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Four SNPs in IFNGR2 (show IFNGR2 Proteins), IL12RB1, IL12RB2 (show IL12RB2 Proteins), and IL23R (show IL23R Proteins) were found to be associated with the MAP infection status of the resource population.
A novel IL12RB1 N-terminal signal peptide stop-gain loss-of-function homozygous genotype connects three unrelated Brazilian kindreds with IL-12Rbeta1 deficiency with varying severity and early-onset age mainly regarding susceptibility to Mycobacteria, Histoplasma, and Salmonella infections through the paradoxical diminished cell-surface expression of an impaired IL-12Rbeta1 polypeptide.
Th17 cells expressed consistent high levels of the IL-12Rbeta1 subunit, which appeared a better predictor of responsiveness to IL-23 (show IL23A Proteins) than the expression of the IL-23R (show IL23R Proteins) subunit.
Polymorphisms of IFNG (show IFNG Proteins), IL12B (show IL12B Proteins) and IL12RB1 genes in paracoccidioidomycosis Brazilian patients do not affect the susceptibility or resistance to the disease.
The results of this case-control study suggest that IL-12A (show IL12A Proteins), IL-12B (show IL12B Proteins), IL12RB1, IL12RB2 (show IL12RB2 Proteins) and IL23R (show IL23R Proteins) make no genetic contribution to the susceptibility of Takayasu arteritis in Chinese populations
Truncated IL12rbeta1/Fc is a novel fusion protein for specific binding multiple forms of p40 subunit to exert potent anti-inflammatory effects.
the introduction of RNA-DNA differences into an individual's IL12RB1 mRNA repertoire is a novel determinant of IL12 (show IL12A Proteins)/23 sensitivity.
we describe cosegregation of a heterozygous germline defect in IL12RB1 and gastric cancer development in a family with IL-12Rbeta1 deficiency
individual variability in IL12RB1 function is introduced at the epigenetic, genomic polymorphism, and mRNA splicing levels [review]
Early coupled up-regulation of IL12RB1 in CD8 (show CD8A Proteins)+ central memory and effector T cells result in better clinical outcomes in liver transplant recipients.
Genetic variations of IL-12B (show IL12B Proteins), IL-12Rbeta1, IL-12Rbeta2 in Behcet's disease and VKH syndrome.
the data support a model wherein IL12Rbeta1DeltaTM is a secreted product of il12rb1 that promotes resistance to M. tuberculosis infection by potentiating T(H) cells response to IL-12 (show IL12A Proteins).
Although they share a common subunit, IL-23 (show IL23A Proteins) and IL-12 (show IL12A Proteins) receptors are not expressed on the same cell populations.
IL12RB1 is essential for human resistance to Mycobacterium tuberculosis infection
IL-12p40 is induced rapidly in response to Francisella tularensis LVS and is required for DC migration through an IL-12Rbeta1-IL-12(p40 (show IL12B Proteins))2 dependent mechanism.
IL-12Rbeta1DeltaTM represents a novel regulator of IL12Rbeta1-dependent dendritic cell function and of the immune response to Mycobacterium tuberculosis.
IL-12R beta 1 deficiency results in decreased viral replication and inflammation following coxsackievirus B3-induced myocarditis, decreasing IL-1 beta (show IL1B Proteins) and IL-18 (show IL18 Proteins) in the heart.
The binding domain in the IL-12 receptor beta 1 cytoplasmic region has been mapped to sphingosine kinase 2 (show SPHK2 Proteins).
Expression of the IL-12 (show IL12A Proteins) beta 1 receptor is upregulated in both microglia and splenic macrophages.
IL-12 receptor beta 1 subunit plays an essential role in the activation and differentiation of Th1-type myelin oligodendrocyte glycoprotein (MOG)-specific autoreactive T cells in vivo.
IL-12 receptor beta 1 (Rbeta1) mediates IL-12 p40 (show IL12B Proteins) homodimer (p80 (show COIL Proteins))-dependent macrophage chemotaxis and inhibition of the p80 (show COIL Proteins)-Rbeta1 interaction, a novel anti-inflammatory strategy to manipulate inflammation associated with respiratory viral infection.
The protein encoded by this gene is a type I transmembrane protein that belongs to the hemopoietin receptor superfamily. This protein binds to interleukine 12 (IL12) with a low affinity, and is thought to be a part of IL12 receptor complex. This protein forms a disulfide-linked oligomer, which is required for its IL12 binding activity. The coexpression of this and IL12RB2 proteins was shown to lead to the formation of high-affinity IL12 binding sites and reconstitution of IL12 dependent signaling. The lack of expression of this gene was found to result in the immunodeficiency of patients with severe mycobacterial and Salmonella infections. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
interleukin-12 receptor subunit beta-1
, interleukin 12 receptor, beta 1
, IL12 receptor beta 1 subunit
, interleukin-12 receptor subunit beta-1-like
, IL-12 receptor beta component
, IL-12 receptor subunit beta-1
, IL-12R subunit beta-1
, interleukin-12 receptor beta-1 chain
, Interleukin-12 receptor beta-1 chain precursor (IL-12R-beta1) (Interleukin-12 receptor beta) (IL-12 receptor beta component)