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Mitochondrial apoptosis-inducing factor was found to translocate to the nucleus during porcine epidemic diarrhea virus infection.
Drosophila Apoptosis-inducing factor (AIF) is a mitochondrial effector of cell death that plays roles in developmentally regulated cell death and normal mitochondrial function.
apoptosis-inducing factor(AIF) was expressed in luminal alveolar cells and in concert with a change in bax (show BAX Proteins) protein to bcl-2 (show BCL2 Proteins) protein ratio might contribute to signalling of a change in the dynamic balance of the cell population as lactation progresses(AIF)
Mycobacterium bovis-induced macrophage cell death is caspase (show CASP3 Proteins) independent with apoptosis-inducing factor participation.
X-ray irradiation induces apoptosis of mouse GC1 sperm cells via nuclear translocation of AIF.
The first structure of a pathogenic AIF variant in complex with NAD+ is reported. The G307E mutation leads to wrong positioning of NAD+ adenylate moiety.
AIF deficiency is a risk factor for the development of diabetic kidney disease.
In conclusion, calpain was involved in oxygen glucose deprivation-induced RGC-5 necroptosis with the increased expression of its downstream molecule tAIF.
The results identify new protein-protein interactions between AIF-Cx43 (show GJA1 Proteins), ETFB (show ETFB Proteins)-Cx43 (show GJA1 Proteins) and AIF-ETFB (show ETFB Proteins) as possible players in the regulation of the mitochondrial redox state.
our findings suggest that MIA40 (show CHCHD4 Proteins) reduction contributes to the effects of AIF deficiency on OXPHOS, as it may impact on the correct assembly and maintenance of the respiratory subunits.
These results indicate that the adenylate moiety of NAD(+)/H is crucial for the association with AIF and for the subsequent structural reorganization of the complex, but not for protein dimerization.
Taken together, these data suggest that AIF is likely to play a region-specific role in AD-related caspase-independent PCD, which is consistent with aging-associated mitochondrial impairment and oxidative stress.
findings postulate that AIF depletion mediates a preconditioning effect protecting neuronal cells from subsequent glutamate (show GRIN1 Proteins) toxicity through reduced levels of complex I protein
AIF downregulation provides not only long-term overall neuroprotection after hypoxia-ischemia, but also protects neural progenitor cells, thereby rescuing hippocampal neurogenesis.
Data revealed that under a nutrient deficient condition, CD317 (show BST2 Proteins) functions as an anti-apoptotic factor through AIF-mediated caspase (show CASP3 Proteins) and autophagy-independent manner.
we report that AIF-independent PARP-1 (show PARP1 Proteins)-dependent necrosis constitutes a major mechanism of RPE (show RPE Proteins) cell death leading to retinal degeneration in dry age-related macular degeneration .
Downregulation of AIF by hypoxia causes oxidative inactivation of the lipid phosphatase activity of phosphatase and tensin homolog on chromosome 10 (PTEN), with ensuing activation of Akt (show AKT1 Proteins) kinase, phosphorylation of the Akt (show AKT1 Proteins) substrate GSK-3beta and activation of WNT (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling in colon cancer cells.
novel pathway for mda-7/IL-24 (show IL24 Proteins)-induced caspase (show CASP3 Proteins)-independent apoptosis in neuroblastoma (show ARHGEF16 Proteins) cells mediated through modulation of AIF, ATM (show ATM Proteins), and gamma-H2AX (show H2AFX Proteins).
Study defines the mechanism whereby AIF is allosterically modulated by charge-complex formation with NADH. Two distinct molecular pathways couple AIF's active site to dimerization and release of its regulatory C-loop insert with implications for AIF allosteric switching in cell survival and death.
Whole exome sequencing indicated a single plausible candidate - the p.Asp237Gly variant in apoptosis inducing factor mitochondria associated 1 (AIFM1; chr. Xq26.1), and the p.Asp237Gly segregated with disease in two families.
Only a drastic decrease in the expression level or/and redox activity of AIF tends to cause an early and severe neurodegeneration, whereas less pronounced changes in the AIF properties could lead to a broad range of slowly progressive neurological disorders.
AIF translocation plays a role in influenza-virus-induced apoptosis.
Copper induces the activation of apoptosis through casp3 (show CASP3 Proteins)/casp8 (show CASP8 Proteins)/casp9 (show CASP9 Proteins)/AIF/TP53 (show TP53 Proteins) signaling pathways. Suggest that apoptosis activation mechanism is dependent on the concentration, time of exposure to Cu and cell type.
Estradiol inhibits oxidative stress-induced (show SQSTM1 Proteins) accumulation of AIF in nucleolus and PARP1 (show PARP1 Proteins)-dependent cell death via estrogen receptor alpha (show ESR1 Proteins) in MCF-7 cells.
This gene encodes a flavoprotein essential for nuclear disassembly in apoptotic cells, and it is found in the mitochondrial intermembrane space in healthy cells. Induction of apoptosis results in the translocation of this protein to the nucleus where it affects chromosome condensation and fragmentation. In addition, this gene product induces mitochondria to release the apoptogenic proteins cytochrome c and caspase-9. Mutations in this gene cause combined oxidative phosphorylation deficiency 6, which results in a severe mitochondrial encephalomyopathy. Alternative splicing results in multiple transcript variants. A related pseudogene has been identified on chromosome 10.
programmed cell death 8 (apoptosis-inducing factor)
, programmed cell death 8
, apoptosis-inducing factor, mitochondrion-associated, 1
, mammary apoptosis inducing factor
, flavoprotein and apoptosis inductor
, apoptosis-inducing factor 1, mitochondrial-like
, apoptosis inducing factor
, anti-inflammatory factor 1
, apoptosis-inducing factor 1, mitochondrial
, programmed cell death protein 8
, striatal apoptosis-inducing factor