Analysis of a variety of properties of supramolecular aggregates in aqueous urea supports an explanation for the urea effect that differs from traditional explanations based on the direct mechanism of urea-water solvation or the indirect mechanism via rupture of the three-dimensional (3-D) structure of water. The urea-induced effects investigated are increases in amphiphile critical micelle concentrations, ionization degrees (alpha), and aggregation numbers; decreases in percolation thresholds of reversed micelles; expansion of minimum areas of monolayers; increases in the radii of gyration of polyelectrolytes; changes in morphologies of sodium bis-2-ethylhexylsulfosuccinate thin films on glass substrates; and direct evidence for urea-induced reduction in ion pairing. All of these effects are attributed to an urea-induced enhancement of the hydrophilic properties of water that results in more strongly solvated polar groups and ions and a. reduction in ion pair formation. The implications of this analysis for urea effects on protein 3-D structure are briefly highlighted.