Structural characterization of autoinhibited c-Met kinase produced by coexpression in bacteria with phosphatase.

Protein kinases are a large family of cell signaling mediators undergoing intensive research to identify inhibitors or modulators useful for medicine. As one strategy, small-molecule compounds that bind the active site with high affinity can be used to inhibit the enzyme activity. X-ray crystallography is a powerful method to reveal the structures of the kinase active sites, and thus aid in the design of high-affinity, selective inhibitors.

Stable drop shapes under disjoining pressure. II. Multiplicity and stability.

The stability of the contact line region as affected by the disjoining pressure has been analyzed by solving the augmented Young-Laplace equation. Because of the results in Part I (Zhang, X., Neogi, P.

Full and partial deuterium solvent isotope effect studies of alpha-thrombin-catalyzed reactions of natural substrates.

Proton inventory studies of the thrombin-catalyzed fibrinogen activation to fibrinopeptide A are most consistent with a two-proton bridge forming at the transition state probably between Ser195 OgammaH and His57 Nepsilon2 and His57 Ndelta1 and Asp102 COObeta- at the active site, with fractionation factors 0.66 +/- 0.03 under enzyme saturation with substrate and 0.

Safety and patient tolerance of standard and slow-release formulations of NSAIDs.

Objective: To examine the rates of co-prescribing of gastro-protective drugs (GPDs) and the frequency of gastrointestinal (GI) investigations associated with standard and slow-release (SR) formulations of nonsteroidal antiinflammatory drugs (NSAIDs).

Methods: Patients were identified from the MediPlus database, which contains the medical records of some 2 million patients throughout the United Kingdom. We selected all new NSAID users who received at least one prescription between 1 July 1997 and 31 December 1997.