Bcl-2

BCL2
ساختارهای موجود
PDB	جستجوی هم‌ساخت‌شناسی: PDBe RCSB
فهرست شناسه‌های PDB
	1G5M, 1GJH, 1YSW, 2O21, 2O22, 2O2F, 2W3L, 2XA0, 4AQ3, 4IEH, 4LVT, 4LXD, 4MAN, 5AGW, 5AGX, 5FCG
معین‌کننده‌ها
نام‌های دیگر	BCL2, Bcl-2, PPP1R50, B-cell CLL/lymphoma 2, apoptosis regulator, BCL2 apoptosis regulator, Genes, bcl-2
شناسه‌های بیرونی	OMIM: 151430 MGI: 88138 HomoloGene: 527 GeneCards: BCL2
موقعیت ژن (موش)
کروموزوم	کروموزوم ۱ (موش)
پایان	106,642,004 bp
الگوی گسترش RNA
	; ; ; ;
	More reference expression data
هستی‌شناسی ژن
عملکرد ملکولی	• protein phosphatase binding; • transcription factor binding; • protein phosphatase 2A binding; • channel inhibitor activity; • protein homodimerization activity; • channel activity; • protease binding; • GO:0001948، GO:0016582 پیوند پروتئینی; • sequence-specific DNA binding; • BH3 domain binding; • identical protein binding; • protein heterodimerization activity; • ubiquitin protein ligase binding;
ترکیبات سلولی	• سیتوپلاسم; • سیتوزول; • پوشش هسته‌ای; • membrane; • میتوکندری; • هسته یاخته; • mitochondrial membranes; • myelin sheath; • mitochondrial outer membrane; • شبکه آندوپلاسمی; • pore complex; • integral component of membrane; • intracellular anatomical structure; • endoplasmic reticulum membrane; • نوکلئوپلاسم; • GO:0009327 protein-containing complex;
فرایند زیستی	• GO:1904089 negative regulation of neuron apoptotic process; • intrinsic apoptotic signaling pathway in response to oxidative stress; • ureteric bud development; • renal system process; • organ growth; • T cell differentiation in thymus; • lymphocyte homeostasis; • response to steroid hormone; • GO:0048554 positive regulation of catalytic activity; • ear development; • glomerulus development; • post-embryonic development; • cellular response to DNA damage stimulus; • T cell homeostasis; • negative regulation of ossification; • GO:1990376 negative regulation of G1/S transition of mitotic cell cycle; • positive regulation of smooth muscle cell migration; • regulation of protein localization; • T cell differentiation; • B cell lineage commitment; • پاسخ به ایسکمی; • regulation of mitochondrial membrane permeability; • humoral immune response; • defense response to virus; • mesenchymal cell development; • positive regulation of multicellular organism growth; • animal organ morphogenesis; • developmental pigmentation; • hair follicle morphogenesis; • B cell differentiation; • تکثیر سلولی; • metanephros development; • melanocyte differentiation; • negative regulation of autophagy; • positive regulation of neuron maturation; • negative regulation of myeloid cell apoptotic process; • cellular response to hypoxia; • pigment granule organization; • negative regulation of cell population proliferation; • B cell receptor signaling pathway; • cellular response to organic substance; • regulation of apoptotic process; • response to cytokine; • cellular response to glucose starvation; • regulation of protein stability; • استخوان‌سازی; • positive regulation of melanocyte differentiation; • axon regeneration; • kidney development; • actin filament organization; • thymus development; • negative regulation of intrinsic apoptotic signaling pathway; • negative regulation of apoptotic signaling pathway; • response to nicotine; • spleen development; • endoplasmic reticulum calcium ion homeostasis; • positive regulation of skeletal muscle fiber development; • GO:0001306 پاسخ به استرس اکسیداتیو; • lymphoid progenitor cell differentiation; • positive regulation of peptidyl-serine phosphorylation; • CD8-positive, alpha-beta T cell lineage commitment; • reactive oxygen species metabolic process; • negative regulation of retinal cell programmed cell death; • branching involved in ureteric bud morphogenesis; • gland morphogenesis; • positive regulation of cell growth; • positive regulation of B cell proliferation; • negative regulation of cell growth; • واکنش به پرتو گاما; • positive regulation of intrinsic apoptotic signaling pathway; • response to toxic substance; • digestive tract morphogenesis; • neuron apoptotic process; • male gonad development; • regulation of protein heterodimerization activity; • regulation of glycoprotein biosynthetic process; • regulation of viral genome replication; • female pregnancy; • negative regulation of mitochondrial depolarization; • GO:0016576 protein dephosphorylation; • protein polyubiquitination; • cellular calcium ion homeostasis; • B cell homeostasis; • behavioral fear response; • oocyte development; • regulation of cell-matrix adhesion; • response to iron ion; • negative regulation of cell migration; • regulation of autophagy; • positive regulation of developmental pigmentation; • developmental growth; • regulation of transmembrane transporter activity; • ovarian follicle development; • ساماندهی بیان ژن; • negative regulation of calcium ion transport into cytosol; • negative regulation of osteoblast proliferation; • homeostasis of number of cells within a tissue; • pigmentation; • response to radiation; • GO:0048552 regulation of catalytic activity; • peptidyl-threonine phosphorylation; • regulation of protein homodimerization activity; • negative regulation of anoikis; • response to hydrogen peroxide; • T cell lineage commitment; • cochlear nucleus development; • leukocyte homeostasis; • regulation of programmed cell death; • regulation of calcium ion transport; • axonogenesis; • negative regulation of cellular pH reduction; • response to glucocorticoid; • regulation of cell cycle; • regulation of mitochondrial membrane potential; • melanin metabolic process; • focal adhesion assembly; • positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; • B cell proliferation; • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; • immune system development; • apoptotic mitochondrial changes; • GO:0035404 peptidyl-serine phosphorylation; • regulation of nitrogen utilization; • GO:0000767 cell morphogenesis; • positive regulation of cell population proliferation; • negative regulation of reactive oxygen species metabolic process; • response to UV-B; • regulation of developmental pigmentation; • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; • extrinsic apoptotic signaling pathway via death domain receptors; • release of cytochrome c from mitochondria; • negative regulation of mitotic cell cycle; • extrinsic apoptotic signaling pathway in absence of ligand; • GO:0097285 مرگ برنامه‌ریزی‌شده یاخته; • transmembrane transport; • intrinsic apoptotic signaling pathway in response to DNA damage; • growth; • cell-cell adhesion; • cytokine-mediated signaling pathway; • negative regulation of apoptotic process; • هماتوپوئز; • regulation of growth; • negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator;
	منابع: آمیگو / کوئیک‌گو
هم‌ساخت‌شناسی
	596
	12043
	ENSG00000171791
	ENSMUSG00000057329
	P10415
	P10417
	NM_000657، XM_011526135، XM_017025917، XM_047437733، XM_047437734 NM_000633، NM_000657، XM_011526135، XM_017025917، XM_047437733، XM_047437734
	NM_177410 NM_009741، NM_177410
	NP_000648، XP_011524437، XP_016881406 NP_000624، NP_000648، XP_011524437، XP_016881406
	NP_803129 NP_033871، NP_803129
	ویکی‌داده
مشاهده/ویرایش انسان	مشاهده/ویرایش موش

لنفومای ۲ لنفوسیت‌های بی (انگلیسی: B-cell lymphoma 2) که بیشتر با نام اختصاری Bcl-2 شناخته می‌شود، یک پروتئین است که در انسان توسط ژن «BCL2» کُدگذاری می‌شود. این مولکول یکی از اعضای اصلی خانواده Bcl-2 است که در ساماندهی بیان ژن و همچنین القا یا مهار آپوپتوز نقش دارند.^[۴]^[۵] این مولکول نخستین تنظیم‌کنندهٔ آپوپتوزی بود که در موجودات زنده کشف شد.^[۶] پروتئین Bcl-2 یکی از نخستین پروتئین‌هایی که در جریان کشف فرایند جابه‌جایی کروموزومی میان کروموزوم‌های ۱۴ و ۱۸ در لنفوم فولیکولار شناسایی شد. اُرتولوگ‌های^[۷] این پروتئین در بسیاری از پستانداران کشف شده و نقشهٔ کامل ژنی آن در دسترس است. همچون BCL3، BCL5، BCL9، BCL7A، BCL6 و BCL10، این پروتئین نیز نقش مهمی در سرطان لنفوم دارد.

ایزوفرم‌ها

دو ایزوفرم این مولکول، یعنی ایزوفرم‌های ۱ و ۲، تاشدگی مشابهی دارند. اما توانایی متفاوت این ایزوفرم‌ها در اتصال به پروتئین‌های BAD و BAK1 و همچنین توپولوژی ساختمانی و پتانسیل الکتریکی شیارهای اتصالی آنان نشان می‌دهد که فعالیت‌های ضد آپوپتوزی مختلفی از یکدیگر دارند.^[۸]

اهمیت بالینی

آسیب به ژن سازندهٔ Bcl-2 در بروز چندین نوع سرطان از جمله ملانوما،^[۹]^[۱۰] سرطان پستان، سرطان پروستات، لوسمی مزمن لنفاوی و سرطان ریه (کارسینومای سلول کوچک)^[۱۱] نقش دارد. همچنین نقص ژنی BCL2 ممکن است سبب‌ساز اسکیزوفرنی^[۱۲] و اختلالات خودایمنی^[۱۳] شود. علاوه بر اینها، این پروتئین در شکل‌گیری مقاومت‌های درمانی در سرطان حائز اهمیت است.^[۱۴]

تعامل‌های شیمیایی

خلاصه‌ای از مسیرهای پیام‌رسانی سلولی که در آپوپتوز نقش دارند.

پروتئینِ Bcl-2 با مولکول‌های زیر تعامل پروتئین-پروتئین دارد:

BAK1,^[۱۵]^[۱۶]
BCL2L1,^[۱۵]^[۱۷]
BID,^[۱۸]^[۱۹]
BNIP2,^[۲۰]^[۲۱]
BNIP3,^[۲۱]^[۲۲]
BNIPL,^[۲۰]^[۲۳]
RAD9A,^[۲۴]
BAD^[۱۸]^[۲۵]
BAX,^[۱۵]^[۲۴]^[۲۶]^[۲۷]
BIK,^[۱۸]^[۲۸]
C-Raf,^[۲۹]
کاسپاز ۸,^[۳۰]^[۳۱]
SMN1,^[۳۲]
SOD1,^[۳۳]
BCL2L11,^[۱۸]^[۳۴]^[۳۵]

جستارهای وابسته

منابع

1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000057329 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Tsujimoto Y, Finger LR, Yunis J, Nowell PC, Croce CM (Nov 1984). "Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation". Science. 226 (4678): 1097–9. Bibcode:1984Sci...226.1097T. doi:10.1126/science.6093263. PMID 6093263.
↑ Cleary ML, Smith SD, Sklar J (Oct 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. doi:10.1016/0092-8674(86)90362-4. PMID 2875799. S2CID 31493780.
↑ Kelly GL, Strasser A (2020). "Toward Targeting Antiapoptotic MCL-1 for Cancer Therapy". Annual Review of Cancer Biology. 4: 299–313. doi:10.1146/annurev-cancerbio-030419-033510.
↑ "OrthoMaM phylogenetic marker: Bcl-2 coding sequence". Archived from the original on 24 September 2015. Retrieved 20 December 2009.
↑ پی‌دی‌بی 1G5M; Petros AM, Medek A, Nettesheim DG, Kim DH, Yoon HS, Swift K, Matayoshi ED, Oltersdorf T, Fesik SW (March 2001). "Solution structure of the antiapoptotic protein bcl-2". Proceedings of the National Academy of Sciences of the United States of America. 98 (6): 3012–7. Bibcode:2001PNAS...98.3012P. doi:10.1073/pnas.041619798. PMC 30598. PMID 11248023.
↑ Otake Y, Soundararajan S, Sengupta TK, Kio EA, Smith JC, Pineda-Roman M, Stuart RK, Spicer EK, Fernandes DJ (Apr 2007). "Overexpression of nucleolin in chronic lymphocytic leukemia cells induces stabilization of bcl2 mRNA". Blood. 109 (7): 3069–75. doi:10.1182/blood-2006-08-043257. PMC 1852223. PMID 17179226.
↑ Vaux DL, Cory S, Adams JM (Sep 1988). "Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells". Nature. 335 (6189): 440–2. Bibcode:1988Natur.335..440V. doi:10.1038/335440a0. PMID 3262202. S2CID 23593952.
↑ Kaiser, U.; Schilli, M.; Haag, U.; Neumann, K.; Kreipe, H.; Kogan, E.; Havemann, K. (August 1996). "Expression of bcl-2 — protein in small cell lung cancer". Lung Cancer. 15 (1): 31–40. doi:10.1016/0169-5002(96)00568-5. PMID 8865121.
↑ Glantz LA, Gilmore JH, Lieberman JA, Jarskog LF (Jan 2006). "Apoptotic mechanisms and the synaptic pathology of schizophrenia". Schizophrenia Research. 81 (1): 47–63. doi:10.1016/j.schres.2005.08.014. PMID 16226876. S2CID 22388783.
↑ Li A, Ojogho O, Escher A (2006). "Saving death: apoptosis for intervention in transplantation and autoimmunity". Clinical & Developmental Immunology. 13 (2–4): 273–82. doi:10.1080/17402520600834704. PMC 2270759. PMID 17162368.
↑ Garcia-Aranda M, Perez-Ruiz E, Redondo M (Dec 2018). "Bcl-2 Inhibition to Overcome Resistance to Chemo- and Immunotherapy". International Journal of Molecular Sciences. 19 (12): 3950. doi:10.3390/ijms19123950. PMC 6321604. PMID 30544835.
1 2 3 Lin B, Kolluri SK, Lin F, Liu W, Han YH, Cao X, Dawson MI, Reed JC, Zhang XK (Feb 2004). "Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3". Cell. 116 (4): 527–40. doi:10.1016/s0092-8674(04)00162-x. PMID 14980220. S2CID 17808479.
↑ 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 (Dec 2001). "Discovery of small-molecule inhibitors of Bcl-2 through structure-based computer screening". Journal of Medicinal Chemistry. 44 (25): 4313–24. doi:10.1021/jm010016f. PMID 11728179.
↑ Zhang H, Nimmer P, Rosenberg SH, Ng SC, Joseph M (Aug 2002). "Development of a high-throughput fluorescence polarization assay for Bcl-x(L)". Analytical Biochemistry. 307 (1): 70–5. doi:10.1016/s0003-2697(02)00028-3. PMID 12137781.
1 2 3 4 Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (Feb 2005). "Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function". Molecular Cell. 17 (3): 393–403. doi:10.1016/j.molcel.2004.12.030. PMID 15694340.
↑ Real PJ, Cao Y, Wang R, Nikolovska-Coleska Z, Sanz-Ortiz J, Wang S, Fernandez-Luna JL (Nov 2004). "Breast cancer cells can evade apoptosis-mediated selective killing by a novel small molecule inhibitor of Bcl-2". Cancer Research. 64 (21): 7947–53. doi:10.1158/0008-5472.CAN-04-0945. PMID 15520201.
1 2 Qin W, Hu J, Guo M, Xu J, Li J, Yao G, Zhou X, Jiang H, Zhang P, Shen L, Wan D, Gu J (Aug 2003). "BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis". Biochemical and Biophysical Research Communications. 308 (2): 379–85. doi:10.1016/s0006-291x(03)01387-1. PMID 12901880.
1 2 Boyd JM, Malstrom S, Subramanian T, Venkatesh LK, Schaeper U, Elangovan B, D'Sa-Eipper C, Chinnadurai G (Oct 1994). "Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins". Cell. 79 (2): 341–51. doi:10.1016/0092-8674(94)90202-X. PMID 7954800. S2CID 38609845.
↑ Ray R, Chen G, Vande Velde C, Cizeau J, Park JH, Reed JC, Gietz RD, Greenberg AH (Jan 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". The Journal of Biological Chemistry. 275 (2): 1439–48. doi:10.1074/jbc.275.2.1439. PMID 10625696.
↑ Yasuda M, Han JW, Dionne CA, Boyd JM, Chinnadurai G (Feb 1999). "BNIP3alpha: a human homolog of mitochondrial proapoptotic protein BNIP3". Cancer Research. 59 (3): 533–7. PMID 9973195.
1 2 Komatsu K, Miyashita T, Hang H, Hopkins KM, Zheng W, Cuddeback S, Yamada M, Lieberman HB, Wang HG (Jan 2000). "Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis". Nature Cell Biology. 2 (1): 1–6. doi:10.1038/71316. PMID 10620799. S2CID 52847351.
↑ Yang E, Zha J, Jockel J, Boise LH, Thompson CB, Korsmeyer SJ (Jan 1995). "Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death". Cell. 80 (2): 285–91. doi:10.1016/0092-8674(95)90411-5. PMID 7834748. S2CID 10343291.
↑ Hoetelmans RW (Jun 2004). "Nuclear partners of Bcl-2: Bax and PML". DNA and Cell Biology. 23 (6): 351–4. doi:10.1089/104454904323145236. PMID 15231068.
↑ Oltvai ZN, Milliman CL, Korsmeyer SJ (Aug 1993). "Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death". Cell. 74 (4): 609–19. doi:10.1016/0092-8674(93)90509-O. PMID 8358790. S2CID 31151334.
↑ Gillissen B, Essmann F, Graupner V, Stärck L, Radetzki S, Dörken B, Schulze-Osthoff K, Daniel PT (Jul 2003). "Induction of cell death by the BH3-only Bcl-2 homolog Nbk/Bik is mediated by an entirely Bax-dependent mitochondrial pathway". The EMBO Journal. 22 (14): 3580–90. doi:10.1093/emboj/cdg343. PMC 165613. PMID 12853473.
↑ Wang HG, Rapp UR, Reed JC (Nov 1996). "Bcl-2 targets the protein kinase Raf-1 to mitochondria". Cell. 87 (4): 629–38. doi:10.1016/s0092-8674(00)81383-5. PMID 8929532. S2CID 16559750.
↑ Poulaki V, Mitsiades N, Romero ME, Tsokos M (Jun 2001). "Fas-mediated apoptosis in neuroblastoma requires mitochondrial activation and is inhibited by FLICE inhibitor protein and Bcl-2". Cancer Research. 61 (12): 4864–72. PMID 11406564.
↑ Guo Y, Srinivasula SM, Druilhe A, Fernandes-Alnemri T, Alnemri ES (Apr 2002). "Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria". The Journal of Biological Chemistry. 277 (16): 13430–7. doi:10.1074/jbc.M108029200. PMID 11832478.
↑ Iwahashi H, Eguchi Y, Yasuhara N, Hanafusa T, Matsuzawa Y, Tsujimoto Y (Nov 1997). "Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy". Nature. 390 (6658): 413–7. Bibcode:1997Natur.390..413I. doi:10.1038/37144. PMID 9389483. S2CID 1936633.
↑ Pasinelli P, Belford ME, Lennon N, Bacskai BJ, Hyman BT, Trotti D, Brown RH (Jul 2004). "Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria". Neuron. 43 (1): 19–30. doi:10.1016/j.neuron.2004.06.021. PMID 15233914. S2CID 18141051.
↑ O'Connor L, Strasser A, O'Reilly LA, Hausmann G, Adams JM, Cory S, Huang DC (Jan 1998). "Bim: a novel member of the Bcl-2 family that promotes apoptosis". The EMBO Journal. 17 (2): 384–95. doi:10.1093/emboj/17.2.384. PMC 1170389. PMID 9430630.
↑ Hsu SY, Lin P, Hsueh AJ (Sep 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". Molecular Endocrinology. 12 (9): 1432–40. doi:10.1210/mend.12.9.0166. PMID 9731710.

مشارکت‌کنندگان ویکی‌پدیا. «Bcl-2». در دانشنامهٔ ویکی‌پدیای انگلیسی، بازبینی‌شده در ۱۴ نوامبر ۲۰۲۰.

پیوند به بیرون

bcl-2 Genes در سرعنوان‌های موضوعی پزشکی (MeSH) در کتابخانهٔ ملی پزشکی ایالات متحدهٔ آمریکا
c-bcl-2 Proteins در سرعنوان‌های موضوعی پزشکی (MeSH) در کتابخانهٔ ملی پزشکی ایالات متحدهٔ آمریکا
مکان ژنوم BCL2 انسانی و صفحهٔ جزئیات ژنی BCL2 در سامانه جستجوی بانک ژنی دانشگاه کالیفرنیا، سانتا کروز.
خلاصه‌ای از اطلاعات ساختاری موجود در بانک داده پروتئین برای یونی‌پروت: P10415 (Human Apoptosis regulator Bcl-2) در PDBe-KB.

[refGRCm38Ensembl-1] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000057329 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid6093263-4] Tsujimoto Y, Finger LR, Yunis J, Nowell PC, Croce CM (Nov 1984). "Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation". Science. 226 (4678): 1097–9. Bibcode:1984Sci...226.1097T. doi:10.1126/science.6093263. PMID 6093263.

[pmid2875799-5] Cleary ML, Smith SD, Sklar J (Oct 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. doi:10.1016/0092-8674(86)90362-4. PMID 2875799. S2CID 31493780.

[6] Kelly GL, Strasser A (2020). "Toward Targeting Antiapoptotic MCL-1 for Cancer Therapy". Annual Review of Cancer Biology. 4: 299–313. doi:10.1146/annurev-cancerbio-030419-033510.

[OrthoMaM-7] "OrthoMaM phylogenetic marker: Bcl-2 coding sequence". Archived from the original on 24 September 2015. Retrieved 20 December 2009.

[Human_Bcl2_1G5M-8] پی‌دی‌بی 1G5M; Petros AM, Medek A, Nettesheim DG, Kim DH, Yoon HS, Swift K, Matayoshi ED, Oltersdorf T, Fesik SW (March 2001). "Solution structure of the antiapoptotic protein bcl-2". Proceedings of the National Academy of Sciences of the United States of America. 98 (6): 3012–7. Bibcode:2001PNAS...98.3012P. doi:10.1073/pnas.041619798. PMC 30598. PMID 11248023.

[pmid17179226-9] Otake Y, Soundararajan S, Sengupta TK, Kio EA, Smith JC, Pineda-Roman M, Stuart RK, Spicer EK, Fernandes DJ (Apr 2007). "Overexpression of nucleolin in chronic lymphocytic leukemia cells induces stabilization of bcl2 mRNA". Blood. 109 (7): 3069–75. doi:10.1182/blood-2006-08-043257. PMC 1852223. PMID 17179226.

[pmid3262202-10] Vaux DL, Cory S, Adams JM (Sep 1988). "Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells". Nature. 335 (6189): 440–2. Bibcode:1988Natur.335..440V. doi:10.1038/335440a0. PMID 3262202. S2CID 23593952.

[11] Kaiser, U.; Schilli, M.; Haag, U.; Neumann, K.; Kreipe, H.; Kogan, E.; Havemann, K. (August 1996). "Expression of bcl-2 — protein in small cell lung cancer". Lung Cancer. 15 (1): 31–40. doi:10.1016/0169-5002(96)00568-5. PMID 8865121.

[pmid16226876-12] Glantz LA, Gilmore JH, Lieberman JA, Jarskog LF (Jan 2006). "Apoptotic mechanisms and the synaptic pathology of schizophrenia". Schizophrenia Research. 81 (1): 47–63. doi:10.1016/j.schres.2005.08.014. PMID 16226876. S2CID 22388783.

[pmid17162368-13] Li A, Ojogho O, Escher A (2006). "Saving death: apoptosis for intervention in transplantation and autoimmunity". Clinical & Developmental Immunology. 13 (2–4): 273–82. doi:10.1080/17402520600834704. PMC 2270759. PMID 17162368.

[pmid30544835-14] Garcia-Aranda M, Perez-Ruiz E, Redondo M (Dec 2018). "Bcl-2 Inhibition to Overcome Resistance to Chemo- and Immunotherapy". International Journal of Molecular Sciences. 19 (12): 3950. doi:10.3390/ijms19123950. PMC 6321604. PMID 30544835.

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