BCL-2 family member BOK promotes apoptosis in response to endoplasmic reticulum stress

The BCL-2 protein family: opposing activities that mediate cell death

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The landscape of somatic copy-number alteration across human cancers

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Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death

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ER Stress Triggers Apoptosis by Activating BH3-Only Protein Bim

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The Combined Functions of Proapoptotic Bcl-2 Family Members Bak and Bax Are Essential for Normal Development of Multiple Tissues

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The BCL-2 Family Reunion

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BAX and BAK Regulation of Endoplasmic Reticulum Ca 2+ : A Control Point for Apoptosis

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BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and BakPreprint

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Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members

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BOK and NOXA Are Essential Mediators of p53-dependent Apoptosis

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Drob-1, a Drosophila member of the Bcl-2/CED-9 family that promotes cell death

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Intracellular localization of the BCL-2 family member BOK and functional implications

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Mtd, a Novel Bcl-2 Family Member Activates Apoptosis in the Absence of Heterodimerization with Bcl-2 and Bcl-XL

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BCL-2 family member BOK is widely expressed but its loss has only minimal impact in mice

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Drosophila Pro-apoptotic Bcl-2/Bax Homologue Reveals Evolutionary Conservation of Cell Death Mechanisms

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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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Drosophila pro-apoptotic Bcl-2/Bax homologue reveals evolutionary conservation of cell death mechanisms.

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Consequences of the combined loss of BOK and BAK or BOK and BAX

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Hypoxic Switch in Mitochondrial Myeloid Cell Leukemia Factor-1/Mtd Apoptotic Rheostat Contributes to Human Trophoblast Cell Death in Preeclampsia

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Bok, Bcl-2-related Ovarian Killer, Is Cell Cycle-regulated and Sensitizes to Stress-induced Apoptosis

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Nuclear translocation of the pro-apoptotic Bcl-2 family member Bok induces apoptosis

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Evolutionarily conserved Bok proteins in the Bcl‐2 family

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BH3 Peptides Induce Mitochondrial Fission and Cell Death Independent of BAX/BAK

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The Expression of Bok Is Regulated by Serum in HC11 Mammary Epithelial Cells

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Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018.

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Mitochondria—Judges and Executioners of Cell Death Sentences

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Inactivation of prosurvival Bcl-2 proteins activates Bax/Bak through the outer mitochondrial membrane

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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

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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

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

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

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

ER Stress에 의해 유발된 C6 Glial Cells의 손상에 대한 龍腦의 보호효과

전인철, 방창호, 문병순, et al. (2009)

PERK regulated miR-424(322)-503 cluster fine-tunes activation of IRE1 and ATF6 during Unfolded Protein Response

Gupta, A., Hossain, M. M., Read, D. E., et al. (2015) · Scientific Reports · doi:10.1038/srep18304 · Cited by 45 · see citing works

IRE1 signaling increases PERK expression during chronic ER stress

Ong, G., Ragetli, R., Mnich, K., Doble, B. W., Kammouni, W., & Logue, S. E. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06663-0 · Cited by 96 · see citing works

Modeling Acute ER Stress in Vivo and in Vitro

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The regulatory mechanism of 4-phenylbutyric acid against ER stress-induced autophagy in human gingival fibroblasts

Kim, D., Li, B., Rhew, K. Y., Oh, H., Lim, H., Lee, W., Chae, H., & Kim, H. (2012) · Archives of Pharmacal Research · doi:10.1007/s12272-012-0718-2 · Cited by 46 · see citing works