Volodymyr M. Korkhov

This study designs a chimeric adenylyl cyclase (AC95) to investigate isoform-specific regulation, revealing structural insights and drug target possibilities.

This study identifies HPCAL1 as a Ca2+-dependent regulator of AC8, revealing a new mechanism for cAMP signaling regulation.

This study evaluates the impact of X-ray radiation doses on cryo-preserved biological samples, showing that high doses do not prevent subsequent cryo-EM analysis for intermediate to high-resolution structural insights.

The paper determines the cryo-EM structures of Cx32 gap junction channels reconstituted in nanodiscs, showing that phospholipids block the pore by binding to the N-terminal gating helix, contingent on sterol presence.

The paper reports cryo-EM structures of PfNCR1 bound to four inhibitors, revealing distinct binding modes that inform drug discovery targeting this malaria parasite transporter.

The paper identifies two distinct binding sites for connexin channel inhibitors mefloquine and 2APB, showing they block channel function through different mechanisms.

The paper reports the cryo-EM structure of connexin-36 bound to mefloquine, revealing how small molecules inhibit gap junction channels by partially occluding the pore and altering electrostatics.

This study systematically identifies structure-specific protein-protein interactions using LiP-MS, demonstrating its application to alpha-synuclein in Parkinson's disease.