Additional file 2 of Correction to: Phospho-heavy-labeled-spiketide FAIMS stepped-CV DDA (pHASED) provides real-time phosphoproteomics data to aid in cancer drug selection

Additional file 2: Table S1. SBDS heavy-labeled phosphorylated peptide standards. Table S2. Common and unique phosphoproteins identifed across all four CVs based on PSM acquisition. Table S3. High confdence modifcation sites identifed in LFQ (p < 0.01). Table S4. High confdence modifcation sites identifed in pHASED (p < 0.01). Table S5. Unique and common phosphoproteins identifed in LFQ and pHASED datasets. Table S6. Phosphorylated master protein kinases identifed in LFQ dataset (p < 0.01). Table S7. Phosphorylated master protein kinases identifed in pHASED dataset (p < 0.01). Table S8. FLT3-D835 mutations associated with resistance to tyrosine kinase FLT3 inhibitors. Table S9. Kinase-Substrate analysis of LFQ dataset for resistant cells in comparison to FLT3-ITD (log2 fold change±0.5). Table S10. Kinase-Substrate analysis of pHASED data?set for resistant cells in comparison to FLT3-ITD (log2 fold change±0.5). Table S11. Canonical pathways identifed as signifcantly associated with LFQ dataset for resistant cells in comparison to FLT3-ITD. Table S12. Canonical pathways identifed as signifcantly associated with pHASED dataset for resistant cells in comparison to FLT3-ITD. Table S13. Kinase activity inferred by KSEA analysis of phosphorylation changes in pHASED dataset (log2±0.5, p≤0.05) for resistant cells in comparison to FLT3-ITD. Table S14. Mutation-specifc response to sorafenib. IC50 compared to FLT3-ITD. Table S15. Bliss Synergy scores for sorafenib in combination with KU-60019 at diferent doses. Table S16. Unique ATM substrates identifed with increased phosphorylation (log2≥0.5) in pHASED dataset for resistant cells in comparison to FLT3-ITD. Table S17. Vector mutations in FLT3 gene.

附加文件2：表S1。SBDS重标记磷酸化肽段标准品。
表S2。基于肽谱匹配（PSM，Peptide Spectrum Match）获取结果，在全部4个CV样本中鉴定得到的共有与特有磷酸化蛋白质。
表S3。无标记定量（LFQ，Label-Free Quantification）数据集内鉴定得到的高置信度修饰位点（p < 0.01）。
表S4。pHASED数据集内鉴定得到的高置信度修饰位点（p < 0.01）。
表S5。在LFQ与pHASED数据集中共鉴定得到的特有与共有磷酸化蛋白质。
表S6。LFQ数据集（p < 0.01）中鉴定得到的磷酸化核心蛋白激酶。
表S7。pHASED数据集（p < 0.01）中鉴定得到的磷酸化核心蛋白激酶。
表S8。与酪氨酸激酶FLT3抑制剂耐药相关的FLT3-D835突变。
表S9。相较于FLT3-ITD，耐药细胞LFQ数据集的激酶-底物分析结果（log₂倍变化±0.5）。
表S10。相较于FLT3-ITD，耐药细胞pHASED数据集的激酶-底物分析结果（log₂倍变化±0.5）。
表S11。相较于FLT3-ITD，耐药细胞LFQ数据集显著关联的经典通路鉴定结果。
表S12。相较于FLT3-ITD，耐药细胞pHASED数据集显著关联的经典通路鉴定结果。
表S13。针对耐药细胞相较于FLT3-ITD的pHASED数据集磷酸化变化，通过激酶-底物富集分析（KSEA，Kinase-Substrate Enrichment Analysis）推断的激酶活性结果（log₂±0.5，p≤0.05）。
表S14。索拉非尼的突变特异性响应：IC50与FLT3-ITD的对比数据。
表S15。不同剂量下索拉非尼与KU-60019联合使用的布利斯协同评分。
表S16。相较于FLT3-ITD，耐药细胞pHASED数据集中共鉴定得到的磷酸化水平上调（log₂≥0.5）的特有ATM底物。
表S17。FLT3基因的载体突变。