Protein phosphorylation is a key posttranslational modification, which reversibly regulates
almost all processes in the living cell. Deregulated signaling is a hallmark of cancer and other …

… Similarly, the serine/threonine kinase PrkC from B. subtilis was found to phosphorylate
the response regulator WalR 28 . Both of these phosphorylation events occur on threonine …

Cell signaling mechanisms often transmit information via posttranslational protein modifications,
most importantly reversible protein phosphorylation. Here we develop and apply a …

Mass accuracy is a key parameter of mass spectrometric performance. TOF instruments can
reach low parts per million, and FT-ICR instruments are capable of even greater accuracy …

Peptide sequencing is the basis of mass spectrometry–driven proteomics. Here we show
that in the linear ion trap–orbitrap mass spectrometer (LTQ Orbitrap) peptide ions can be …

… adaptor of the IκB kinases (IKKs) and subsequent activation of NF-κB signalling, whereas
SHARPIN deficiency in mice causes an impaired activation of the IKK complex and NF-κB in B …

… In 2007, the first site-specific bacterial phosphoproteome was published for the bacterium B.
subtilis, using a gel-free approach coupled with high-accuracy mass spectrometry (Macek et …

… We thank B. Valent and CH Khang for alerting us to the fact that Magnaporthe grisea possesses
a secreted chorismate mutase, and are grateful to M. Dickman for allowing us to cite his …

Protein phosphorylation on serine, threonine, and tyrosine (Ser/Thr/Tyr) is generally
considered the major regulatory posttranslational modification in eukaryotic cells. Increasing …

… (c) Extends set b by one dimension that contains the predicted accessibility. (d) Extends
set a by three dimensions that reflect the conservation of the phosphosite in mammals and …