Identification of Kinases and Interactors of p53 Using Kinase-Catalyzed Cross-Linking and Immunoprecipitation.

Kinase enzymes phosphorylate protein substrates in a highly ordered manner to control cell signaling. Unregulated kinase activity is associated with a variety of disease states, most notably cancer, making the characterization of kinase activity in cells critical to understand disease formation. However, the paucity of available tools has prevented a full mapping of the substrates and interacting proteins of kinases involved in cellular function.

A comparative study of ATP analogs for phosphorylation-dependent kinase-substrate crosslinking.

Kinase-catalyzed protein phosphorylation is an important post-translational modification that regulates a variety of cellular functions. Identification of the many substrates of a specific kinase is critical to fully characterize cell biology. Unfortunately, kinase-substrate interactions are often transient, which makes their identification challenging.

Structural analysis of ATP analogues compatible with kinase-catalyzed labeling.

Kinase-catalyzed protein phosphorylation is an important biochemical process involved in cellular functions. We recently discovered that kinases promiscuously accept γ-modified ATP analogues as cosubstrates and used several ATP analogues as tools for studying protein phosphorylation. Herein, we explore the structural requirements of γ-modified ATP analogues for kinase compatibility.

Design and synthesis of bistereogenic chiral ionic liquids and their use as solvents for asymmetric Baylis-Hillman reactions.

Three novel chiral ionic liquids (CILs) containing two chiral centers in the side chain bonded to the 2-position of the imidazolium cation and different anions have been synthesized, characterized and used as chiral solvents for asymmetric Baylis-Hillman (BH) reactions; good yields and fair enantioselectivities were obtained.