Higher-order QED effects in hadronic processes

In this presentation, we describe the computation of higher-order QED effects relevant in hadronic collisions. In particular, we discuss the calculation of mixed QCD-QED one-loop contributions to the Altarelli-Parisi splittings functions, as well as the pure two-loop QED corrections. We explain how to extend the DGLAP equations to deal with new parton distributions, emphasizing the consequences of the novel corrections in the determination (and evolution) of the photon distributions.Comment: 7 pages, 2 figures. Contribution to the Proceedings of the EPS-HEP 2017 Conferenc

Additional file 2: of A precision therapeutic strategy for hexokinase 1-null, hexokinase 2-positive cancers

Table S1. The list of 119 FDA-approved oncology drugs provided by the National Cancer Institute (NCI) tested for synergy with DOX treatment in Hep3B/shHK2DOX cells. Table S2. Synergy between HK2 inhibition and DPI. (DOCX 44 kb

Additional file 1: of A precision therapeutic strategy for hexokinase 1-null, hexokinase 2-positive cancers

Figure S1. HK1−HK2+ cancer cells are highly sensitive to HK2 knockdown-induced growth inhibition. Figure S2. DPI synergizes with HK2 knockdown or inhibition in HK1−HK2+ liver cancer cells. Figure S3. DPI synergizes with HK2 silencing/inhibition by targeting mitochondrial complex I in HK1−HK2+ liver cancer cells. Figure S4. HK isoform expression in Hep3B/shHK2DOX xenograft tumors with DOX and/or DPI treatments. Figure S5. Inhibition of fatty acid oxidation sensitizes HK1−HK2+ liver cancer cells to the HK2 inhibition/DPI combination. Figure S6. Modulation of HK1−HK2+ liver cancer cellular metabolism by the HK2i/DPI/PER combination. Figure S7. PER as a single agent does not have a significantly detectable effect on growth of subcutaneous Hep3B/shHK2DOX tumors. (PPTX 782 kb

Additional file 8: of Metabolic characterization of isocitrate dehydrogenase (IDH) mutant and IDH wildtype gliomaspheres uncovers cell type-specific vulnerabilities

IDH1 mutant overexpression leads to high levels of 2-HG and the c227 inhibitor is an effective inhibitor of 2-HG formation. IDH wildtype gliomaspheres transduced with the IDH1 mutant enzyme (308 + IDH1mut) and endogenous IDH1 mutant cells treated with 5 μM c227 inhibitor (213 + c227) for 24 h are compared to their respective controls (308 and 213) for 2-HG levels as determined by LC-MS. Data represent the means ± SEM of three replicates per condition. (PDF 22 kb

Additional file 9: of Metabolic characterization of isocitrate dehydrogenase (IDH) mutant and IDH wildtype gliomaspheres uncovers cell type-specific vulnerabilities

IDH1 mutant enzyme does not affect glucose labeling of nucleotide precursors. Cells were treated and analyzed as described for Supporting Figure S4 in order to determine the percent labeling of nucleotide precursors. There is no significant difference when comparing IDH1 mutant overexpression or endogenous mutant inhibition to their respective controls. (PDF 64 kb

Additional file 6: of Metabolic characterization of isocitrate dehydrogenase (IDH) mutant and IDH wildtype gliomaspheres uncovers cell type-specific vulnerabilities

Glucose labeling of metabolites. Glucose fractional contribution was computed for all 159 metabolites. Metabolites that were significantly different between groups (uncorrected t test p < 0.05) are shown here. (PDF 137 kb

Additional file 8: of Metabolic characterization of isocitrate dehydrogenase (IDH) mutant and IDH wildtype gliomaspheres uncovers cell type-specific vulnerabilities

IDH1 mutant overexpression leads to high levels of 2-HG and the c227 inhibitor is an effective inhibitor of 2-HG formation. IDH wildtype gliomaspheres transduced with the IDH1 mutant enzyme (308 + IDH1mut) and endogenous IDH1 mutant cells treated with 5 μM c227 inhibitor (213 + c227) for 24 h are compared to their respective controls (308 and 213) for 2-HG levels as determined by LC-MS. Data represent the means ± SEM of three replicates per condition. (PDF 22 kb

Additional file 7: of Metabolic characterization of isocitrate dehydrogenase (IDH) mutant and IDH wildtype gliomaspheres uncovers cell type-specific vulnerabilities

Radiation leads to low levels of TUNEL staining in gliomaspheres. Representative images and quantification of cells stained for TUNEL positivity 4 days after exposure to increasing doses of radiation. There is no significant difference between groups. Error bars represent ¹ SEM. (PDF 2212 kb

Additional file 1: of Metabolic characterization of isocitrate dehydrogenase (IDH) mutant and IDH wildtype gliomaspheres uncovers cell type-specific vulnerabilities

Patient-derived gliomasphere culture characteristics. Relevant patient information and clinical characteristics for the primary, patient-derived gliomasphere cultures used in this study. Summary of selected copy-number alterations and mutations are also shown. (PDF 42 kb

Additional file 10: of Metabolic characterization of isocitrate dehydrogenase (IDH) mutant and IDH wildtype gliomaspheres uncovers cell type-specific vulnerabilities

Effects of pharmacologic inhibition of the IDH1 mutant enzyme on TCA cycle intermediates. Cells were analyzed as described in Supporting Figure S5. Left: Metabolites with significantly different percent glucose labeling of metabolites in the endogenous IDH1 mutant line 213 treated with c227 inhibitor or control (p < 0.05). Right: Percent labeling from endogenous IDH1 mutant and IDH wildtype groups for metabolites that were not significantly different. (PDF 206 kb