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The protein encoded by BMF belongs to the BCL2 protein family.
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The findings are consistent with rs539846 influencing chronic lymphocytic leukemia (CLL) susceptibility through differential RELA (show NFkBP65 ELISA Kits) binding, with direct modulation of BMF expression impacting on anti-apoptotic BCL2 (show BCL2 ELISA Kits), a hallmark of oncogenic dependency in CLL.
Reciprocal regulation of BMF and BIRC5 (show BIRC5 ELISA Kits) is linked to Eomes (show EOMES ELISA Kits) overexpression in colorectal cancer.
Early generated B1 B cells with restricted BCRs become chronic lymphocytic leukemia with continued c-Myc (show MYC ELISA Kits) and low Bmf expression
these findings suggest that p53 (show TP53 ELISA Kits)-R273H can specifically drive AKT (show AKT1 ELISA Kits) signaling and suppress BMF expression, resulting in enhanced cell survivability and anoikis resistance.
On the corresponding BMF gene promoter, loss of HDAC8 (show HDAC8 ELISA Kits) was associated with signal transducer and activator of transcription 3 (STAT3 (show STAT3 ELISA Kits))/specificity protein 3 (Sp3) transcription factor exchange and recruitment of p300 (show EP300 ELISA Kits).
Overexpression of ApoL2 (show APOL2 ELISA Kits) did not induce cell death on its own. ApoL2 (show APOL2 ELISA Kits) did not sensitize or protect cells from overexpression of the BH3-only (show BBC3 ELISA Kits) proteins Bmf or Noxa (show PMAIP1 ELISA Kits).
Diva binds peptides derived from the BH3 domain of several other proapoptotic Bcl-2 (show BCL2 ELISA Kits) proteins, including mouse Harakiri (show HRK ELISA Kits), Bid (show BID ELISA Kits), Bak (show BAK1 ELISA Kits) and Bmf.
BMF is induced in human IEC by the loss of cell attachment and is likely to play an important role in the regulation of IEC survival
characterization of the bmf gene locus; molecular basis of the generation of the 2 major isoforms of Bmf; provide evidence that Bmf can act as a sensor for stress that associates with the repression of the conventional CAP-dependent translation machinery
Data show that hypoxic conditions inhibit anoikis and block expression of proapoptotic BH3-only (show BBC3 ELISA Kits) family members Bim (show BCL2L11 ELISA Kits) and Bmf in epithelial cells.
demonstrate that this sudden and dramatic loss of primordial follicles is hormonally triggered and identify the pro-apoptotic BH3-only (show BBC3 ELISA Kits) protein, BCL-2 modifying factor (BMF), as essential for this process, implicating the intrinsic apoptotic pathway as a key mechanism.
FOXO (show FOXO3 ELISA Kits)-dependent BMF expression is repressed in E-cadherin (show CDH1 ELISA Kits)-negative and metastatic breast cancer cells and that expression of BMFis sufficient to inhibit tumour growth and dissemination in mice.
BMF loss is associated with germ cell loss during oogenesis.
Bcl2 interacting mediator of cell death (Bim (show BCL2L11 ELISA Kits)) and Bcl2 modifying factor (Bmf), mediate apoptosis in the context of TACI (show TNFRSF13B ELISA Kits)-Ig overexpression that effectively neutralizes BAFF (show TNFSF13B ELISA Kits) as well as APRIL.
Bmf deficiency induced significant protection against oxygen/glucose deprivation injury in cultured neurons.
Our findings support an important role for BMF in determining the number of primordial follicles maintained in the ovary throughout adult reproductive life.
Bim (show BCL2L11 ELISA Kits) and Bmf act in concert to prevent autoimmunity and malignant disease
Bmf-deficient mice showed normal sensitivity to the convulsant effects of KA, displayed significantly more neuronal death in the hippocampal CA1 (show CA1 ELISA Kits) and CA3 (show CA3 ELISA Kits) subfields after SE.
deacetylation of p53 (show TP53 ELISA Kits) suppresses Bmf expression and facilitates autophagy.
critical role for Bim (show BCL2L11 ELISA Kits) and Bmf as regulators of hematopoietic stem and progenitor cell dynamics both during early engraftment and long-term reconstitution
The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein contains a single BCL2 homology domain 3 (BH3), and has been shown to bind BCL2 proteins and function as an apoptotic activator. This protein is found to be sequestered to myosin V motors by its association with dynein light chain 2, which may be important for sensing intracellular damage and triggering apoptosis. Alternatively spliced transcript variants encoding different isoforms have been identified.
Bcl2 modifying factor
, bcl-2-modifying factor
, Bcl-2 modifying factor
, Bcl-2-modifying factor