Although most tissues in an organism are genetically identical, the biochemistry of each is
optimized to fulfill its unique physiological roles, with important consequences for human …

Despite the diverse biological pathways known to be regulated by ubiquitylation, global
identification of substrates that are targeted for ubiquitylation has remained a challenge. To …

Protein interactions form a network whose structure drives cellular function and whose
organization informs biological inquiry. Using high-throughput affinity-purification mass …

The physiology of a cell can be viewed as the product of thousands of proteins acting in
concert to shape the cellular response. Coordination is achieved in part through networks of …

Multiplexed quantitation via isobaric chemical tags (eg, tandem mass tags (TMT) and
isobaric tags for relative and absolute quantitation (iTRAQ)) has the potential to revolutionize …

Quantitative mass spectrometry–based proteomics is highly versatile but not easily
multiplexed. Isobaric labeling strategies allow mass spectrometry–based multiplexed proteome …

Thousands of interactions assemble proteins into modules that impart spatial and functional
organization to the cellular proteome. Through affinity-purification mass spectrometry, we …

Fewer than half of all tandem mass spectrometry (MS/MS) spectra acquired in shotgun
proteomics experiments are typically matched to a peptide with high confidence. Here we …

Protein phosphorylation modulates a myriad of biological functions, and its regulation is
vital for proper cellular activity. Mass spectrometry is the enabling tool for phosphopeptide …

Multiplexed quantitative analyses of complex proteomes enable deep biological insight.
While a multitude of workflows have been developed for multiplexed analyses, the most …