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Showing 1–10 of 10 results
Advanced filters: Author: "Gerhard Wagner" Clear advanced filters

  • The structure of the apo thiolation-thioesterase di-domain fragment of the EntF non-ribosomal peptide synthetase subunit of enterobactin synthetase is solved. Extensive inter- and intra-domain motions are observed, and these are modulated by interactions with other proteins that participate in the biosynthesis of enterobactin.

    • Dominique P. Frueh
    • Haribabu Arthanari
    • Gerhard Wagner
    Research
    Nature
    Volume: 454, P: 903-906

  • Structures of GPCR neurotensin receptor 1 (NTSR1) in complex with neurotensin and Gαi1β1γ1 in a lipid bilayer environment and without stabilizing antibodies reveal extensive interactions at the GPCR–G protein interface.

    • Meng Zhang
    • Miao Gui
    • Gerhard Wagner
    Research
    Nature Structural & Molecular Biology
    Volume: 28, P: 258-267

  • miRNAs are incorporated into ribonucleoprotein complexes called RNA-induced silencing complexes (RISCs) to exert RNA interference. Here the authors show that translation initiation factor eIF1A interacts with the RISCs component Ago2 to promote miR-451 biogenesis and RNA interference.

    • Tingfang Yi
    • Haribabu Arthanari
    • Gerhard Wagner
    Research
    Nature Communications
    Volume: 6, P: 1-11

  • Herpesvirus VP16 is a classic example of a transcriptional activator and interacts with the Mediator complex via MED25 (ARC92). The structure of the VP16 interaction domain from MED25 is now solved and the binding site for the VP16 transactivation domain defined, giving insight into how a transcription activator contacts a key component involved in transcription initiation.

    • Alexander G Milbradt
    • Madhura Kulkarni
    • Gerhard Wagner
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 410-415

  • The applications of solution-state NMR of membrane proteins are often limited by difficulty in finding a suitable membrane mimetic of tailored size that shows native-like membrane properties and provides long-term stability. This protocol describes how to assemble phospholipid nanodiscs and incorporate membrane proteins for NMR-structural studies.

    • Franz Hagn
    • Mahmoud L Nasr
    • Gerhard Wagner
    Protocols
    Nature Protocols
    Volume: 13, P: 79-98

  • Intracellular protein-protein interactions form the basis of most biological processes. Structural aspects of these reactions can now be analyzed in living prokaryotic cells and in atomic detail by nuclear magnetic resonance spectroscopy.

    • Philipp Selenko
    • Gerhard Wagner
    News & Views
    Nature Methods
    Volume: 3, P: 80-81

  • Membrane proteins can be stabilized in a native-like setting using lipid-bilayer-based nanodiscs encircled by a membrane scaffold protein. Covalently circularized nanodiscs now offer enhanced stability and control over nanodisc diameter size, improving the quality of structural data.

    • Mahmoud L Nasr
    • Diego Baptista
    • Gerhard Wagner
    Research
    Nature Methods
    Volume: 14, P: 49-52

  • A small molecule, inhibitor of a protein–protein interaction between the transcription factor Pdr1 and the Med15 subunit of Mediator in the fungal pathogen Candida glabrata, is identified and characterized here; the compound iKIX1 inhibits Pdr1-mediated gene activation and resensitizes drug-resistant C. glabrata to azole antifungals in vitro and in animal models of disseminated and urinary tract infection.

    • Joy L. Nishikawa
    • Andras Boeszoermenyi
    • Haribabu Arthanari
    Research
    Nature
    Volume: 530, P: 485-489