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.

附加文件1：表S1 1分钟与15分钟时间点下具有显著倍数变化的肽段磷酸化蛋白质组学数据。表S2 本研究、CXCR4-HIV信号通路及HIV-1人类蛋白质相互作用数据库中共同鉴定获得的蛋白质。表S3 针对HIV响应性磷酸化蛋白质的富集REACTOME通路的生物信息学分析数据。表S4 HIV响应性磷酸化蛋白质的聚类通路富集分析数据。表S5 激酶抑制剂对原代CD4+ T细胞中HIV-1融合、感染及进入后效率的影响。表S6 未处理的蛋白质组学原始数据。表S7 按变异系数（coefficient of variation, CV）筛选得到的磷酸化蛋白质组学数据。表S8 经假发现率（false discovery rate, FDR）校正计算的磷酸化蛋白质组学数据。表S9 来自磷酸化蛋白质组学数据的激酶-底物富集分析（Kinase-Substrate Enrichment Analysis, KSEA）得分数据。表S10 用于激酶-底物富集分析（KSEA）的数据集。