| Autor: |
Yi Liu, Pingda Ren, Anjali Babbar, Sarah J. Firdaus, Jeffrey H. Chen, Tess Ely, Jun Feng, Jeff M. Kucharski, Yuching Chen, Linda V. Kessler, Ulf Peters, Rasmus Hansen, Lian-Sheng Li, Matthew R. Janes, Matthew P. Patricelli |
| Rok vydání: |
2023 |
| Popis: |
Supplementary Table 1. Biochemical and Cell engagement SAR. Supplementary Table 2. Data collection and refinement statistics (Molecular replacement). Supplementary Table 3. Selectivity of ARS-853 across KRAS isoforms and GTP vs. GDP states. Supplementary Table 5. Kinetics of intrinsic KRAS-G12C GTP hydrolysis/exchange at 37 oC. Supplementary Table 6. LC-MS/MS Target and standard peptide information. Supplementary Figure 1. Additional structural details from the ARS-853 bound KRAS-G12C crystal structure. Supplementary Figure 2. KRAS-G12C inhibitors block SOS and EDTA mediated nucleotide exchange. Supplementary Figure 3. Global cysteine reactivity profiling of ARS-853. Supplementary Figure 4. Effects of ARS-853 on long-term signaling and cell cycle. Supplementary Figure 5. Effects of ARS-853 on KRAS-mediated NIH-3T3 transformation. Supplementary Figure 6. Proliferation structure activity relationship across ARS-853 analogs. Supplementary Figure 7. Assessment of KRAS dependence and ARS-853 in 2D versus 3D assay formats. Supplementary Figure 8. Comparison of KRAS-G12C and off-target Reticulon-4 (RTN4) cell engagement profiles. Supplementary Figure 9. Schematic of the methods workflow for the RBD-MS assay and determination of percent RAS-GTP in cells and percent RAS abundance on RAF-RBD. Supplementary Figure 10. Time dependent reduction in GTP-bound KRAS-G12C following erlotinib treatment. Supplementary Figure 11. EGFR combinations augment the efficacy of ARS-853. Supplementary Figure 12. A, synthesis of ARS-107. B, synthesis of ARS-853. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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