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 …

This review focuses on one family of the known cAMP receptors, the exchange proteins
directly activated by cAMP (EPACs), also known as the cAMP-regulated guanine nucleotide …

The surface comparison of different serine–threonine and tyrosine kinases reveals a set of
30 residues whose spatial positions are highly conserved. The comparison between active …

cAMP‐mediated signaling pathways regulate a multitude of important biological processes
under both physiological and pathological conditions, including diabetes, heart failure and …

Structures of set of serine-threonine and tyrosine kinases were investigated by the recently
developed bioinformatics tool Local Spatial Patterns (LSP) alignment. We report a set of …

Cellular signal transmission requires the dynamic formation of spatiotemporally controlled
molecular interactions. At the cell surface information is received by receptor complexes and …

Cyclic adenosine monophosphate (cAMP) signaling integrates information from diverse G-
protein-coupled receptors, such as neuromodulator receptors, to regulate pivotal biological …

The mycobacterial repressor, DarR, a TetR family regulator (TFR), was the first transcription
regulator shown to bind c-di-AMP. However, the molecular basis for this interaction and the …

Protein kinase A (PKA) holoenzyme is one of the major receptors for cyclic adenosine
monophosphate (cAMP), where an extracellular stimulus is translated into a signaling …

The 2.0-angstrom structure of the cyclic adenosine monophosphate (cAMP)–dependent
protein kinase (PKA) catalytic subunit bound to a deletion mutant of a regulatory subunit …