Assessing posttranslational modification (PTM) patterns within protein molecules and
reading their functional implications present grand challenges for plant biology. We combine …

Several mechanisms have been proposed for histone marks to exert their functions,
including altering the physical properties of nucleosomes by neutralization of charge via …

Histidine phosphorylation, the so-called hidden phosphoproteome, is a poorly characterized
post-translational modification of proteins,. Here we describe a role of histidine …

Site-selective bioconjugation to native protein residues is a powerful tool for protein
functionalization, with cysteine and lysine side chains being the most common points for …

Reversible phosphorylation is the most widespread posttranslational protein modification,
playing regulatory role in almost every aspect of cell life. The majority of protein …

Highlights•Classical site-directed mutagenesis is limited in studying protein
phosphorylation.•We discuss synthetic, semisynthetic, and genetic methods to make …

Protein phosphorylation serves as a primary mechanism of signal transduction in the cells of
biological organisms. Technical advancements over the last several years in mass …

Protein phosphorylation is one of the most common and extensively studied
posttranslational modifications (PTMs). Compared to the O-phosphorylation of Ser, Thr, and …

In this paper, we presented a novel, rapid and highly sensitive sensor for glutathione (GSH),
cysteine (Cys) and histidine (His) based on the recovered fluorescence of the carbon …

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