Robert J. Chalkley

TL;DR: The PX submission tool simplifies the process of submitting data to PRIDE by automating the very labor-intensive and therefore time-heavy and expensive process of manually downloading and editing files.

TL;DR: Methods for direct enrichment and identification of in vivo O-GlcNAc-modified peptides through lectin weak affinity chromatography (LWAC) and mass spectrometry are reported and suggest specific roles for O- GlcNAC modification in synaptic transmission, establish a basis for site-specific regulatory studies, and provide methods that will facilitate O- GloverNAc proteome analysis across a wide variety of cells and tissues.

TL;DR: A protocol has been established that combines the differential profiling strength of a new cleavable 13C isotope-coded affinity tag (cICAT) reagent with the high sequence coverage provided by multidimensional liquid chromatography and two modes of tandem mass spectrometry to identify and compare the protein content of very low quantity samples of high complexity.

TL;DR: A robust, high-sensitivity strategy able to assign O-GlcNAcylation sites of native modified peptides using electron transfer dissociation mass spectrometry is described, which fulfills a long-standing need in the biological community by facilitating modification site identifications that will accelerate understanding of the biological significance of this elusive regulatory posttranslational modification.

TL;DR: Results indicate that O-GlcNAcylation serves as a metabolic sensor for clock regulation and works coordinately with phosphorylation to fine-tune circadian clock.