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Electronic coupling of the phycobilisome with the orange carotenoid protein and fluorescence quenching
TLDR
Using computational modeling and known 3D structure of proteins, a rational spatial model of the orange carotenoid protein (OCP) and phycobilisome (PBS) interaction in the non-photochemical fluorescence quenching is arrived at and the complete scheme of OCP and PBS interaction that includes participation of the FRP is proposed. Expand
Cyanobacterial phycobilisomes and phycobiliproteins
TLDR
In cyanobacteria, phycobilisomes (PBS) act as antenna of the photosynthetic pigment apparatus and form giant supramolecular complexes (up to 3000–7000 kDa) containing 200 to 500 phyCobilin chromophores covalently bound to the proteins. Expand
The Signaling State of Orange Carotenoid Protein.
TLDR
The obtained results suggest that the photoactivated form of OCP represents a molten globule-like state that is characterized by increased mobility of tertiary structure elements and solvent accessibility. Expand
Assembly of photoactive orange carotenoid protein from its domains unravels a carotenoid shuttle mechanism
TLDR
Physiological roles are assigned to the multitude of CTD homologs in cyanobacteria and explain the evolutionary process of OCP formation. Expand
Role of inter-domain cavity in the attachment of the orange carotenoid protein to the phycobilisome core and to the fluorescence recovery protein
TLDR
A universal 3D model of the orange carotenoid protein (OCP) and phycobilisome (PBS) interaction in the process of non-photochemical PBS quenching is derived and in cyanobacteria, the small fluorescence recovery protein is wedged in the OCP’s central cavity, weakening the PBS and OCP interaction. Expand
Phycobilisomes from the mutant cyanobacterium Synechocystis sp. PCC 6803 missing chromophore domain of ApcE.
Phycobilisome (PBS) is a giant photosynthetic antenna associated with the thylakoid membranes of cyanobacteria and red algae. PBS consists of two domains: central core and peripheral rods assembledExpand
The fibrils untwisting limits the rate of cellulose nitration process.
TLDR
It is proposed that the nan ofibrils' untwisting limits the rate of the nitronium ion transport into the cellulose nanofibrils and, thus, the rateof the nitration reaction as a whole. Expand
Assembly of photoactive Orange Carotenoid Protein from its domains unravels a carotenoid shuttle mechanism
TLDR
It is shown how OCP can be reassembled from its functional domains, assigning physiological roles to CTD homologs and explaining the evolutionary process of OCP formation. Expand
Interaction of the orange carotenoid protein with the phycobilisome core and fluorescence recovery protein
TLDR
A universal spatial model of the orange carotenoid protein (OCP) and phycobilisome (PBS) core interaction in process of energy excess dissipation and the small fluorescence recovery protein (FRP) also interacts with the OCPs central cavity weakening the PBS and OCP binding. Expand
The Novel Short Isoform of Securin Stimulates the Expression of Cyclin D3 and Angiogenesis Factors VEGFA and FGF2, but Does Not Affect the Expression of MYC Transcription Factor
TLDR
A novel isoform of securin which is able to activate a more restricted repertoire of genes compared to the full-size protein is found, which does not affect the MYC gene expression. Expand
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