Uranyl Binding to Proteins and Structural-Functional Impacts

Structural and functional analysis of fatty acid-binding proteins.

The mammalian FA-binding proteins (FABPs) bind long-chain FA with high affinity. The large number of FABP types is suggestive of distinct functions in specific tissues. Multiple experimental approaches have shown that individual FABPs possess both unique and overlapping functions, some of which are based on specific elements in the protein structure. Although FA binding affinities for all FABPs...

Fatty acid-binding proteins: structural and functional diversity.

Introduction Fatty acids are important molecules for all cells either as energy-delivering substrates or as precursors for synthesis of membrane lipids and lipid mediators such as thromboxanes, prostaglandins and leukotrienes, and for protein acylation. Fatty acids may directly or indirectly interact with membranes, transporters, ion channels, enzymes or hormone receptors [ l , 21. Fatty acids ...

Selectivity in ligand binding to uranyl compounds: A synthetic, structural, thermodynamic and computational study

Pipit: visualizing functional impacts of structural variations

SUMMARY Pipit is a gene-centric interactive visualization tool designed to study structural genomic variations. Through focusing on individual genes as the functional unit, researchers are able to study and generate hypotheses on the biological impact of different structural variations, for instance, the deletion of dosage-sensitive genes or the formation of fusion genes. Pipit is a cross-platf...

BINDING OF NAPROXEN TO SERUM PROTEINS IN PATIENTS WITH LIVER CIRRHOSIS AND HEALTHY INDIVIDUALS

A three-fold decrease of the in vitro ability of serum proteins to bind naproxen was shown in patients with cirrhosis of the liver compared to healthy individuals. This decrease was caused by quantitative changes in serum proteins in the sera of patients with liver damage. Lower doses of naproxen are therefore suggested in the treatment of patients with liver dysfunction.