Quantitative proteomics has traditionally been performed by two-dimensional gel electrophoresis,
but recently, mass spectrometric methods based on stable isotope quantitation have …

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

… To bypass receptor-induced dimerization, we fused MyD88 or the TRAF6 effector domain
to subunit B of Escherichia coli DNA gyrase (GyrB; Fig. 1a and Supplementary Fig. 1a), which …

Mass spectrometry–based proteomics 1 can reveal protein-protein interactions on a large
scale 2 , 3 , but it has been difficult to separate background binding from functionally important …

To study the global dynamics of phosphotyrosine-based signaling events in early growth
factor stimulation, we developed a mass spectrometric method that converts temporal changes …

… cells by cotransfecting PDGFR along with c-Cbl or Cbl-b (fig. S3), supporting our finding that
at least in some cell types Cbl-b is the Cbl ubiquitin ligase downstream of PDGF receptors. …

To elucidate cellular events underlying the pluripotency of human embryonic stem cells (hESCs),
we performed parallel quantitative proteomic and phosphoproteomic analyses of …

… of the peptides from the sample analyzed by MALDI in B. V shows a peak corresponding to
Vav-… shown as well as one from the B series (N-terminal fragments; b 2 ). The sequence of the …

Ubiquitination is a post-translational modification (PTM) that is essential for balancing
numerous physiological processes. To enable delineation of protein ubiquitination at a site-…

During recent years, increased efforts have focused on elucidating the secretory function of
skeletal muscle. Through secreted molecules, skeletal muscle affects local muscle biology in …