Lewis Base-Enhanced C-H Bond Functionalization Mediated by a Diiron Imido Complex.

Herein, we investigate the effects of ligand design on the nuclearity and reactivity of metal-ligand multiply bonded (MLMB) complexes to access an exclusively bimetallic reaction pathway for C-H bond functionalization. To this end, the diiron alkoxide [Fe(Dbf)] () was treated with 3,5-bis(trifluoromethyl)phenyl azide to access the diiron imido complex [Fe(Dbf)(μ-NCHF)] () that promotes hydrogen atom abstraction (HAA) from a variety of C-H and O-H bond containing substrates. A diiron bis(amide) complex [Fe(Dbf)(μ-NHCHF)(NHCHF)] () was generated, prompting the isolation of the analogous bridging amide terminal alkoxide [Fe(Dbf)(μ-NHCHF)(OCH)] () and the asymmetric pyridine-bound diiron imido [Fe(Dbf)(μ-NCHF)(NCH)] ().

T. Muris Infection Dynamics of a Fresh, Wild Isolate: Is the Established E Isolate Still Relevant?

For decades, parasitic worms such as Trichuris muris have been maintained in laboratory animals, providing insights into host-parasite interactions and host immune responses. The most used T. muris isolate is the E isolate, established in the laboratory in 1954.

Phosphorylation-driven epichaperome assembly is a regulator of cellular adaptability and proliferation.

The intricate network of protein-chaperone interactions is crucial for maintaining cellular function. Recent discoveries have unveiled the existence of specialized chaperone assemblies, known as epichaperomes, which serve as scaffolding platforms that orchestrate the reconfiguration of protein-protein interaction networks, thereby enhancing cellular adaptability and proliferation. This study explores the structural and regulatory aspects of epichaperomes, with a particular focus on the role of post-translational modifications (PTMs) in their formation and function.