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There were higher expressions of XIAP (p = 0.0032) and Bcl-2 (show BCL2 Proteins) (p = 0.0351) in the glioblastoma samples compared to the control samples of normal brain. These results raise the question of whether Bcl-2 (show BCL2 Proteins) and XIAP genes can be responsible for the inhibition of programmed cell death in glioblastomas.
These results show that significantly increased levels of FOXO3 (show FOXO3 Proteins), IRF4 (show IRF4 Proteins), and xIAP mRNA in Chinese HIV-1-infected patients.
the aim of this review is to emphasize to clinicians that XIAP deficiency should be considered in patients suspected to have Crohn disease with early onset or an aggravated clinical course resistant to conventional therapy, and that appropriate treatment strategies are available.
uncovered a novel function of BIR (show KCNJ11 Proteins) domain of XIAP in regulating the EGFR (show EGFR Proteins) translation
our study revealed a novel microRNA signaling pathway involved in cholangiocarcinoma and suggests that manipulation of the miR (show MLXIP Proteins)-410/XIAP pathway could have a therapeutic potential for cholangiocarcinoma
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.
There was a significantly decreased percentage of IL-17A (show IL17A Proteins)-producing CD4 (show CD4 Proteins) T cells in mice receiving Tregs from xIAP mice. xIAP appears dispensable for the generation of induced Treg cells as well as function of natural Treg cells. There appeared to be a role of xIAP in generation of IL-17 (show IL17A Proteins)-producing cells from either naive CD4 (show CD4 Proteins) T cells or Treg cells.
Drugs targeting XIAP and cIAP1 (show BIRC2 Proteins)/2 may be effective for osteosarcoma patients whose tumors express abundant RIPK1 (show RIPK1 Proteins) and contain high levels of TNFalpha (show TNF Proteins).
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.
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.
E3 ubiquitin-protein ligase XIAP
, IAP-like protein
, X-linked IAP
, baculoviral IAP repeat-containing protein 4
, inhibitor of apoptosis protein 3
, Baculoviral IAP repeat-containing protein 4
, X-linked inhibitor of apoptosis protein
, baculoviral IAP repeat-containing 4
, baculoviral IAP-repeat containing protein 4
, IAP homolog A
, apoptosis inhibitor 3
, apoptosis inhibitor protein 3
, baculoviral IAP repeat containing 8