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Showing 1–17 of 17 results
Advanced filters: Author: "Martin Beck" Clear advanced filters

  • Importins are known to facilitate nucleocytoplasmic transport and cytoplasmic chaperoning of some proteins. Here, the authors uncover that these proteins also act as co-translational chaperones for specific sets of proteins, for example ribonucleic acid binding factors.

    • Maximilian Seidel
    • Natalie Romanov
    • Martin Beck
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-15

  • The most comprehensive architectural model to date of the nuclear pore complex reveals previously unknown local interactions, and a role for nucleoporin 358 in Y-complex oligomerization.

    • Alexander von Appen
    • Jan Kosinski
    • Martin Beck
    Research
    Nature
    Volume: 526, P: 140-143

  • Metabolic labeling is often used to measure protein turnover. Here the authors show that for interconvertible protein species like phosphoforms metabolic labeling does not provide information on turnover differences, but that the relative order of modification can determine the observed dynamics.

    • Henrik M. Hammarén
    • Eva-Maria Geissen
    • Mikhail M. Savitski
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-15

  • The translational states of eukaryotic ribosomes have so far been only investigated in vitro. Here, authors obtained the 3.8 Å in situ 80S ribosome structure, the distribution of translational states and unique arrangement of rRNA expansion segments.

    • Patrick C. Hoffmann
    • Jan Philipp Kreysing
    • Martin Beck
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-9

  • The biogenesis of nuclear pores imposes a logistic challenge for cells. Here, the authors investigate structural motifs for co-translational interactions in nucleoporins and find that co-translational assembly events differ between paralogous assembly pathways thus contributing to faithful assembly.

    • Maximilian Seidel
    • Anja Becker
    • Martin Beck
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-15

  • Here the authors systematically benchmark cryo-electron tomography acquisition schemes to optimize the attainable resolution for subtomogram averaging, and find that dose-symmetric acquisition with even angular sampling provides a better outcome than most currently used acquisition schemes.

    • Beata Turoňová
    • Wim J. H. Hagen
    • Martin Beck
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-9

  • In-cell structural studies in Saccharomyces cerevisiae reveal that the configuration of the Nup159 complex is a key determinant of the mRNA export function of the nuclear pore complex, and suggest a model in which nuclear pore complexes are degraded via the autophagy machinery.

    • Matteo Allegretti
    • Christian E. Zimmerli
    • Martin Beck
    Research
    Nature
    Volume: 586, P: 796-800

  • Cryo-EM structures of the S. cerevisiae condensin holo complex reveal that ATP binding triggers exchange of the two HEAT-repeat subunits bound to the SMC ATPase head domains, potentially leading to an interconversion of DNA-binding sites in the catalytic core of condensin that might form the basis of its DNA translocation and loop-extrusion activities.

    • Byung-Gil Lee
    • Fabian Merkel
    • Christian H. Haering
    Research
    Nature Structural & Molecular Biology
    Volume: 27, P: 743-751

  • While the architecture of vertebrate nuclear pore complexes (NPCs) is well understood, the extent of its evolutionary conservation is still unclear. Here, the authors analyze the in situ architecture of an algal NPC, revealing distinct structural features that provide insights into NPC evolution.

    • Shyamal Mosalaganti
    • Jan Kosinski
    • Martin Beck
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-8

  • The proteome-wide characterization of proteostasis depends on robust approaches to determine protein half-lives. Here, the authors improve the accuracy and precision of mass spectrometry-based quantification, enabling reliable protein half-life determination in several non-dividing cell types.

    • Toby Mathieson
    • Holger Franken
    • Mikhail M. Savitski
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-10

  • The Nup82–Nup159–Nsp1 complex, which plays a key role in mRNA export, is recruited late during the process of nuclear pore complex (NPC) assembly. Here the authors combine crosslinking mass spectrometry, biochemical reconstitution and molecular modeling to gain insights into the mechanism of Nup82 recruitment to the NPC.

    • Roman Teimer
    • Jan Kosinski
    • Ed Hurt
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-11

  • Lee et al. show that, after nitrogen starvation and genetic interference with the architecture of nuclear pore complexes, nucleoporins are degraded by autophagy, constituting a quality-control step at the nuclear envelope.

    • Chia-Wei Lee
    • Florian Wilfling
    • Boris Pfander
    Research
    Nature Cell Biology
    Volume: 22, P: 159-166

  • Nuclear pore complexes (NPCs) are large protein assemblies that form channels in the nuclear envelope and constitute major routes for nucleocytoplasmic communication. Insights into the complex structure of NPCs provide the basis for understanding their functions and reveal how the dysfunction of their structural components, nucleoporins, contributes to human disease.

    • Martin Beck
    • Ed Hurt
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 18, P: 73-89

  • Formalin fixation and paraffin embedding (FFPE) of human tissue is a central strategy for preserving pathological specimens. This protocol describes how to process these specimens for spatially resolved LC-MS by laser-capture microdissection.

    • Katarzyna Buczak
    • Joanna M. Kirkpatrick
    • Alessandro Ori
    Protocols
    Nature Protocols
    Volume: 15, P: 2956-2979