This year (2012) marks the 50th anniversary of the discovery of protein histidine
phosphorylation. Phosphorylation of histidine (pHis) is now widely recognized as being …

Highlights•Histidine phosphorylation (pHis) is reversible by specific kinases and
phosphatases.•pHis is heat and acid labile, but stable under alkaline conditions.•Stable pHis …

Protein phosphorylation is a reversible post-translational modification. Nine of the 20 natural
amino acids in proteins can be phosphorylated, but most of what we know about the roles of …

Histidine phosphorylation is an important and ubiquitous post-translational modification.
Histidine undergoes phosphorylation on either of the nitrogens in its imidazole side chain …

Protein phosphorylation is an important post-translational modification that is an integral part
of cellular function. The O-phosphorylated amino-acid residues, such as phosphoserine …

It has been suggested that in mammalian cells histidine residues in proteins may become as
frequently phosphorylated as serine, threonine and tyrosine, and may play a key role in …

Histidine phosphorylation (pHis) is well studied in bacteria; however, its role in mammalian
signaling remains largely unexplored due to the lack of pHis-specific antibodies and the …

Protein histidine phosphorylation plays a crucial role in cell signaling and central
metabolism. However, its detailed functions remain elusive due to technical challenges in …

Protein histidine phosphorylation plays a vital role in cell signaling and metabolic processes,
and phosphohistidine (pHis) phosphatases such as protein histidine phosphatase 1 …

Protein phosphorylation is the most common type of post-translational modification in
eukaryotes. The phosphoproteome is defined as the complete set of experimentally …