BOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation

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BCL-2 family deregulation in colorectal cancer: potential for BH3 mimetics in therapy

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Found in Translation: How Preclinical Research Is Guiding the Clinical Development of the BCL2-Selective Inhibitor Venetoclax

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Mitochondrial pores at the crossroad between cell death and inflammatory signaling

Flores‐Romero, H., Dadsena, S., & García‐Sáez, A. J. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.02.021 · Cited by 125 · see citing works

Control of Cell Death in Health and Disease

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Mitochondria as a target in cancer treatment

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The ubiquitin system: a critical regulator of innate immunity and pathogen–host interactions

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Viewing BCL2 and cell death control from an evolutionary perspective

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Spatial Transcriptomics Reveals Genes Associated with Dysregulated Mitochondrial Functions and Stress Signaling in Alzheimer Disease

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Ceramide-induced BOK promotes mitochondrial fission in preeclampsia

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Different modalities of host cell death and their impact on Mycobacterium tuberculosis infection

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The evolution of regulated cell death pathways in animals and their evasion by pathogens

Tummers, B., & Green, D. R. (2021) · Physiological Reviews · doi:10.1152/physrev.00002.2021 · Cited by 95 · see citing works

Mechanisms of mitochondrial cell death

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The ER-mitochondria interface, where Ca2+ and cell death meet

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Crosstalk between mitochondria–ER contact sites and the apoptotic machinery as a novel health meter

Larrañaga-SanMiguel, A., Bengoa‐Vergniory, N., & Flores‐Romero, H. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.08.007 · Cited by 93 · see citing works

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

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miR-378a-3p promotes differentiation and inhibits proliferation of myoblasts by targeting HDAC4 in skeletal muscle development

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

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Exploring the Therapeutic Potentials of Exopolysaccharides Derived From Lactic Acid Bacteria and Bifidobacteria: Antioxidant, Antitumor, and Periodontal Regeneration

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Metabolic tricks of cancer cells

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Targeting VCP enhances anticancer activity of oncolytic virus M1 in hepatocellular carcinoma

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Metal ions overloading and cell death

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The role of cell death in SARS-CoV-2 infection

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

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The third model of Bax/Bak activation: a Bcl-2 family feud finally resolved?

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

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

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Proteotoxic Stress and Cell Death in Cancer Cells

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PINK1 Content in Mitochondria is Regulated by ER-Associated Degradation

Guardia‐Laguarta, C., Liu, Y., Lauritzen, K. H., Erdjument‐Bromage, H., Martin, B. M. S., Swayne, T. C., Jiang, X., & Przedborski, S. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.1691-18.2019 · Cited by 70 · 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

BCL-2: Long and winding path from discovery to therapeutic target

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Molecular dissection of box jellyfish venom cytotoxicity highlights an effective venom antidote

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Cell deaths: Involvement in the pathogenesis and intervention therapy of COVID-19

Li, X., Zhang, Z., Wang, Z., Gutiérrez-Castrellón, P., & Shi, H. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01043-6 · Cited by 67 · 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

Mitophagy restricts BAX/BAK-independent, Parkin-mediated apoptosis

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How to unleash mitochondrial apoptotic blockades to kill cancers?

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Bok regulates mitochondrial fusion and morphology

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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

Transmembrane E3 ligase RNF183 mediates ER stress-induced apoptosis by degrading Bcl-xL

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The Role of Mitochondria in Pyroptosis

Li, Q., Shi, N., Cai, C., Zhang, M., He, J., Tan, Y., & Fu, W. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.630771 · Cited by 59 · see citing works

Ca2+-mediated mitochondrial inner membrane permeabilization induces cell death independently of Bax and Bak

Quarato, G., Llambi, F., Guy, C. S., Min, J., Actis, M., Sun, H., Narina, S., Pruett‐Miller, S. M., Peng, J., Ranković, Z., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01025-9 · Cited by 70 · see citing works

TMBIM-mediated Ca2+ homeostasis and cell death

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Caspase-mediated cleavage of IRE1 controls apoptotic cell commitment during endoplasmic reticulum stress

Shemorry, A., Harnoss, J. M., Guttman, O., Marsters, S. A., Kömüves, L. G., Lawrence, D. A., & Ashkenazi, A. (2019) · eLife · doi:10.7554/elife.47084 · Cited by 57 · 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

Mitochondria-targeted graphene for advanced cancer therapeutics

Tabish, T. A., & Narayan, R. J. (2021) · Acta Biomaterialia · doi:10.1016/j.actbio.2021.04.054 · Cited by 55 · 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

Selenium unmasks protective iron armor: A possible defense against cutaneous inflammation and cancer

Arbiser, J. L., Bonner, M. Y., Ward, N. L., Elsey, J., & Rao, S. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.05.018 · Cited by 52 · see citing works

The 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

Endoplasmic reticulum stress–induced degradation of DNAJB12 stimulates BOK accumulation and primes cancer cells for apoptosis

Sopha, P., Ren, H. Y., Grove, D. E., & Cyr, D. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.785113 · Cited by 51 · see citing works

Potential of Therapeutic Small Molecules in Apoptosis Regulation in the Treatment of Neurodegenerative Diseases: An Updated Review

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Bcl-2 family proteins, beyond the veil

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Potency and Selectivity of SMAC/DIABLO Mimetics in Solid Tumor Therapy

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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

Extra-mitochondrial prosurvival BCL-2 proteins regulate gene transcription by inhibiting the SUFU tumour suppressor

Wu, X., Zhang, L.-S., Toombs, J. E., Kuo, Y.-C., Piazza, J. T., Tuladhar, R., Barrett, Q., Fan, C.-W., Zhang, X., Walensky, L. D., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3616 · Cited by 47 · see citing works

Application of Artificial Neural Network in miRNA Biomarker Selection and Precise Diagnosis of Colorectal Cancer

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Overview of BCL-2 Family Proteins and Therapeutic Potentials

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Death sentence: The tale of a fallen endoplasmic reticulum

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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

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

Deciphering the Mechanism of Action of the Proapoptotic Protein BOK

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

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

The Multifaceted Roles of the BCLL-2 Family Member BOK

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