Phosphorylation events on proteins during growth and stress/starvation can represent
crucial regulation processes inside the bacterial cell. Therefore, serine, threonine and …

Staphylococcus aureus is an important human pathogen responsible for a variety of
infections including skin and soft tissue infections, endocarditis, and sepsis. The …

Increasing evidence shows that protein phosphorylation on serine (Ser), threonine (Thr) and
tyrosine (Tyr) residues is a major regulatory post‐translational modification in the bacteria …

In this study, the in vitro and in vivo functions of the only two identified protein phosphatases,
Saci-PTP and Saci-PP2A, in the crenarchaeal model organism Sulfolobus acidocaldarius …

Abstract The serine (Ser)/threonine (Thr)/tyrosine (Tyr) phosphoproteome of exponentially
growing Streptomyces coelicolor A3 (2) was analysed using the gel‐free approaches of …

Understanding phosphorylation-mediated regulation of metabolic enzymes, pathways, and
cell phenotypes under metabolic shifts represents a major challenge. The kinases …

Phosphorylation is a posttranslational modification that can affect both housekeeping
functions and virulence characteristics in bacterial pathogens. In the Gram-positive …

Reversible protein phosphorylation, regulated by protein kinases and phosphatases,
mediates a switch between protein activity and cellular pathways that contribute to a large …

Reversible protein phosphorylation at serine, threonine and tyrosine is a well-known
dynamic post-translational modification with stunning regulatory and signalling functions in …

Listeria monocytogenes is the causative agent of listeriosis, a very serious food-borne
human disease. The analysis of the proteins coded by the L. monocytogenes genome …