.

    • Un Seng Chio
    • Eugene Palovcak
    • Yifan Cheng
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-12

  • A cryo-electron microscopy structure of fungal mitochondrial calcium uniporter shows that the channel is tetrameric and sheds light on channel assembly and function.

    • Nam X. Nguyen
    • Jean-Paul Armache
    • Youxing Jiang
    Research
    Nature
    Volume: 559, P: 570-574

  • The authors solve the cryo-EM structure of nucleotide-free Chd1 bound to a nucleosome to dissect how Chd1 shifts DNA onto the histone core, and also report that recognition of the acidic patch by Chd1 blocks action of competing chromatin remodelers.

    • Ilana M. Nodelman
    • Sayan Das
    • Jean-Paul Armache
    Research
    Nature Structural & Molecular Biology
    Volume: 29, P: 121-129

  • Cryo-EM maps of different clathrin cage architectures and accompanying analyses lead to a consensus model of the clathrin triskelion hub, suggesting a universal assembly mode that still allows adaptation to various vesicle sizes and shapes.

    • Kyle L. Morris
    • Joseph R. Jones
    • Corinne J. Smith
    Research
    Nature Structural & Molecular Biology
    Volume: 26, P: 890-898

  • Messenger RNAs (mRNAs) that induce stalling during translation are degraded by a quality control mechanism known as no-go decay (NGD). The aberrant mRNAs are recognized by two factors, Dom34 and Hbs1. Using cryo-EM to visualize NGD intermediates bound to a stalled ribosome, Beckman and coworkers suggest how binding of Dom34-Hbs1 may lead to ribosome disassembly and recruitment of mRNA degradation factors.

    • Thomas Becker
    • Jean-Paul Armache
    • Roland Beckmann
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 715-720

  • A saposin protein–lipid nanoparticle system stabilizes diverse, fragile membrane proteins in a lipid environment for structural and functional studies.

    • Jens Frauenfeld
    • Robin Löving
    • Pär Nordlund
    Research
    Nature Methods
    Volume: 13, P: 345-351

  • Nascent secretory and membrane proteins are targeted to the Sec61 protein-conducting channel for translocation across or insertion into the endoplasmic reticulum membrane; here cryo-electron microscopy structures of eukaryotic ribosome–channel complexes show how this channel opens vertically during translocation of a secretory protein into the lumen of the endoplasmic reticulum and how it opens laterally during insertion of a transmembrane domain into the lipid bilayer.

    • Marko Gogala
    • Thomas Becker
    • Roland Beckmann
    Research
    Nature
    Volume: 506, P: 107-110