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 1–6 of 6 results
Advanced filters: Author: Frank D Sönnichsen Clear advanced filters

  • Controlled switching of the spin state of transition metal ions is key in many enzymatic reactions, but difficult to replicate in synthetic systems. Here the authors report on an iron(III) porphyrin with a photochromic axial ligand that, in solution, reversibly switches between low-spin and high-spin upon irradiation with two different wavelengths.

    • Sreejith Shankar
    • Morten Peters
    • Rainer Herges
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-12

  • Acanthaporin is identified as a pore-forming protein from the infectious Acanthamoeba culbertsoni with a previously unknown structure. The newly identified structure includes a pH-dependent histidine switch that controls partitioning between the inactive dimer and the active monomer, which assembles into larger species to cause toxicity.

    • Matthias Michalek
    • Frank D Sönnichsen
    • Matthias Leippe
    Research
    Nature Chemical Biology
    Volume: 9, P: 37-42

  • ADAM17 is a member of the ‘Disintegrin and Metalloproteinase’ family of proteases, that cleaves transmembrane substrates from the surfaces of cells. Here the authors show that surface exposure of phosphatidylserine is required for ADAM17 sheddase activity, possibly by directing the protease to its substrates.

    • Anselm Sommer
    • Felix Kordowski
    • Karina Reiss
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-14

  • A comparison of the structures of two cyanobacterial toxins yields insights into how they may inhibit protein phosphatase-1 and -2A and why microcystins but not motuporin may covalently modify their protein phosphatase targets.

    • John R. Bagu
    • Frank D. Sönnichsen
    • Charles F.B. Holmes
    Correspondence
    Nature Structural Biology
    Volume: 2, P: 114-116

  • Designing systems to drive endergonic reactions using light as an energy source is a major challenge. Here a photoswitchable ligand is used to generate unstable cyclic tetravanadate species in solution.

    • Hanno Sell
    • Anika Gehl
    • Rainer Herges
    ResearchOpen Access
    Communications Chemistry
    Volume: 2, P: 1-6