Pulsed Stable Isotope labeling of amino acid has been used to study host-cell function, survival, the precise intracellular pathways in protein synthesis of HIV-1 infected human monocytederived macrophages. Identification of viral proteins from coronavirus infectious bronchitis-infected cells has been achieved with Stable Isotope labeling in conjunction with LC-MS/MS.
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Import and oxidative folding of proteins in the mitochondrial intermembrane space differ among eukaryotic lineages. While opisthokonts such as yeast rely on the receptor and oxidoreductase Mia40 in combination with the Mia40:cytochrome c oxidoreductase Erv, kinetoplastid parasites and other Excavata/Discoba
Virus-host interactions involve complex interplay between viral and host factors, rendering them an ideal target for proteomic analysis. Here we detail a high throughput quantitative proteomics analysis of Vero cells infected with the coronavirus infectious bronchitis virus (IBV), a positive
Journal of proteome research, 10(6), 2852-2862 (2011-04-20)
Dynamic interactions between human immunodeficiency virus-1 (HIV-1) and the macrophage govern the tempo of viral dissemination and replication in its human host. HIV-1 affects macrophage phenotype, and the macrophage, in turn, can modulate the viral life cycle. While these processes
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