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1. Zakut-Houri, R., Bienz-Tadmor, B., Givol, D., & Oren, M. (1985). Human p53 cellular tumor antigen: cDNA sequence and expression in COS cells. The EMBO journal, 4(5), 1251–1255. https://doi.org/10.1002/j.1460-2075.1985.tb03768.x 2. Lamb, P., & Crawford, L. (1986). Characterization of the human p53 gene. Molecular and cellular biology, 6(5), 1379–1385. https://doi.org/10.1128/mcb.6.5.1379-1385.1986 3.Oltvai, Z. N., Milliman, C. L., & Korsmeyer, S. J. (1993). Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell, 74(4), 609–619. https://doi.org/10.1016/0092-8674(93)90509-o 4. Apte, S. S., Mattei, M. G., & Olsen, B. R. (1995). Mapping of the human BAX gene to chromosome 19q13.3-q13.4 and isolation of a novel alternatively spliced transcript, BAX delta. Genomics, 26(3), 592–594. https://doi.org/10.1016/0888-7543(95)80180-t 5. Tsujimoto, Y., & Croce, C. M. (1986). Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma. Proceedings of the National Academy of Sciences of the United States of America, 83(14), 5214–5218. https://doi.org/10.1073/pnas.83.14.5214 6. Du, C., Fang, M., Li, Y., Li, L., & Wang, X. (2000). Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell, 102(1), 33–42. https://doi.org/10.1016/s0092-8674(00)00008-8 7. Evans, M. J., & Scarpulla, R. C. (1988). The human somatic cytochrome c gene: two classes of processed pseudogenes demarcate a period of rapid molecular evolution. Proceedings of the National Academy of Sciences of the United States of America, 85(24), 9625–9629. https://doi.org/10.1073/pnas.85.24.9625 8. Zou, H., Henzel, W. J., Liu, X., Lutschg, A., & Wang, X. (1997). Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell, 90(3), 405–413. https://doi.org/10.1016/s0092-8674(00)80501-2 9.Seol, D. W., & Billiar, T. R. (1999). A caspase-9 variant missing the catalytic site is an endogenous inhibitor of apoptosis. The Journal of biological chemistry, 274(4), 2072–2076. https://doi.org/10.1074/jbc.274.4.2072 10. Fernandes-Alnemri, T., Litwack, G., & Alnemri, E. S. (1994). CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme. The Journal of biological chemistry, 269(49), 30761–30764. 11. Pelletier, M., Cartron, P. F., Delaval, F., Meflah, K., Vallette, F. M., & Oliver, L. (2004). Caspase 3 activation is controlled by a sequence located in the N-terminus of its large subunit. Biochemical and biophysical research communications, 316(1), 93–99. https://doi.org/10.1016/j.bbrc.2004.02.021 12.Elmore S. (2007). Apoptosis: a review of programmed cell death. Toxicologic pathology, 35(4), 495–516. https://doi.org/10.1080/01926230701320337 13. Akgün, Ş., Küçüksayan, H., & Akça, H. TÜMÖR BASKILAYICI GENLER. 14. For Protein structures: https://www.uniprot.org 15. https://alphafold.ebi.ac.uk