E. G. Maksimov

The paper uses spectroscopy and X-ray structures to reveal two distinct mechanisms by which flavin-binding proteins tune their fluorescence spectra.

The paper presents the first crystal structures of OCP2 from different cyanobacteria and compares them with OCP1 and OCP3 to correlate structural features with spectroscopic and functional properties.

This paper determines the structure of AstaP, a carotenoid-binding protein, and explains its ligand promiscuity through structural and biochemical analyses.

This study characterizes the structure and function of BmCBP, a silkworm carotenoprotein, showing its ability to bind and deliver carotenoids for biomedical applications.

The paper presents the first crystal structure of OCPX and compares it with OCP1, revealing structural and functional differences that explain its unique photoprotection mechanism.

This study characterizes AstaP, a microalgal protein that efficiently solubilizes and delivers multiple carotenoids, showing its potential as an antioxidant nanocarrier.

This paper develops a method using antigenic membrane vesicles to specifically stimulate and expand CAR-T cells, showing improved efficacy compared to existing protocols.

The paper investigates how phosphorylation of STARD1 at specific sites enables interaction with 14-3-3 proteins, modulating its activity and mitochondrial import.

This paper demonstrates a cyanobacterial carotenoprotein (CTDH) that efficiently delivers carotenoids to liposomes and mammalian cells, providing antioxidant protection against oxidative stress.

The paper investigates the radioprotective role of cyanobacterial phycobilisomes by exposing Synechocystis sp. PCC6803 to ionizing radiation and space flight, revealing their potential role in stress response and recovery.

The paper investigates the functional interaction of low-homology FRPs from different cyanobacteria with Synechocystis OCP, revealing distinct binding properties despite similar structural conformations.

This study identifies two novel photocycle intermediates in the Orange Carotenoid Protein (OCP) using time-resolved spectroscopy, revealing asynchronous changes in carotenoid and protein components.

This study examines how disrupting Na+,K+-ATPase interactions with ankyrin B and caveolin-1 affects its lateral diffusion in HEK293 cells using fluorescence techniques.

The paper demonstrates a unique protein-to-protein carotenoid transfer mechanism using COCP to assemble photoactive OCP from photoinactive species.

The paper identifies the main site of OCP-FRP interactions by analyzing structural and functional similarities between the NTE and FRP.

The study reassembles the Orange Carotenoid Protein (OCP) from its domains, revealing a carotenoid shuttle mechanism where the CTD binds carotenoid and transfers it to the NTD.