Cleary ML, Smith SD, Sklar J (October 1986). „Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation”. Cell47 (1): 19–28. DOI:10.1016/0092-8674(86)90362-4. PMID2875799.
Komatsu, K; Miyashita T, Hang H, Hopkins K M, Zheng W, Cuddeback S, Yamada M, Lieberman H B, Wang H G (January 2000). „Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis”. Nat. Cell Biol. (ENGLAND) 2 (1): 1–6. DOI:10.1038/71316. ISSN1465-7392. PMID10620799.
Lin, Bingzhen; Kolluri Siva Kumar, Lin Feng, Liu Wen, Han Young-Hoon, Cao Xihua, Dawson Marcia I, Reed John C, Zhang Xiao-kun (February 2004). „Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3”. Cell (United States) 116 (4): 527–40. DOI:10.1016/S0092-8674(04)00162-X. ISSN0092-8674. PMID14980220.
Enyedy, I J; Ling Y, Nacro K, Tomita Y, Wu X, Cao Y, Guo R, Li B, Zhu X, Huang Y, Long Y Q, Roller P P, Yang D, Wang S (December 2001). „Discovery of small-molecule inhibitors of Bcl-2 through structure-based computer screening”. J. Med. Chem. (United States) 44 (25): 4313–24. DOI:10.1021/jm010016f. ISSN0022-2623. PMID11728179.
Tagami, S; Eguchi Y, Kinoshita M, Takeda M, Tsujimoto Y (November 2000). „A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity”. Oncogene (England) 19 (50): 5736–46. DOI:10.1038/sj.onc.1203948. ISSN0950-9232. PMID11126360.
Oltvai, Z N; Milliman C L, Korsmeyer S J (August 1993). „Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death”. Cell (UNITED STATES) 74 (4): 609–19. DOI:10.1016/0092-8674(93)90509-O. ISSN0092-8674. PMID8358790.
Guo, Yin; Srinivasula Srinivasa M, Druilhe Anne, Fernandes-Alnemri Teresa, Alnemri Emad S (April 2002). „Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria”. J. Biol. Chem. (United States) 277 (16): 13430–7. DOI:10.1074/jbc.M108029200. ISSN0021-9258. PMID11832478.
Pasinelli, Piera; Belford Mary Elizabeth, Lennon Niall, Bacskai Brian J, Hyman Bradley T, Trotti Davide, Brown Robert H (July 2004). „Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria”. Neuron (United States) 43 (1): 19–30. DOI:10.1016/j.neuron.2004.06.021. ISSN0896-6273. PMID15233914.
Chen, Lin; Willis Simon N, Wei Andrew, Smith Brian J, Fletcher Jamie I, Hinds Mark G, Colman Peter M, Day Catherine L, Adams Jerry M, Huang David C S (February 2005). „Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function”. Mol. Cell (United States) 17 (3): 393–403. DOI:10.1016/j.molcel.2004.12.030. ISSN1097-2765. PMID15694340.
Real, Pedro Jose; Cao Yeyu, Wang Renxiao, Nikolovska-Coleska Zaneta, Sanz-Ortiz Jaime, Wang Shaomeng, Fernandez-Luna Jose Luis (November 2004). „Breast cancer cells can evade apoptosis-mediated selective killing by a novel small molecule inhibitor of Bcl-2”. Cancer Res. (United States) 64 (21): 7947–53. DOI:10.1158/0008-5472.CAN-04-0945. ISSN0008-5472. PMID15520201.
Fernandez-Sarabia, M J; Bischoff J R (November 1993). „Bcl-2 associates with the ras-related protein R-ras p23”. Nature (ENGLAND) 366 (6452): 274–5. DOI:10.1038/366274a0. ISSN0028-0836. PMID8232588.
Hsu, S Y; Lin P, Hsueh A J (September 1998). „BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members”. Mol. Endocrinol. (UNITED STATES) 12 (9): 1432–40. DOI:10.1210/me.12.9.1432. ISSN0888-8809. PMID9731710.
Qin, Wenxin; Hu Jian, Guo Minglei, Xu Jian, Li Jinjun, Yao Genfu, Zhou Xiaomei, Jiang Huiqiu, Zhang Pingping, Shen Li, Wan Dafang, Gu Jianren (August 2003). „BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis”. Biochem. Biophys. Res. Commun. (United States) 308 (2): 379–85. DOI:10.1016/S0006-291X(03)01387-1. ISSN0006-291X. PMID12901880.
Alberici, A; Moratto D, Benussi L, Gasparini L, Ghidoni R, Gatta L B, Finazzi D, Frisoni G B, Trabucchi M, Growdon J H, Nitsch R M, Binetti G (October 1999). „Presenilin 1 protein directly interacts with Bcl-2”. J. Biol. Chem. (UNITED STATES) 274 (43): 30764–9. DOI:10.1074/jbc.274.43.30764. ISSN0021-9258. PMID10521466.
Puthalakath, H; Villunger A, O'Reilly L A, Beaumont J G, Coultas L, Cheney R E, Huang D C, Strasser A (September 2001). „Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis”. Science (United States) 293 (5536): 1829–32. DOI:10.1126/science.1062257. ISSN0036-8075. PMID11546872.
Boyd, J M; Malstrom S, Subramanian T, Venkatesh L K, Schaeper U, Elangovan B, D'Sa-Eipper C, Chinnadurai G (October 1994). „Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins”. Cell (UNITED STATES) 79 (2): 341–51. DOI:10.1016/0092-8674(94)90202-X. ISSN0092-8674. PMID7954800.
Ray, R; Chen G, Vande Velde C, Cizeau J, Park J H, Reed J C, Gietz R D, Greenberg A H (January 2000). „BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites”. J. Biol. Chem. (UNITED STATES) 275 (2): 1439–48. DOI:10.1074/jbc.275.2.1439. ISSN0021-9258. PMID10625696.
Zhang, Haichao; Nimmer Paul, Rosenberg Saul H, Ng Shi-Chung, Joseph Mary (August 2002). „Development of a high-throughput fluorescence polarization assay for Bcl-x(L)”. Anal. Biochem. (United States) 307 (1): 70–5. DOI:10.1016/S0003-2697(02)00028-3. ISSN0003-2697. PMID12137781.
Jin, Zhaohui; Gao Fengqin, Flagg Tammy, Deng Xingming (September 2004). „Tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone promotes functional cooperation of Bcl2 and c-Myc through phosphorylation in regulating cell survival and proliferation”. J. Biol. Chem. (United States) 279 (38): 40209–19. DOI:10.1074/jbc.M404056200. ISSN0021-9258. PMID15210690.
Iwahashi, H; Eguchi Y, Yasuhara N, Hanafusa T, Matsuzawa Y, Tsujimoto Y (November 1997). „Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy”. Nature (ENGLAND) 390 (6658): 413–7. DOI:10.1038/37144. ISSN0028-0836. PMID9389483.
Gil-Parrado, Shirley; Fernández-Montalván Amaury, Assfalg-Machleidt Irmgard, Popp Oliver, Bestvater Felix, Holloschi Andreas, Knoch Tobias A, Auerswald Ennes A, Welsh Katherine, Reed John C, Fritz Hans, Fuentes-Prior Pablo, Spiess Eberhard, Salvesen Guy S, Machleidt Werner (July 2002). „Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members”. J. Biol. Chem. (United States) 277 (30): 27217–26. DOI:10.1074/jbc.M202945200. ISSN0021-9258. PMID12000759.
Deng, X; Ito T, Carr B, Mumby M, May W S (December 1998). „Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A”. J. Biol. Chem. (UNITED STATES) 273 (51): 34157–63. DOI:10.1074/jbc.273.51.34157. ISSN0021-9258. PMID9852076.
Oda, E; Ohki R, Murasawa H, Nemoto J, Shibue T, Yamashita T, Tokino T, Taniguchi T, Tanaka N (May 2000). „Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis”. Science (UNITED STATES) 288 (5468): 1053–8. DOI:10.1126/science.288.5468.1053. ISSN0036-8075. PMID10807576.
Cleary ML, Smith SD, Sklar J (October 1986). „Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation”. Cell47 (1): 19–28. DOI:10.1016/0092-8674(86)90362-4. PMID2875799.
Komatsu, K; Miyashita T, Hang H, Hopkins K M, Zheng W, Cuddeback S, Yamada M, Lieberman H B, Wang H G (January 2000). „Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis”. Nat. Cell Biol. (ENGLAND) 2 (1): 1–6. DOI:10.1038/71316. ISSN1465-7392. PMID10620799.
Lin, Bingzhen; Kolluri Siva Kumar, Lin Feng, Liu Wen, Han Young-Hoon, Cao Xihua, Dawson Marcia I, Reed John C, Zhang Xiao-kun (February 2004). „Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3”. Cell (United States) 116 (4): 527–40. DOI:10.1016/S0092-8674(04)00162-X. ISSN0092-8674. PMID14980220.
Enyedy, I J; Ling Y, Nacro K, Tomita Y, Wu X, Cao Y, Guo R, Li B, Zhu X, Huang Y, Long Y Q, Roller P P, Yang D, Wang S (December 2001). „Discovery of small-molecule inhibitors of Bcl-2 through structure-based computer screening”. J. Med. Chem. (United States) 44 (25): 4313–24. DOI:10.1021/jm010016f. ISSN0022-2623. PMID11728179.
Tagami, S; Eguchi Y, Kinoshita M, Takeda M, Tsujimoto Y (November 2000). „A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity”. Oncogene (England) 19 (50): 5736–46. DOI:10.1038/sj.onc.1203948. ISSN0950-9232. PMID11126360.
Oltvai, Z N; Milliman C L, Korsmeyer S J (August 1993). „Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death”. Cell (UNITED STATES) 74 (4): 609–19. DOI:10.1016/0092-8674(93)90509-O. ISSN0092-8674. PMID8358790.
Poulaki, V; Mitsiades N, Romero M E, Tsokos M (June 2001). „Fas-mediated apoptosis in neuroblastoma requires mitochondrial activation and is inhibited by FLICE inhibitor protein and Bcl-2”. Cancer Res. (United States) 61 (12): 4864–72. ISSN0008-5472. PMID11406564.
Guo, Yin; Srinivasula Srinivasa M, Druilhe Anne, Fernandes-Alnemri Teresa, Alnemri Emad S (April 2002). „Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria”. J. Biol. Chem. (United States) 277 (16): 13430–7. DOI:10.1074/jbc.M108029200. ISSN0021-9258. PMID11832478.
Pasinelli, Piera; Belford Mary Elizabeth, Lennon Niall, Bacskai Brian J, Hyman Bradley T, Trotti Davide, Brown Robert H (July 2004). „Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria”. Neuron (United States) 43 (1): 19–30. DOI:10.1016/j.neuron.2004.06.021. ISSN0896-6273. PMID15233914.
Chen, Lin; Willis Simon N, Wei Andrew, Smith Brian J, Fletcher Jamie I, Hinds Mark G, Colman Peter M, Day Catherine L, Adams Jerry M, Huang David C S (February 2005). „Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function”. Mol. Cell (United States) 17 (3): 393–403. DOI:10.1016/j.molcel.2004.12.030. ISSN1097-2765. PMID15694340.
Real, Pedro Jose; Cao Yeyu, Wang Renxiao, Nikolovska-Coleska Zaneta, Sanz-Ortiz Jaime, Wang Shaomeng, Fernandez-Luna Jose Luis (November 2004). „Breast cancer cells can evade apoptosis-mediated selective killing by a novel small molecule inhibitor of Bcl-2”. Cancer Res. (United States) 64 (21): 7947–53. DOI:10.1158/0008-5472.CAN-04-0945. ISSN0008-5472. PMID15520201.
Fernandez-Sarabia, M J; Bischoff J R (November 1993). „Bcl-2 associates with the ras-related protein R-ras p23”. Nature (ENGLAND) 366 (6452): 274–5. DOI:10.1038/366274a0. ISSN0028-0836. PMID8232588.
Hsu, S Y; Lin P, Hsueh A J (September 1998). „BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members”. Mol. Endocrinol. (UNITED STATES) 12 (9): 1432–40. DOI:10.1210/me.12.9.1432. ISSN0888-8809. PMID9731710.
Qin, Wenxin; Hu Jian, Guo Minglei, Xu Jian, Li Jinjun, Yao Genfu, Zhou Xiaomei, Jiang Huiqiu, Zhang Pingping, Shen Li, Wan Dafang, Gu Jianren (August 2003). „BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis”. Biochem. Biophys. Res. Commun. (United States) 308 (2): 379–85. DOI:10.1016/S0006-291X(03)01387-1. ISSN0006-291X. PMID12901880.
Alberici, A; Moratto D, Benussi L, Gasparini L, Ghidoni R, Gatta L B, Finazzi D, Frisoni G B, Trabucchi M, Growdon J H, Nitsch R M, Binetti G (October 1999). „Presenilin 1 protein directly interacts with Bcl-2”. J. Biol. Chem. (UNITED STATES) 274 (43): 30764–9. DOI:10.1074/jbc.274.43.30764. ISSN0021-9258. PMID10521466.
Puthalakath, H; Villunger A, O'Reilly L A, Beaumont J G, Coultas L, Cheney R E, Huang D C, Strasser A (September 2001). „Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis”. Science (United States) 293 (5536): 1829–32. DOI:10.1126/science.1062257. ISSN0036-8075. PMID11546872.
Boyd, J M; Malstrom S, Subramanian T, Venkatesh L K, Schaeper U, Elangovan B, D'Sa-Eipper C, Chinnadurai G (October 1994). „Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins”. Cell (UNITED STATES) 79 (2): 341–51. DOI:10.1016/0092-8674(94)90202-X. ISSN0092-8674. PMID7954800.
Ray, R; Chen G, Vande Velde C, Cizeau J, Park J H, Reed J C, Gietz R D, Greenberg A H (January 2000). „BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites”. J. Biol. Chem. (UNITED STATES) 275 (2): 1439–48. DOI:10.1074/jbc.275.2.1439. ISSN0021-9258. PMID10625696.
Zhang, Haichao; Nimmer Paul, Rosenberg Saul H, Ng Shi-Chung, Joseph Mary (August 2002). „Development of a high-throughput fluorescence polarization assay for Bcl-x(L)”. Anal. Biochem. (United States) 307 (1): 70–5. DOI:10.1016/S0003-2697(02)00028-3. ISSN0003-2697. PMID12137781.
Jin, Zhaohui; Gao Fengqin, Flagg Tammy, Deng Xingming (September 2004). „Tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone promotes functional cooperation of Bcl2 and c-Myc through phosphorylation in regulating cell survival and proliferation”. J. Biol. Chem. (United States) 279 (38): 40209–19. DOI:10.1074/jbc.M404056200. ISSN0021-9258. PMID15210690.
Iwahashi, H; Eguchi Y, Yasuhara N, Hanafusa T, Matsuzawa Y, Tsujimoto Y (November 1997). „Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy”. Nature (ENGLAND) 390 (6658): 413–7. DOI:10.1038/37144. ISSN0028-0836. PMID9389483.
Gil-Parrado, Shirley; Fernández-Montalván Amaury, Assfalg-Machleidt Irmgard, Popp Oliver, Bestvater Felix, Holloschi Andreas, Knoch Tobias A, Auerswald Ennes A, Welsh Katherine, Reed John C, Fritz Hans, Fuentes-Prior Pablo, Spiess Eberhard, Salvesen Guy S, Machleidt Werner (July 2002). „Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members”. J. Biol. Chem. (United States) 277 (30): 27217–26. DOI:10.1074/jbc.M202945200. ISSN0021-9258. PMID12000759.
Deng, X; Ito T, Carr B, Mumby M, May W S (December 1998). „Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A”. J. Biol. Chem. (UNITED STATES) 273 (51): 34157–63. DOI:10.1074/jbc.273.51.34157. ISSN0021-9258. PMID9852076.
Oda, E; Ohki R, Murasawa H, Nemoto J, Shibue T, Yamashita T, Tokino T, Taniguchi T, Tanaka N (May 2000). „Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis”. Science (UNITED STATES) 288 (5468): 1053–8. DOI:10.1126/science.288.5468.1053. ISSN0036-8075. PMID10807576.
Komatsu, K; Miyashita T, Hang H, Hopkins K M, Zheng W, Cuddeback S, Yamada M, Lieberman H B, Wang H G (January 2000). „Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis”. Nat. Cell Biol. (ENGLAND) 2 (1): 1–6. DOI:10.1038/71316. ISSN1465-7392. PMID10620799.
Lin, Bingzhen; Kolluri Siva Kumar, Lin Feng, Liu Wen, Han Young-Hoon, Cao Xihua, Dawson Marcia I, Reed John C, Zhang Xiao-kun (February 2004). „Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3”. Cell (United States) 116 (4): 527–40. DOI:10.1016/S0092-8674(04)00162-X. ISSN0092-8674. PMID14980220.
Enyedy, I J; Ling Y, Nacro K, Tomita Y, Wu X, Cao Y, Guo R, Li B, Zhu X, Huang Y, Long Y Q, Roller P P, Yang D, Wang S (December 2001). „Discovery of small-molecule inhibitors of Bcl-2 through structure-based computer screening”. J. Med. Chem. (United States) 44 (25): 4313–24. DOI:10.1021/jm010016f. ISSN0022-2623. PMID11728179.
Tagami, S; Eguchi Y, Kinoshita M, Takeda M, Tsujimoto Y (November 2000). „A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity”. Oncogene (England) 19 (50): 5736–46. DOI:10.1038/sj.onc.1203948. ISSN0950-9232. PMID11126360.
Oltvai, Z N; Milliman C L, Korsmeyer S J (August 1993). „Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death”. Cell (UNITED STATES) 74 (4): 609–19. DOI:10.1016/0092-8674(93)90509-O. ISSN0092-8674. PMID8358790.
Poulaki, V; Mitsiades N, Romero M E, Tsokos M (June 2001). „Fas-mediated apoptosis in neuroblastoma requires mitochondrial activation and is inhibited by FLICE inhibitor protein and Bcl-2”. Cancer Res. (United States) 61 (12): 4864–72. ISSN0008-5472. PMID11406564.
Guo, Yin; Srinivasula Srinivasa M, Druilhe Anne, Fernandes-Alnemri Teresa, Alnemri Emad S (April 2002). „Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria”. J. Biol. Chem. (United States) 277 (16): 13430–7. DOI:10.1074/jbc.M108029200. ISSN0021-9258. PMID11832478.
Pasinelli, Piera; Belford Mary Elizabeth, Lennon Niall, Bacskai Brian J, Hyman Bradley T, Trotti Davide, Brown Robert H (July 2004). „Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria”. Neuron (United States) 43 (1): 19–30. DOI:10.1016/j.neuron.2004.06.021. ISSN0896-6273. PMID15233914.
Chen, Lin; Willis Simon N, Wei Andrew, Smith Brian J, Fletcher Jamie I, Hinds Mark G, Colman Peter M, Day Catherine L, Adams Jerry M, Huang David C S (February 2005). „Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function”. Mol. Cell (United States) 17 (3): 393–403. DOI:10.1016/j.molcel.2004.12.030. ISSN1097-2765. PMID15694340.
Real, Pedro Jose; Cao Yeyu, Wang Renxiao, Nikolovska-Coleska Zaneta, Sanz-Ortiz Jaime, Wang Shaomeng, Fernandez-Luna Jose Luis (November 2004). „Breast cancer cells can evade apoptosis-mediated selective killing by a novel small molecule inhibitor of Bcl-2”. Cancer Res. (United States) 64 (21): 7947–53. DOI:10.1158/0008-5472.CAN-04-0945. ISSN0008-5472. PMID15520201.
Fernandez-Sarabia, M J; Bischoff J R (November 1993). „Bcl-2 associates with the ras-related protein R-ras p23”. Nature (ENGLAND) 366 (6452): 274–5. DOI:10.1038/366274a0. ISSN0028-0836. PMID8232588.
Hsu, S Y; Lin P, Hsueh A J (September 1998). „BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members”. Mol. Endocrinol. (UNITED STATES) 12 (9): 1432–40. DOI:10.1210/me.12.9.1432. ISSN0888-8809. PMID9731710.
Qin, Wenxin; Hu Jian, Guo Minglei, Xu Jian, Li Jinjun, Yao Genfu, Zhou Xiaomei, Jiang Huiqiu, Zhang Pingping, Shen Li, Wan Dafang, Gu Jianren (August 2003). „BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis”. Biochem. Biophys. Res. Commun. (United States) 308 (2): 379–85. DOI:10.1016/S0006-291X(03)01387-1. ISSN0006-291X. PMID12901880.
Alberici, A; Moratto D, Benussi L, Gasparini L, Ghidoni R, Gatta L B, Finazzi D, Frisoni G B, Trabucchi M, Growdon J H, Nitsch R M, Binetti G (October 1999). „Presenilin 1 protein directly interacts with Bcl-2”. J. Biol. Chem. (UNITED STATES) 274 (43): 30764–9. DOI:10.1074/jbc.274.43.30764. ISSN0021-9258. PMID10521466.
Puthalakath, H; Villunger A, O'Reilly L A, Beaumont J G, Coultas L, Cheney R E, Huang D C, Strasser A (September 2001). „Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis”. Science (United States) 293 (5536): 1829–32. DOI:10.1126/science.1062257. ISSN0036-8075. PMID11546872.
Boyd, J M; Malstrom S, Subramanian T, Venkatesh L K, Schaeper U, Elangovan B, D'Sa-Eipper C, Chinnadurai G (October 1994). „Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins”. Cell (UNITED STATES) 79 (2): 341–51. DOI:10.1016/0092-8674(94)90202-X. ISSN0092-8674. PMID7954800.
Ray, R; Chen G, Vande Velde C, Cizeau J, Park J H, Reed J C, Gietz R D, Greenberg A H (January 2000). „BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites”. J. Biol. Chem. (UNITED STATES) 275 (2): 1439–48. DOI:10.1074/jbc.275.2.1439. ISSN0021-9258. PMID10625696.
Zhang, Haichao; Nimmer Paul, Rosenberg Saul H, Ng Shi-Chung, Joseph Mary (August 2002). „Development of a high-throughput fluorescence polarization assay for Bcl-x(L)”. Anal. Biochem. (United States) 307 (1): 70–5. DOI:10.1016/S0003-2697(02)00028-3. ISSN0003-2697. PMID12137781.
Jin, Zhaohui; Gao Fengqin, Flagg Tammy, Deng Xingming (September 2004). „Tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone promotes functional cooperation of Bcl2 and c-Myc through phosphorylation in regulating cell survival and proliferation”. J. Biol. Chem. (United States) 279 (38): 40209–19. DOI:10.1074/jbc.M404056200. ISSN0021-9258. PMID15210690.
Iwahashi, H; Eguchi Y, Yasuhara N, Hanafusa T, Matsuzawa Y, Tsujimoto Y (November 1997). „Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy”. Nature (ENGLAND) 390 (6658): 413–7. DOI:10.1038/37144. ISSN0028-0836. PMID9389483.
Gil-Parrado, Shirley; Fernández-Montalván Amaury, Assfalg-Machleidt Irmgard, Popp Oliver, Bestvater Felix, Holloschi Andreas, Knoch Tobias A, Auerswald Ennes A, Welsh Katherine, Reed John C, Fritz Hans, Fuentes-Prior Pablo, Spiess Eberhard, Salvesen Guy S, Machleidt Werner (July 2002). „Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members”. J. Biol. Chem. (United States) 277 (30): 27217–26. DOI:10.1074/jbc.M202945200. ISSN0021-9258. PMID12000759.
Deng, X; Ito T, Carr B, Mumby M, May W S (December 1998). „Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A”. J. Biol. Chem. (UNITED STATES) 273 (51): 34157–63. DOI:10.1074/jbc.273.51.34157. ISSN0021-9258. PMID9852076.
Oda, E; Ohki R, Murasawa H, Nemoto J, Shibue T, Yamashita T, Tokino T, Taniguchi T, Tanaka N (May 2000). „Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis”. Science (UNITED STATES) 288 (5468): 1053–8. DOI:10.1126/science.288.5468.1053. ISSN0036-8075. PMID10807576.
