Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–29 of 29 results
Advanced filters: Author: Alexander G Myasnikov Clear advanced filters

  • During translation, several ribosomes assemble on an mRNA strand to form polyribosomes. Here the authors describe—using cryo electron tomography—a compact state of the eukaryotic polysome where individual ribosomes contact each other and form a tight helical assembly that creates a continuous inner channel for the mRNA.

    • Alexander G. Myasnikov
    • Zhanna A. Afonina
    • Bruno P. Klaholz
    Research
    Nature Communications
    Volume: 5, P: 1-8

  • The ribosome of bacteria and other unicellular pathogens is a common target for antibiotic drugs. Here the authors determine a structure of the human ribosome bound to the translation inhibitor cycloheximide, and provide evidence that targeting the ribosome is a promising avenue for cancer therapy.

    • Alexander G. Myasnikov
    • S. Kundhavai Natchiar
    • Bruno P. Klaholz
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-8

  • ABCB6 has been implicated in dyschromatosis universalis hereditaria, a condition that can present with hearing loss. Here, the authors use zebrafish and mice to perform experiments suggesting that ABCB6 plays a role in inner ear development.

    • Stefanie A. Baril
    • Katie A. Wilson
    • John D. Schuetz
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-17

  • Cryo-electron microscopy, nuclear magnetic resonance and X-ray crystallography are used to provide structural and mechanistic details of the activation of anaplastic lymphoma kinase by the ligands ALKAL1 and ALKAL2.

    • Andrey V. Reshetnyak
    • Paolo Rossi
    • Charalampos G. Kalodimos
    Research
    Nature
    Volume: 600, P: 153-157

  • 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

  • A high-resolution structure of the human ribosome determined by cryo-electron microscopy visualizes numerous RNA modifications that are concentrated at functional sites with an extended shell, and suggests the possibility of designing more specific ribosome-targeting drugs.

    • S. Kundhavai Natchiar
    • Alexander G. Myasnikov
    • Bruno P. Klaholz
    Research
    Nature
    Volume: 551, P: 472-477

  • The structure of the human ribosome at high resolution has been solved; by combining single-particle cryo-EM and atomic model building, local resolution of 2.9 Å was achieved within the most stable areas of the structure.

    • Heena Khatter
    • Alexander G. Myasnikov
    • Bruno P. Klaholz
    Research
    Nature
    Volume: 520, P: 640-645

  • Cryo-electron microscopy and single-molecule fluorescence methods are used to elucidate the mechanism of early translocation events on the bacterial ribosome.

    • Emily J. Rundlet
    • Mikael Holm
    • Scott C. Blanchard
    ResearchOpen Access
    Nature
    Volume: 595, P: 741-745

  • Ghrelin is a central orexigenic peptide hormone in human energy homeostasis that is also known as ‘hunger hormone’ and signals through its GPCR, GHSR. Here, the authors present the cryo-EM structures of the human GHSR-Gi signaling complex with bound ghrelin and the synthetic non-peptide agonist ibutamoren that are of interest for drug design.

    • Heng Liu
    • Dapeng Sun
    • Cheng Zhang
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-8

  • The accuracy of eukaryotic ribosome translocation relies on eukaryote-specific elements of the 80S ribosome, elongation factor 2 and transfer RNAs, all of which contribute to the maintenance of the messenger RNA reading frame.

    • Nemanja Milicevic
    • Lasse Jenner
    • Gulnara Yusupova
    Research
    Nature
    Volume: 625, P: 393-400

  • The paenilamicins are hybrid nonribosomal peptide–polyketide compounds that inhibit protein synthesis. Here the authors reveal that paenilamicins bind to a unique site on the ribosome, where they interfere with the translocation of mRNA and tRNAs during elongation.

    • Timm O. Koller
    • Max J. Berger
    • Daniel N. Wilson
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 20, P: 1691-1700

  • The reaction coordinate of aminoacyl-tRNA movement is altered on the human ribosome and the process is an order of magnitude slower compared with bacteria due to eukaryote-specific structural elements in the human ribosome and in the elongation factor eEF1A.

    • Mikael Holm
    • S. Kundhavai Natchiar
    • Scott C. Blanchard
    ResearchOpen Access
    Nature
    Volume: 617, P: 200-207

  • Prokaryotic translation initiation involves mRNA-ribosomal RNA base pairing interactions. Here, the authors provide evidence for a similar base pairing interactions occurring between the human h4 mRNA and helix 16 of the small subunit rRNA to position the correct AUG codon in the decoding site.

    • Franck Martin
    • Jean-François Ménétret
    • Gilbert Eriani
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-7

  • Here the authors present the high-resolution structures of 17 antibiotics bound to Escherichia coli ribosomes, which may inform the development of new antibacterial agents. Their results unveil a conserved manner of antibiotic binding to the ribosome, including ordered water molecules.

    • Helge Paternoga
    • Caillan Crowe-McAuliffe
    • Daniel N. Wilson
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 30, P: 1380-1392

  • The 26S proteasome is a protein degradation machine composed of a 20S core particle (CP) flanked at one or both ends by a 19S ATPase regulatory particle (RP). Here the authors reconstitute asymmetric archaeal proteasomes and reveal allosteric coupling between the conformations of gates in the α-rings positioned at opposite ends of the CP, which modulates RP assembly and substrate entry.

    • Zanlin Yu
    • Yadong Yu
    • Yifan Cheng
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-11

  • Human OPA1 embeds itself into cardiolipin-containing membranes through a lipid-binding paddle domain, and OPA1 oligomerization through multiple assembly interfaces promotes the helical assembly of a flexible OPA1 lattice on the membrane, driving mitochondrial fusion in cells.

    • Alexander von der Malsburg
    • Gracie M. Sapp
    • Halil Aydin
    Research
    Nature
    Volume: 620, P: 1101-1108

  • The cryo-electron microscopy structure of the glucocorticoid receptor (GR)-loading complex—a complex in which Hsp70 loads GR onto Hsp90 and Hop—is described, providing insights into how the chaperones Hsp90 and Hsp70 coordinate to facilitate GR remodelling for activation.

    • Ray Yu-Ruei Wang
    • Chari M. Noddings
    • David A. Agard
    Research
    Nature
    Volume: 601, P: 460-464

  • The transcription co-activator complex SAGA is recruited to promoters by transcriptional activators and promotes the formation of the pre-initiation complex. Here, the authors present the cryo-EM structure of the SAGA complex and resolve the major target of activator binding, the 430 kDa Tra1 protein.

    • Grigory Sharov
    • Karine Voltz
    • Patrick Schultz
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-7

  • Here the authors use cryo-EM and biochemical analysis to show how the ancillary protein TPR-CHAT regulates the nuclease function of the CRISPR-guided nuclease Cas7-11.

    • Babatunde Ekundayo
    • Davide Torre
    • Dongchun Ni
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 30, P: 135-139