Sila K. Ultanir

This paper shows that presynaptic filopodia, driven by activity, calcium, and actin, physically modulate membrane mechanics to enhance synchronous neurotransmission and contribute to seizure generation.

This study identifies CDKL5 as a kinase that phosphorylates nELAVL proteins, enhancing mRNA binding and protein synthesis, and shows its role in visual cortex development.

This study performs phosphoproteomic analysis of TSC brain lesions, finding strong mTORC1 activation and widespread mRNA splicing changes in SEGAs but not tubers.

This study investigates how CDKL5 phosphorylation of MAP1S affects microtubule function and cognitive processes, showing impaired dynein motility and synaptic defects in mutant mice.

The paper identifies and characterizes a chemical probe for CDKL2, demonstrating its selectivity and biological impact in neurons and cancer cells.

This study identifies CDKL5 as a kinase that phosphorylates Cav2.3, altering its function and contributing to neuronal excitability in CDKL5 deficiency disorder.

This study identifies a novel RNA-binding function of PGC-1alpha that couples transcriptional co-activation with mRNA nuclear export and mitochondrial homeostasis.

The paper develops specific CDKL5 inhibitors that do not affect GSK3β activity and shows their effects on synaptic function and LTP in rat hippocampal slices.

This study identifies Unkempt as a novel mTORC1 substrate whose phosphorylation regulates cellular morphology by inhibiting its ability to induce bipolar morphology.

The paper maps the regulatory landscape of neuronal and glial differentiation in the enteric nervous system using single-cell RNA sequencing and identifies gene modules and epigenetic memory associated with neurogenesis and gliogenesis.

This study shows that dual loss of NDR1/2 kinases in neurons causes neurodegeneration, disrupts endocytosis, and impairs autophagy by affecting membrane trafficking and protein homeostasis.

The paper identifies the molecular mechanism by which Phactr1/PP1 phosphatase achieves substrate specificity through structural and phosphoproteomic analysis.

This study identifies Cdkl5's role in pain signaling through its interaction with CaMKII in both human neurons and mouse models of Cdkl5 deficiency disorder.