Nikolai N. Sluchanko

This paper presents the cryo-EM structure of the Gloeobacter violaceus phycobilisome, revealing its unique bundle-shaped architecture and regulation by orange carotenoid proteins.

The paper identifies and characterizes double ferritin-like proteins (DFLPs) that form homodimers, bind heme, and exhibit ferroxidase activity, with some targeted to encapsulin shells.

The paper shows that short prokaryotic Argonautes (pAgos) activate HNH nuclease effectors after RNA-guided DNA recognition, forming filaments that degrade DNA and confer bacterial immunity.

This study identifies biochemical signatures that categorize plant 14-3-3 isoforms into epsilon and non-epsilon groups, revealing key amino acid positions responsible for phylogenetic demarcation.

The paper identifies a unique hexameric structure of Arthropoda-specific TTK-type BTB domains and shows their lineage-specific expansion in insects.

This study identifies four phosphorylation sites in NPM1 that enable 14-3-3 protein binding, revealing how phosphorylation regulates NPM1's nucleocytoplasmic shuttling and structural dynamics.

The paper shows that NbaAgo forms a complex with an effector nuclease to cleave DNA/RNA upon target recognition, providing bacterial immunity against invaders.

The paper develops a system to autonomously produce phosphorylated proteins in E. coli, demonstrating that non-hydrolyzable phosphoserine mimics phosphoserine function in three biological contexts.

This study investigates the solution structure of STARD1 and its interaction with NBD-labeled cholesterol analogs, revealing structural stability and fluorescence properties that challenge previous models of cholesterol binding.