Browse our BAD Proteins (BAD)

Zebrafish BCL2-Associated Agonist of Cell Death (BAD) interaction partners

1. Bad functions as an essential sensitizer and Puma as an essential activator of IR-induced mitochondrial apoptosis specifically in embryonic neural tissue.

2. Stage-specific expression of TNFalpha regulates bad/bid-mediated apoptosis and RIP1/ROS-mediated secondary necrosis in Birnavirus-infected fish cells.

3. Results indicate that zebrafish BH3-only proapoptotic protein (BAD) could induce apoptosis in vitro and in vivo and may have biological implications in apoptosis during zebrafish development.

Human BCL2-Associated Agonist of Cell Death (BAD) interaction partners

1. A non-canonical role for BAD and reconciles BAD-mediated tumor growth with favorable outcomes in BAD-high breast cancer patients.

2. Targeting BCL-xL improves the efficacy of bromodomain and extra-terminal protein inhibitors in triple-negative breast cancer by eliciting the death of senescent cells.

3. High BAD expression is associated with cisplatinresistant oral cancer.

4. Bcl-2 agonist of cell death (BAD) has pro-apoptosis and pro-survival functions involved in cancer development [Review].

5. The findings suggest that experimental hyperthermia (EH) exposure leads to simultaneous activation of molecular switches of apoptosis (BCL2 and BAD) in cells of the follicular epithelium of the ovaries on days 3 and 4 after EH.

6. The positive correlation of Bad expression with nodule size and a relative decrease in the mRNA expression level of Bad in benign thyroid nodules suggest that Bad may be an important regulator of thyroid cell apoptosis.

7. Data suggest that ECAD, STAT3, Bak, and Bcl-xL are expressed in affected endometrial tissues of women with endometrioid adenocarcinoma depending on neoplasm staging and cell differentiation. This study was conducted using immunohistochemistry of surgically resected tissues. (ECAD = E-cadherin; STAT3 = signal transducer and activator of transcription 3 protein; Bak = pro-apoptotic protein BAK)

8. cyclin D1 was downregulated, whereas Bcell lymphoma 2associated agonist of cell death (BAD) was upregulated following RAC1 knockdown in colon cancer cells.

9. we have found that a subgroup of colorectal cancers, defined by having either KRAS or BRAF (KRAS/BRAF) mutations and BCL2L1 (encoding BCL-XL) amplification, can be effectively targeted by simultaneous inhibition of BCL-XL (with ABT-263) and MCL1 (with YM-155).

10. BAD phosphorylation is essential in the cytoprotective effect of vasoactive intestinal peptide on cancer stem cells.

11. NDRG2 could inhibit Bad degradation by increasing its protein stability in breast cancer cells.

12. Taken together, our results provide a structural basis for the binding mechanism between DJ-1 and Bcl-XL, which will contribute to molecular understanding of the role of mitochondrial DJ-1 in Bcl-XL regulation in response to oxidative stress.

13. We will then review how the apoptotic and autophagic functions of Bcl-xL are modified by this post-translational modifications, and how this impacts on its oncogenic properties.

14. the membrane localization of BCL-xL enforces its control over cell survival and, importantly, limits the pro-apoptotic effects of BH3 mimetics by selectively influencing BCL-xL binding to key pro-apoptotic effectors.

15. The long unstructured region of Bcl-xl modulates its structural dynamics.

16. Short-term treatment of nascent melanoma tumors with PAK inhibitors that block RhoJ signaling halts the growth of BRAF mutant melanoma tumors in vivo and induces apoptosis in melanoma cells in vitro via a BAD-dependent mechanism. As up to 50% of BRAF mutant human melanomas express high levels of RhoJ, these studies nominate the RhoJ-BAD signaling network as a therapeutic vulnerability for fledgling BRAF mutant human tumor

17. Recent studies that combine experiments in yeast and in mammalian cells have shown the unexpected effect of the anti-apoptotic protein Bcl-xL on the priming of Bax. As demonstrated with the BH3-mimetic molecule ABT-737, this property of Bcl-xL, and of Bcl-2, is crucial to elaborate about how apoptosis could be reactivated in tumoral cells.

18. the accumulation of reactive oxygen species (ROS) in cells expressing JAK2V617F compromises the NHE-1/Bcl-xL deamidation pathway by repressing NHE-1 upregulation in response to DNA damage. hematopoietic stem cells (HSCs), FOXO3A is largely localized within the nuclei despite the presence of JAK2V617F mutation, suggesting that JAK2-FOXO signaling has a different effect on progenitors compared with stem cells.

19. These results identify beta3 integrin signaling via repression of BAD as an important survival pathway used by breast cancer cells to evade chemotherapy induced stress.

20. BAD mutation is associated with maturity-onset diabetes of the young.

Mouse (Murine) BCL2-Associated Agonist of Cell Death (BAD) interaction partners

1. SAD-A is activated by the incretin hormone GLP-1 in pancreatic beta-cell. SAD-A promotes the phosphorylation of Bad S155.

2. The authors report that BAD is essential for mediating TNFalpha cytotoxicity for tissue damage of multiple orgrans and mortality despite concurrent activation of the IKK-NF-kappaB pathway in septic shock.

3. further identified the pro-apoptotic protein BAD as a potential mitochondrial substrate of PINK1 both in vitro and in vivo, and found that cells more susceptible to a12poptosis induced by mitochondrial damage can be rescued by phosphorylation mimic BAD.

4. This study shows for the first time that genetic knockout of Bad provides epileptic seizure protection in Kcna1-/- mice, a genetic model of epilepsy with sudden unexplained death.

5. BAD knockout reduced epileptiform activity, and this effect was lost upon knockout or pharmacological inhibition of KATP channels.

6. Bad is dispensable for TNF-mediated cell death.

7. Results suggest that regulation of the proapoptotic activity of BAD plays a key role in the pathogenic mechanisms resulting in primary pigmented nodular adrenocortical disease tumor formation.

8. fasting may increase the uptake beta-hydroxybutyrate by decreasing BAD in the brain during hypoglycemia

9. Results indicate the downstream targets of insulin, cyclin D1, BAD, alpha-MHC, and GATA-4, elucidate a molecular mechanism of insulin in promoting cell proliferation and differentiation.

10. our study suggests that Bad and Bmf co-regulate lymphocyte homeostasis and limit spontaneous transformation by mechanisms that may not exclusively be linked to the induction of lymphocyte apoptosis.

11. Results reveal that IKK inhibits TNFalpha-induced apoptosis through two distinct but cooperative mechanisms: activation of the survival factor NF-kappaB and inactivation of the proapoptotic BH3-only BAD protein.

12. RNAi-mediated silencing of STAT1 in soft tissue sarcoma (STS) cells was sufficient to increase expression of the apoptotic mediators Fas and Bad and to elevate the sensitivity of STS cells to Fas-mediated apoptosis

13. BAD modulates counterregulatory responses to hypoglycemia and protective glucoprivic feeding

14. the regulation of BAD by uremic toxins and report the sensitization of vascular smooth muscle cells to apoptosis upon BAD induction was explored.

15. Tonicity-induced COX-2 expression and PGE2 synthesis in the renal medulla entails phosphorylation and inactivation of the pro-apoptotic protein Bad, thereby counteracting apoptosis in renal medullary epithelial cells.

16. Caspase-3 is activated by the BAD-BAX cascade resulting in long term depression induction in the hippocampus.

17. JNK1 is required for erythropoietin-mediated cell survival through phosphorylation and inactivation of the pro-apoptotic, Bcl-2 homology domain 3 (BH3)-only Bcl-associated death protein (Bad).

18. Bad protein cooperate with bim protein in certain apoptotic responses and in the suppression of g-irradiation-induced thymic lymphoma.(Bad protein)

19. Data show that loss of Bmf reduced the pressure to inactivate p53, whereas Bad deficiency did not, identifying Bmf as a novel component of the p53-independent tumor suppressor pathway triggered by c-Myc.

20. The beta-arrestin 1-dependent ERK1/2 activation engaged by GLP-1 mediates the Ser-112 phosphorylation of Bad.

Cow (Bovine) BCL2-Associated Agonist of Cell Death (BAD) interaction partners

1. This indicates a gradient of sensitivity (epiblast > hypoblast > TE) to BAD overexpression