| BOK controls apoptosis by Ca(2+) transfer through ER-mitochondrial contact sites. | BOK controls apoptosis by Ca(2+) transfer through ER-mitochondrial contact sites.
Carpio MA, Means RE, Brill AL, Sainz A, Ehrlich BE, Katz SG., Free PMC Article | 01/29/2022 |
| Loss of BOK Has a Minor Impact on Acetaminophen Overdose-Induced Liver Damage in Mice. | Loss of BOK Has a Minor Impact on Acetaminophen Overdose-Induced Liver Damage in Mice.
Naim S, Fernandez-Marrero Y, de Brot S, Bachmann D, Kaufmann T., Free PMC Article | 05/1/2021 |
| Bok regulates mitochondrial fusion and morphology. | Bok regulates mitochondrial fusion and morphology.
Schulman JJ, Szczesniak LM, Bunker EN, Nelson HA, Roe MW, Wagner LE 2nd, Yule DI, Wojcikiewicz RJH., Free PMC Article | 10/3/2020 |
| a role for BOK in nucleotide metabolism and cell cycle regulation, is reported. | 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, Glab J, Menassa J, Osellame L, Nelson T, Fernandez-Marrero Y, Brown F, Wei A, Ke F, O'Reilly L, Doerflinger M, Allison C, Kueh A, Ramsay R, Smith BJ, Mathivanan S, Kaufmann T, Puthalakath H., Free PMC Article | 04/4/2020 |
| BH3 and transmembrane domains of BOK were vital for BOK regulation of fission. | Ceramide-induced BOK promotes mitochondrial fission in preeclampsia.
Ausman J, Abbade J, Ermini L, Farrell A, Tagliaferro A, Post M, Caniggia I., Free PMC Article | 10/26/2019 |
| BOK is induced by diethylnitrosamine (DEN), contributes to DEN-induced hepatocellular apoptosis and resulting hepatocarcinogenesis. | BOK promotes chemical-induced hepatocarcinogenesis in mice.
Rabachini T, Fernandez-Marrero Y, Montani M, Loforese G, Sladky V, He Z, Bachmann D, Wicki S, Villunger A, Stroka D, Kaufmann T., Free PMC Article | 09/14/2019 |
| results suggest that in addition to induction of apoptosis in response to ER stress, BOK may regulate erythropoiesis when certain erythroid progenitors experience cell stress. | BOK promotes erythropoiesis in a mouse model of myelodysplastic syndrome.
Kang SH, Perales O, Michaud M, Katz SG., Free PMC Article | 08/31/2019 |
| we show that BOK(C) can permeabilize liposomes, and cooperate with cBID, but its role in directly mediating mitochondrial permeabilization is unclear and may underlie a yet to be determined negative regulation. | The membrane activity of BOK involves formation of large, stable toroidal pores and is promoted by cBID.
Fernández-Marrero Y, Bleicken S, Das KK, Bachmann D, Kaufmann T, Garcia-Saez AJ. | 06/24/2017 |
| Bok controls neuronal Ca(2+) homeostasis and bioenergetics in seizure-induced neuronal injury. | 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, Nandi S, Kaufmann T, Henshall DC, Prehn JH., Free PMC Article | 09/17/2016 |
| Study reports that BCL-2 ovarian killer (BOK) is a bona fide yet unconventional effector of mitochondrial outer membrane permeabilization that can trigger apoptosis in the absence of both BAX and BAK. | BOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation.
Llambi F, Wang YM, Victor B, Yang M, Schneider DM, Gingras S, Parsons MJ, Zheng JH, Brown SA, Pelletier S, Moldoveanu T, Chen T, Green DR., Free PMC Article | 09/3/2016 |
| findings support a selective and distinguishing role for BOK in regulating the apoptotic response to ER stress, revealing--to our knowledge--the first bona fide apoptotic defect linked to Bok deletion | BCL-2 family member BOK promotes apoptosis in response to endoplasmic reticulum stress.
Carpio MA, Michaud M, Zhou W, Fisher JK, Walensky LD, Katz SG., Free PMC Article | 09/26/2015 |
| BOK-deficient mice have no readily discernible abnormalities, and its function therefore remains unresolved. | Consequences of the combined loss of BOK and BAK or BOK and BAX.
Ke F, Bouillet P, Kaufmann T, Strasser A, Kerr J, Voss AK., Free PMC Article | 03/1/2014 |
| Bok may govern IP3R cleavage and activity during apoptosis. | 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.
Schulman JJ, Wright FA, Kaufmann T, Wojcikiewicz RJH., Free PMC Article | 12/14/2013 |
| two proapoptotic Bcl-2 family members Bok and Noxa/Pmaip are directly transcriptionally induced by activated MAL and upon activation of the actin-MAL-SRF pathway | Myocardin-related transcription factor A regulates expression of Bok and Noxa and is involved in apoptotic signalling.
Shaposhnikov D, Descot A, Schilling J, Posern G. | 09/22/2012 |
| Bok protein 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. | BCL-2 family member BOK is widely expressed but its loss has only minimal impact in mice.
Ke F, Voss A, Kerr JB, O'Reilly LA, Tai L, Echeverry N, Bouillet P, Strasser A, Kaufmann T., Free PMC Article | 09/15/2012 |
| Bok represents a cell cycle-regulated pro-apoptotic member of the Bcl-2 family | Bok, Bcl-2-related Ovarian Killer, Is Cell Cycle-regulated and Sensitizes to Stress-induced Apoptosis.
Rodriguez JM, Glozak MA, Ma Y, Cress WD., Free PMC Article | 01/21/2010 |