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 1–9 of 9 results
Advanced filters: Author: Iwan Zimmermann Clear advanced filters

  • Although it has shown high efficacy in many tumor types, interleukin-12 (IL-12) treatment provokes severe systemic toxicity. Here, the authors discover that use of an IL-12Fc fusion cytokine with abolished binding to the neonatal Fc receptor presents efficacy in local glioblastoma therapy while preventing toxicity.

    • Michal Beffinger
    • Linda Schellhammer
    • Johannes vom Berg
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-19

  • A method for protein binder selection and identification, NestLink, uses barcoding peptides detectable by mass spectrometry to select and biophysically characterize thousands of binders without requiring the handling of individual clones.

    • Pascal Egloff
    • Iwan Zimmermann
    • Markus A. Seeger
    Research
    Nature Methods
    Volume: 16, P: 421-428

  • Elevator transporters, like SLC23 proteins, transport solutes by a mechanism involving a reorientation of two rigid domains. Here, the authors show that linkers connecting these domains control the carrier’s conformational space and thus its function.

    • Benedikt T. Kuhn
    • Jonathan Zöller
    • Eric R. Geertsma
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-12

  • Lateral opening of the LptDE transporter in the outer membrane of Gram-negative bacteria is necessary for insertion of lipopolysaccharides. Here, Botte et al. report a cryo-EM structure of a partially opened LptDE transporter, in complex with rigid chaperones derived from nanobodies.

    • Mathieu Botte
    • Dongchun Ni
    • Michael Hennig
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-10

  • Serial synchrotron crystallography reveals the structure of the human glycine transporter GlyT1, showing how a state-specific inhibitor exerts its effects, and potentially informing the design of new GlyT1 inhibitors to treat a range of disorders of the central nervous system.

    • Azadeh Shahsavar
    • Peter Stohler
    • Poul Nissen
    Research
    Nature
    Volume: 591, P: 677-681

  • The mycobacterial ABC transporter IrtAB functions as a siderophore importer despite exhibiting an exporter fold in its structure, and contains a siderophore interaction domain capable of siderophore reduction and iron release inside the cell.

    • Fabian M. Arnold
    • Miriam S. Weber
    • Markus A. Seeger
    Research
    Nature
    Volume: 580, P: 413-417

  • ABC exporters hydrolyze ATP to pump substrates across membranes, but critical steps of the transport mechanism remain poorly understood. Here, the authors solve the crystal structure of outward-facing TM287/288 with the help of a state-specific sybody and gain insights into the role of the extracellular gate.

    • Cedric A. J. Hutter
    • M. Hadi Timachi
    • Markus A. Seeger
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-13

  • Open channel blockers are very different in their chemistry and structure. Now GLIC, a bacterial model for pentameric ligand-gated channels, is used to investigate the structural basis of open channel block. The work identifies two extended interaction sites, with large blockers binding to the center of the membrane and small blockers binding to the narrow intracellular region.

    • Ricarda J C Hilf
    • Carlo Bertozzi
    • Raimund Dutzler
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 1330-1336

  • This protocol describes in vitro procedures for generation of synthetic single-domain antibodies called ‘sybodies’. Sybodies can be engineered to target specific protein conformations, labile membrane proteins or protein complexes.

    • Iwan Zimmermann
    • Pascal Egloff
    • Markus A. Seeger
    Protocols
    Nature Protocols
    Volume: 15, P: 1707-1741