Bcl-2 (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "Bcl-2" in Japanese language version.

refsWebsite

Global rank Japanese rank

82nih.gov

4^th place

24^th place

56doi.org

2^nd place

6^th place

8harvard.edu

18^th place

107^th place

4worldcat.org

5^th place

19^th place

2ensembl.org

1,626^th place

2,625^th place

2wikipedia.org

low place

2web.archive.org

1^st place

2medpagetoday.com

9,274^th place

low place

1univ-montp2.fr

low place

1rcsb.org

8,838^th place

low place

1drugs.com

399^th place

1,603^rd place

1asianscientist.com

low place

1stokesentinel.co.uk

5,309^th place

low place

1fda.gov

447^th place

1,043^rd place

asianscientist.com (Global: low place; Japanese: low place)

Liao, Grace (2011年8月12日). “ABT-199 BH-3 Mimetic Enters Phase Ia Trial For Chronic Lymphocytic Leukemia”. Asian Scientist. オリジナルの2012年7月18日時点におけるアーカイブ。 2016年2月11日閲覧。 {{cite news}}: 不明な引数|name-list-format=は無視されます。（もしかして：|name-list-style=） (説明)⚠

doi.org (Global: 2^nd place; Japanese: 6^th place)

“Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation”. Science 226 (4678): 1097–9. (Nov 1984). Bibcode: 1984Sci...226.1097T. doi:10.1126/science.6093263. PMID 6093263.
“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. (Oct 1986). doi:10.1016/0092-8674(86)90362-4. PMID 2875799.
PDB: 1G5M; “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. (March 2001). Bibcode: 2001PNAS...98.3012P. doi:10.1073/pnas.041619798. PMC 30598. PMID 11248023.
“Multiple functions of BCL-2 family proteins”. Cold Spring Harb Perspect Biol 5 (2): a008722. (2013). doi:10.1101/cshperspect.a008722. PMC 3552500. PMID 23378584.
“Bcl-2 Regulates Reactive Oxygen Species Signaling and a Redox-Sensitive Mitochondrial Proton Leak in Mouse Pancreatic ß-Cells”. Endocrinology 157 (6): 2270–2281. (2016). doi:10.1210/en.2015-1964. PMID 27070098.
“Bcl-2 Inhibition to Overcome Resistance to Chemo- and Immunotherapy”. International Journal of Molecular Sciences 19 (12): 3950. (Dec 2018). doi:10.3390/ijms19123950. PMC 6321604. PMID 30544835.
“Overexpression of nucleolin in chronic lymphocytic leukemia cells induces stabilization of bcl2 mRNA”. Blood 109 (7): 3069–75. (Apr 2007). doi:10.1182/blood-2006-08-043257. PMC 1852223. PMID 17179226.
“Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells”. Nature 335 (6189): 440–2. (Sep 1988). Bibcode: 1988Natur.335..440V. doi:10.1038/335440a0. PMID 3262202.
Kaiser, U.; Schilli, M.; Haag, U.; Neumann, K.; Kreipe, H.; Kogan, E.; Havemann, K. (1996-08). “Expression of bcl-2--protein in small cell lung cancer”. Lung Cancer (Amsterdam, Netherlands) 15 (1): 31–40. doi:10.1016/0169-5002(96)00568-5. ISSN 0169-5002. PMID 8865121.
“Saving death: apoptosis for intervention in transplantation and autoimmunity”. Clinical & Developmental Immunology 13 (2–4): 273–82. (2006). doi:10.1080/17402520600834704. PMC 2270759. PMID 17162368.
Hou, Wu-Shiun; Van Parijs, Luk (2004-06). “A Bcl-2-dependent molecular timer regulates the lifespan and immunogenicity of dendritic cells”. Nature Immunology 5 (6): 583–589. doi:10.1038/ni1071. ISSN 1529-2908. PMID 15133508.
“Apoptotic mechanisms and the synaptic pathology of schizophrenia”. Schizophrenia Research 81 (1): 47–63. (Jan 2006). doi:10.1016/j.schres.2005.08.014. PMID 16226876.
“Potential roles of antisense oligonucleotides in cancer therapy. The example of Bcl-2 antisense oligonucleotides”. European Journal of Pharmaceutics and Biopharmaceutics 54 (3): 263–9. (Nov 2002). doi:10.1016/S0939-6411(02)00060-7. PMID 12445555.
Vogler, M.; Dinsdale, D.; Dyer, M. J. S.; Cohen, G. M. (2009-03). “Bcl-2 inhibitors: small molecules with a big impact on cancer therapy”. Cell Death and Differentiation 16 (3): 360–367. doi:10.1038/cdd.2008.137. ISSN 1476-5403. PMID 18806758.
“An inhibitor of Bcl-2 family proteins induces regression of solid tumours”. Nature 435 (7042): 677–81. (June 2005). Bibcode: 2005Natur.435..677O. doi:10.1038/nature03579. PMID 15902208.
“Therapeutic efficacy of ABT-737, a selective inhibitor of BCL-2, in small cell lung cancer”. Cancer Research 68 (7): 2321–8. (April 2008). doi:10.1158/0008-5472.can-07-5031. PMC 3159963. PMID 18381439.
Hauck, Paula; Chao, Bo H.; Litz, Julie; Krystal, Geoffrey W. (2009-04). “Alterations in the Noxa/Mcl-1 axis determine sensitivity of small cell lung cancer to the BH3 mimetic ABT-737”. Molecular Cancer Therapeutics 8 (4): 883–892. doi:10.1158/1535-7163.MCT-08-1118. ISSN 1535-7163. PMID 19372561.
“Phase I study of Navitoclax (ABT-263), a novel Bcl-2 family inhibitor, in patients with small-cell lung cancer and other solid tumors”. Journal of Clinical Oncology 29 (7): 909–16. (March 2011). doi:10.1200/JCO.2010.31.6208. PMC 4668282. PMID 21282543.
“Phase II study of single-agent navitoclax (ABT-263) and biomarker correlates in patients with relapsed small cell lung cancer”. Clinical Cancer Research 18 (11): 3163–9. (June 2012). doi:10.1158/1078-0432.CCR-11-3090. PMC 3715059. PMID 22496272.
“Mechanism-based pharmacokinetic/pharmacodynamic meta-analysis of navitoclax (ABT-263) induced thrombocytopenia”. Cancer Chemotherapy and Pharmacology 74 (3): 593–602. (September 2014). doi:10.1007/s00280-014-2530-9. PMID 25053389.
“Selective BCL-2 inhibition by ABT-199 causes on-target cell death in acute myeloid leukemia”. Cancer Discovery 4 (3): 362–75. (March 2014). doi:10.1158/2159-8290.CD-13-0609. PMC 3975047. PMID 24346116.
“Targeting BCL2 with Venetoclax in Relapsed Chronic Lymphocytic Leukemia”. The New England Journal of Medicine 374 (4): 311–22. (January 2016). doi:10.1056/NEJMoa1513257. PMID 26639348.
“Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3”. Cell 116 (4): 527–40. (Feb 2004). doi:10.1016/s0092-8674(04)00162-x. PMID 14980220.
“Discovery of small-molecule inhibitors of Bcl-2 through structure-based computer screening”. Journal of Medicinal Chemistry 44 (25): 4313–24. (Dec 2001). doi:10.1021/jm010016f. PMID 11728179.
“p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum”. The Journal of Cell Biology 139 (2): 327–38. (Oct 1997). doi:10.1083/jcb.139.2.327. PMC 2139787. PMID 9334338.
“Development of a high-throughput fluorescence polarization assay for Bcl-x(L)”. Analytical Biochemistry 307 (1): 70–5. (Aug 2002). doi:10.1016/s0003-2697(02)00028-3. PMID 12137781.
“Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function”. Molecular Cell 17 (3): 393–403. (Feb 2005). doi:10.1016/j.molcel.2004.12.030. PMID 15694340.
“Bim: a novel member of the Bcl-2 family that promotes apoptosis”. The EMBO Journal 17 (2): 384–95. (Jan 1998). doi:10.1093/emboj/17.2.384. PMC 1170389. PMID 9430630.
“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. (Sep 1998). doi:10.1210/mend.12.9.0166. PMID 9731710.
“Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein”. Journal of Virology 72 (11): 8586–96. (Nov 1998). doi:10.1128/JVI.72.11.8586-8596.1998. PMC 110269. PMID 9765397.
“Breast cancer cells can evade apoptosis-mediated selective killing by a novel small molecule inhibitor of Bcl-2”. Cancer Research 64 (21): 7947–53. (Nov 2004). doi:10.1158/0008-5472.CAN-04-0945. PMID 15520201.
“Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis”. Science 293 (5536): 1829–32. (Sep 2001). Bibcode: 2001Sci...293.1829P. doi:10.1126/science.1062257. PMID 11546872.
“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. (Aug 2003). doi:10.1016/s0006-291x(03)01387-1. PMID 12901880.
“Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins”. Cell 79 (2): 341–51. (Oct 1994). doi:10.1016/0092-8674(94)90202-X. PMID 7954800.
“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. (Jan 2000). doi:10.1074/jbc.275.2.1439. PMID 10625696.
“Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death”. Cell 80 (2): 285–91. (Jan 1995). doi:10.1016/0092-8674(95)90411-5. PMID 7834748.
“Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis”. Nature Cell Biology 2 (1): 1–6. (Jan 2000). doi:10.1038/71316. PMID 10620799.
“Nuclear partners of Bcl-2: Bax and PML”. DNA and Cell Biology 23 (6): 351–4. (Jun 2004). doi:10.1089/104454904323145236. PMID 15231068.
“Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death”. Cell 74 (4): 609–19. (Aug 1993). doi:10.1016/0092-8674(93)90509-O. PMID 8358790.
“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. (Jul 2003). doi:10.1093/emboj/cdg343. PMC 165613. PMID 12853473.
“Bcl-2 targets the protein kinase Raf-1 to mitochondria”. Cell 87 (4): 629–38. (Nov 1996). doi:10.1016/s0092-8674(00)81383-5. PMID 8929532.
“Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members”. The Journal of Biological Chemistry 277 (30): 27217–26. (Jul 2002). doi:10.1074/jbc.M202945200. PMID 12000759.
“Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria”. The Journal of Biological Chemistry 277 (16): 13430–7. (Apr 2002). doi:10.1074/jbc.M108029200. PMID 11832478.
“Microtubule-targeting drugs induce bcl-2 phosphorylation and association with Pin1”. Neoplasia 3 (6): 550–9. (2001). doi:10.1038/sj.neo.7900213. PMC 1506558. PMID 11774038.
“Microtubule-targeting drugs induce Bcl-2 phosphorylation and association with Pin1”. Neoplasia 3 (1): 70–9. (2001). doi:10.1038/sj.neo.7900131. PMC 1505024. PMID 11326318.
“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)”. The EMBO Journal 16 (7): 1686–94. (Apr 1997). doi:10.1093/emboj/16.7.1686. PMC 1169772. PMID 9130713.
“Association of insulin receptor substrate proteins with Bcl-2 and their effects on its phosphorylation and antiapoptotic function”. Molecular Biology of the Cell 11 (2): 735–46. (Feb 2000). doi:10.1091/mbc.11.2.735. PMC 14806. PMID 10679027.
“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”. The Journal of Biological Chemistry 279 (38): 40209–19. (Sep 2004). doi:10.1074/jbc.M404056200. PMID 15210690.
“Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis”. Science 288 (5468): 1053–8. (May 2000). Bibcode: 2000Sci...288.1053O. doi:10.1126/science.288.5468.1053. PMID 10807576.
“Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A”. The Journal of Biological Chemistry 273 (51): 34157–63. (Dec 1998). doi:10.1074/jbc.273.51.34157. PMID 9852076.
“Presenilin 1 protein directly interacts with Bcl-2”. The Journal of Biological Chemistry 274 (43): 30764–9. (Oct 1999). doi:10.1074/jbc.274.43.30764. PMID 10521466.
“Bcl-2 associates with the ras-related protein R-ras p23”. Nature 366 (6452): 274–5. (Nov 1993). Bibcode: 1993Natur.366..274F. doi:10.1038/366274a0. PMID 8232588.
“A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity”. Oncogene 19 (50): 5736–46. (Nov 2000). doi:10.1038/sj.onc.1203948. PMID 11126360.
“Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy”. Nature 390 (6658): 413–7. (Nov 1997). Bibcode: 1997Natur.390..413I. doi:10.1038/37144. PMID 9389483.
“Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria”. Neuron 43 (1): 19–30. (Jul 2004). doi:10.1016/j.neuron.2004.06.021. PMID 15233914.
“The p53-binding protein 53BP2 also interacts with Bc12 and impedes cell cycle progression at G2/M”. Molecular and Cellular Biology 16 (7): 3884–92. (Jul 1996). doi:10.1128/MCB.16.7.3884. PMC 231385. PMID 8668206.

drugs.com (Global: 399^th place; Japanese: 1,603^rd place)

“Genasense (oblimersen sodium) FDA Approval Status - Drugs.com”. www.drugs.com. 2016年2月11日閲覧。

ensembl.org (Global: 1,626^th place; Japanese: 2,625^th place)

May2017.archive.ensembl.org

GRCh38: Ensembl release 89: ENSG00000171791 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000057329 - Ensembl, May 2017

fda.gov (Global: 447^th place; Japanese: 1,043^rd place)

“FDA approves venetoclax for CLL or SLL, with or without 17p deletion, after one prior therapy” (英語). U.S. Food and Drug Administration. 2020年5月4日閲覧。

harvard.edu (Global: 18^th place; Japanese: 107^th place)

ui.adsabs.harvard.edu

“Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation”. Science 226 (4678): 1097–9. (Nov 1984). Bibcode: 1984Sci...226.1097T. doi:10.1126/science.6093263. PMID 6093263.
PDB: 1G5M; “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. (March 2001). Bibcode: 2001PNAS...98.3012P. doi:10.1073/pnas.041619798. PMC 30598. PMID 11248023.
“Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells”. Nature 335 (6189): 440–2. (Sep 1988). Bibcode: 1988Natur.335..440V. doi:10.1038/335440a0. PMID 3262202.
“An inhibitor of Bcl-2 family proteins induces regression of solid tumours”. Nature 435 (7042): 677–81. (June 2005). Bibcode: 2005Natur.435..677O. doi:10.1038/nature03579. PMID 15902208.
“Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis”. Science 293 (5536): 1829–32. (Sep 2001). Bibcode: 2001Sci...293.1829P. doi:10.1126/science.1062257. PMID 11546872.
“Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis”. Science 288 (5468): 1053–8. (May 2000). Bibcode: 2000Sci...288.1053O. doi:10.1126/science.288.5468.1053. PMID 10807576.
“Bcl-2 associates with the ras-related protein R-ras p23”. Nature 366 (6452): 274–5. (Nov 1993). Bibcode: 1993Natur.366..274F. doi:10.1038/366274a0. PMID 8232588.
“Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy”. Nature 390 (6658): 413–7. (Nov 1997). Bibcode: 1997Natur.390..413I. doi:10.1038/37144. PMID 9389483.

medpagetoday.com (Global: 9,274^th place; Japanese: low place)

Smith, Michael (2015年12月7日). “Hard-to-Treat CLL Yields to Investigational Drug”. 2020年5月4日閲覧。
Bankhead, Charles (2016年4月11日). “FDA Approves AbbVie's BCL-2 Targeting Drug for CLL” (英語). Medpage Today {{cite news}}: 不明な引数|name-list-format=は無視されます。（もしかして：|name-list-style=） (説明)⚠

nih.gov (Global: 4^th place; Japanese: 24^th place)

pubmed.ncbi.nlm.nih.gov

“Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation”. Science 226 (4678): 1097–9. (Nov 1984). Bibcode: 1984Sci...226.1097T. doi:10.1126/science.6093263. PMID 6093263.
“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. (Oct 1986). doi:10.1016/0092-8674(86)90362-4. PMID 2875799.
PDB: 1G5M; “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. (March 2001). Bibcode: 2001PNAS...98.3012P. doi:10.1073/pnas.041619798. PMC 30598. PMID 11248023.
“Multiple functions of BCL-2 family proteins”. Cold Spring Harb Perspect Biol 5 (2): a008722. (2013). doi:10.1101/cshperspect.a008722. PMC 3552500. PMID 23378584.
“Bcl-2 Regulates Reactive Oxygen Species Signaling and a Redox-Sensitive Mitochondrial Proton Leak in Mouse Pancreatic ß-Cells”. Endocrinology 157 (6): 2270–2281. (2016). doi:10.1210/en.2015-1964. PMID 27070098.
“Bcl-2 Inhibition to Overcome Resistance to Chemo- and Immunotherapy”. International Journal of Molecular Sciences 19 (12): 3950. (Dec 2018). doi:10.3390/ijms19123950. PMC 6321604. PMID 30544835.
“Overexpression of nucleolin in chronic lymphocytic leukemia cells induces stabilization of bcl2 mRNA”. Blood 109 (7): 3069–75. (Apr 2007). doi:10.1182/blood-2006-08-043257. PMC 1852223. PMID 17179226.
“Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells”. Nature 335 (6189): 440–2. (Sep 1988). Bibcode: 1988Natur.335..440V. doi:10.1038/335440a0. PMID 3262202.
Kaiser, U.; Schilli, M.; Haag, U.; Neumann, K.; Kreipe, H.; Kogan, E.; Havemann, K. (1996-08). “Expression of bcl-2--protein in small cell lung cancer”. Lung Cancer (Amsterdam, Netherlands) 15 (1): 31–40. doi:10.1016/0169-5002(96)00568-5. ISSN 0169-5002. PMID 8865121.
“Saving death: apoptosis for intervention in transplantation and autoimmunity”. Clinical & Developmental Immunology 13 (2–4): 273–82. (2006). doi:10.1080/17402520600834704. PMC 2270759. PMID 17162368.
Hou, Wu-Shiun; Van Parijs, Luk (2004-06). “A Bcl-2-dependent molecular timer regulates the lifespan and immunogenicity of dendritic cells”. Nature Immunology 5 (6): 583–589. doi:10.1038/ni1071. ISSN 1529-2908. PMID 15133508.
“Apoptotic mechanisms and the synaptic pathology of schizophrenia”. Schizophrenia Research 81 (1): 47–63. (Jan 2006). doi:10.1016/j.schres.2005.08.014. PMID 16226876.
“Potential roles of antisense oligonucleotides in cancer therapy. The example of Bcl-2 antisense oligonucleotides”. European Journal of Pharmaceutics and Biopharmaceutics 54 (3): 263–9. (Nov 2002). doi:10.1016/S0939-6411(02)00060-7. PMID 12445555.
Vogler, M.; Dinsdale, D.; Dyer, M. J. S.; Cohen, G. M. (2009-03). “Bcl-2 inhibitors: small molecules with a big impact on cancer therapy”. Cell Death and Differentiation 16 (3): 360–367. doi:10.1038/cdd.2008.137. ISSN 1476-5403. PMID 18806758.
“An inhibitor of Bcl-2 family proteins induces regression of solid tumours”. Nature 435 (7042): 677–81. (June 2005). Bibcode: 2005Natur.435..677O. doi:10.1038/nature03579. PMID 15902208.
“Therapeutic efficacy of ABT-737, a selective inhibitor of BCL-2, in small cell lung cancer”. Cancer Research 68 (7): 2321–8. (April 2008). doi:10.1158/0008-5472.can-07-5031. PMC 3159963. PMID 18381439.
Hauck, Paula; Chao, Bo H.; Litz, Julie; Krystal, Geoffrey W. (2009-04). “Alterations in the Noxa/Mcl-1 axis determine sensitivity of small cell lung cancer to the BH3 mimetic ABT-737”. Molecular Cancer Therapeutics 8 (4): 883–892. doi:10.1158/1535-7163.MCT-08-1118. ISSN 1535-7163. PMID 19372561.
“Phase I study of Navitoclax (ABT-263), a novel Bcl-2 family inhibitor, in patients with small-cell lung cancer and other solid tumors”. Journal of Clinical Oncology 29 (7): 909–16. (March 2011). doi:10.1200/JCO.2010.31.6208. PMC 4668282. PMID 21282543.
“Phase II study of single-agent navitoclax (ABT-263) and biomarker correlates in patients with relapsed small cell lung cancer”. Clinical Cancer Research 18 (11): 3163–9. (June 2012). doi:10.1158/1078-0432.CCR-11-3090. PMC 3715059. PMID 22496272.
“Mechanism-based pharmacokinetic/pharmacodynamic meta-analysis of navitoclax (ABT-263) induced thrombocytopenia”. Cancer Chemotherapy and Pharmacology 74 (3): 593–602. (September 2014). doi:10.1007/s00280-014-2530-9. PMID 25053389.
“Selective BCL-2 inhibition by ABT-199 causes on-target cell death in acute myeloid leukemia”. Cancer Discovery 4 (3): 362–75. (March 2014). doi:10.1158/2159-8290.CD-13-0609. PMC 3975047. PMID 24346116.
“Targeting BCL2 with Venetoclax in Relapsed Chronic Lymphocytic Leukemia”. The New England Journal of Medicine 374 (4): 311–22. (January 2016). doi:10.1056/NEJMoa1513257. PMID 26639348.
“Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3”. Cell 116 (4): 527–40. (Feb 2004). doi:10.1016/s0092-8674(04)00162-x. PMID 14980220.
“Discovery of small-molecule inhibitors of Bcl-2 through structure-based computer screening”. Journal of Medicinal Chemistry 44 (25): 4313–24. (Dec 2001). doi:10.1021/jm010016f. PMID 11728179.
“p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum”. The Journal of Cell Biology 139 (2): 327–38. (Oct 1997). doi:10.1083/jcb.139.2.327. PMC 2139787. PMID 9334338.
“Development of a high-throughput fluorescence polarization assay for Bcl-x(L)”. Analytical Biochemistry 307 (1): 70–5. (Aug 2002). doi:10.1016/s0003-2697(02)00028-3. PMID 12137781.
“Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function”. Molecular Cell 17 (3): 393–403. (Feb 2005). doi:10.1016/j.molcel.2004.12.030. PMID 15694340.
“Bim: a novel member of the Bcl-2 family that promotes apoptosis”. The EMBO Journal 17 (2): 384–95. (Jan 1998). doi:10.1093/emboj/17.2.384. PMC 1170389. PMID 9430630.
“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. (Sep 1998). doi:10.1210/mend.12.9.0166. PMID 9731710.
“Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein”. Journal of Virology 72 (11): 8586–96. (Nov 1998). doi:10.1128/JVI.72.11.8586-8596.1998. PMC 110269. PMID 9765397.
“Breast cancer cells can evade apoptosis-mediated selective killing by a novel small molecule inhibitor of Bcl-2”. Cancer Research 64 (21): 7947–53. (Nov 2004). doi:10.1158/0008-5472.CAN-04-0945. PMID 15520201.
“Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis”. Science 293 (5536): 1829–32. (Sep 2001). Bibcode: 2001Sci...293.1829P. doi:10.1126/science.1062257. PMID 11546872.
“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. (Aug 2003). doi:10.1016/s0006-291x(03)01387-1. PMID 12901880.
“Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins”. Cell 79 (2): 341–51. (Oct 1994). doi:10.1016/0092-8674(94)90202-X. PMID 7954800.
“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. (Jan 2000). doi:10.1074/jbc.275.2.1439. PMID 10625696.
“BNIP3alpha: a human homolog of mitochondrial proapoptotic protein BNIP3”. Cancer Research 59 (3): 533–7. (Feb 1999). PMID 9973195.
“Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death”. Cell 80 (2): 285–91. (Jan 1995). doi:10.1016/0092-8674(95)90411-5. PMID 7834748.
“Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis”. Nature Cell Biology 2 (1): 1–6. (Jan 2000). doi:10.1038/71316. PMID 10620799.
“Nuclear partners of Bcl-2: Bax and PML”. DNA and Cell Biology 23 (6): 351–4. (Jun 2004). doi:10.1089/104454904323145236. PMID 15231068.
“Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death”. Cell 74 (4): 609–19. (Aug 1993). doi:10.1016/0092-8674(93)90509-O. PMID 8358790.
“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. (Jul 2003). doi:10.1093/emboj/cdg343. PMC 165613. PMID 12853473.
“Bcl-2 targets the protein kinase Raf-1 to mitochondria”. Cell 87 (4): 629–38. (Nov 1996). doi:10.1016/s0092-8674(00)81383-5. PMID 8929532.
“Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members”. The Journal of Biological Chemistry 277 (30): 27217–26. (Jul 2002). doi:10.1074/jbc.M202945200. PMID 12000759.
“Fas-mediated apoptosis in neuroblastoma requires mitochondrial activation and is inhibited by FLICE inhibitor protein and Bcl-2”. Cancer Research 61 (12): 4864–72. (Jun 2001). PMID 11406564.
“Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria”. The Journal of Biological Chemistry 277 (16): 13430–7. (Apr 2002). doi:10.1074/jbc.M108029200. PMID 11832478.
“Microtubule-targeting drugs induce bcl-2 phosphorylation and association with Pin1”. Neoplasia 3 (6): 550–9. (2001). doi:10.1038/sj.neo.7900213. PMC 1506558. PMID 11774038.
“Microtubule-targeting drugs induce Bcl-2 phosphorylation and association with Pin1”. Neoplasia 3 (1): 70–9. (2001). doi:10.1038/sj.neo.7900131. PMC 1505024. PMID 11326318.
“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)”. The EMBO Journal 16 (7): 1686–94. (Apr 1997). doi:10.1093/emboj/16.7.1686. PMC 1169772. PMID 9130713.
“Association of insulin receptor substrate proteins with Bcl-2 and their effects on its phosphorylation and antiapoptotic function”. Molecular Biology of the Cell 11 (2): 735–46. (Feb 2000). doi:10.1091/mbc.11.2.735. PMC 14806. PMID 10679027.
“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”. The Journal of Biological Chemistry 279 (38): 40209–19. (Sep 2004). doi:10.1074/jbc.M404056200. PMID 15210690.
“Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis”. Science 288 (5468): 1053–8. (May 2000). Bibcode: 2000Sci...288.1053O. doi:10.1126/science.288.5468.1053. PMID 10807576.
“Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A”. The Journal of Biological Chemistry 273 (51): 34157–63. (Dec 1998). doi:10.1074/jbc.273.51.34157. PMID 9852076.
“Presenilin 1 protein directly interacts with Bcl-2”. The Journal of Biological Chemistry 274 (43): 30764–9. (Oct 1999). doi:10.1074/jbc.274.43.30764. PMID 10521466.
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“A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity”. Oncogene 19 (50): 5736–46. (Nov 2000). doi:10.1038/sj.onc.1203948. PMID 11126360.
“Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy”. Nature 390 (6658): 413–7. (Nov 1997). Bibcode: 1997Natur.390..413I. doi:10.1038/37144. PMID 9389483.
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pmc.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

Human PubMed Reference:
Mouse PubMed Reference:
Kaiser, U.; Schilli, M.; Haag, U.; Neumann, K.; Kreipe, H.; Kogan, E.; Havemann, K. (1996-08). “Expression of bcl-2--protein in small cell lung cancer”. Lung Cancer (Amsterdam, Netherlands) 15 (1): 31–40. doi:10.1016/0169-5002(96)00568-5. ISSN 0169-5002. PMID 8865121.
Hou, Wu-Shiun; Van Parijs, Luk (2004-06). “A Bcl-2-dependent molecular timer regulates the lifespan and immunogenicity of dendritic cells”. Nature Immunology 5 (6): 583–589. doi:10.1038/ni1071. ISSN 1529-2908. PMID 15133508.
Vogler, M.; Dinsdale, D.; Dyer, M. J. S.; Cohen, G. M. (2009-03). “Bcl-2 inhibitors: small molecules with a big impact on cancer therapy”. Cell Death and Differentiation 16 (3): 360–367. doi:10.1038/cdd.2008.137. ISSN 1476-5403. PMID 18806758.
Hauck, Paula; Chao, Bo H.; Litz, Julie; Krystal, Geoffrey W. (2009-04). “Alterations in the Noxa/Mcl-1 axis determine sensitivity of small cell lung cancer to the BH3 mimetic ABT-737”. Molecular Cancer Therapeutics 8 (4): 883–892. doi:10.1158/1535-7163.MCT-08-1118. ISSN 1535-7163. PMID 19372561.

rcsb.org (Global: 8,838^th place; Japanese: low place)

PDB: 1G5M; “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. (March 2001). Bibcode: 2001PNAS...98.3012P. doi:10.1073/pnas.041619798. PMC 30598. PMID 11248023.

stokesentinel.co.uk (Global: 5,309^th place; Japanese: low place)

“'Miracle drug cured my cancer!': Amazing three-week recovery of Staffordshire sufferer”. Stoke Sentinel. 2014年5月12日時点のオリジナルよりアーカイブ。2014年5月10日閲覧。

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“ENSG00000171791_BCL2”. www.orthomam.univ-montp2.fr. 2020年5月14日閲覧。

web.archive.org (Global: 1^st place; Japanese: 1^st place)

Liao, Grace (2011年8月12日). “ABT-199 BH-3 Mimetic Enters Phase Ia Trial For Chronic Lymphocytic Leukemia”. Asian Scientist. オリジナルの2012年7月18日時点におけるアーカイブ。 2016年2月11日閲覧。 {{cite news}}: 不明な引数|name-list-format=は無視されます。（もしかして：|name-list-style=） (説明)⚠
“'Miracle drug cured my cancer!': Amazing three-week recovery of Staffordshire sufferer”. Stoke Sentinel. 2014年5月12日時点のオリジナルよりアーカイブ。2014年5月10日閲覧。

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GRCh38: Ensembl release 89: ENSG00000171791 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000057329 - Ensembl, May 2017

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Kaiser, U.; Schilli, M.; Haag, U.; Neumann, K.; Kreipe, H.; Kogan, E.; Havemann, K. (1996-08). “Expression of bcl-2--protein in small cell lung cancer”. Lung Cancer (Amsterdam, Netherlands) 15 (1): 31–40. doi:10.1016/0169-5002(96)00568-5. ISSN 0169-5002. PMID 8865121.
Hou, Wu-Shiun; Van Parijs, Luk (2004-06). “A Bcl-2-dependent molecular timer regulates the lifespan and immunogenicity of dendritic cells”. Nature Immunology 5 (6): 583–589. doi:10.1038/ni1071. ISSN 1529-2908. PMID 15133508.
Vogler, M.; Dinsdale, D.; Dyer, M. J. S.; Cohen, G. M. (2009-03). “Bcl-2 inhibitors: small molecules with a big impact on cancer therapy”. Cell Death and Differentiation 16 (3): 360–367. doi:10.1038/cdd.2008.137. ISSN 1476-5403. PMID 18806758.
Hauck, Paula; Chao, Bo H.; Litz, Julie; Krystal, Geoffrey W. (2009-04). “Alterations in the Noxa/Mcl-1 axis determine sensitivity of small cell lung cancer to the BH3 mimetic ABT-737”. Molecular Cancer Therapeutics 8 (4): 883–892. doi:10.1158/1535-7163.MCT-08-1118. ISSN 1535-7163. PMID 19372561.

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