MassIVEapplication/xmlftp://massive.ucsd.edu/v01/MSV000079524/primaryOK2000000ProteomicsJacob D. JaffeQ ExactiveHomo Sapiens (ncbitaxon:9606)https://massive.ucsd.edu/ProteoSAFe/dataset.jsp?task=8d3f2ad7ccb0413c961580bf6d8fa686MassIVE864UNIMOD:21 - "Phosphorylation."SILAC-R-0,6,10-K-0,4,8M-oxidationC-carbamidomethylprojections, DmelCG6944, IPP2A2, DmLamin, nip, AW046674, LamDm[[0]], 5730420M11Rik, dmTAF[[II]]230, diseases, B1, l(2)SH1330, pathogenesis, diseases and disorders, present in fewer numbers in organism, lymphangio-myomatosis, strong, SET, human disease, lamin Dm0, Gene Expressions, TFIID TAF250, cel, TAF-I, 74/76, phosphatase 2A inhibitor I2PP2A, hypoplasia, 35Bb, nlam, DM[[O]], genetic, DmelCG4299, set, IGAAD, FBgn0002526, decreased, DmelCG10574, scientific observation, papilla, signaling process, D5, 2459, Lamin Dm[[0]], Homo sapiens disease, Lam(Dm0), single organism signaling, phapii, dTAF[[II]]230, anatomical protrusion, lamina, familial, TAF200, flanges, StF-IT-1, DmelCG10236, 5]], TAFII-250, somatic, TAF250/230, lamin, any method, TAFII250, Dm0, l(2)br3, l35Bb, Dm2, Dm1, Dm, shelf, Diseases, jf27, CG6944, END, Dm[[2]], misg, DmO, HLA-DR-associated protein II, DI-2, LM-A/alpha1, alpha[[3, shelves, I-2Dm, cArr, lamDm[[0]], common, CG4299, inhibitor of granzyme A-activated DNase, CG17603, TAF[[II]], projection, ridge, l(2)SH2 1330, I-2PP1, Phenotypes, disease, Cone arrestin, Dmo, TAF-IBETA, Taf250, spine, SR3-5, inherited genetic, TAF-Ibeta, BG:DS01219.1, i2pp2a, TAF230, B130007O04Rik, Lam[[Dm0]], other disease, d230, biological signaling, 5430428I19, mol, Peptidomics, lamellae, CT28769, Gene, dTAFII250, EfW1, DmelCG4482, process of organ, PHAPII, protrusion, lamella, protein amino acid phosphorylation, Dm(0), reduced, template-activating factor I, resilient, dmTAF1, Taf230, subnumerary, disease or disorder, Dm[[0]], tiny, TSC4, l(2)br23, TAF250, alpha3/5, Taf200, dTAF[[II]]250, cell, hdln, ipp2a2, X-arrestin, l(2)gdh-7, 2pp2a, Taf1p, ridges, causes, decreased number, Expressions, study assay, CG10574, non-neoplastic, dTAF250, pulmonary lymphangioleiomyomatosis, 2PP2A, laminin alpha3/5, taf-ibeta, causality, Lam-A, dSET, dSet, Retinal cone arrestin-3, disorder, Expression, Lan, TAF, Lam, LAM, laminae, constitutitional genetic, Dm[[1]], HHT1, CG10236, small, measuring, data, TAF[[II]]250, adequate, CG4482, anatomical process, Dm[[mit]], l(2)35Bb, disorders, igaad, l(3)84Ab, tough., l(2)25Ec, BG:DS00004.13, medical condition, lam, lamA, lymphangioleiomyomatosis, Cell, LamDm[[o]], dTAF230, TSC, l(2)04643, Phosphopeptide, I-2PP2A, lung lymphangioleiomyomatosis, p230, Dm I-2, I2PP2A, TAF[[II]]250/230, TFIID, condition, Dm[[o]], flange, organ process, Taf[[II]]250, lymphangiomyomatosis, Lam A, TAF[[II]]230, l(2)jf27, underdeveloped, C-arrestin, PPP1R160, TAF[II]250, CG15268, lamDm0, Lamp, signalling, br3, processes, process, l(2)gdh7, dSET/TAF-Ibeta, 2610030F17Rik, D930023J12Rik, DmelCG17603, signalling process, Lam Dm[[0]], LamA, processus, lamin Dm[[0]], NIP, ORW1, AA407739, lanA, hereditary, TAF1small, count in organism, presence or absence in organism., decreased, reduced, underdeveloped, subnumerary, number, hypoplasia, tiny, quantitative, decreased number, present in fewer numbers in organism, presence0PXD003679trueReduced-representation Phosphosignatures Measured by Quantitative Targeted MSAbelin JG, Patel J, Lu X, Feeney CM, Fagbami L, Creech AL, Hu R, Lam D, Davison D, Pino L, Qiao JW, Kuhn E, Officer A,Li J, Abbatiello S, Subramanian A, Sidman R, Snyder E, Carr SA, Jaffe JD. Mol Cell Proteomics, 2016. Profiling posttranslational modifications represents an alternative dimension to gene expression data in characterizing cellular processes, as genetic processes alone are not sufficient to explain the entirety of biochemical mechanisms or disease etiology. For example, some cellular phenotypes resulting from chemical perturbations are partially or entirely mediated by changes in cell signaling through protein phosphorylation. To access this dimension of cellular information, we sought to develop a common platform on which cellular phosphosignaling responses could be profiled across thousands of samples. To this end, we developed a targeted MS assay that profiles a reduced-representation set of phosphopeptides that we show to be strong indicators of cellular responses to chemical perturbagens. Tue Feb 23 11:22:00 GMT 2016MSV000079524