The endoplasmic reticulum (ER) is an important site for protein folding and maturation in
eukaryotes. The cellular requirement to synthesize proteins within the ER is matched by its …

Eukaryotic protein kinases are key regulators of cell processes. Comparison of the structures
of protein kinase domains, both alone and in complexes, allows generalizations to be made …

Protein kinases have emerged as one of the most successful families of drug targets. To
date, most selective kinase inhibitors have been discovered serendipitously either through …

Aberrant folding of proteins in the endoplasmic reticulum activates the bifunctional
transmembrane kinase/endoribonuclease Ire1. Ire1 excises an intron from HAC1 messenger …

Phosphorylation of proteins is a ubiquitous mechanism of regulating their function,
localization, or activity. Protein kinases, enzymes that use ATP to phosphorylate protein …

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 …

Ire1 (Ern1) is an unusual transmembrane protein kinase essential for the endoplasmic
reticulum (ER) unfolded protein response (UPR). Activation of Ire1 by association of its N …

Tank-binding kinase (TBK) 1 plays a central role in innate immunity: it serves as an
integrator of multiple signals induced by receptor-mediated pathogen detection and as a …

The epidermal growth factor receptor (EGFR) is a key protein in cellular signaling, and its
kinase domain (EGFR kinase) is an intensely pursued target of small-molecule drugs …

Tank-binding kinase 1 (TBK1) serves as an important component of multiple signaling
pathways. While the majority of research on TBK1 has focused on its role in innate immunity …