Project description:Proteomic data from mouse lung; Treated with wild-type and mutant H7N9 and mockulum; Time points 1, 2, 4 & 7 days; 5 biological replicates
Project description:Data includes proteomics analysis of P450-ABP (2EN, ATW8, ATW12), FP-2, and ATP-ABP labeled mouse lung lysate S9. Lungs from the following developmental stages were used in the study: gestational day 17, post natal days 0, 21, and 42. Also included are global analyses of the same mice lungs.
Project description:Lipidomics, proteomics and metabolomics characterization of the ontogeny of lipid, protein and metabolite changes during normal postnatal lung development
Project description:Metabolomics data from mouse lung; Treated with wild-type and mutant H7N9 and mockulum; Time points 1, 2, 4 & 7 days; 5 biological replicates
Project description:Proteomic data from mouse lung; Treated with wild-type and mutant H7N9 and mockulum; Time points 1, 2, 4 & 7 days; 5 biological replicates
Project description:Lipidomics data from mouse lung; Treated with wild-type and mutant H7N9 and mockulum; Time points 1, 2, 4 & 7 days; 5 biological replicates
Project description:Identification of human proteins targeted by Citrobacter secreted effectors by affinity purification followed by mass spectrometry.
Project description:We have developed a quantitative chemical probe approach for live cell labeling of proteins that are sensitive to redox modifications. We utilize this in vivo strategy coupled to mass spectrometry-based proteomics to identify 176 proteins undergoing ~5-10 fold dynamic redox change in response to nutrient limitation and subsequent replenishment in the photoautotrophic cyanobacterium, Synechococcus sp. PCC 7002. This method enables the identification of redox changes in as little as 30 seconds after nutrient perturbation, and oscillations in reduction and oxidation for 60 minutes following the perturbation. The redox changes were validated by demonstrating that protein abundances did not change per global proteomic analyses. Peptides identified by MS for global and probe-labeled samples were required to be at least six amino acids in length having a mass spectra generating function score of <=1E-10, which corresponds to an FDR of <1%. Additionally, only peptides unique in identifying a single protein were utilized to estimate protein abundances, and proteins represented by <2 unique peptides were removed. This resulted in the identification of 176 redox probe labeled protein identifications, and 808 protein identifications in the global data.