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anti-Human BOK Anticorps:
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BOK-mediated membrane permeabilization is governed in part by its unique metastability of the hydrophobic groove and helix alpha1 and not through activation by BH3 ligands.
CER/BOK-induced regulation of mitochondrial fission and its functional consequence for heightened trophoblast cell autophagy in preeclampsia.
BOK downregulation may be associated with tumorigenesis of testicular cancer (TC); BOK had the potency to suppress TC cell proliferation and invasion, and BOK also contributes to Cisplatin resistance.
These data indicate BOK as a prognostic marker in colorectal cancer.
Loss of BOK is associated with non-small-cell lung carcinoma.
These results not only establish Bok as a Bak- and Bax-independent apoptosis inducer, but also suggest a potential impact of Bok expression in ovarian cancer therapy.
Data suggest that endoplasmic reticulum (ER) stress-induced apoptosis in hepatoma cells is regulated by highly labile and ER-associated BCL-2 family member BOK, which is controlled at level of protein stability by ER-associated degradation components; DNAJB12 is required in hepatoma cells to maintain BOK at low levels and suppress ER stress. (DNAJB12 = DnaJ (Hsp40) homolog, subfamily B, member 12)
Data suggest that hypoxia-induced expression of BOK in placental cells is regulated via promoter region, hypoxia-response element, and binding of hypoxia-inducible factors (HIF1A, HIF2A/EPAS1, HIF1B/ARNT) but is not affected by its antisense transcript.
First evidence for a key role of the BOK-MCL1 system in regulating autophagy in the human placenta, whereby an adverse environment as seen in preeclampsia tilts the BOK-MCL1 balance toward the build-up of isoforms that triggers placental autophagy.
Bok may govern IP3R cleavage and activity during apoptosis.
The results suggest important roles for Bok and Bcl-X(L) in human ovarian development, follicle maturation and apoptosis.
Data conclude that Mtd-L functions to regulate trophoblast cell proliferation during early placentation and that the elevated levels of Mtd found in PE may contribute to increased trophoblast proliferation.
BOK and NOXA are essential mediators of p53-dependent apoptosis
A novel Mtd/BOK splice isoform is responsible for trophoblast cell death in pre-eclampsia.
Studies showed that hBok was distributed in both the cytosol and intracellular membranes of healthy cells.
a link between the apoptotic activity and nuclear localization of a pro-apoptotic Bok
Bok represents a cell cycle-regulated pro-apoptotic member of the Bcl-2 family
BOKAS is a natural antisense transcript that regulates the pro-apoptotic activity of human Bok
BH3 and transmembrane domains of BOK were vital for BOK regulation of fission.
BOK is induced by diethylnitrosamine (DEN), contributes to DEN-induced hepatocellular apoptosis and resulting hepatocarcinogenesis.
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.
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.
Bok controls neuronal Ca(2+) homeostasis and bioenergetics in seizure-induced neuronal injury.
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.
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
BOK-deficient mice have no readily discernible abnormalities, and its function therefore remains unresolved.
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
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.
The protein encoded by this gene belongs to the BCL2 family, members of which form homo- or heterodimers, and act as anti- or proapoptotic regulators that are involved in a wide variety of cellular processes. Studies in rat show that this protein has restricted expression in reproductive tissues, interacts strongly with some antiapoptotic BCL2 proteins, not at all with proapoptotic BCL2 proteins, and induces apoptosis in transfected cells. Thus, this protein represents a proapoptotic member of the BCL2 family.
bcl-2-related ovarian killer protein
, BCL2-related ovarian killer
, Bcl-2-related ovarian killer
, bcl-2-related ovarian killer protein homolog A
, bcl-2-related ovarian killer protein homolog B
, bcl-2-like protein 9
, apoptosis activator Mtd
, protein matador