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Inhibition of BET bromodomain-dependent XIAP and FLIP expression sensitizes KRAS-mutated non-small cell lung cancer to pro-apoptotic agents.
XIAP interacts with FAF1 (show FAF1 Proteins) and blocks FAF1 (show FAF1 Proteins)-induced cell death.
The study identifies an unanticipated role for the X-linked inhibitor of apoptosis (XIAP) protein as a regulator of Lys63-linked polyubiquitination of HIF1alpha (show HIF1A Proteins).
The authors find that primary human aggressive B-cell lymphoma samples exhibit high USP9X (show USP9X Proteins) expression that correlate with XIAP overexpression.
Findings reveal important new insights into how XIAP 3'UTR works, suggesting that the non-coding XIAP 3'UTR serves as a competitor for miRNA binding and subsequently inactivates miRNA functions, by which XIAP 3'UTR frees the target mRNAs from being repressed.
XIAP is stable during mitotic arrest, but its function is controlled through phosphorylation by the mitotic kinase CDK1 (show CDK1 Proteins)-cyclin-B1 (show CCNB1 Proteins) at S40.
our findings suggest that X-linked inhibitor of apoptosis protein 3'-untranslated region serves as a competitive endogenous RNA for HMGA2 to activate hepatocellular carcinoma progression by arresting endogenous let-7a-5p.
In chronic myeloid leukemia (show BCL11A Proteins) cells, EZH2 (show EZH2 Proteins) modulates epigenetic changes at DNA methylated regions encoding miR (show MLXIP Proteins)-219 and downregulates the level of miR (show MLXIP Proteins)-219. Downregulation of miR (show MLXIP Proteins)-219 results in upregulation of XIAP and supports the survival of leukemia cells.
IFNgamma positively affects NOD2-mediated signaling in human conventional dendritic cells, in a manner considerably dependent on XIAP and partially dependent on mTOR (show FRAP1 Proteins).
miR (show MLXIP Proteins)-137 expression is inversely correlated with the level of XIAP protein in both ovarian cancer tissues and cell lines. these data suggest that multiple miRNAs can regulate XIAP via its 3'UTR. miR (show MLXIP Proteins)-137 can sensitise ovarian cancer cells to cisplatin-induced apoptosis, providing new insight into overcoming drug resistance in ovarian cancer
Deletion of XIAP switches cell death away from necrosis to apoptosis.
These results indicate that XIAP plays an important physiologic role in regulating sublethal CASP-3 (show CASP3 Proteins) activity within central neurons and thereby facilitates synaptic plasticity and memory acquisition.
XIAP antagonizes the switch from TNFalpha (show TNF Proteins)-induced apoptosis to necroptosis in mouse neutrophils.
Results show that XIAP binds to the C terminus of Ptch1 (show PTCH1 Proteins) and mediates the death-dependent function of Ptch1 (show PTCH1 Proteins).
XIAP modulates ubiquitylation of RIP1 (show RALBP1 Proteins) and suppresses RIP3-dependent cell death and inflammasome activation in response to TNF (show TNF Proteins)-signaling in innate immune cells.
XIAP deficiency selectively impaired B-cell chronic lymphocytic leukemia/lymphoma 10 (BCL10 (show BCL10 Proteins))-mediated innate responses to dectin-1 (show CLEC7A Proteins) ligands but did not affect responses to various Toll (show TLR4 Proteins)-like receptor agonists.
XIAP mRNA level was also reduced in the BRE (show BRE Proteins)-depleted cells, but the level of reduction was less profound than that of the protein level. However, BRE (show BRE Proteins) could not delay protein turnover of XIAP.
Identify xIAP and cIAP1 (show BIRC2 Proteins) as molecular targets of ceramide and show ceramide analog LCL85 is an effective sensitizer in overcoming resistance of metastatic colon and breast cancers to apoptosis induction to suppress metastasis in vivo.
XIAP-/- DRG sensory neurons degenerate more rapidly and contain more active caspase-3 (show CASP3 Proteins).
XIAP ubiquitylates RIPK2 and recruits the linear ubiquitin chain assembly complex to NOD2
This gene encodes a protein that belongs to a family of apoptotic suppressor proteins. Members of this family share a conserved motif termed, baculovirus IAP repeat, which is necessary for their anti-apoptotic function. This protein functions through binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2 and inhibits apoptosis induced by menadione, a potent inducer of free radicals, and interleukin 1-beta converting enzyme. This protein also inhibits at least two members of the caspase family of cell-death proteases, caspase-3 and caspase-7. Mutations in this gene are the cause of X-linked lymphoproliferative syndrome. Alternate splicing results in multiple transcript variants. Pseudogenes of this gene are found on chromosomes 2 and 11.
X-linked inhibitor of apoptosis protein
, baculoviral IAP repeat-containing 4
, baculoviral IAP-repeat containing protein 4
, Baculoviral IAP repeat-containing protein 4
, E3 ubiquitin-protein ligase XIAP
, X-linked IAP
, IAP-like protein
, baculoviral IAP repeat-containing protein 4
, inhibitor of apoptosis protein 3
, IAP homolog A
, apoptosis inhibitor 3
, apoptosis inhibitor protein 3