Eukayotic protein kinases evolved as a family of highly dynamic molecules with strictly
organized internal architecture. A single hydrophobic F-helix serves as a central scaffold for …

Protein kinases are dynamic molecular switches that have evolved to be only transiently
activated. Kinase activity is embedded within a conserved kinase core, which is typically …

Although most tissues in an organism are genetically identical, the biochemistry of each is
optimized to fulfill its unique physiological roles, with important consequences for human …

Protein kinases are dynamically regulated signaling proteins that act as switches in the cell
by phosphorylating target proteins. To establish a framework for analyzing linkages between …

The first protein kinase structure, solved in 1991, revealed the fold that is shared by all
members of the eukaryotic protein kinase superfamily and showed how the conserved …

Protein kinases have evolved in eukaryotes to be highly dynamic molecular switches that
regulate a plethora of biological processes. Two motifs, a dynamic activation segment and a …

Eukaryotic protein kinases (EPKs) control most biological processes and play central roles
in many human diseases. To become catalytically active, EPKs undergo conversion from an …

The quest for ever more selective kinase inhibitors as potential future drugs has yielded a
large repertoire of chemical probes that are selective for specific kinase conformations …

A new model of kinase regulation based on the assembly of hydrophobic spines has been
proposed. Changes in their positions can explain the mechanism of kinase activation. Here …

TOR and PKA signaling are the major growth-regulatory nutrient-sensing pathways in S.
cerevisiae. A number of experimental findings demonstrated a close relationship between …