[1. Abdel-Magid A. F. (2015). Inhibitors of the Antiapoptotic Myeloid Cell Leukemia-1 (Mcl-1) May Provide Effective Treatment for Cancer. ACS Medical Chemistry Letter, 6: 1171–1173. dx.doi.org/10.1021/acsmedchemlett.5b0043810.1021/acsmedchemlett.5b00438]Open DOISearch in Google Scholar
[2. AlBakr R. B, Khojah O. T. (2014). Incidence Trend of the Leukemia Reported Cases in the Kingdom of Saudi Arabia, Observational Descriptive Statistic from Saudi Cancer Registry. International Journal Biomedical Research, 5(8).10.7439/ijbr.v5i8.736]Search in Google Scholar
[3. Anderson M. A, Huang D, Robertsa A. 2014. Targeting BCL2 for the Treatment of Lymphoid Malignancies. Seminar of Hematolology, 51(3), 219–227.10.1053/j.seminhematol.2014.05.008]Search in Google Scholar
[4. Marshall K. D & Baines C. P. 2014. Necroptosis: Is there a role for mitochondria? Frontier of Physiology, 5, 323.10.3389/fphys.2014.00323]Search in Google Scholar
[5. Asif N, Hassan K. 2013. Acute Myeloid Leukemia amongst Adults. Journal of Islamabad Medical & Dentistry College (JIMDC), 2(4), 58-63.]Search in Google Scholar
[6. Zhao H, Jaffer T, Eguchi S, Wang Z, Linkermann A, Ma D. (2015). Role of necroptosis in the pathogenesis of solid organ injury. Cell death and disease, 6, 1-10.10.1038/cddis.2015.316]Search in Google Scholar
[7. Gozuacik D, Kimchi A. (2007). Autophagy and Cell Death. Current topics in developmental biology, 78, 217-245. https://doi.org/10.1016/S0070-2153(06)78006-110.1016/S0070-2153(06)78006-1]Open DOISearch in Google Scholar
[8. Martin S. J, Henry C. M, Cullen S.P. (2012). A perspective on mammalian caspases as positive and negative regulators of inflammation. Molecular, 46(4), 387–397. doi: 10.1016/j.molcel.2012.04.026.2263348710.1016/j.molcel.2012.04.026]Search in Google Scholar
[9. Mohana-Kumaran N, Hill D. S, Allen J. D, Haass N. K. (2014). Targeting the intrinsic apoptosis pathway as a strategy for melanoma therapy. Pigment Cell Melanoma Research, 4, 525-39. doi:10.1111/pcmr. 12242. Epub 2014.10.1111/pcmr.12242.Epub2014]Open DOISearch in Google Scholar
[10. Hajji N. Joseph B. (2010). Epigenetic regulation of cell life and death decisions and deregulation in cancer. Essays in Biochemistry, 48, 121-146.10.1042/bse048012120822491]Search in Google Scholar
[11. Hockenbery D. M. (1994). bcl-2 in cancer, development and apoptosis. Journal of Cell Science, Supplement, 18, 51–55.10.1242/jcs.1994.Supplement_18.77883792]Search in Google Scholar
[12. Yip K. W, Reed J. C. (2008). Bcl-2 family proteins and cancer. Oncogene, 27(50), 6398–6406. https://doi.org/10.1038/onc.2008.30710.1038/onc.2008.30718955968]Open DOISearch in Google Scholar
[13. Frenzel, A., Grespi, F., Chmelewskij, W. & Villunger. A. (2009). Bcl2 family proteins in carcinogenesis and the treatment of cancer. Apoptosis. 14(4); 584–596. doi:10.1007/s10495-008-0300-z.10.1007/s10495-008-0300-z327240119156528]Open DOISearch in Google Scholar
[14. Kelly P, Strasser A. (2011). The role of Bcl-2 and its prosurvival relatives in tumourigenesis and cancer therapy. Cell Death and Different, 18(10), 1414–1424. https://doi.org/10.1038/cdd.2011.1710.1038/cdd.2011.17314974021415859]Search in Google Scholar
[15. Susan F. L, Brad C. T. (2005). Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells. Infection and immunity, 73(4), 1907-16.10.1128/IAI.73.4.1907-1916.2005]Search in Google Scholar
[16. Doerflinger M, Glab J. A, Puthalakath H. (2015). BH3- only proteins: a 20-year stock-take. FEBS Journal, 282,1006–1016. doi:10.1111/febs.1319010.1111/febs.13190]Search in Google Scholar
[17. Dewson, G, Kluck R. M. (2009). Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis. Journal of Cell Science, 122, 2801-8.10.1242/jcs.038166]Search in Google Scholar
[18. Ghatage D D, Gosavi S R, Ganvir S. M, Hazarey V. K. (2012). Apoptosis: Molecular mechanism. Journal Orofacial Science, 4 (2).10.4103/0975-8844.106199]Search in Google Scholar
[19. Barak Y, Juven T, Haffner R. (1993). mdm2 expression is induced by wild type p53 activity. EMBO Journal, 12, 461–468.10.1002/j.1460-2075.1993.tb05678.x]Search in Google Scholar
[20. Belizário J, Cordeiro L. V, Enns S. (2015). Necroptotic Cell Death Signaling and Execution Pathway: Lessons from Knockout Mice. Hindawi Publishing Corporation Mediators of Inflammation, 15.10.1155/2015/128076]Search in Google Scholar
[21. Bensi L, Longo R, Vecchi A, Messora C, Garagnani L, Bernardi M. S, Tamassia G, Sacchi S. (1995). BCL-2 Oncoprotein Expression in Acute Myeloid Leukemia. Haematology, 80, 98-102.]Search in Google Scholar
[22. Billard C. (2015). Apoptosis as a Therapeutic Target in Chronic Lymphocytic Leukemia. Lymphocytitc and Chonic Lymphocytic Leukemia, 5, 11–15. doi:10.4137/LCLL.S13718.10.4137/LCLL.S13718]Open DOISearch in Google Scholar
[23. Blau O. (2015). Gene Mutations in Acute Myeloid Leukemia- Incidence, Prognostic Influence, and Association with Other Molecular Markers. INTECH, 75-100.10.5772/60928]Search in Google Scholar
[24. Blatt N. B, Glick G. D. (2001). Signaling pathways and effector mechanisms pre-programmed cell death. Bioorganic and Medical Chemistry, 9(6), 1371-84.10.1016/S0968-0896(01)00041-4]Search in Google Scholar
[25. Fisher A. (1937). The theory of the developmental physiology of malignant tumor. The American journal of cancer, 31(10).]Search in Google Scholar
[26. Breckenridge D. G, Germain M, Mathai J. P, Nguyen M, Shore G. C. (2003) Regulation of apoptosis by endoplasmic reticulum pathways. Oncogene, 22, 8608–8618. doi:10.1038/sj.onc.120710810.1038/sj.onc.120710814634622]Open DOISearch in Google Scholar
[27. Bruin E. C, Medema J. P. (2008). Apoptosis and nonapoptotic deaths in cancer development and treatment response. Cancer Treatment Reviews, 34(8), 737-749. doi: http://dx.doi.org/10.1016/j.ctrv.2008.07.00110.1016/j.ctrv.2008.07.00118722718]Search in Google Scholar
[28. Brunelle J. K, Letai A. (2009). Control of mitochondrial apoptosis by the Bcl-2 family. J Cell Science, 122, 437-441.10.1242/jcs.031682271443119193868]Search in Google Scholar
[29. Chaabane W, User S. D, El-Gazzah M, Jaksik R, Sajjadi E, Rzeszowska-Wolny J, Łos M. J. (2013). Autophagy, Apoptosis, Mitoptosis and Necrosis: Interdependence Between Those Pathways and Effects on Cancer. Archive of Immunology Therapy and Experimental, 61, 43–58, (2013). DOI 10.1007/s00005-012-0205-y10.1007/s00005-012-0205-y23229678]Open DOISearch in Google Scholar
[30. Chipuk J. E. (2015). BCL-2 proteins: melanoma lives on the edge. Oncoscience, 34(7), 857-67.10.18632/oncoscience.193460599726501069]Search in Google Scholar
[31. Chonghaile T. N, Letai A. (2009). Mimicking the BH3 domain to kill cancer cells. Oncogene, 27, 149–157. doi:10.1038/onc.2009.5210.1038/onc.2009.52373326519641500]Open DOISearch in Google Scholar
[32. Thorburn A. (2008). Apoptosis and autophagy: regulatory connections between two supposedly different processes. Apoptosis, 13(1), 1-9. Doi: 10.1007/s10495-007-0154-910.1007/s10495-007-0154-9260159517990121]Open DOISearch in Google Scholar
[33. Kelly P, Strasser A. (2011). The role of Bcl-2 and its prosurvival relatives in tumourigenesis and cancer therapy. Cell Death and Differentiation, 18(10), 1414–1424. https://doi.org/10.1038/cdd.2011.1710.1038/cdd.2011.17314974021415859]Search in Google Scholar
[34. Palai T. K, Mishra S. R. (2015). Caspases: An apoptosis mediator. Journal of Advanced Veerinary and Animal Research, 2(1), 18-22. doi: 10.5455/javar.2015.b5210.5455/javar.2015.b52]Open DOISearch in Google Scholar
[35. Shimizu S, Yoshida T, Tsujioka M, Arakawa S. (2014). Autophagic Cell Death and Cancer. International Journal of Molecular Science, 15, 3145-3153. doi:10.3390/ijms1502314510.3390/ijms15023145395890224566140]Open DOISearch in Google Scholar
[36. Siddiqui W. A, Ahad A, Ahsan H. (2015). The mystery of BCL2 family: Bcl-2 proteins and apoptosis: an update. Archives of Toxicology, 89, 289-317.10.1007/s00204-014-1448-725618543]Search in Google Scholar
[37. Singh L, Pushker N, Saini N, Sen S, Sharma A, Bakhshi S, Chawla B, Kashyap S. (2015). Expression of proapoptotic Bax and anti-apoptotic Bcl-2 proteins in human retinoblastoma. Clinical Experimental Ophthopedic, 43, 259–267. doi: 10.1111/ceo.123910.1111/ceo.1239]Open DOISearch in Google Scholar
[38. Su Z, Yang Z, Xu Y, Chen Y, Qiang Y. Q. (2015). Apoptosis, autophagy, necroptosis, and cancer metastasis. Molecular Cancer, 14(48). Doi:10.1186/s12943-015-0321-510.1186/s12943-015-0321-5]Open DOISearch in Google Scholar
[39. Guicciardi M. E, Gores G. J. (2009). Life and death by death receptors. FASEBJ, 23(6), 1625-37. doi: 10.1096/fj.08-111005.10.1096/fj.08-111005]Open DOISearch in Google Scholar
[40. Marsden V. S, Ekert P. G, Delft M. V, Vaux D. L, Adams J. M, Strasser A. (2004). Bcl-2–regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase- 9. The Journal of Cell Biology, 165(6),775–780. http://www.jcb.org/cgi/doi/10.1083/jcb.20031203010.1083/jcb.200312030]Open DOISearch in Google Scholar
[41. Mason K, Vandenberga C. J, Scotta C. L, Wei A. H, Corya S, Huanga D. (2008). In vivo ef cacy of the Bcl- 2 antagonist ABT-737 against aggressive Myc-driven lymphomas. The Proceedings of the National Academy of Sciences, 105, 17961-17966.10.1073/pnas.0809957105]Search in Google Scholar
[42. Mérino D, Khaw S. L, Glaser S. P, Anderson D. J, Belmont L. D, Wong C. (2012). Bcl-2, Bcl-xL, and Bcl-w are not equivalent targets of ABT-737 and navitoclax (ABT-263 in lymphoid and leukemic cells. Blood, 119, 5807-5816.10.1182/blood-2011-12-400929]Search in Google Scholar
[43. Mehdipour P, Santoro F, Minucci S.(2015). Epigenetic alterations in acute myeloid leukemias. FEBS Journal, 282, 1786–1800. doi:10.1111/febs.1314210.1111/febs.13142]Open DOISearch in Google Scholar
[44. Momand J, Zambetti G. P, Olson D. C. (1991). The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell, 69, 1237–1245.10.1016/0092-8674(92)90644-R]Search in Google Scholar
[45. Kang M. H, Reynolds C. P. (2009). Bcl-2 Inhibitors: Targeting Mitochondrial Apoptotic Pathways in Cancer Therapy. Clinical Cancer Research, 15(4). doi:10.1158/1078-0432.CCR-08-014410.1158/1078-0432.CCR-08-0144318226819228717]Open DOISearch in Google Scholar
[46. Koff J. L, Ramachandiran S, Bernal-Mizrachi L. (2015). A Time to Kill: Targeting Apoptosis in Cancer. International Journal Molecular Science, 16, 2942-2955. doi:10.3390/ijms1602294210.3390/ijms16022942434687425636036]Open DOISearch in Google Scholar
[47. Kontny U, Lissat A. (2015). Apoptosis and drug resistance in malignant bone tumors. Primary bone tumours. Doi: 10.1016/B978-0-12-416721-6.00036-410.1016/B978-0-12-416721-6.00036-4]Open DOISearch in Google Scholar
[48. Lavrik I. N. (2014). Systems biology of death receptor networks: live and let die. Cell Death and Disease, 5. doi:10.1038/cddis.2014.16010.1038/cddis.2014.160404788124874731]Open DOISearch in Google Scholar
[49. Leber B, Lin J, Andrews D. W. (2010). Still embedded together binding to membranes regulates Bcl-2 protein interactions. Oncogene, 29, 5221-30.10.1038/onc.2010.283645940720639903]Open DOISearch in Google Scholar
[50. Letai A, Sorcinelli M. D, Beard C, Korsmeyer S. J. (2002). Antiapoptotic BCL-2 is required for maintenance of a model leukemia. Cancer Cell, 6, 241–9.10.1016/j.ccr.2004.07.01115380515]Search in Google Scholar
[51. Le´veille F, Papadia S, Fricker M, Bell K. F. S, Soriano F. X, Martel M, Puddifoot C, Habel M, Wyllie D. J, Ikonomidou C, Tolkovsky A. M, Hardingham G. E. (2010). Suppression of the Intrinsic Apoptosis Pathway by Synaptic Activity. The Journal of Neurology, 30(7), 2623–2635.10.1523/JNEUROSCI.5115-09.2010283492720164347]Search in Google Scholar
[52. Liu B, Bhatt D, Oltvai Z. N, Greenberger J. S, Bahar I. (2014). Significance of p53 dynamics in regulating apoptosis in response to ionizing radiation, and polypharmacological strategies. Scientific Reports, 4, 6245. Doi: 10.1038/srep0624510.1038/srep06245415010625175563]Open DOISearch in Google Scholar
[53. Li M. X, Dewson G. (2015). Mitochondria and apoptosis: emerging concepts. F1000Prime Reports, 7(42). doi:10.12703/P7-42.10.12703/P7-42444703226097715]Open DOISearch in Google Scholar
[54. Abramowitz J, Neuman T, Perlman R, Ben-Yehuda D. (2017). Gene and protein analysis reveals that p53 pathway is functionally inactivated in cytogenetically normal Acute Myeloid Leukemia and Acute Promyelocytic Leukemia. BMC Medical Genomics, 10(1),18. https://doi.org/10.1186/s12920-017-0249-210.1186/s12920-017-0249-2542342128340577]Open DOISearch in Google Scholar
[55. Petitjean A, Mathe E, Kato S, Ishioka C, Tavtigian S. V, Hainaut P, Olivier M. (2007). Impact of Mutant p53 Functional Properties on TP53 Mutation Patterns and Tumor Phenotype: Lessons from Recent Developments in the IARC TP53 Database. Human mutation, 28(6), 622-629.10.1002/humu.2049517311302]Search in Google Scholar
[56. Llambi F, Moldoveanu T, Tait Stephen W. G, Bouchier- Hayes L, Temirov J, McCormick L. L, Dillon C. P, Green D. R. (2011). A unified model of mammalian BCL-2 protein family interactions at the mitochondria. Molecular Cell, 44, 517-31.10.1016/j.molcel.2011.10.001322178722036586]Open DOISearch in Google Scholar
[57. Fulda S, Debatin K. M. (2006). Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy. Oncogene, 25(34), 4798-811.10.1038/sj.onc.1209608]Search in Google Scholar
[58. Löwenberg B, Rowe J. M. (2015). Introduction to the review series on advances in acute myeloid leukemia (AML). Blood, 127(1). doi:10.1182/blood-2015-10-6626810.1182/blood-2015-10-66268]Open DOISearch in Google Scholar
[59. Mongiat M, Ligresti G, Marastoni S, Lorenzon E, Doliana R, Alfonso C. Regulation of the Extrinsic Apoptotic Pathway by the Extracellular Matrix Glycoprotein EMILIN2. (2007). Molecular Cell Biology, 27(20), 7176–7187. doi:10.1128/MCB.00696-0710.1128/MCB.00696-07]Open DOISearch in Google Scholar
[60. Moore V. D. G, Letai A. (2012). BH3 profiling – measuring integrated function of the mitochondrial apoptotic pathway to predict cell fate decisions. Cancer Letter, 332(2), 202–205. doi:10.1016/j.canlet.2011.12.021.10.1016/j.canlet.2011.12.021]Open DOISearch in Google Scholar
[61. Moore D. G. V, Brown J. R, Certo M. (2007). Chronic lymphocytic leukemia requires BCL2 to sequester prodeath BIM, explaining sensitivity to BCL2 antagonist ABT-737. Journal of Clinical Investiment, 117, 112–21.10.1172/JCI28281]Search in Google Scholar
[62. Naseri H. M, Mahdavi M, Davoodi J, Tackallou S. H, Goudarzvand M, Neishabouri S. H. (2015). Up regulation of Bax and down regulation of Bcl2 during 3-NC mediated apoptosis in human cancer cells. Cancer Cell International, 15(55). Doi: 10.1186/s12935-015-0204-210.1186/s12935-015-0204-2]Open DOISearch in Google Scholar
[63. Ng S. Y, Davids M. S. (2014). Selective Bcl-2 inhibition to treat chronic lymphocytic leukemia and non-Hodgkin lymphoma. Clinical Advanced Hematology Oncology, 12(4), 224-9.]Search in Google Scholar
[64. Noguchi M, Hirata N, Edamura T, Ishigaki S, Suizu F. (2015). Intersection of Apoptosis and Autophagy Cell Death Pathways. Austin Journal of Molecular & Cell Biology, 2(1), 1004.]Search in Google Scholar
[65. Oltersdorf T, Steven W, Elmore S. W, Shoemaker A. R, Armstrong R. C, Augeri D. J, Belli B. A. (2005). An inhibitor of Bcl-2 family proteins induces regression of solid tumours. Nature, 435, 677-681.10.1038/nature03579]Search in Google Scholar
[67. Gibson L, Holmgreen S. P, Huang D. C, Bernard O, Copeland N. G, Jenkins N. A, Sutherland G. R, Baker E, Adams J. M, Cory S. (1996). Bcl-w, a novel member of the bcl-2 family, promotes cell survival. Oncology, 13(4), 665-75.]Search in Google Scholar
[68. Zhong Q, Gao W, Du F, Wang X. (2005). Mule/ARFBP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquiti-nation of Mcl-1 and regulates apoptosis. Cell, 121, 1085–1095.10.1016/j.cell.2005.06.009]Search in Google Scholar
[69. Czabotar P. E, Lee E. F, Delft M. F, Day C. L, Smith B. J, Huang D. C. S, Fairlie W. D, Hinds M. G, Colman P.M. (2007). Structural insights into the degradation of Mcl-1 induced by BH3 domain. Proceedings of the National Academy of Sciences, 104 (15) 6217-6222. DOI:10.1073/pnas.070129710410.1073/pnas.0701297104]Open DOISearch in Google Scholar
[70. Huang D. C. S, Strasser A. (2000). BH3-Only Proteins— Essential Initiators of Apoptotic Cell Death. Cell, 103, 839–842.10.1016/S0092-8674(00)00187-2]Search in Google Scholar
[71. Shamas-Din A, Kale J, Leber B, Andrews D. W. (2013). Mechanisms of Action of Bcl-2 Family Proteins. Cold Spring Harbor Perspective in Biology. doi: 10.1101/cshperspect. a00871410.1101/cshperspect.a008714368389723545417]Open DOISearch in Google Scholar
[72. Belka C, Budach W. (2002). Anti-apoptotic Bcl-2 proteins: structure, function and relevance for radiation biology. International journal of radiation Biology, 78(8), 643-658. Doi: 10.1080/0955300021013768 010.1080/09553000210137680]Search in Google Scholar
[73. Bouillet P, Metcalf D, Huang D. C, Tarlinton D. M, Kay T. W, Kontgen F, Adams J. M, Strasser A. (1999). Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity. Science, 286, 1735–1738.10.1126/science.286.5445.173510576740]Search in Google Scholar
[74. Polcic P, Jaká P, Mentel M. (2015). Yeast as a tool for studying proteins of the Bcl-2 family. Microbiology Cell, 2(3), 74-87. doi: 10.15698/mic2015.03.19310.15698/mic2015.03.193534918128357280]Open DOISearch in Google Scholar
[75. Sáez G. A. J. (2012). The secrets of the Bcl-2 family. Cell Death Differentiation, 11, 1733-40. doi: 10.1038/cdd.2012.105.10.1038/cdd.2012.105346906522935609]Open DOISearch in Google Scholar
[76. Scaffidi C, Fulda S, Srinivasan A, Friesen C, Li F, Tomaselli K. J, Debatin K. M, Krammer P. H, Peter M. E. (1998). Two CD95 (APO-1/Fas) signaling pathways. The EMBO Journal, 17(6), 1675–1687.10.1093/emboj/17.6.167511705159501089]Open DOISearch in Google Scholar
[77. Schnerch D, Yalcintepe J, Schmidts A, Becker H, Follo M, Engelhardt M, Wäsch R. (2012). Cell cycle control in acute myeloid leukemia. American Journal of Cancer Research, 2(5), 508-528.]Search in Google Scholar
[78. Scandura J. M, Boccuni P, Cammenga J, Nimer S. D. (2002). Transcription factor fusions in acute leukemia: variations on a theme. Oncogene, 21, 3422-3444. Doi: 10.1038/sj/onc/120531510.1038/sj/onc/1205315]Open DOISearch in Google Scholar
[79. Shimizu S, Yoshida T, Tsujioka M, Arakawa S. (2014). Autophagic Cell Death and Cancer. International Journal of Molecular Science, 15, 3145-3153. doi:10.3390/ijms1502314510.3390/ijms15023145395890224566140]Open DOISearch in Google Scholar
[80. Smaili S. S, Hsu Y. T, Carvalho A. C. P, Rosenstock T. R, Sharpe J. C, Youle, R. J. (2003). Mitochondria, calcium and pro-apoptotic proteins as mediators in cell death signaling. Brazilian Journal of Medical Biology Research. 36(2), 183-190.10.1590/S0100-879X200300020000412563519]Search in Google Scholar
[81. Strasser A. (2005). The role of BH3-only proteins in the immune system. Nature Reviews Immunology, 5, 189-200.doi:10.1038/nri156810.1038/nri156815719025]Open DOISearch in Google Scholar
[82. Sun Z, Cheng Z, Taylor C. A, McConkey B, Thompson J. E. (2010). Apoptosis Induction by eIF5A1 Involves Activation of the Intrinsic Mitochondrial Pathway. Journal of Cell Physiology, 223, 798–809. Doi: 10.1002/jcp.2210010.1002/jcp.2210020232312]Open DOISearch in Google Scholar
[83. Tian K.Y, Liu X. J, Xu J.D, Deng L. J, Wang G. (2015). Propofol inhibits burn injury-induced hyperpermeability through an apoptotic signal pathway in microvascular endothelial cells. Brazilian Journal of Medical Biology Research, 48(5), 401-407. http://dx.doi.org/10.1590/1414-431X2014410710.1590/1414-431X20144107]Open DOISearch in Google Scholar
[84. Trump B. F, Berezesky I. K, Chang, S. H, Phelps P. C. (1997). The Pathways of Cell Death: Oncosis, Apoptosis, and Necrosis. Toxicologic Pathology, 25(1), 82-8. Doi: 10.1177/01926233970250011610.1177/019262339702500116]Search in Google Scholar
[85. Tiwari M, Sharma L. K, Saxena A. K, Godbole M. M. (2015). Interaction Between Mitochondria and Caspases: Apoptotic and Non-Apoptotic Roles. Cell Biology, 3(2), 22-30. doi: 10.11648/j.cb.s.2015030201.1410.11648/j.cb.s.2015030201.14]Open DOISearch in Google Scholar
[86. Tzifi F, Economopoulou C, Gourgiotis D, Ardavanis A, Papageorgiou S, Scorilas A. (2012). The Role of BCL2 Family of Apoptosis Regulator Proteins in Acute and Chronic Leukemias. Hindawi Public Corporation Advanced Hematology, doi:10.1155/2012/524308.10.1155/2012/524308]Open DOISearch in Google Scholar
[87. Vela L, Gonzalo O, Naval J, Marzo I. (2013). Revealed by fluorescence complementation. Journal of Biological Chemistry, doi:10.1074/jbc.M112.42220410.1074/jbc.M112.422204]Open DOISearch in Google Scholar
[88. Verbrugge I, Johnstone R. W, Smyth M. J. (2010). Snap- Shot: Extrinsic Apoptosis Pathways. Cell, 143(7), 1192. DOI 10.1016/j.cell.2010.12.00410.1016/j.cell.2010.12.004]Open DOISearch in Google Scholar
[89. Vo T. T, Ryan J, Carrasco R, Neuberg D, Rossi D. J, Stone R. M, Letai A. (2012). Relative mitochondrial priming of myeloblasts and normal HSCs determines chemotherapeutic success in AML. Cell, 151(2), 344-355.10.1016/j.cell.2012.08.038]Search in Google Scholar
[90. El-Shakankiry N. H, El-Sayed G. M, El-Maghraby S, Moneer M. M. (2009). Bcl-2 protein expression in egyptian acute myeloid leukemia. Journal of Egypt Natural Cancer Institute, 21(1), 71–6.]Search in Google Scholar
[91. Shi Y. (2002). Mechanisms of caspase activation and inhibition during apoptosis. Molecular Cell. https://doi.org/10.1016/S1097-2765(02)00482-310.1016/S1097-2765(02)00482-3]Open DOISearch in Google Scholar
[92. Wang R. A, Li Z. S, Yan Q. Q, Bian X. W, Ding Y. Q, Xiang D. X, Sun B. C, Yun-Tian S. Y. T, Xiang-Hong Zhang X. H. (2014). Resistance to apoptosis should not be taken as a hallmark of cancer. Chinese Journal of Cancer, 33(2).10.5732/cjc.013.10131393500524417874]Search in Google Scholar
[93. Wei A. Teh T. C. (2012). Primed for the kill: occupying Bcl-2 to target death in acute myeloid leukaemia. Bio- Discovery, 6(1). doi:10.7750/BioDiscovery.2012.610.7750/BioDiscovery.2012.6]Open DOISearch in Google Scholar
[94. Weyhenmeyer B, Murphy A. C, Prehn J. H. M, Murphy B. M. (2012). Targeting the anti-apoptotic BCL-2 family members for the treatment of cancer. Experimental Oncology, 34, 192–199.23070004]Search in Google Scholar
[95. Woess C, Tuzlak S, Labi V, Drach M, Bertele D, Schneider P, Villunger A. (2015). Combined loss of the BH3- only proteins Bim and Bmf restores B-cell development and function in TACI-Ig transgenic mice. Cell Death Differentiation, 22, 1477–1488. doi: 10.1038/cdd.2015.810.1038/cdd.2015.8453278425698446]Open DOISearch in Google Scholar
[96. Wu M, Ding H. F, Fisher D. E. Apoptosis: Molecular Mechanisms. Encyclopedia of Life Science 2001.10.1023/A:1011342220621]Open DOISearch in Google Scholar
[97. Yip K. W, Reed J. C. (2008). Bcl-2 family proteins and cancer. Oncology, 27, 6398–6406.10.1038/onc.2008.307]Search in Google Scholar
[98. Yohe S. (2015). Molecular Genetic Markers in Acute Myeloid Leukemia. Journal of Clinical Medicine, 4, 460-478 (2015). doi:10.3390/jcm403046010.3390/jcm4030460447013926239249]Open DOISearch in Google Scholar
[99. Youle R. J, Strasser A. (2005). The BCL-2 protein family: op- posing activities that mediate cell death. Nature Reviews of Molecular and Cell Biology, 9, 47–59.10.1038/nrm2308]Search in Google Scholar
[100. Perez-Stable C, Parrondo R, De Las Pozas A, Reiner T. (2013). ABT-737, a small molecule Bcl-2/Bcl-xL antagonist, increases antimitotic- mediated apoptosis in human prostate cancer cells. Biochemistry, biophysics and molecular biology, https://doi.org/10.7717/peerj.14410.7717/peerj.144377563124058878]Open DOISearch in Google Scholar
[101. Zhao G, Zhu Y, Eno C. O, Liu Y, DeLeeuw L, Joseph A, Burlison J. A, Chaires J. B, Trent J. O, Li C. (2014). Activation of the Proapoptotic Bcl-2 Protein Bax by a Small Molecule Induces Tumor Cell Apoptosis. Molecular Cell Biology, 34(7), 1198–1207. doi:10.1128/MCB.00996-1310.1128/MCB.00996-13399356124421393]Open DOISearch in Google Scholar
[102. Zong W. X, Lindsten T, Ross A. J, MacGregor G. R, Thompson C. B. (2001). BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Gene & Development, 15, 1481–1486.10.1101/gad.89760131272211410528]Open DOISearch in Google Scholar