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We report that an Smac-mimetic selectively induces TNF-alpha (show TNF Proteins)-dependent cystic renal epithelial cell death, leading to the removal of cystic epithelial cells from renal tissues and delaying cyst formation.
Results demonstrate an essential and apoptosis-independent function of SMAC in tumor suppression and provide new insights into the biology and targeting of colon cancer.
Identification of a novel anti-apoptotic E3 ubiquitin ligase (show MUL1 Proteins) that ubiquitinates antagonists of inhibitor of apoptosis proteins SMAC, HtrA2 (show HTRA2 Proteins), and ARTS.
Loss of Smac/DIABLO alters both caspase (show CASP3 Proteins)-dependent and caspase (show CASP3 Proteins)-independent intrinsic programmed cell death.
Membrane-associated XIAP (show XIAP Proteins) induces mitochondrial outer membrane permeabilization leading to cytochrome c (show CYCS Proteins) and Smac release, which is dependent on Bax (show BAX Proteins) and Bak (show BAK1 Proteins).
data suggest the existence of a redundant molecule or molecules capable of compensating for a loss of Smac/DIABLO function.
mitochondrial activation by Bid (show BID Proteins) is required for reversing the inhibitor-of-apoptosis proteins inhibition through Smac release
Diablo was present within the mitochondria of healthy cells, but released into the cytosol following the induction of apoptosis by UV.
Transient focal ischemia was produced for 1 hour in mice. Mitochondrial levels of DIABLO increased after 2-11 h reperfusion. DIABLO increased in the cytosol after 5 h reperfusion, implying the translocation of DIABLO into the cytosol.
Bax (show BAX Proteins) and Bak (show BAK1 Proteins) differentially regulate the release of cytochrome c (show CYCS Proteins) and Smac/DIABLO from mitochondria, and Smac/DIABLO can be used to sensitize cells that are deficient in Bax (show BAX Proteins) and Bak (show BAK1 Proteins) genes, or resistant to TRAIL.
analysis of Smac-mediated apoptosis in chronic lymphocytic leukemia cells
Data show that oncolytic viruses (OV) and second mitochondrial activator of caspase (show CASP3 Proteins) (Smac)-mimetic compounds (SMC (show DYM Proteins)) synergistically kill cancer cells directly.
Expressions of SDF-1 (show CXCL12 Proteins), survivin (show BIRC5 Proteins) and smac were significantly higher in epithelial ovarian cancer tissue than those in normal tissue.
Results indicate that Smac plays an important role in reticulum stress-induced apoptosis in human lens epithelial cells, suggesting its close association with cataract development.
Smac mimetic APG (show SMAD1 Proteins)-1387 exerts a potent antitumor effect on nasopharyngeal carcinoma cells by inducing apoptosis.
These results reveal a pro-apoptotic function of PARL (show PARL Proteins) and identify PARL (show PARL Proteins)-mediated Smac processing and cytochrome c (show CYCS Proteins) release facilitated by OPA1 (show OPA1 Proteins)-dependent cristae remodelling as two independent pro-apoptotic pathways in mitochondria.
Study found a negative correlation between Smac and XIAP (show XIAP Proteins) at the level of protein but not mRNA in non-small cell lung carcinoma (NSCLC) patients. Overexpressed XIAP (show XIAP Proteins) could degrade through ubiquitination, the mature Smac inhibiting NSCLC apoptosis.
Report role of RIP1 (show UQCRFS1 Proteins) in Smac mimetic mediated chemosensitization of neuroblastoma (show ARHGEF16 Proteins) cells.
This review discusses the promise as well as some challenges at the translational interface of exploiting Smac mimetics as cancer therapeutics.
Data indicate that Smac/DIABLO showed an inverse correlation with inhibitor of apoptosis proteins XIAP (show XIAP Proteins), cIAP-1 (show BIRC2 Proteins) and cIAP-2 (show BIRC3 Proteins).
hyperosmotic shock induces rapid calpain activation and high levels of Smac/DIABLO release from the mitochondria before significant amounts of cytochrome c (show CYCS Proteins) are released to promote caspase-3 (show CASP3 Proteins) activation
Identification of the third vertebrate homologue of Smac/DIABLO.
This gene encodes an inhibitor of apoptosis protein (IAP)-binding protein. The encoded mitochondrial protein enters the cytosol when cells undergo apoptosis, and it moderates the caspase inhibition of IAPs. Multiple polyadenylation sites have been found for this gene. Four alternatively spliced transcript variants have been described for this gene, with two of them encoding different isoforms and the other two probably not encoding a protein.
Direct IAP-binding protein with low pI
, diablo homolog, mitochondrial
, second mitochondria-derived activator of caspase
, direct IAP binding protein with low PI
, direct IAP-binding protein with low pI
, diablo homolog
, mitochondrial diablo-like protein
, mitochondrial diablo
, second mitochondrial derived activator of caspases
, Second mitochondria-derived activator of caspase