Protein phosphorylation is a covalent post-translational modification event that is essential for regulation and maintenance of most biological processes in eukaryotes 1. Conventionally ...

each containing a fixed serine or threonine residue and another fixed amino acid in one of nine flanking positions 4. However, unlike with the OPAL approach, the phosphorylation reactions were ...

The team uncovered the role of phosphorylation at the 881st threonine residue (Thr881) of the plasma membrane proton pump in response to red and blue light in this process. This research opens up ...

Much of this control is via protein phosphorylation. MAP kinase is activated by dual phosphorylation at tyrosine and threonine residues, occurring in a TEY motif, catalyzed by a protein- ...

J. Raingeaud, S. Gupta, J.S. Rogers, M. Dickens, J. Han, R.J. Ulevitch, R.J. Davis, "Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual ...

The emergence of pseudokinases and pseudophosphatases has made phosphorylation cascades even more complicated. My lab focuses on various functional characteristics of the pseudophosphatase map kinase ...

In the PamStation®12 system, active kinases within a cellular/tissue lysate will phosphorylate specific peptide substrates within the microarray which survey the particular kinome (tyrosine or ...

kinase that selectively targets and inhibits ATR activity and blocks the downstream phosphorylation of the serine/threonine protein kinase checkpoint kinase 1 (CHK1). Lloyd Segal, president of ...