T. I. Igumenova

This study uses in-cell and lysate NMR spectroscopy to investigate how cadmium interacts with protein targets in crowded environments, revealing its ability to replace zinc in structural sites and its potential for bioremediation.

This paper shows Pin1 regulates PKC through a non-catalytic mechanism by binding its C-terminal tail via a novel bivalent interaction mode.

This study investigates how small molecule inhibitors affect Sec14 phosphatidylinositol transfer protein activity using structural analysis to inform antifungal drug design.

The paper reports high-resolution crystal structures of a C1 domain bound to DAG and agonists, revealing mechanisms of lipid recognition and guiding drug design.

The paper shows that using Bis-Tris buffer helps identify high-affinity Pb2+ binding sites in Syt1's Ca2+-sensing domains, revealing differences in membrane-binding responses between C2A and C2B domains.

This study shows that partial metal ion saturation of Syt1's C2 domains primes its membrane interactions by restricting conformational plasticity and positioning for full activation.

This study identifies two high-affinity Pb2+ binding sites in Synaptotagmin I and shows Pb2+ can act as a kinetic and thermodynamic trap, interfering with Ca2+-dependent function.