Search Results - "Viertler, Martin"

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  1. 1

    Multiple regulatory intrinsically disordered motifs control FOXO4 transcription factor binding and function by Bourgeois, Benjamin, Gui, Tianshu, Hoogeboom, Diana, Hocking, Henry G., Richter, Gesa, Spreitzer, Emil, Viertler, Martin, Richter, Klaus, Madl, Tobias, Burgering, Boudewijn M.T.

    Published in Cell reports (Cambridge) (27-07-2021)
    “…Transcription factors harbor defined regulatory intrinsically disordered regions (IDRs), which raises the question of how they mediate binding to structured…”
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    Journal Article
  2. 2

    Type‐II NADH:quinone oxidoreductase from Staphylococcus aureus has two distinct binding sites and is rate limited by quinone reduction by Sena, Filipa V., Batista, Ana P., Catarino, Teresa, Brito, José A., Archer, Margarida, Viertler, Martin, Madl, Tobias, Cabrita, Eurico J., Pereira, Manuela M.

    Published in Molecular microbiology (01-10-2015)
    “…Summary A prerequisite for any rational drug design strategy is understanding the mode of protein–ligand interaction. This motivated us to explore…”
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    Journal Article
  3. 3

    Activity based subcellular resolution imaging of lipases by Viertler, Martin, Schittmayer, Matthias, Birner-Gruenberger, Ruth

    Published in Bioorganic & medicinal chemistry (15-01-2012)
    “…Lipases play a key role in whole body energy homeostasis. Dysregulation of lipolytic activities affects lipid absorption, mobilization, and transport, and is…”
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    Journal Article
  4. 4

    Increasing the Chemical-Shift Dispersion of Unstructured Proteins with a Covalent Lanthanide Shift Reagent by Göbl, Christoph, Resch, Moritz, Strickland, Madeleine, Hartlmüller, Christoph, Viertler, Martin, Tjandra, Nico, Madl, Tobias

    Published in Angewandte Chemie International Edition (14-11-2016)
    “…The study of intrinsically disordered proteins (IDPs) by NMR often suffers from highly overlapped resonances that prevent unambiguous chemical‐shift…”
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    Type‐ II NADH :quinone oxidoreductase from S taphylococcus aureus has two distinct binding sites and is rate limited by quinone reduction by Sena, Filipa V., Batista, Ana P., Catarino, Teresa, Brito, José A., Archer, Margarida, Viertler, Martin, Madl, Tobias, Cabrita, Eurico J., Pereira, Manuela M.

    Published in Molecular microbiology (01-10-2015)
    “…A prerequisite for any rational drug design strategy is understanding the mode of protein–ligand interaction. This motivated us to explore protein–substrate…”
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    Journal Article
  9. 9

    Verbesserung der Dispersion der chemischen Verschiebungen von unstrukturierten Proteinen durch einen kovalent gebundenen Lanthanoidkomplex by Göbl, Christoph, Resch, Moritz, Strickland, Madeleine, Hartlmüller, Christoph, Viertler, Martin, Tjandra, Nico, Madl, Tobias

    Published in Angewandte Chemie (14-11-2016)
    “…Die Erforschung von intrinsisch unstrukturierten Proteinen (IDPs) mit NMR‐spektroskopischen Methoden wird oftmals durch starke Überlagerung der Proteinsignale…”
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    Journal Article
  10. 10

    Verbesserung der Dispersion der chemischen Verschiebungen von unstrukturierten Proteinen durch einen kovalent gebundenen Lanthanoidkomplex by Göbl, Christoph, Resch, Moritz, Strickland, Madeleine, Hartlmüller, Christoph, Viertler, Martin, Tjandra, Nico, Madl, Tobias

    Published in Angewandte Chemie (14-11-2016)
    “…Die Erforschung von intrinsisch unstrukturierten Proteinen (IDPs) mit NMR‐spektroskopischen Methoden wird oftmals durch starke Überlagerung der Proteinsignale…”
    Get full text
    Journal Article