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Dorothea Fiedler

Researcher at Humboldt University of Berlin

Publications -  98
Citations -  5794

Dorothea Fiedler is an academic researcher from Humboldt University of Berlin. The author has contributed to research in topics: Inositol & Kinase. The author has an hindex of 33, co-authored 85 publications receiving 5000 citations. Previous affiliations of Dorothea Fiedler include University of California, San Francisco & Howard Hughes Medical Institute.

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MLKL Requires the Inositol Phosphate Code to Execute Necroptosis.

TL;DR: It is shown that IP kinases are essential for necroptosis triggered by death receptor activation, herpesvirus infection, or a pro-necrotic MLKL mutant, and that a highly phosphorylated product, but not a lowlyosphorylated precursor, potently displaces theMLKL auto-inhibitory brace region.
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Guest Exchange Dynamics in an M4L6 Tetrahedral Host

TL;DR: Guest displacement reactions demonstrate the sensitivity of guest exchange to thermodynamic endohedral guest binding affinities and blocking the exohedral host sites with high concentrations of the smaller NMe(4)(+) cation (a weak endo Cathedral guest) enhances PEt(4)+) for NEt( 4)(+) guest exchange rates.
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A Complex-based Reconstruction of the Saccharomyces cerevisiae Interactome

TL;DR: This study provides a new algorithm for reconstruction of stable complexes from a variety of heterogeneous biological assays and provides novel insights regarding the protein-protein interaction network, reinterpreting the finding that “hubs” in the network are enriched for being essential, showing instead that essential proteins tend to be clustered together in essential complexes and that these essential complexes tend to been large.
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Inositol Pyrophosphates Mediate the DNA-PK/ATM-p53 Cell Death Pathway by Regulating CK2 Phosphorylation of Tti1/Tel2

TL;DR: It is demonstrated that IP7, formed by IP6K2, binds CK2 to enhance its phosphorylation of the TTT complex, thereby stabilizing DNA-PKcs and ATM and stimulating p53 phosphorylated at serine 15 to activate the cell death program in human cancer cells and in murine B cells.