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IL1B (show IL1B Proteins) regulates expression of IL1R1 (show IL1RN Proteins) and IL1RAP and stimulates expression of PTGS1 (show PTGS1 Proteins) and PTGS2 (show PTGS2 Proteins) that are considered to be the most rate-limiting enzymes for endometrial synthesis of prostaglandins during the peri (show PLIN1 Proteins)-implantation period of pregnancy in pigs.
These results provide novel insights into the role of IL1RAP in CML and a strong rationale for the development of an IL1RAP antibody therapy to target residual CML stem cells.
single nucleotide polymorphism A471T in the Toll (show TLR4 Proteins)-interleukin 1 receptor domain (TIR) of the IL-1Rrp2 (show IL1RL2 Proteins) that is present in approximately 2% of the human population, down-regulated IL-36R (show IL1RL2 Proteins) signaling by a decrease of interaction with IL-1RAcP.
The findings of this study support IL1RAP as a novel potential Alzheimer's disease target and highlight the use of amyloid PET as a valuable Alzheimer's disease endophenotype, particularly in a longitudinal framework.
The SNP rs4624606 in IL-1RAcP was nominally associated with CAD risk.
Data suggest serum levels of soluble IL1RAP (from alternative splicing) are down-regulated in endometriosis throughout menstrual cycle; IL1RAP levels (which peak in proliferative phase in fertile women) exhibit minor variations in endometriosis.
Combined crystallography and small-angle X-ray-scattering studies reveal that ST2 (show SULT2A1 Proteins) possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution.
MARCH8 (show MARCH8 Proteins)-mediated polyubiquitination and degradation of IL1RAP is an important mechanism for negative regulation of IL-1beta (show IL1B Proteins)-induced signaling pathways.
Knockdown of IL1RAP decreased clonogenicity and increased cell death of AML (show RUNX1 Proteins) cells.
Interleukin-1R3 mediates interleukin-1-induced potassium current increase through fast activation of Akt (show AKT1 Proteins) kinase.
The genetic polymorphisms of IL-1ss-2023 C allele, IL- 1RAcP -8261 T allele and -8183 A allele are probable host factors for persistent HBV infection.
These results thus reveal the decoding mechanism of splice-insert signaling codes for synaptic differentiation induced by trans-synaptic adhesion between PTPdelta and IL1RAPL1 (show IL1RAPL1 Proteins)/IL-1RAcP.
In experimental biliary atresia, miR (show MLXIP Proteins)-29a/29b1 are upregulated, and reporter assays confirmed that Igf1 (show IGF1 Proteins) and Il1RAP are down-regulated by miR (show MLXIP Proteins)-29.
The results of this study suggested that IL-1RAcP represents an interesting molecular link between immune systems and synapse formation in the brain.
IL-1RAcP is essential for physiological activities of peripheral IL-1 (show IL1A Proteins).
Identification of essential regions in the cytoplasmic tail of interleukin-1 receptor accessory protein critical for interleukin-1 signaling
data suggest that domain III of IL-1RAcP may be involved in the formation or stabilization of the IL-1RI/IL-1 (show IL1A Proteins) complex by binding to epitopes on domain III of the IL-1RI created following IL-1 (show IL1A Proteins) binding to the IL-1RI
IL-33 (show IL33 Proteins) and ST2 (show SULT2A1 Proteins) form a complex with IL-1R accessory protein (IL-1RAcP), a signaling receptor subunit that is also a member of the IL-1R complex.
IL-1RAcP is used by more than one alpha-chain (show FCGRT Proteins) of the IL-1 (show IL1A Proteins) receptor family and thus may resemble a common beta-chain (show CSF2RB Proteins) of that family
these observations establish AcP (show NDUFAB1 Proteins) as co-receptor for IL-33 (show IL33 Proteins) signaling via ST2 (show SULT2A1 Proteins) and suggest a novel role for sAcP in modulating the biological activity of IL-33 (show IL33 Proteins)
an isoform of the IL-1 receptor accessory protein (termed AcPb) was identified that is expressed exclusively in the CNS.
Interleukin 1 induces synthesis of acute phase and proinflammatory proteins during infection, tissue damage, or stress, by forming a complex at the cell membrane with an interleukin 1 receptor and an accessory protein. This gene encodes the interleukin 1 receptor accessory protein. The protein is a necessary part of the interleukin 1 receptor complex which initiates signalling events that result in the activation of interleukin 1-responsive genes. Alternative splicing of this gene results in two transcript variants encoding two different isoforms, one membrane-bound and one soluble. The ratio of soluble to membrane-bound forms increases during acute-phase induction or stress.
interleukin 1 receptor accessory protein
, interleukin-1 receptor accessory protein
, interleukin-1 receptor accessory protein-like
, IL-1 receptor accessory protein
, interleukin-1 receptor 3
, interleukin-1 receptor accessory protein beta