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Taken together, we report here for the first time that lung Rip2 level was markedly elevated in cigarette smoke (CS)-challenged mice lungs, and Rip2 gene silencing evidently attenuated CS-induced airway inflammation and oxidative damage, probably via disruption of the NF-kappaB signaling pathway.
These data illustrate that RIP2 can be activated by a relevant allergic stimulus and that such activation can contribute to allergic airway inflammation
Our data suggest that RIP2 has a T cell-intrinsic role in determining the balance between homeostatic and pathogenic Th17 cell responses.
This study provides a complete overview of the polyubiquitins in NOD2:RIP2 signaling and reveal MYSM1 as a central negative regulator restricting these polyubiquitins to prevent excessive inflammation.
These findings demonstrate that Dectin-1, Irak1, and Rip2 are involved in response to Aspergillus fumigatus infection. Dectin-1 modulates the expression of Irak1 and Rip2.
RIP2-knockout attenuates cardiac injury and dysfunction in hypertrophic heart. RIP2-deficience alleviates inflammation in heart of hypertrophic mice. RIP2-deletion inhibits fibrosis in the heart of hypertrophic mice.
this study reveals that LRRK2 is a new positive regulator of Rip2 and promotes inflammatory cytokine induction through the Nod1/2-Rip2 pathway.
Overall, our study has identified a new role of PS-341 in the cell death of BMDMs and provided a novel insight into the atherosclerotic inflammation caused by proteasome-mediated macrophage necroptosis.
that Rip2 modifies VEGF-induced signalling and vascular permeability in myocardial ischaemia
serves as a novel positive modulator of ventricular remodelling after myocardial infarction via the regulation of NF-kappaB and p38 signalling
Bacterial polysaccharide-responsive miR-150 and miR-143 RIPK2 and TAK1 to suppress NOD2-induced immunomodulators.
related to islet dysfunction during the development of type 2 diabetes
NOD2 downregulates colonic inflammation by IRF4-mediated inhibition of K63-linked polyubiquitination of RICK and TRAF6.
RIPK2 has a role in NOD signalling and in inflammatory cytokine production
Rip2-deficient tumors showed enhanced epithelial-to-mesenchymal transition, with elevated expression of zeb1, zeb2, twist, and snail in the tumor microenvironment.
data show that Nod1, Nod2 and Rip2 are not required for local chemokine production and neutrophil recruitment during CLP-induced sepsis, and they reinforce the importance of MyD88-dependent signaling for initiation of a protective host response.
Suggest that the Nod2-Rip2 axis may contribute to the innate immune response of neutrophils against bacterial infection.
Nod/Ripk2 signaling in dendritic cells activates IL-17A-secreting innate lymphoid cells and drives colitis in T-bet-/-.Rag2-/- (TRUC) mice.
SMS suppressed the activation of NF-kappaB and receptor interacting protein-2/caspase-1.
In this work, we show that RIP2 has important role on proinflammatory cytokine production in Y. enterocolitica infected macrophages in TLR4-tolerant condition.
We analyzed a family with dominant inheritance of early-onset Osteoarthritis found that affected individuals harbored a rare variant allele encoding a significant amino acid change (p.Asn104Asp) in the kinase domain of receptor interacting protein kinase 2 (RIPK2)
can form long filaments mediated by its caspase recruitment domain (CARD), in common with other innate immune adaptor proteins; NOD2 tandem CARDs bind to one end of the RIP2 CARD filament
molecular mechanisms how RIP2 is activated and self-propagating signal, are reported.
Two Single-Nucleotide Polymorphisms associated with susceptibility to develop dengue in NOD1 or RIPK2 genes were observed Children from Colombia.
Nine compounds from the ZINC database show satisfactory results, yielding among those selected, the compound ZINC01540228, as the most promising RIPK2 inhibitor. After binding free energy calculations, the following molecular dynamics simulations showed that the receptor protein's backbone remained stable after the introduction of ligands.
Results showed that the expressions of RIP2 and BclxL were positively correlated with the malignant grade of astrocytoma. RIP2 promoted human glioblastoma cell proliferation by inducing expression of BclxL.
Together, these data show that RIP2 promotes survival of breast cancer cells through NF-kappaB activation and that targeting RIP2 may be therapeutically beneficial for treatment of TNBC.
RIP2 kinase auto-phosphorylation is intimately coupled to dimerization.
study provides structural and dynamic insights into the NOD1-RIP2 oligomer formation, which will be crucial in understanding the molecular basis of NOD1-mediated CARD-CARD interaction in higher and lower eukaryotes
a new function of PAX5 in regulating RIP1 and RIP2 activation, which is at least involved in chemotherapeutic drug resistance in B-lymphoproliferative disorders, is reported.
Data indicate that receptor-interacting protein 2 (Rip2) polymorphisms are associated with increased risk of subclinical atherosclerosis (SA) and with some clinical and metabolic parameters.
Together, the data demonstrate that the NOD2-RIP2 pathway is activated in murine and human visceral leishmaniasis and plays a role in shaping adaptive immunity toward a Th1 profile.
RIP2 and RhoGDI bind to p75(NTR) death domain at partially overlapping epitopes with over 100-fold difference in affinity, revealing the mechanism by which RIP2 recruitment displaces RhoGDI upon ligand binding.
Barettin has inhibitory activity against two protein kinases related to inflammation, namely the receptor-interacting serine/threonine kinase 2 (RIPK2) and calcium/calmodulin-dependent protein kinase 1alpha (CAMK1alpha).
up-regulated in failing hearts
RIPK1 and RIPK2 are targets of HIV-1 Protease activity during infection, and their inactivation may contribute to modulation of cell death and host defense pathways by HIV-1
SNPs and haplotypes from RIPK2 were associated with tick burden in both dairy and beef cattle.
Genetic mapping of RIPK2 in cattle.
This gene encodes a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases. The encoded protein contains a C-terminal caspase activation and recruitment domain (CARD), and is a component of signaling complexes in both the innate and adaptive immune pathways. It is a potent activator of NF-kappaB and inducer of apoptosis in response to various stimuli.
receptor-interacting serine-threonine kinase 2
, receptor-interacting serine/threonine-protein kinase 2-like
, receptor-interacting serine/threonine-protein kinase 2
, tyrosine-protein kinase RIPK2
, CARD-carrying kinase
, CARD-containing IL-1 beta ICE-kinase
, CARD-containing interleukin-1 beta-converting enzyme (ICE)-associated kinase
, growth-inhibiting gene 30
, receptor-interacting protein (RIP)-like interacting caspase-like apoptosis regulatory protein (CLARP) kinase
, receptor-interacting protein 2
, receptor (TNFRSF)-interacting serine-threonine kinase 2