MOESM1 of Global phosphoproteomics of CCR5-tropic HIV-1 signaling reveals reprogramming of cellular protein production pathways and identifies p70-S6K1 and MK2 as HIV-responsive kinases required for optimal infection of CD4+ T cells

Additional file 1: Table S1. Phosphoproteomics data for peptides with large fold-changes at the 1- and 15- minute time points. Table S2. Shared proteins identified in the current study, CXCR4-HIV signaling, and the HIV-1 human protein interaction database. Table S3. Bioinformatic analysis of REACTOME pathways enriched for HIV-responsive phosphoproteins. Table S4. Cluster pathway enrichment analysis of HIV-responsive phosphoproteins. Table S5. Effects of kinase inhibitors on HIV-1 fusion, infection, and post-entry efficiency in primary CD4+ T cells.Table S6. Unprocessed proteomics data. Table S7. Phosphoproteomics data filtered by coefficient of variation (CV). Table S8. Phosphoproteomics data processed for false discovery rate (FDR) calculations. Table S9. Kinase-substrate enrichment analysis (KSEA) scores from phosphoproteomics data. Table S10. Dataset used for kinase-substrate enrichment analysis (KSEA) analysis

MOESM1 of HIV signaling through CD4 and CCR5 activates Rho family GTPases that are required for optimal infection of primary CD4+ T cells

Additional file 1: Table 1. Small molecule inhibitors tested with the combination reporter virus system. All compounds were initially tested with an assigned identifier (left column) to remove result bias. Listed half-maximal inhibitory concentrations (IC50) were compiled from previously published studies