Dorothea Fiedler

The paper shows that the PPIP5K enzyme Asp1 produces opposite effects on fungal morphology and actin organization in different species, depending on the host cellular environment.

The paper develops a mass spectrometry method to quantify inositol pyrophosphate-protein interactions on a proteome-wide scale, identifying new pyrophosphorylated proteins and highlighting Mg2+ effects on binding.

The paper identifies VIH2 in Lotus japonicus as an inositol pyrophosphate synthase that regulates arbuscular mycorrhiza by linking phosphate starvation responses to root endosymbiosis.

This paper develops [13C6]scyllo-inositol as an isotopic tracer to study its metabolism and shows its incorporation into phosphatidylinositols in mammalian cells.

The paper identifies PP-InsP-interacting complexes in Arabidopsis, including CK2 subunits, and shows InsP6 modulates CK2 activity by blocking substrate binding.

This study identifies oligophosphorylation as a new phosphorylation mode, showing NME1 can catalyze its own oligophosphorylation using ATP, with implications for phosphoregulation.

This study identifies a GAF signaling domain that regulates PPIP5K phosphatase activity in phosphate homeostasis through structural and functional analyses.

This study identifies three phosphatase families involved in inositol pyrophosphate catabolism in plants, showing their roles in growth, development, and nutrient signaling.

This study investigates the regulatory role of pyrophosphorylation on NAGK activity and protein interactions, revealing its impact on kinase function and stability.

This study compares four lysis buffers for proteomics, finding SDS most reliable and advocating a dual-sample approach to maximize proteome coverage.