Complex N-acetyl-L-cysteine compounds with biometals as self-defense factors of biological system.

We studied the effects of complex N-acetyl-L-cysteine compounds with transitional biometals on the inflammatory and adaptation reactions. Some compounds were superior to known antihypoxants and actoprotectors and exhibited significant antiinflammatory activity.

Adaptor protein Ruk1 forms protein-protein complexes with endonuclease activity in HEK293 cells.

The structural and functional organization of the adaptor protein Ruk(1) is characterized by the presence of three SH3-domains at the N-terminus followed by Pro- and Ser-rich sequences and a C-terminal coiled-coil region. Multiple modules in the Ruk(1) structure involved in protein-protein interactions can provide for formation of ligand clusters with varied properties and subcellular location. To study the nature and biological role of such complexes, the recombinant protein Ruk(1) with a Glu-epitope at the C-terminus (Ruk(1) Glu-tagged) was purified from transfected HEK293 cells by affinity chromatography on protein G-Sepharose with covalently conjugated anti-Glu-tag antibodies.