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Subcellular Localization and Dynamics of the Bcl-2 Family of Proteins

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Inositol 1,4,5-trisphosphate receptor-isoform diversity in cell death and survival

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BAX, BAK, and BOK: A Coming of Age for the BCL-2 Family Effector ProteinsPreprint

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Apoptosis regulation at the mitochondria membrane level

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Targeting BCL-2-like Proteins to Kill Cancer Cells

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Mitochondrial calcium: Transport and modulation of cellular processes in homeostasis and cancer (Review)

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ER functions of oncogenes and tumor suppressors: Modulators of intracellular Ca2+ signaling

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The Bcl-2 Family: Ancient Origins, Conserved Structures, and Divergent Mechanisms

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Control of mitochondrial physiology and cell death by the Bcl-2 family proteins Bax and Bok

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Ceramide-induced BOK promotes mitochondrial fission in preeclampsia

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Emerging biomarkers and potential therapeutics of the BCL-2 protein family: the apoptotic and anti-apoptotic context

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The Bcl-2 Protein Family Member Bok Binds to the Coupling Domain of Inositol 1,4,5-Trisphosphate Receptors and Protects Them from Proteolytic Cleavage

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Apoptotic Pathway as the Therapeutic Target for Anticancer Traditional Chinese Medicines

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Bag6 complex contains a minimal tail-anchor–targeting module and a mock BAG domain

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SARS-CoV-2 membrane protein causes the mitochondrial apoptosis and pulmonary edema via targeting BOK

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BOK controls apoptosis by Ca2+ transfer through ER-mitochondrial contact sites

Carpio, M. A., Means, R. E., Brill, A. L., Sainz, A. G., Ehrlich, B. E., & Katz, S. G. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108827 · Cited by 86 · see citing works

Bcl-2-Protein Family as Modulators of IP 3 Receptors and Other Organellar Ca 2+ ChannelsPreprint

Ivanova, H., Vervliet, T., Monaco, G., Terry, L. E., Rosa, N., Baker, M. R., Parys, J. B., Serysheva, I. I., Yule, D. I., & Bultynck, G. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a035089 · Cited by 79 · see citing works

Contribution of apoptosis-associated signaling pathways to epileptogenesis: lessons from Bcl-2 family knockouts

Henshall, D. C., & Engel, T. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00110 · Cited by 78 · see citing works

Too much death can kill you: inhibiting intrinsic apoptosis to treat disease

Li, K., van Delft, M. F., & Dewson, G. (2021) · The EMBO Journal · doi:10.15252/embj.2020107341 · Cited by 76 · see citing works

Interrogating the relevance of mitochondrial apoptosis for vertebrate development and postnatal tissue homeostasisPreprint

Tuzlak, S., Kaufmann, T., & Villunger, A. (2016) · Genes & Development · doi:10.1101/gad.289298.116 · Cited by 73 · see citing works

Consequences 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

Ca2+ signaling and cell death

Dhaouadi, N., Vitto, V. A. M., Pinton, P., Galluzzi, L., & Marchi, S. (2023) · Cell Calcium · doi:10.1016/j.ceca.2023.102759 · Cited by 71 · see citing works

Regulating 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

BCL2 Family, Mitochondrial Apoptosis, and Beyond

Dai, H., Meng, W., & Kaufmann, S. H. (2016) · Cancer translational medicine · doi:10.4103/2395-3977.177558 · Cited by 69 · see citing works

Bok 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

Bcl-2 Family Members and the Mitochondrial Import Machineries: The Roads to Death

Lalier-Bretaudeau, L., Vallette, F. M., & Manon, S. (2022) · Biomolecules · doi:10.3390/biom12020162 · Cited by 63 · 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

Functional conservation of the apoptotic machinery from coral to man: the diverse and complex Bcl-2 and caspase repertoires of Acropora millepora

Moya, A., Sakamaki, K., Mason, B. M., Huisman, L., Forêt, S., Weiss, Y., Bull, T. E., Tomii, K., Imai, K., Hayward, D. C., et al. (2016) · BMC Genomics · doi:10.1186/s12864-015-2355-x · Cited by 62 · see citing works

Raptinal bypasses BAX, BAK, and BOK for mitochondrial outer membrane permeabilization and intrinsic apoptosis

Heimer, S., Knoll, G., Schulze‐Osthoff, K., & Ehrenschwender, M. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1790-z · Cited by 62 · see citing works

Oncogenic and oncosuppressive signal transduction at mitochondria-associated endoplasmic reticulum membranes

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

The Stability and Expression Level of Bok Are Governed by Binding to Inositol 1,4,5-Trisphosphate Receptors

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

The 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

Intrinsic 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

Bok Is Not Pro-Apoptotic But Suppresses Poly ADP-Ribose Polymerase-Dependent Cell Death Pathways and Protects against Excitotoxic and Seizure-Induced Neuronal Injury

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

Regulation 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

Attenuating apoptosis in Chinese hamster ovary cells for improved biopharmaceutical production

Henry, M. N., MacDonald, M. A., Orellana, C. A., Gray, P. P., Gillard, M., Baker, K. N., Nielsen, L. K., Marcellin, E., Mahler, S. M., & Martínez, V. S. (2020) · Biotechnology and Bioengineering · doi:10.1002/bit.27269 · Cited by 51 · see citing works

The membrane activity of <scp>BOK</scp> involves formation of large, stable toroidal pores and is promoted by <scp>cBID</scp>

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

Pharmacological inhibition of Bcl-xL sensitizes osteosarcoma to doxorubicin

Baranski, Z., de Jong, Y., Ilkova, T., Peterse, E. F. P., Cleton-Jansen, A., van de Water, B., Hogendoorn, P. C. W., Bovée, J. V. M. G., & Danen, E. H. J. (2015) · Oncotarget · doi:10.18632/oncotarget.5333 · Cited by 45 · see citing works

Functions of the C-terminal domains of apoptosis-related proteins of the Bcl-2 family

Gómez-Fernández, J. C. (2014) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2014.05.003 · Cited by 43 · see citing works

BCL-2 family protein BOK is a positive regulator of uridine metabolism in mammals

Srivastava, R., Cao, Z., Nedeva, C., Naim, S., Bachmann, D., Rabachini, T., Gangoda, L., Shahi, S. K., Glab, J., Menassa, J., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1904523116 · Cited by 41 · see citing works

Mcl-1 and Bok transmembrane domains: Unexpected players in the modulation of apoptosis

Lucendo, E., Sancho, M., Lolicato, F., Javanainen, M., Kulig, W., Leiva, D., Duart, G., Andreu-Férnández, V., Mingarro, I., & Orzáez, M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2008885117 · Cited by 40 · see citing works

Mechanisms of Biological Effects of Ionic Liquids: From Single Cells to Multicellular Organisms

Egorova, K. S., Кибардин, А. В., Posvyatenko, A. V., & Ananikov, V. P. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00420 · Cited by 39 · see citing works

Monocytes enhance neutrophil‐induced blister formation in an ex vivo model of bullous pemphigoid

de Graauw, E., Sitaru, C., Horn, M. P., Borradori, L., Yousefi, S., Simon, D., & Simon, H. (2017) · Allergy · doi:10.1111/all.13376 · Cited by 38 · 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

Impact of the combined loss of BOK, BAX and BAK on the hematopoietic system is slightly more severe than compound loss of BAX and BAK

Ke, 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

Is 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

The 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

Modeling 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

Visualization of BOK pores independent of BAX and BAK reveals a similar mechanism with differing regulation

Shalaby, R., Diwan, A., Flores‐Romero, H., Hertlein, V., & García‐Sáez, A. J. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01078-w · Cited by 30 · see citing works

Making the head: Caspases in life and death

Švandová, E., Lesot, H., Sharpe, P. T., & Matalová, E. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1075751 · Cited by 29 · see citing works

Pharmacological Targeting of Executioner Proteins: Controlling Life and Death

Pogmore, J. P., Uehling, D., & Andrews, D. W. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c02200 · Cited by 28 · see citing works

The BCL-2 selective inhibitor ABT-199 sensitizes soft tissue sarcomas to proteasome inhibition by a concerted mechanism requiring BAX and NOXA

Muenchow, A., Weller, S., Hinterleitner, C., Malenke, E., Bugl, S., Wirths, S., Müller, M., Schulze‐Osthoff, K., Aulitzky, W. E., Kopp, H., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02910-2 · Cited by 28 · see citing works

Novel post-transcriptional and post-translational regulation of pro-apoptotic protein BOK and anti-apoptotic protein Mcl-1 determine the fate of breast cancer cells to survive or die

Onyeagucha, B. C., Subbarayalu, P., Abdelfattah, N., Rajamanickam, S., Timilsina, S., Guzman, R. M., Zeballos, C. R., Eedunuri, V. K., Bansal, S., Mohammad, T. A., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.20841 · Cited by 27 · see citing works

Cellular demolition: Proteins as molecular players of programmed cell death

Dhuriya, Y. K., Sharma, D., & Naik, A. A. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.07.113 · Cited by 26 · see citing works

Engineering death resistance in CHO cells for improved perfusion culture

MacDonald, M. A., Nöbel, M., Martínez, V. S., Baker, K. N., Shave, E., Gray, P. P., Mahler, S. M., Munro, T. P., Nielsen, L. K., & Marcellin, E. (2022) · mAbs · doi:10.1080/19420862.2022.2083465 · Cited by 24 · see citing works

Lymphoma cells lacking pro-apoptotic BAX are highly resistant to BH3-mimetics targeting pro-survival MCL-1 but retain sensitivity to conventional DNA-damaging drugs

Diepstraten, S. T., Young, S., Marca, J. E. L., Wang, Z., Kluck, R. M., Strasser, A., & Kelly, G. L. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01117-0 · 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

BCL-2 and BOK regulate apoptosis by interaction of their C-terminal transmembrane domains

Beigl, T. B., Paul, A., Fellmeth, T., Nguyen, D. Q., Barber, L., Weller, S., Schäfer, B., Gillissen, B. F., Aulitzky, W. E., Kopp, H., et al. (2024) · EMBO Reports · doi:10.1038/s44319-024-00206-6 · Cited by 23 · see citing works

Intrinsically Connected: Therapeutically Targeting the Cathepsin Proteases and the Bcl-2 Family of Protein Substrates as Co-regulators of Apoptosis

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

Contribution of BH3-domain and Transmembrane-domain to the Activity and Interaction of the Pore-forming Bcl-2 Proteins Bok, Bak, and Bax

Stehle, D., Grimm, M., Einsele‐Scholz, S., Wanke, F., Johänning, J., Fischer, G., Gillissen, B. F., Schulze‐Osthoff, K., & Eßmann, F. (2018) · Scientific Reports · doi:10.1038/s41598-018-30603-6 · Cited by 20 · see citing works

The C-terminal sequences of Bcl-2 family proteins mediate interactions that regulate cell death

Nguyen, D. Q., Osterlund, E. J., Kale, J., & Andrews, D. W. (2024) · Biochemical Journal · doi:10.1042/bcj20210352 · Cited by 20 · 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

Context-dependent roles of mitochondrial LONP1 in orchestrating the balance between airway progenitor versus progeny cells

Xu, L., Tan, C., Barr, J., Talaba, N., Verheyden, J. M., Chin, J., Gaboyan, S., Kasaraneni, N., Elgamal, R. M., Gaulton, K. J., et al. (2024) · Cell stem cell · doi:10.1016/j.stem.2024.08.001 · Cited by 20 · see citing works

Overexpression of CREB protein protects from tunicamycin-induced apoptosis in various rat cell types

Balogh, A., Németh, M., Koloszár, I., Markó, L., Przybyl, L., Jinno, K., Szigeti, C., Heffer, M., Gebhardt, M., Szeberényi, J., et al. (2014) · Apoptosis · doi:10.1007/s10495-014-0986-z · 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

Golgi Fragmentation and Sphingomyelin Transport to Chlamydia trachomatis during Penicillin-Induced Persistence Do Not Depend on the Cytosolic Presence of the Chlamydial Protease CPAF

Dille, S., Herbst, K., Volceanov, L., Nölke, T., Kretz, O., & Häcker, G. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103220 · Cited by 14 · see citing works

Bok: 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

Role of B-Cell Lymphoma 2 Ovarian Killer (BOK) in Acute Toxicity of Human Lung Epithelial Cells Caused by Cadmium Chloride

Zhang, F., Ren, L., Zhou, S., Duan, P., Xue, J., Chen, H., Feng, Y., Yue, X., Yuan, P., Liu, Q., et al. (2019) · Medical Science Monitor · doi:10.12659/msm.913706 · Cited by 12 · see citing works

Necrostatin-1 prevents skeletal muscle ischemia reperfusion injury by regulating Bok-mediated apoptosis

Cao, Y. C., Wang, H., Ni, C., Chen, S., Wang, W.-T., & Wang, L.-R. (2023) · Journal of the Chinese Medical Association · doi:10.1097/jcma.0000000000000806 · Cited by 11 · see citing works

Negative Regulation of BOK Expression by Recruitment of TRIM28 to Regulatory Elements in Its 3′ Untranslated Region

Fernández‐Marrero, Y., Bachmann, D., Lauber, E., & Kaufmann, T. (2018) · iScience · doi:10.1016/j.isci.2018.11.005 · Cited by 11 · see citing works

SpBOK inhibits WSSV infection by regulating the apoptotic pathway in mud crab (Scylla paramamosain)

Lin, S., He, Y., Gong, Y., Zhang, Y., Ma, H., Zheng, H., & Li, S. (2019) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2019.103603 · Cited by 11 · 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

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

Endogenous Bok is stable at the endoplasmic reticulum membrane and does not mediate proteasome inhibitor-induced apoptosis

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

Loss of BID Delays FASL-Induced Cell Death of Mouse Neutrophils and Aggravates DSS-Induced Weight Loss

Wicki, S., Gurzeler, U., Corazza, N., Genitsch, V., Wong, W. W.-L., & Kaufmann, T. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030684 · Cited by 10 · see citing works

In Vitro Differentiation of Mouse Granulocytes

Reinhart, R., Wicki, S., & Kaufmann, T. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3581-9_8 · Cited by 9 · 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

Deciphering the Mechanism of Action of the Proapoptotic Protein BOK

Shalaby, R. (2024) · Universitätsbibliothek Tübingen · doi:10.15496/publikation-90220

BCL-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

Is 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

Bok: 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

The Multifaceted Roles of the BCLL-2 Family Member BOK

Naim, S., & Kaufmann, T. (2020) · doi:10.7892/boris.146667