References analysis of the Wikipedia article "Bcl-2" in the Serbian version

doi.org

Tsujimoto Y, Finger LR, Yunis J, Nowell PC, Croce CM (1984). „Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation”. Science. 226 (4678): 1097—99. PMID 6093263. doi:10.1126/science.6093263.

Cleary ML, Smith SD, Sklar J (1986). „Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation”. Cell. 47 (1): 19—28. PMID 2875799. doi:10.1016/0092-8674(86)90362-4.

Komatsu K, Miyashita T, Hang H, Hopkins KM, Zheng W, Cuddeback S, Yamada M, Lieberman HB, Wang HG (2000). „Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis”. Nat. Cell Biol. ENGLAND. 2 (1): 1—6. ISSN 1465-7392. PMID 10620799. doi:10.1038/71316.

Lin, Bingzhen; Kolluri Siva Kumar; Lin Feng (2004). Liu Wen, Han Young-Hoon, Cao Xihua, Dawson Marcia I, Reed John C, Zhang Xiao-kun. „Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3”. Cell. United States. 116 (4): 527—40. ISSN 0092-8674. PMID 14980220. doi:10.1016/S0092-8674(04)00162-X.

Enyedy IJ, Ling Y, Nacro K, Tomita Y, Wu X, Cao Y, Guo R, Li B, Zhu X, Huang Y, Long YQ, Roller PP, Yang D, Wang S (2001). „Discovery of small-molecule inhibitors of Bcl-2 through structure-based computer screening”. J. Med. Chem. United States. 44 (25): 4313—24. ISSN 0022-2623. PMID 11728179. doi:10.1021/jm010016f.

Tagami S, Eguchi Y, Kinoshita M, Takeda M, Tsujimoto Y (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. ISSN 0950-9232. PMID 11126360. doi:10.1038/sj.onc.1203948.

Hoetelmans, R W M (2004). „Nuclear partners of Bcl-2: Bax and PML”. DNA Cell Biol. United States. 23 (6): 351—4. ISSN 1044-5498. PMID 15231068. doi:10.1089/104454904323145236.

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. UNITED STATES. 74 (4): 609—19. ISSN 0092-8674. PMID 8358790. doi:10.1016/0092-8674(93)90509-O.

Guo, Yin; Srinivasula Srinivasa M; Druilhe Anne; Fernandes-Alnemri Teresa; Alnemri Emad S (2002). „Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria”. J. Biol. Chem. United States. 277 (16): 13430—7. ISSN 0021-9258. PMID 11832478. doi:10.1074/jbc.M108029200.

Pasinelli, Piera; Belford Mary Elizabeth; Lennon Niall; Bacskai Brian J; Hyman Bradley T; Trotti Davide; Brown Robert H (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. ISSN 0896-6273. PMID 15233914. doi:10.1016/j.neuron.2004.06.021.

Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (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. ISSN 1097-2765. PMID 15694340. doi:10.1016/j.molcel.2004.12.030.

Gillissen, Bernhard; Essmann Frank; Graupner Vilma; Stärck Lilian; Radetzki Silke; Dörken Bernd; Schulze-Osthoff Klaus; Daniel Peter T (2003). „Induction of cell death by the BH3-only Bcl-2 homolog Nbk/Bik is mediated by an entirely Bax-dependent mitochondrial pathway”. EMBO J. England. 22 (14): 3580—90. ISSN 0261-4189. PMC 165613 

. PMID 12853473. doi:10.1093/emboj/cdg343.

Real, Pedro Jose; Cao Yeyu; Wang Renxiao; Nikolovska-Coleska Zaneta (2004). Sanz-Ortiz Jaime, Wang Shaomeng, Fernandez-Luna Jose Luis. „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. ISSN 0008-5472. PMID 15520201. doi:10.1158/0008-5472.CAN-04-0945.

Fernandez-Sarabia, M J; Bischoff J R (1993). „Bcl-2 associates with the ras-related protein R-ras p23”. Nature. ENGLAND. 366 (6452): 274—5. ISSN 0028-0836. PMID 8232588. doi:10.1038/366274a0.

Wang, H G; Rapp U R; Reed J C (1996). „Bcl-2 targets the protein kinase Raf-1 to mitochondria”. Cell. UNITED STATES. 87 (4): 629—38. ISSN 0092-8674. PMID 8929532. doi:10.1016/S0092-8674(00)81383-5.

O'Connor, L; Strasser A; O'Reilly L A; Hausmann G; Adams J M; Cory S; Huang D C (1998). „Bim: a novel member of the Bcl-2 family that promotes apoptosis”. EMBO J. ENGLAND. 17 (2): 384—95. ISSN 0261-4189. PMC 1170389 

. PMID 9430630. doi:10.1093/emboj/17.2.384.

Hsu, S Y; Lin P; Hsueh A J (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. ISSN 0888-8809. PMID 9731710. doi:10.1210/me.12.9.1432.

Qin, Wenxin; Hu Jian; Guo Minglei; Xu Jian (2003). Li Jinjun, Yao Genfu, Zhou Xiaomei, Jiang Huiqiu, Zhang Pingping, Shen Li, Wan Dafang, Gu Jianren. „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. ISSN 0006-291X. PMID 12901880. doi:10.1016/S0006-291X(03)01387-1.

Inohara, N; Ding L; Chen S; Núñez G (1997). „harakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins Bcl-2 and Bcl-X(L)”. EMBO J. ENGLAND. 16 (7): 1686—94. ISSN 0261-4189. PMC 1169772 

. PMID 9130713. doi:10.1093/emboj/16.7.1686.

Alberici A, Moratto D, Benussi L, Gasparini L, Ghidoni R, Gatta LB, Finazzi D, Frisoni GB, Trabucchi M, Growdon JH, Nitsch RM, Binetti G (1999). „Presenilin 1 protein directly interacts with Bcl-2”. J. Biol. Chem. UNITED STATES. 274 (43): 30764—9. ISSN 0021-9258. PMID 10521466. doi:10.1074/jbc.274.43.30764.

Puthalakath H, Villunger A, O'Reilly LA, Beaumont JG, Coultas L, Cheney RE, Huang DC, Strasser A (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. ISSN 0036-8075. PMID 11546872. doi:10.1126/science.1062257.

Boyd JM, Malstrom S, Subramanian T, Venkatesh LK, Schaeper U, Elangovan B, D'Sa-Eipper C, Chinnadurai G (1994). „Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins”. Cell. UNITED STATES. 79 (2): 341—51. ISSN 0092-8674. PMID 7954800. doi:10.1016/0092-8674(94)90202-X.

Ray R, Chen G, Vande VC, Cizeau J, Park JH, Reed JC, Gietz RD, Greenberg AH (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. ISSN 0021-9258. PMID 10625696. doi:10.1074/jbc.275.2.1439.

Zhang, Haichao; Nimmer Paul; Rosenberg Saul H; Ng Shi-Chung; Joseph Mary (2002). „Development of a high-throughput fluorescence polarization assay for Bcl-x(L)”. Anal. Biochem. United States. 307 (1): 70—5. ISSN 0003-2697. PMID 12137781. doi:10.1016/S0003-2697(02)00028-3.

Jin, Zhaohui; Gao Fengqin; Flagg Tammy; Deng Xingming (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. ISSN 0021-9258. PMID 15210690. doi:10.1074/jbc.M404056200.

Ng FW, Nguyen M, Kwan T, Branton PE, Nicholson DW, Cromlish JA, Shore GC (1997). „p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum”. J. Cell Biol. UNITED STATES. 139 (2): 327—38. ISSN 0021-9525. PMC 2139787 

. PMID 9334338. doi:10.1083/jcb.139.2.327.

Iwahashi H, Eguchi Y, Yasuhara N, Hanafusa T, Matsuzawa Y, Tsujimoto Y (1997). „Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy”. Nature. ENGLAND. 390 (6658): 413—7. ISSN 0028-0836. PMID 9389483. doi:10.1038/37144.

Gil-Parrado, Shirley; Fernández-Montalván Amaury; Assfalg-Machleidt Irmgard; Popp Oliver; Bestvater Felix (2002). 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. „Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members”. J. Biol. Chem. United States. 277 (30): 27217—26. ISSN 0021-9258. PMID 12000759. doi:10.1074/jbc.M202945200.

Deng X, Ito T, Carr B, Mumby M, May WS (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. ISSN 0021-9258. PMID 9852076. doi:10.1074/jbc.273.51.34157.

Oda E, Ohki R, Murasawa H, Nemoto J, Shibue T, Yamashita T, Tokino T, Taniguchi T, Tanaka N (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. ISSN 0036-8075. PMID 10807576. doi:10.1126/science.288.5468.1053.

Pathan N, Aime-Sempe C, Kitada S, Basu A, Haldar S, Reed JC (2001). „Microtubule-targeting drugs induce bcl-2 phosphorylation and association with Pin1”. Neoplasia. United States. 3 (6): 550—9. ISSN 1522-8002. PMC 1506558 

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Pathan N, Aime-Sempe C, Kitada S, Haldar S, Reed JC (2001). „Microtubule-targeting drugs induce Bcl-2 phosphorylation and association with Pin1”. Neoplasia. United States. 3 (1): 70—9. ISSN 1522-8002. PMC 1505024 

. PMID 11326318. doi:10.1038/sj/neo/7900131.

Yang E, Zha J, Jockel J, Boise LH, Thompson CB, Korsmeyer SJ (1995). „Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death”. Cell. UNITED STATES. 80 (2): 285—91. ISSN 0092-8674. PMID 7834748. doi:10.1016/0092-8674(95)90411-5.

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ncbi.nlm.nih.gov

Hoetelmans, R W M (2004). „Nuclear partners of Bcl-2: Bax and PML”. DNA Cell Biol. United States. 23 (6): 351—4. ISSN 1044-5498. PMID 15231068. doi:10.1089/104454904323145236.

Poulaki V, Mitsiades N, Romero ME, Tsokos M (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. ISSN 0008-5472. PMID 11406564.

Liang XH, Kleeman LK, Jiang HH, Gordon G, Goldman JE, Berry G, Herman B, Levine B (1998). „Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein”. J. Virol. UNITED STATES. 72 (11): 8586—96. ISSN 0022-538X. PMC 110269 

. PMID 9765397.

. PMID 12853473. doi:10.1093/emboj/cdg343.

. PMID 9430630. doi:10.1093/emboj/17.2.384.

Yasuda, M; Han J W; Dionne C A; Boyd J M; Chinnadurai G (1999). „BNIP3alpha: a human homolog of mitochondrial proapoptotic protein BNIP3”. Cancer Res. UNITED STATES. 59 (3): 533—7. ISSN 0008-5472. PMID 9973195.

. PMID 9130713. doi:10.1093/emboj/16.7.1686.

. PMID 9334338. doi:10.1083/jcb.139.2.327.

. PMID 11774038. doi:10.1038/sj/neo/7900213.

. PMID 11326318. doi:10.1038/sj/neo/7900131.

Naumovski, L; Cleary M L (1996). „The p53-binding protein 53BP2 also interacts with Bc12 and impedes cell cycle progression at G2/M”. Mol. Cell. Biol. UNITED STATES. 16 (7): 3884—92. ISSN 0270-7306. PMC 231385 

. PMID 8668206.

Ueno H, Kondo E, Yamamoto-Honda R, Tobe K, Nakamoto T, Sasaki K, Mitani K, Furusaka A, Tanaka T, Tsujimoto Y, Kadowaki T, Hirai H (2000). „Association of insulin receptor substrate proteins with Bcl-2 and their effects on its phosphorylation and antiapoptotic function”. Mol. Biol. Cell. UNITED STATES. 11 (2): 735—46. ISSN 1059-1524. PMC 14806 

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worldcat.org

Hoetelmans, R W M (2004). „Nuclear partners of Bcl-2: Bax and PML”. DNA Cell Biol. United States. 23 (6): 351—4. ISSN 1044-5498. PMID 15231068. doi:10.1089/104454904323145236.