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Human Polyclonal PELI1 Primary Antibody für IHC (p), WB - ABIN252617
Ceppi, Pereira, Dunand-Sauthier, Barras, Reith, Santos, Pierre: MicroRNA-155 modulates the interleukin-1 signaling pathway in activated human monocyte-derived dendritic cells. in Proceedings of the National Academy of Sciences of the United States of America 2009
Show all 2 Pubmed References
Peli1-mediated regulation of Mdmx.
Pellino1 (Peli1) is a DSB-responsive ubiquitin ligase required for the accumulation of DNA damage response proteins and efficient homologous recombination (HR) repair.
PELI1 may function to control inadvertent activation of RIP3, thus preventing aberrant cell death and maintaining cellular homeostasis.
Overexpression of Peli1 inhibits noncanonical NF-kappaB activation and alleviates lupus-like disease. PELI1 levels negatively correlate with disease severity in SLE patients.
Pellino-1 may be critically important for cell survival.
This study demonstrates Pellino 1 (PELI1) as an important modulator that exerts opposite regulatory functions on apoptosis and necroptosis, two distinct forms of regulated cell death mechanisms.
The study demonstrates that cytosolic Pellino-1-mediated K63-linked ubiquitination of IRF5 in M1 macrophages regulates glucose intolerance in obesity, suggesting a cytosolic mediator function of Pellino-1 in TLR4/IFN-gamma receptor-IRF5 axis during M1 polarization.
Pellino 1 expression acts as an inhibitory signal of the homeostatic regulation of mitotic cell cycle and checkpoint, and thus contributes to the initiation and progression of neoplastic chromosome aneuploidy.
Pellino-1 overexpression activated PI3K/Akt and ERK signaling pathways and elicited an epithelial-mesenchymal transition (EMT) phenotype of lung adenocarcinoma cells. Pellino-1-mediated EMT was demonstrated through morphology, the upregulation of Vimentin, Slug and Snail expression and the downregulation of E-cadherin and beta-catenin expression.
Results indicate that Pellino-1 contributes to lung oncogenesis through the overexpression of inhibitor of apoptosis protein 2 (cIAP2) and promotion of cell survival and chemoresistance.
Our results suggest that PELI1 might participate in B-cell maturation or oncogenic activation of aggressive B-cell lymphomas, both during and after germinal center stages
The combination of low Pellino3 levels together with high and inducible Pellino1 expression may be an important determinant of the degree of inflammation triggered upon Toll-like receptor 2 engagement by Helicobacter pylori and/or its components, contributing to Helicobacter pylori-associated pathogenesis by directing the incoming signal toward an NF-kB-mediated proinflammatory response.
Our observations suggested that Peli-1 gene polymorphism rs329498 might contribute to SLE susceptibility in Chinese Han Population.
The study results in the Chinese Han population showed that PELI1 is a member of a constellation of genetic factors that may contribute to the pathogenesis of systemic lupus erythematosus.
Increased PELI1 expression and subsequent induction of BCL6 promotes lymphomagenesis.
Peptide PEL1 derived from the interleukin-1 receptor-associated kinase (IRAK)1-binding motif reveals a distinct phosphothreonine peptide binding preference.
GWAS study found two new SNPs associated with nickel dermatitis; SNPs are located in the NTN4 and PELI1 genes
Pellino1 interacts with the transcription factor Deformed Epidermal Autoregulatory Factor 1 (DEAF1).
incomplete KD, IVIG nonresponsiveness, long febrile days, and the rs7604693 genetic variant in the PELI1 gene are major risk factors for the development of CALs
role in interleukin-1-mediated signalling through interaction with interleukin-1 receptor-associated kinase 4-IRAK-tumor necrosis factor receptor-associated factor 6 complex
findings suggest a nonimmune regulatory role for Peli1 in promoting microglia activation during WNV infection and identify a potentially novel host factor for flavivirus cell entry and replication.
Data suggests that miR-590-5p attenuates brain injury in Intracerebral haemorrhage mice through inhibiting Peli1 gene expression.
Peli1 has a B cell-intrinsic function to protect against lupus-like autoimmunity. Peli1 deficiency in B cells induces autoantibody production via noncanonical NF-kappaB signaling. Mechanically, Peli1 functions as an E3 ligase to associate with NF-kappaB inducing kinase (NIK) and mediates NIK Lys48 ubiquitination and degradation.
Peli1 is a proangiogenic molecule that acts downstream of VEGF-Flk-1 and restores angiogenesis and enhances skin flap survivability.
a novel miR-155-Peli1-c-Rel pathway that specifically regulates Tfh cell generation and function.
These findings reveal a novel mechanism that endotoxin tolerance reprograms mitogen-activated protein kinase signaling by suppressing Pellino 1-mediated K63-linked ubiquitination of cIAP2, K48-linked ubiquitination, and degradation of TRAF3.
Pellino1 plays an important role in the pathogenesis of myocardial infarction
The nonredundant role of Pellino1 in immune receptor signaling is in part due to its different substrate specificity.
Peli1 is a microglia-specific mediator of autoimmune neuroinflammation that works by regulating Traf3 degradation
These results demonstrate that the ligands that signal via MyD88 do not always employ the same protein kinase to activate Pellino 1 and show that the activiation of NF-kappaB and mitogen-activated protein kinases.
Peli1 as a critical factor in the maintenance of peripheral T cell tolerance and demonstrate a previously unknown mechanism of c-Rel regulation.
Pellino-1 protein may have a cellular function distinct from previously identified functions.
IKKepsilon/TBK1 mediate the activation of Pellino 1's E3 ligase activity, as well as inducing the transcription of its gene and protein expression in response to TLR3 and TLR4 agonists.
miR-21 expression was upregulated during early stages of liver regeneration. Targeting of Peli1 by miR-21 could potentially provide the basis for a negative feedback cycle regulating NF-kappaB signaling.
Peli1 is a ubiquitin ligase needed for the transmission of TRIF-dependent TLR signals.
E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6. Mediates 'Lys-63'-linked polyubiquitination of IRAK1 allowing subsequent NF-kappa-B activation (By similarity).
E3 ubiquitin-protein ligase pellino homolog 1
, pellino homolog 1
, pellino-related intracellular-signaling molecule
, protein pellino homolog 1
, pellino 1
, pellino protein
, pellino E3 ubiquitin protein ligase 1 L homeolog
, pellino E3 ubiquitin protein ligase 1 S homeolog
, pellino homolog 1b