The DOI matches its Crossref record.
Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Hanahan, D., & Weinberg, R. A. (2000) · Cell · doi:10.1016/s0092-8674(00)81683-9 · Cited by 29,219
Apoptosis: A Review of Programmed Cell Death
Elmore, S. (2007) · Toxicologic Pathology · doi:10.1080/01926230701320337 · Cited by 13,853
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680
Apoptosis in the Pathogenesis and Treatment of Disease
Thompson, C. B. (1995) · Science · doi:10.1126/science.7878464 · Cited by 6,524
Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death
Oltval, Z. N., Milliman, C. L., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)90509-o · Cited by 6,003
Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
The Bcl2 family: regulators of the cellular life-or-death switch
Cory, S., & Adams, J. M. (2002) · Nature Reviews Cancer · doi:10.1038/nrc883 · Cited by 4,032
Self-citationBcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
Hockenbery, D., Nuñez, G., Milliman, C., Schreiber, R. D., & Korsmeyer, S. J. (1990) · Nature · doi:10.1038/348334a0 · Cited by 3,720
Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy
Czabotar, P. E., Lessene, G., Strasser, A., & Adams, J. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3722 · Cited by 3,219
Self-citationABT-199, a potent and selective BCL-2 inhibitor, achieves antitumor activity while sparing platelets
Souers, A. J., Leverson, J. D., Boghaert, E. R., Ackler, S. L., Catron, N. D., Chen, J., Dayton, B. D., Ding, H., Enschede, S. H., Fairbrother, W. J., et al. (2013) · Nature Medicine · doi:10.1038/nm.3048 · Cited by 3,058
(2001) · PubMed · Cited by 2,381
Reflecting on 25 years with MYC
Meyer, N., & Penn, L. Z. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2231 · Cited by 1,575
Akt Stimulates Aerobic Glycolysis in Cancer Cells
Elstrom, R. L., Bauer, D. E., Buzzai, M., Karnauskas, R., Harris, M. H., Plas, D. R., Zhuang, H., Cinalli, R. M., Alavi, A., Rudin, C. M., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-2904 · Cited by 1,454
Mitochondrial dynamics and apoptosis
Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270
BCL2 protein is topographically restricted in tissues characterized by apoptotic cell death.
Hockenbery, D. M., Zutter, M., Hickey, W., Nahm, M., & Korsmeyer, S. J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.16.6961 · Cited by 1,252
McDonnell, T. J., Deane, N., Platt, F. M., Nunez, G., Jaeger, U., McKearn, J. P., & Korsmeyer, S. J. (1989) · Cell · doi:10.1016/0092-8674(89)90174-8 · Cited by 1,213
Tissue-specific functions of individual glutathione peroxidases
Brigelius-Flohé, R. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00173-2 · Cited by 1,114
From basic apoptosis discoveries to advanced selective BCL-2 family inhibitors
Ashkenazi, A., Fairbrother, W. J., Leverson, J. D., & Souers, A. J. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.253 · Cited by 903
Bcl‐2 and Fas/APO‐1 regulate distinct pathways to lymphocyte apoptosis.
Strasser, A., Harris, A. W., Huang, D. C., Krammer, P. H., & Cory, S. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00304.x · Cited by 784
Self-citationThirty years of BCL-2: translating cell death discoveries into novel cancer therapies
Delbridge, A. R. D., Grabow, S., Strasser, A., & Vaux, D. L. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2015.17 · Cited by 752
Self-citationThe BCL2 Family: Key Mediators of the Apoptotic Response to Targeted Anticancer Therapeutics
Hata, A. N., Engelman, J. A., & Faber, A. C. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-0011 · Cited by 619
The inhibitors of apoptosis (IAPs) as cancer targets
Hunter, A. M., LaCasse, E. C., & Korneluk, R. G. (2007) · Apoptosis · doi:10.1007/s10495-007-0087-3 · Cited by 565
Multiple Functions of BCL-2 Family Proteins
Hardwick, J. M., & Soane, L. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008722 · Cited by 564
The BCL-2 arbiters of apoptosis and their growing role as cancer targets
Adams, J. M., & Cory, S. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.161 · Cited by 530
Self-citationtwist is a potential oncogene that inhibits apoptosis
Maestro, R., Tos, A. P. D., Hamamori, Y., Krasnokutsky, S., Sartorelli, V., Kedes, L., Doglioni, C., Beach, D. H., & Hannon, G. J. (1999) · Genes & Development · doi:10.1101/gad.13.17.2207 · Cited by 516
A fate worse than death: apoptosis as an oncogenic process
Ichim, G., & Tait, S. W. G. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.58 · Cited by 451
The BCL2 family: from apoptosis mechanisms to new advances in targeted therapy
Vogler, M., Braun, Y., Smith, V. M., Westhoff, M.-A., Pereira, R. S., Pieper, N. M., Anders, M., Callens, M., Vervliet, T., Abbas, M., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02176-0 · Cited by 462
Clusterin inhibits apoptosis by interacting with activated Bax
Zhang, H., Kim, J. K., Edwards, C. A., Xu, Z., Taichman, R., & Wang, C.-Y. (2005) · Nature Cell Biology · doi:10.1038/ncb1291 · Cited by 453
Paumen, M. B., Ishida, Y., Muramatsu, M., Yamamoto, M., & Honjo, T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3324 · Cited by 349
Dynamic causal modelling: A critical review of the biophysical and statistical foundations
Daunizeau, J., David, O., & Stephan, K. E. (2011) · NeuroImage · doi:10.1016/j.neuroimage.2009.11.062 · Cited by 331
Mitochondria—Judges and Executioners of Cell Death Sentences
Bhola, P. D., & Letai, A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.019 · Cited by 326
Cellular senescence and cancer treatment
Schmitt, C. A. (2007) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2006.08.005 · Cited by 254
The BCL-2 family of proteins and mitochondrial outer membrane permeabilisation
Birkinshaw, R. W., & Czabotar, P. E. (2017) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2017.04.001 · Cited by 229
Energy Metabolism during Apoptosis
Garland, J. M., & Halestrap, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.8.4680 · Cited by 207
Myeloid Development Is Selectively Disrupted in PU.1 Null Mice
Anderson, K. L., Smith, K. A., Conners, K., McKercher, S. R., Maki, R. A., & Torbett, B. E. (1998) · Blood · doi:10.1182/blood.v91.10.3702 · Cited by 193
Chao, J.-R., Wang, J.-M., Lee, S.-F., Peng, H.-W., Lin, Y.-H., Chou, C.-H., Li, J.-C., Huang, H.-M., Chou, C.-K., Kuo, M.-L., et al. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.8.4883 · Cited by 185
The AML1/ETO fusion protein activates transcription of BCL-2
Klampfer, L., Zhang, J., Zelenetz, A. O., Uchida, H., & Nimer, S. D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.14059 · Cited by 182
Walensky, L. D., & Gavathiotis, E. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.08.009 · Cited by 173
Programmed cell death and the control of cell survival
Raff, M. C., Barres, B. A., Burne, J. F., Coles, H. S. R., Ishizaki, Y., & Jacobson, M. D. (1994) · Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences · doi:10.1098/rstb.1994.0104 · Cited by 166
Rational Design of Proteolytically Stable, Cell-Permeable Peptide-Based Selective Mcl-1 Inhibitors
Muppidi, A., Doi, K., Edwardraja, S., Drake, E. J., Gulick, A. M., Wang, H.-G., & Lin, Q. (2012) · Journal of the American Chemical Society · doi:10.1021/ja306864v · Cited by 156
Akasaka, T., Lossos, I. S., & Levy, R. (2003) · Blood · doi:10.1182/blood-2002-08-2482 · Cited by 156
The Role of Intrinsic Pathway in Apoptosis Activation and Progression in Peyronie’s Disease
Loreto, C., La Rocca, G., Anzalone, R., Caltabiano, R., Vespasiani, G., Castorina, S., Ralph, D. J., Cellek, S., Musumeci, G., Giunta, S., et al. (2014) · BioMed Research International · doi:10.1155/2014/616149 · Cited by 108
AbouAitah, K., Hassan, H. A., Swiderska-Sroda, A., Gohar, L., Shaker, O. G., Wojnarowicz, J., Opalinska, A., Smalc-Koziorowska, J., Gierlotka, S., & Lojkowski, W. (2020) · Cancers · doi:10.3390/cancers12010144 · Cited by 105
Abraham, M., Klein, S., Bulvik, B., Wald, H., Weiss, I. D., Olam, D., Weiss, L., Beider, K., Eizenberg, O., Wald, O., et al. (2017) · Leukemia · doi:10.1038/leu.2017.82 · Cited by 104
Crossing paths: interactions between the cell death machinery and growth factor survival signals
Brumatti, G., Salmanidis, M., & Ekert, P. G. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0288-8 · Cited by 85
Kalemkerian, G. P., Ou, X., Adil, M. R., Rosati, R., Khoulani, M. M., Madan, S. K., & Pettit, G. R. (1999) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s002800050931 · Cited by 84
Small molecule modulators of protein-protein interactions: selected case studies
Aeluri, M., Chamakuri, S., Dasari, B., Guduru, S. K. R., Jimmidi, R., Jogula, S., & Arya, P. (2014) · Chemical Reviews · doi:10.1021/cr4004049 · Cited by 79
Roy, M. K., Kuwabara, Y., Hara, K., Watanabe, Y., & Tamai, Y. (2002) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(02)74284-7 · Cited by 74
Is the endometrium or oocyte/embryo affected in endometriosis?
Garcia-Velasco, J. A., & Arici, A. (1999) · Human Reproduction · doi:10.1093/humrep/14.suppl_2.77 · Cited by 68
Enzyme-cleavable polymeric micelles for the intracellular delivery of proapoptotic peptides
Kern, H. B., Srinivasan, S., Convertine, A. J., Hockenbery, D., Press, O. W., & Stayton, P. S. (2017) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.6b01178 · Cited by 63
Ando, H., Kawaai, K., Bonneau, B., & Mikoshiba, K. (2018) · Advances in Biological Regulation · doi:10.1016/j.jbior.2017.12.001 · Cited by 55
Stat3 Is Required for Cytoprotection of the Respiratory Epithelium during Adenoviral Infection
Matsuzaki, Y., Xu, Y., Ikegami, M., Besnard, V., Park, K.-S., Hull, W. M., Wert, S. E., & Whitsett, J. A. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.1.527 · Cited by 51
BH3 Mimetics in Hematologic Malignancies
Klener, P., Sovilj, D., Renesova, N., & Andera, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810157 · Cited by 31
Phenylpropanoids, eugenol scaffold, and its derivatives as anticancer
Fadilah, F., Yanuar, A., Arsianti, A., & Andrajati, R. (2017) · Asian Journal of Pharmaceutical and Clinical Research · doi:10.22159/ajpcr.2017.v10i3.16071 · Cited by 28
Mu, J., Kanzaki, T., Si, X., Tomimatsu, T., Fukuda, H., Shioji, M., Murata, Y., Sugimoto, Y., & Ichikawa, A. (2003) · Biology of Reproduction · doi:10.1095/biolreprod.102.008029 · Cited by 26
Development of new cell lines for animal cell biotechnology
Macdonald, C. (1990) · Critical Reviews in Biotechnology · doi:10.3109/07388559009068265 · Cited by 25
Therapeutics Targeting the Core Apoptotic Machinery
Hamilton, C., Fox, J. P., Longley, D. B., & Higgins, C. A. (2021) · Cancers · doi:10.3390/cancers13112618 · Cited by 26
Anti-c-myc RNAi-Based Onconanotherapeutics
Habib, S., Ariatti, M., & Singh, M. (2020) · Biomedicines · doi:10.3390/biomedicines8120612 · Cited by 23
Counterselection against Dμ Is Mediated through Immunoglobulin (Ig)α-Igβ
Gong, S., Sanchez, M., & Nussenzweig, M. C. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.6.2079 · Cited by 16
Apoptosis and Related Proteins during Parturition in Prostaglandin F Receptor-Deficient Mice
Mu, J., Kanzaki, T., Si, X., Tomimatsu, T., Fukuda, H., Fujii, E., Hosono, T., Murata, Y., Sugimoto, Y., & Ichikawa, A. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6698 · Cited by 8
Metadata
- Authors
- Vaux, D. L., Cory, S., & Adams, J. M.
- Venue
- Nature
- Published
- 1988-09
- Volume
- 335
- Issue
- 6189
- Pages
- 440-442
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2009183764
- Cited by
- 3,219
- References
- 0
- FWCI
- 29.25
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.