Urszula Golebiewska

Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions.

Reversible - through calmodulin - electrostatic interactions between basic residues on proteins and acidic lipids in the plasma membrane.

Membrane-bound basic peptides sequester multivalent (PIP2), but not monovalent (PS), acidic lipids.

Structure of the membrane reconstituted transmembrane-juxtamembrane peptide EGFR(622-660) and its interaction with Ca2+/calmodulin.

Membrane-permeable calmodulin inhibitors (e.g. W-7/W-13) bind to membranes, changing the electrostatic surface potential: dual effect of W-13 on epidermal growth factor receptor activation.

Diffusion coefficient of fluorescent phosphatidylinositol 4,5-bisphosphate in the plasma membrane of cells.

Galphaq binds two effectors separately in cells: evidence for predetermined signaling pathways.

A self-scaffolding model for G protein signaling.

Evidence for a second, high affinity Gbetagamma binding site on Galphai1(GDP) subunits.

Novel endogenous peptide agonists of cannabinoid receptors.

The effect of membrane domains on the G protein-phospholipase Cbeta signaling pathway.

The small G protein Rac1 activates phospholipase Cdelta1 through phospholipase Cbeta2.

Wnt-dependent assembly of supermolecular Dishevelled-3-based complexes.

Differential response to morphine of the oligomeric state of μ-opioid in the presence of δ-opioid receptors.

Modulation of Ca²+ activity in cardiomyocytes through caveolae-Gαq interactions.

A dynamic model of membrane-bound phospholipase Cβ2 activation by Gβγ subunits.

Evidence for a fence that impedes the diffusion of phosphatidylinositol 4,5-bisphosphate out of the forming phagosomes of macrophages.