BCL-2 family member BOK is widely expressed but its loss has only minimal impact in mice
Open accessAbstract
BOK/MTD was discovered as a protein that binds to the anti-apoptotic Bcl-2 family member MCL-1 and shares extensive amino-acid sequence similarity to BAX and BAK, which are essential for the effector phase of apoptosis. Therefore, and on the basis of its reported expression pattern, BOK is thought to function in a BAX/BAK-like pro-apoptotic manner in female reproductive tissues. In order to determine the function of BOK, we examined its expression in diverse tissues and investigated the consequences of its loss in Bok(-/-) mice. We confirmed that Bok mRNA is prominently expressed in the ovaries and uterus, but also observed that it is present at readily detectable levels in several other tissues such as the brain and myeloid cells. Bok(-/-) mice were produced at the expected Mendelian ratio, appeared outwardly normal and proved fertile. Histological examination revealed that major organs in Bok(-/-) mice displayed no morphological aberrations. Although several human cancers have somatically acquired copy number loss of the Bok gene and BOK is expressed in B lymphoid cells, we found that its deficiency did not accelerate lymphoma development in Eμ-Myc transgenic mice. Collectively, these results indicate that Bok may have a role that largely overlaps with that of other members of the Bcl-2 family, or may have a function restricted to specific stress stimuli and/or tissues.
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
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Bok−/−, Bax−/−Bok−/− as well as Bak1−/−Bok−/− mice display no obvious abnormalities (except for persistence of primordial follicle oocytes in aged Bax−/−Bok−/− females).
“Of note, Bok−/−, Bax−/−Bok−/− as well as Bak1−/−Bok−/− mice display no obvious abnormalities (except for persistence of primordial follicle oocytes in aged Bax−/−Bok−/− females) [154, 155]”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [154]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method
Livak, K. J., & Schmittgen, T. D. (2001) · Methods · doi:10.1006/meth.2001.1262 · Cited by 180,860 · see citing works
The BCL-2 protein family: opposing activities that mediate cell death
Youle, R. J., & Strasser, A. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2308 · Cited by 4,704 · see citing works
Self-citationThe landscape of somatic copy-number alteration across human cancers
Beroukhim, R., Mermel, C. H., Porter, D., Wei, G., Raychaudhuri, S., Donovan, J., Barretina, J., Boehm, J. S., Dobson, J., Urashima, M., et al. (2010) · Nature · doi:10.1038/nature08822 · Cited by 4,017 · see citing works
The c-myc oncogene driven by immunoglobulin enhancers induces lymphoid malignancy in transgenic mice
Adams, J. M., Harris, A. W., Pinkert, C. A., Corcoran, L. M., Alexander, W. S., Cory, S., Palmiter, R. D., & Brinster, R. L. (1985) · Nature · doi:10.1038/318533a0 · Cited by 1,778 · see citing works
Cheng, E. H. Y., Wei, M. C., Weiler, S., Flavell, R. A., Mak, T. W., Lindsten, T., & Korsmeyer, S. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00320-3 · Cited by 1,708 · see citing works
Bouillet, P., Metcalf, D., Huang, D. C. S., Tarlinton, D. M., Kay, T. W. H., Köntgen, F., Adams, J. M., & Strasser, A. (1999) · Science · doi:10.1126/science.286.5445.1735 · Cited by 1,504 · see citing works
Self-citationLindsten, T., Ross, A. J., King, A., Zong, W.-X., Rathmell, J. C., Shiels, H. A., Ulrich, E., Waymire, K. G., Mahar, P., Frauwirth, K., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00136-2 · Cited by 1,489 · see citing works
Bax-Deficient Mice with Lymphoid Hyperplasia and Male Germ Cell Death
Knudson, C. M., Tung, K. S. K., Tourtellotte, W. G., Brown, G. A. J., & Korsmeyer, S. J. (1995) · Science · doi:10.1126/science.270.5233.96 · Cited by 1,480 · see citing works
p53- and Drug-Induced Apoptotic Responses Mediated by BH3-Only Proteins Puma and Noxa
Villunger, A., Michalak, E. M., Coultas, L., Müllauer, F., Böck, G., Ausserlechner, M. J., Adams, J. M., & Strasser, A. (2003) · Science · doi:10.1126/science.1090072 · Cited by 1,327 · see citing works
Self-citationSchwenk, F., Baron, U., & Rajewsky, K. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.24.5080 · Cited by 1,289 · see citing works
Hotchkiss, R. S., Strasser, A., McDunn, J. E., & Swanson, P. E. (2009) · New England Journal of Medicine · doi:10.1056/nejmra0901217 · Cited by 1,150 · see citing works
Self-citationApoptosis Initiated When BH3 Ligands Engage Multiple Bcl-2 Homologs, Not Bax or Bak
Willis, S. N., Fletcher, J. I., Kaufmann, T., van Delft, M. F., Chen, L., Czabotar, P. E., Ierino, H., Lee, E. F., Fairlie, W. D., Bouillet, P., et al. (2007) · Science · doi:10.1126/science.1133289 · Cited by 1,125 · see citing works
Self-citationBH3-Only Proteins—Essential Initiators of Apoptotic Cell Death
Huang, D. C. S., & Strasser, A. (2000) · Cell · doi:10.1016/s0092-8674(00)00187-2 · Cited by 1,044 · see citing works
Self-citationHow do BCL-2 proteins induce mitochondrial outer membrane permeabilization?
Chipuk, J. E., & Green, D. R. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.01.007 · Cited by 982 · see citing works
Zong, W., Lindsten, T., Ross, A. J., MacGregor, G. R., & Thompson, C. B. (2001) · Genes & Development · doi:10.1101/gad.897601 · Cited by 809 · see citing works
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 · see citing works
Self-citationBAX Is Required for Neuronal Death after Trophic Factor Deprivation and during Development
Deckwerth, T. L., Elliott, J. L., Knudson, C. M., Johnson, E. M., Snider, W. D., & Korsmeyer, S. J. (1996) · Neuron · doi:10.1016/s0896-6273(00)80173-7 · Cited by 749 · see citing works
Bax suppresses tumorigenesis and stimulates apoptosis in vivo
Yin, C., Knudson, C. M., Korsmeyer, S. J., & Dyke, T. V. (1997) · Nature · doi:10.1038/385637a0 · Cited by 650 · see citing works
Diagnosing and exploiting cancer's addiction to blocks in apoptosis
Letai, A. G. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2297 · Cited by 577 · see citing works
Expansion and evolution of cell death programmes
Degterev, A., & Yuan, J. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2393 · Cited by 548 · see citing works
Bim is a suppressor of Myc-induced mouse B cell leukemia
Egle, A., Harris, A. W., Bouillet, P., & Cory, S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401471101 · Cited by 482 · see citing works
Self-citationHsu, S. Y., Kaipia, A. J., McGee, E. A., Lomeli, M. R., & Hsueh, A. J. W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12401 · Cited by 369 · see citing works
Deficiency in Bak and Bax perturbs thymic selection and lymphoid homeostasis
Rathmell, J. C., Lindsten, T., Zong, W., Cinalli, R. M., & Thompson, C. B. (2002) · Nature Immunology · doi:10.1038/ni834 · Cited by 297 · see citing works
The role of BH3-only protein Bim extends beyond inhibiting Bcl-2–like prosurvival proteins
Mérino, D., Giam, M., Hughes, P., Siggs, O. M., Heger, K., O’Reilly, L. A., Adams, J. M., Strasser, A., Lee, E. F., Fairlie, W. D., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200905153 · Cited by 186 · see citing works
Self-citationEischen, C. M., Roussel, M. F., Korsmeyer, S. J., & Cleveland, J. L. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.22.7653-7662.2001 · Cited by 183 · see citing works
Suppression of tumorigenesis by the p53 target PUMA
Hemann, M. T., Zilfou, J. T., Zhao, Z., Burgess, D. J., Hannon, G. J., & Lowe, S. W. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403286101 · Cited by 180 · see citing works
Puma and to a lesser extent Noxa are suppressors of Myc-induced lymphomagenesis
Michalak, E. M., Jansen, E. S., Happo, L., Cragg, M. S., Tai, L., Smyth, G. K., Strasser, A., Adams, J. M., & Scott, C. L. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2008.195 · Cited by 152 · see citing works
Self-citationSelection against PUMA Gene Expression in Myc-Driven B-Cell Lymphomagenesis
Garrison, S. P., Jeffers, J. R., Yang, C., Nilsson, J. A., Hall, M. A., Rehg, J. E., Yue, W., Yu, J., Zhang, L., Onciu, M. M., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00907-07 · Cited by 145 · see citing works
Inohara, N., Ekhterae, D., Garcia, I., Carrió, R., Merino, J., Merry, A. C., Chen, S., & Núñez, G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.15.8705 · Cited by 129 · see citing works
Shibata, M., Liu, M., Knudson, C. M., Shibata, E., Yoshidome, K., Bandey, T., Korsmeyer, S. J., & Green, J. E. (1999) · The EMBO Journal · doi:10.1093/emboj/18.10.2692 · Cited by 127 · see citing works
Hsu, S. Y., & Hsueh, A. J. W. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.46.30139 · Cited by 69 · see citing works
A novel Mtd splice isoform is responsible for trophoblast cell death in pre-eclampsia
Soleymanlou, N., Wu, Y., Wang, J., Todros, T., Ietta, F., Jurisicova, A., Post, M., & Caniggia, I. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401593 · Cited by 68 · see citing works
Ray, J. E., Garcia, J., Jurisicova, A., & Caniggia, I. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.167 · Cited by 49 · see citing works
Gao, S., Fu, W., Dürrenberger, M. B., Geyter, C. D., & Zhang, H. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-4543-3 · Cited by 36 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- Hotchkiss RS, Strasser A, McDunn JE, Swanson PE. Cell death. N Engl J Med 2009; 361: 1570-1583.
Cited by
Sorted by citations
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 · see citing works
Self-citationControl 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 · see citing works
Self-citationMitochondria as multifaceted regulators of cell death
Bock, F. J., & Tait, S. W. G. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0173-8 · Cited by 2,482 · see citing works
How does p53 induce apoptosis and how does this relate to p53-mediated tumour suppression
Aubrey, B. J., Kelly, G. L., Janic, A., Herold, M. J., & Strasser, A. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.169 · Cited by 1,395 · see citing works
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 · see citing works
Self-citationMOMP, cell suicide as a BCL-2 family business
Kalkavan, H., & Green, D. R. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.179 · Cited by 667 · see citing works
BCL-2 proteins and apoptosis: Recent insights and unknowns
Edlich, F. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.06.190 · Cited by 631 · see citing works
Targeting BCL-2 regulated apoptosis in cancer
Campbell, K. J., & Tait, S. W. G. (2018) · Open Biology · doi:10.1098/rsob.180002 · Cited by 546 · see citing works
The BCL-2 protein family, BH3-mimetics and cancer therapy
Delbridge, A. R. D., & Strasser, A. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.50 · Cited by 538 · see citing works
Self-citationApoptotic cell death in disease—Current understanding of the NCCD 2023
Vitale, I., Pietrocola, F., Guilbaud, E., Aaronson, S. A., Abrams, J., Adam, D., Agostini, M., Agostinis, P., Alnemri, E. S., Altucci, L., et al. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01153-w · Cited by 359 · see citing works
The concept of intrinsic versus extrinsic apoptosis
Lossi, L. (2022) · Biochemical Journal · doi:10.1042/bcj20210854 · Cited by 355 · see citing works
Why do BCL-2 inhibitors work and where should we use them in the clinic?
Montero, J., & Letai, A. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.183 · Cited by 325 · see citing works
BCL-2 family: integrating stress responses at the ER to control cell demise
Pihán, P., Carreras-Sureda, A., & Hetz, C. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.82 · Cited by 274 · see citing works
BOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation
Llambi, F., Wang, Y.-M., Victor, B., Yang, M., Schneider, D. M., Gingras, S., Parsons, M. J., Zheng, J. H., Brown, S. A., Pelletier, S., et al. (2016) · Cell · doi:10.1016/j.cell.2016.02.026 · Cited by 261 · see citing works
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 · see citing works
Embryogenesis and Adult Life in the Absence of Intrinsic Apoptosis Effectors BAX, BAK, and BOK
Ke, F., Vanyai, H. K., Cowan, A. D., Delbridge, A. R. D., Whitehead, L. W., Grabow, S., Czabotar, P. E., Voss, A. K., & Strasser, A. (2018) · Cell · doi:10.1016/j.cell.2018.04.036 · Cited by 205 · see citing works
Self-citationPro-apoptotic complexes of BAX and BAK on the outer mitochondrial membrane
Wolf, P., Schoeniger, A., & Edlich, F. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119317 · Cited by 205 · see citing works
BAX to basics: How the BCL2 gene family controls the death of retinal ganglion cells
Maes, M. E., Schlamp, C. L., & Nickells, R. W. (2017) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2017.01.002 · Cited by 193 · see citing works
Inositol 1,4,5-trisphosphate receptor-isoform diversity in cell death and survival
Ivanova, H., Vervliet, T., Missiaen, L., Parys, J. B., SMEDT, H. D., & Bultynck, G. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.03.007 · Cited by 187 · see citing works
The essentials of developmental apoptosis
Voss, A. K., & Strasser, A. (2020) · F1000Research · doi:10.12688/f1000research.21571.1 · Cited by 183 · see citing works
Self-citationBAX, BAK, and BOK: A Coming of Age for the BCL-2 Family Effector ProteinsPreprint
Moldoveanu, T., & Czabotar, P. E. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a036319 · Cited by 182 · see citing works
Targeting the Bcl-2 Family in B Cell Lymphoma
Adams, C. M., Clark-Garvey, S., Porcu, P., & Eischen, C. M. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2018.00636 · Cited by 158 · see citing works
Physiological and Pharmacological Control of BAK, BAX, and Beyond
Luna-Vargas, M. P. A., & Chipuk, J. E. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.07.002 · Cited by 142 · see citing works
ER functions of oncogenes and tumor suppressors: Modulators of intracellular Ca2+ signaling
Bittremieux, M., Parys, J. B., Pinton, P., & Bultynck, G. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.01.002 · Cited by 142 · see citing works
Intracellular localization of the BCL-2 family member BOK and functional implications
Echeverry, N., Bachmann, D., Ke, F., Strasser, A., Simon, H. U., & Kaufmann, T. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2013.10 · Cited by 137 · see citing works
Self-citationBCL-2 family member BOK promotes apoptosis in response to endoplasmic reticulum stress
Carpio, M. A., Michaud, M., Zhou, W., Fisher, J. K., Walensky, L. D., & Katz, S. G. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1421063112 · Cited by 127 · see citing works
Control of mitochondrial physiology and cell death by the Bcl-2 family proteins Bax and Bok
D’Orsi, B., Mateyka, J., & Prehn, J. H. M. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.03.010 · Cited by 133 · see citing works
BCL-2 family deregulation in colorectal cancer: potential for BH3 mimetics in therapy
Ramesh, P., & Medema, J. P. (2020) · APOPTOSIS · doi:10.1007/s10495-020-01601-9 · Cited by 131 · see citing works
The Bcl-2 Family in Host-Virus Interactions
Kvansakul, M., Caria, S., & Hinds, M. G. (2017) · Viruses · doi:10.3390/v9100290 · Cited by 117 · see citing works
Viewing BCL2 and cell death control from an evolutionary perspective
Strasser, A., & Vaux, D. L. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.145 · Cited by 114 · see citing works
Self-citationSchulman, J. J., Wright, F. A., Kaufmann, T., & Wojcikiewicz, R. J. H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.496570 · Cited by 98 · see citing works
Self-citationLiu, J., Lai, F.-N., Li, L., Sun, X., Cheng, S., Ge, W., Wang, Y., Li, L., Zhang, X., Felici, M. D., et al. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.350 · Cited by 84 · see citing works
Gonadotropin Signaling in the Ovary
Hunzicker-Dunn, M. E., & Mayo, K. E. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397175-3.00020-x · Cited by 82 · see citing works
Wu, H., Medeiros, L. J., & Young, K. H. (2017) · Blood Reviews · doi:10.1016/j.blre.2017.08.004 · Cited by 79 · see citing works
Tuzlak, S., Kaufmann, T., & Villunger, A. (2016) · Genes & Development · doi:10.1101/gad.289298.116 · Cited by 73 · see citing works
Self-citationConsequences of the combined loss of BOK and BAK or BOK and BAX
Ke, F., Bouillet, P., Kaufmann, T., Strasser, A., Kerr, J., & Voss, A. K. (2013) · Cell Death & Disease · doi:10.1038/cddis.2013.176 · Cited by 72 · see citing works
Self-citationMitochondria and mammalian reproduction
Ramalho‐Santos, J., & Amaral, S. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.06.005 · Cited by 72 · see citing works
BCL-2: Long and winding path from discovery to therapeutic target
Schenk, R. L., Strasser, A., & Dewson, G. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.100 · Cited by 72 · see citing works
Self-citationRegulating cell death at, on, and in membranes
Chi, X., Kale, J., Leber, B. F., & Andrews, D. W. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.06.002 · Cited by 70 · see citing works
Lindqvist, L., Vikstrom, I. B., Chambers, J. M., McArthur, K., Anderson, M. A., Henley, K. J., Happo, L., Cluse, L. A., Johnstone, R. W., Roberts, A. W., et al. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.149 · Cited by 66 · see citing works
Self-citationBok is a genuine multi-BH-domain protein that triggers apoptosis in the absence of Bax and Bak
Einsele-Scholz, S., Malmsheimer, S., Bertram, K., Stehle, D., Johänning, J., Manz, M., Daniel, P. T., Gillissen, B. F., Schulze-Osthoff, K., & Essmann, F. (2016) · Journal of Cell Science · doi:10.1242/jcs.181727 · Cited by 65 · see citing works
Bok regulates mitochondrial fusion and morphology
Schulman, J. J., Szczesniak, L. M., Bunker, E. N., Nelson, H. A., Roe, M. W., Wagner, L. E., Yule, D. I., & Wojcikiewicz, R. J. H. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0327-4 · Cited by 64 · see citing works
To Prime, or Not to Prime: That Is the QuestionPreprint
Potter, D. S., & Letai, A. G. (2016) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2016.81.030841 · Cited by 61 · see citing works
Expanding roles of BCL-2 proteins in apoptosis execution and beyond
King, L., Hohorst, L., & García‐Sáez, A. J. (2023) · Journal of Cell Science · doi:10.1242/jcs.260790 · Cited by 65 · see citing works
Marchi, S., Giorgi, C., Prill, M., Duszyński, J., Wieckowski, M. R., & Pinton, P. (2014) · Molecular & Cellular Oncology · doi:10.4161/23723548.2014.956469 · Cited by 60 · see citing works
Schulman, J. J., Wright, F. A., Han, X., Zluhan, E., Szczesniak, L. M., & Wojcikiewicz, R. J. H. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.711242 · Cited by 59 · see citing works
Delbridge, A. R. D., Kueh, A. J., Ke, F., Zamudio, N., El-Saafin, F., Jansz, N., Wang, G., Iminitoff, M., Beck, T. J., Haupt, S., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.048 · Cited by 61 · see citing works
Self-citationThe Multifaceted Roles of the BCL-2 Family Member BOK
Naim, S., & Kaufmann, T. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.574338 · Cited by 57 · see citing works
Self-citationIntrinsic Instability of BOK Enables Membrane Permeabilization in Apoptosis
Zheng, J. H., Grace, C. R., Guibao, C. D., McNamara, D. E., Llambi, F., Wang, Y., Chen, T., & Moldoveanu, T. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.060 · Cited by 57 · see citing works
D’Orsi, B., Engel, T., Pfeiffer, S. L., Nandi, S., Kaufmann, T., Henshall, D. C., & Prehn, J. H. M. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3780-15.2016 · Cited by 53 · see citing works
Self-citationRegulation of Cell Death by Mitochondrial Transport Systems of Calcium and Bcl-2 Proteins
Naumova, N., & Šachl, R. (2020) · Membranes · doi:10.3390/membranes10100299 · Cited by 51 · see citing works
Proapoptotic Bak and Bax guard against fatal systemic and organ-specific autoimmune disease
Mason, K. D., Lin, A. E.-J., Robb, L., Josefsson, E. C., Henley, K. J., Gray, D. H. D., Kile, B. T., Roberts, A. W., Strasser, A., Huang, D. C. S., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1215097110 · Cited by 52 · see citing works
Self-citationCell death and thymic tolerance
Daley, S. R., Teh, C. E., Hu, D. Y., Strasser, A., & Gray, D. H. D. (2017) · Immunological Reviews · doi:10.1111/imr.12532 · Cited by 52 · see citing works
Self-citationThe BCL-2 protein family: from discovery to drug development
Croce, C. M., Vaux, D. L., Strasser, A., Opferman, J. T., Czabotar, P. E., & Fesik, S. W. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01481-z · Cited by 53 · see citing works
Self-citationBcl-2 family proteins, beyond the veil
Glab, J., Cao, Z., & Puthalakath, H. (2020) · International review of cytology · doi:10.1016/bs.ircmb.2019.12.001 · Cited by 49 · see citing works
Fernández‐Marrero, Y., Bleicken, S., Das, K. K., Bachmann, D., Kaufmann, T., & Garcia‐Saez, A. J. (2017) · The FEBS Journal · doi:10.1111/febs.14008 · Cited by 47 · see citing works
Self-citationGetting away with murder: how does the BCL‐2 family of proteins kill with immunity?
Renault, T. T., & Chipuk, J. E. (2013) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12045 · Cited by 45 · see citing works
Ke, F., Holloway, S., Uren, R. T., Wong, A. W., Little, M. H., Kluck, R. M., Voss, A. K., & Strasser, A. (2022) · The EMBO Journal · doi:10.15252/embj.2021110300 · Cited by 41 · see citing works
Self-citationSubtle Changes in the Levels of BCL-2 Proteins Cause Severe Craniofacial Abnormalities
Grabow, S., Kueh, A. J., Ke, F., Vanyai, H. K., Sheikh, B. N., Dengler, M. A., Chiang, W., Eccles, S., Smyth, I., Jones, L. K., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.08.048 · Cited by 40 · see citing works
Self-citationBcl‐2 proteins in development, health, and disease of the hematopoietic system
Kollek, M., Müller, A., Egle, A., & Erlacher, M. (2016) · FEBS Journal · doi:10.1111/febs.13683 · Cited by 39 · see citing works
BOK promotes chemical-induced hepatocarcinogenesis in mice
Rabachini, T., Fernández‐Marrero, Y., Montani, M., Loforese, G., Sladky, V. C., He, Z., Bachmann, D., Wicki, S., Villunger, A., Stroka, D., et al. (2017) · Cell Death and Differentiation · doi:10.1038/s41418-017-0008-0 · Cited by 38 · see citing works
Self-citationKe, F., Grabow, S., Kelly, G. L., Lin, C., O’Reilly, L. A., & Strasser, A. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.304 · Cited by 37 · see citing works
Self-citationIs BOK required for apoptosis induced by endoplasmic reticulum stress?
Fernández‐Marrero, Y., Ke, F., Echeverry, N., Bouillet, P., Bachmann, D., Strasser, A., & Kaufmann, T. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516347113 · Cited by 36 · see citing works
Self-citationThe BAX/BAK-like protein BOK is a prognostic marker in colorectal cancer
Carberry, S., D’Orsi, B., Monsefi, N., Salvucci, M., Bacon, O., Fay, J., Rehm, M., McNamara, D. A., Kay, E. W., & Prehn, J. H. M. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0140-2 · Cited by 35 · see citing works
The BCL-2 pro-survival protein A1 is dispensable for T cell homeostasis on viral infection
Tuzlak, S., Schenk, R. L., Vasanthakumar, A., Preston, S., Haschka, M. D., Zotos, D., Kallies, A., Strasser, A., Villunger, A., & Herold, M. J. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2016.155 · Cited by 34 · see citing works
Self-citationModeling apoptosis resistance in CHO cells with CRISPR‐mediated knockouts of Bak1, Bax, and Bok
MacDonald, M. A., Barry, C. P., Groves, T., Martínez, V. S., Gray, P. P., Baker, K. N., Shave, E., Mahler, S. M., Munro, T. P., Marcellin, E., et al. (2022) · Biotechnology and Bioengineering · doi:10.1002/bit.28062 · Cited by 31 · see citing works
BOK displays cell death‐independent tumor suppressor activity in non‐small‐cell lung carcinoma
Moravčíková, E., Krepela, E., Donnenberg, V. S., Donnenberg, A. D., Benková, K., Rabachini, T., Fernández‐Marrero, Y., Bachmann, D., & Kaufmann, T. (2017) · International Journal of Cancer · doi:10.1002/ijc.30906 · Cited by 31 · see citing works
Self-citationde Meis, J., de Albuquerque, J. B., dos Santos, D. S., Farias-de-Oliveira, D. A., Berbert, L. R., Cotta-de-Almeida, V., & Savino, W. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00216 · Cited by 28 · see citing works
Targeting the apoptosis pathway to treat tumours of the paediatric nervous system
Fitzgerald, M.-C., O’Halloran, P. J., Connolly, N. M. C., & Murphy, B. M. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04900-y · Cited by 24 · see citing works
Glucocorticoids can induce BIM to trigger apoptosis in the absence of BAX and BAK1
Li, D., & Vaux, D. L. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2599-5 · Cited by 24 · see citing works
The Mysteries around the BCL-2 Family Member BOK
Shalaby, R., Flores‐Romero, H., & García‐Sáez, A. J. (2020) · Biomolecules · doi:10.3390/biom10121638 · Cited by 24 · see citing works
Physiological Functions of Mcl-1: Insights From Genetic Mouse Models
Chin, H. S., & Fu, N. Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.704547 · Cited by 22 · see citing works
Regulation of Oocyte Apoptosis: A View from Gene Knockout Mice
Kaur, S., & Kurokawa, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021345 · Cited by 24 · see citing works
Critical B-lymphoid cell intrinsic role of endogenous MCL-1 in c-MYC-induced lymphomagenesis
Grabow, S., Kelly, G. L., Delbridge, A. R. D., Kelly, P. N., Bouillet, P., Adams, J. M., & Strasser, A. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.43 · Cited by 22 · see citing works
Self-citationModulation of Cell Death in Age-Related Diseases
Tezil, T., & Başağa, H. (2014) · Current Pharmaceutical Design · doi:10.2174/13816128113196660702 · Cited by 21 · see citing works
Soond, S. M., Kozhevnikova, M. V., Savvateeva, L. V., Townsend, P. A., & Zamyatnin, A. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094669 · Cited by 21 · see citing works
Identification of the Bok Interactome Using Proximity Labeling
Szczesniak, L. M., Bonzerato, C. G., & Wojcikiewicz, R. J. H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.689951 · Cited by 19 · see citing works
BOK-engaged mitophagy alleviates neuropathology in Alzheimer’s disease
Yang, Y., Chen, H., Huang, S., Chen, H., Verkhratsky, A., Niu, J., Qu, Y., & Yi, C. (2024) · Brain · doi:10.1093/brain/awae241 · Cited by 19 · see citing works
Chaurasia, M. K., Palanisamy, R., Harikrishnan, R., Arasu, M. V., Al-Dhabi, N. A., & Arockiaraj, J. (2015) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2015.04.031 · Cited by 18 · see citing works
Modeling the function of BAX and BAK in early human brain development using iPSC-derived systems
Joshi, P. K., Bodnya, C., Rasmussen, M. L., Romero-Morales, A. I., Bright, A., & Gama, V. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03002-x · Cited by 16 · see citing works
The BCL-2 family member BOK promotes KRAS-driven lung cancer progression in a p53-dependent manner
Meinhardt, A.-L., Munkhbaatar, E., Höckendorf, U., Dietzen, M., Dechant, M., Anton, M., Jacob, A., Steiger, K., Weichert, W., Brčić, L., et al. (2022) · Oncogene · doi:10.1038/s41388-021-02161-1 · Cited by 15 · see citing works
Self-citationBok: real killer or bystander with non-apoptotic roles?
Bonzerato, C. G., & Wojcikiewicz, R. J. H. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1161910 · Cited by 14 · see citing works
A Glimpse of Programmed Cell Death Among Bacteria, Animals, and Plants
Zhuang, J., Xie, L., & Zheng, L. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.790117 · Cited by 12 · see citing works
BOK: Oddball of the BCL-2 Family
Brem, E. A., & Letai, A. G. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.04.007 · Cited by 11 · see citing works
Ghosh, N., & Sil, P. C. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821562-3.00031-9 · Cited by 11 · see citing works
BOK controls ER proteostasis and physiological ER stress responses in neurons
Walter, F., D’Orsi, B., Jagannathan, A., Düßmann, H., & Prehn, J. H. M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.915065 · Cited by 10 · see citing works
Valent, L., & Strasser, A. (2013) · Biodiscovery · doi:10.7750/biodiscovery.2013.8.3 · Cited by 10 · see citing works
Self-citationMartínez-Pérez, A., Igea, A., Estévez, O., Ferreira, C. M., Torrado, E., Castro, A. G., Fernández, C., Spetz, A., Adam, L., González, M. L., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.589863 · Cited by 10 · see citing works
Bonzerato, C. G., Keller, K. R., Schulman, J. J., Gao, X., Szczesniak, L. M., & Wojcikiewicz, R. J. H. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1094302 · Cited by 10 · see citing works
BOK promotes erythropoiesis in a mouse model of myelodysplastic syndrome
Kang, S., Perales, O., Michaud, M., & Katz, S. G. (2019) · Annals of Hematology · doi:10.1007/s00277-019-03726-7 · Cited by 9 · see citing works
Carpio, M. A., Michaud, M., Zhou, W., Fisher, J. K., Walensky, L. D., & Katz, S. G. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1521979113 · Cited by 9 · see citing works
Cai, J. X., Yu, D., Wei, S., Tang, J., Lu, Y., Wu, Z., Qin, Q., & Jian, J. (2016) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2016.03.026 · Cited by 7 · see citing works
Lessons from Using Genetically Engineered Mouse Models of MYC-Induced Lymphoma
Winkler, R., Piskor, E.-M., & Kosan, C. (2022) · Cells · doi:10.3390/cells12010037 · Cited by 6 · see citing works
Zhao, D., Sun, Y., Wei, X., Liang, H., Zhao, L., Dong, X., Chen, H., Chen, W., Yang, J. Z., Wang, X., et al. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.07.011 · Cited by 6 · see citing works
There is something about BOK we just don't get yet
Haschka, M. D., & Villunger, A. (2017) · FEBS Journal · doi:10.1111/febs.14031 · Cited by 6 · see citing works
Detmar, J., Rovic, I., Ray, J., Caniggia, I., & Jurisicova, A. (2019) · Cell and Tissue Research · doi:10.1007/s00441-019-03055-1 · Cited by 6 · see citing works
Huang, X., Ji, S., Bian, C., Sun, J. H., & Ji, H. (2023) · Journal of Animal Science · doi:10.1093/jas/skad101 · Cited by 5 · see citing works
Cell Biology: ERADicating Survival with BOK
Chipuk, J. E., & Luna‐Vargas, M. P. A. (2016) · Current Biology · doi:10.1016/j.cub.2016.04.003 · Cited by 4 · see citing works
JeanRichard, P., Ananthanarayan, A., Wu, L., Jazaeri, A., Bachmann, D., & Kaufmann, T. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01666-0 · Cited by 3 · see citing works
Self-citationThe programmed death of fetal oocytes and the correlated surveillance mechanisms
Zhou, J., Wang, W., Xia, G., & Wang, C. (2022) · Reproductive and Developmental Medicine · doi:10.1097/rd9.0000000000000016 · Cited by 3 · see citing works
- Authors
- Ke, F., Voss, A., Kerr, J. B., O'Reilly, L. A., Tai, L., Echeverry, N., Bouillet, P., Strasser, A., & Kaufmann, T.
- Affiliations
- Walter and Eliza Hall Institute of Medical Research (AU)
- The University of Melbourne (AU)
- Monash University (AU)
- University of Bern (CH)
- Corresponding author
- Strasser, A
- Venue
- Cell Death & Differentiation
- Published
- 2012-01-27
- Volume
- 19
- Issue
- 6
- Pages
- 915-925
- ISSN
- 1350-9047 (ISSN-L)
- 1476-5403
- PMC
- PMC3354060
- OpenAlex
- W2013268562
- Cited by
- 113
- References
- 34
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 1 · 2023: 6 · 2022: 11 · 2021: 6 · 2020: 9 · 2019: 7 · 2018: 7 · 2017: 19 · 2016: 17 · 2015: 7 · 2014: 6 · 2013: 10 · 2012: 1
- FWCI
- 3.08
- Type
- journal article
- Language
- en
- Update notices
- erratum (2012-12-10)
- Open access
- bronze
- doi.org
- Locations
- Cell Death and Differentiation (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Bern Open Repository and Information System (University of Bern) (submittedVersion)
- Funders
- National Science Foundation
- Leukemia and Lymphoma Society
- Leukemia Research Foundation
- Australian Government
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (119203)
- National Institutes of Health
- Stanford Institute for Research in the Social Sciences
- Medical Research Council (461221)
- National Health and Medical Research Council (461221)
- National Cancer Institute (R01CA043540, CA 43540)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- BOK, Bcl-2 family proteins, apoptosis, Bax/Bak, Mcl-1, tissue expression, female reproductive tissues, ovarian development, uterus, fertility, lymphoma, Eμ-myc transgenic mice, B cells, stress-induced cell death
- MeSH terms
- Animals, Female, Mice, Inbred C57BL, Mice, Transgenic, Ovary, RNA, Messenger, Uterus, T-Lymphocyte Subsets, Proto-Oncogene Proteins c-myc, Apoptosis, Mice, Knockout, Proto-Oncogene Proteins c-bcl-2, Myeloid Cells, Mice
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