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Findings indicate that protein inhibitor of activated STAT 4 (PIAS4) mediated SIRT1 (zeige SIRT1 Proteine) repression in response to nutrient surplus contributes to the pathogenesis of Nonalcoholic Steatohepatitis (NASH (zeige SAMSN1 Proteine)).
new protein isoform encoded by KIAA0317, termed fibrosis-inducing E3 ligase 1 (FIEL1), which potently stimulates the TGFbeta (zeige TGFB1 Proteine) signaling pathway through the site-specific ubiquitination of PIAS4.
PKA-induced SREBP1c (zeige SREBF1 Proteine) sumoylation by PIASy.
the SUMO E3 ligase (zeige PIAS1 Proteine) PIASy (also known as PIAS4) was induced by hypoxia and prevented Sp1 (zeige SP1 Proteine) from binding to the SIRT1 (zeige SIRT1 Proteine) promoter.
Piasy represses the synergistic activation of PITX2 (zeige PITX2 Proteine) with interacting co-factors and Piasy represses Pias1 (zeige PIAS1 Proteine) activation of PITX2 (zeige PITX2 Proteine) transcriptional activity.
Protein inhibitor of activated STAT (zeige STAT1 Proteine), PIASy regulates alpha-smooth muscle actin (zeige ACTG2 Proteine) expression by interacting with E12 (zeige ELSPBP1 Proteine) in mesangial cells.
PIASy negatively regulates both IFN transcription and IFN-stimulated gene expression through multiple mechanisms utilizing the function of different domains.
Studies define an important role of PIASy in hypoxia signaling through promoting HIF1alpha (zeige HIF1A Proteine) SUMOylation.
PIASgamma as a transcriptional co-regulator of Nurr1 (zeige NR4A2 Proteine) and suggest that this interaction may have a physiological role in regulating the expression of Nurr1 (zeige NR4A2 Proteine) target genes.
Piasy(-/-) mice appear phenotypically normal, activation of STAT1 (zeige STAT1 Proteine) is not significantly perturbed, and sumoylation patterns for SUMO-1 (zeige SUMO1 Proteine) or SUMO-3 (zeige SUMO3 Proteine) modification are similar in wild-type and knockout mice
post-translational modification of Nkx3.2 (zeige NKX3-2 Proteine) employing HDAC9 (zeige HDAC9 Proteine)-PIASy-RNF4 (zeige RNF4 Proteine) axis plays a crucial role in controlling chondrocyte viability and hypertrophic maturation during skeletal development in vertebrates.
these findings provide evidence for the effects of PIAsxalpha (zeige PIAS2 Proteine) and its mechanism on osteosarcoma progression, which offers novel insight into sumoylation and the cell cycle in osteosarcoma.
PIAS4 was identified as a candidate gene for abnormal head size in 13 patients with proximal 19p13.3 submicroscopic rearrangements .
Our data reveal a novel and dynamic role for PIAS4 in the cellular-mediated restriction of herpesviruses and establish a new functional role for the PIAS family of SUMO ligases in the intrinsic antiviral immune response to DNA virus infection.
PIAS4 activity are required for the AMPKalpha1 (zeige PRKAA1 Proteine) SUMOylation and the inhibition of AMPKalpha1 (zeige PRKAA1 Proteine) activity towards mTORC1 signalling.
PIAS4 (rs735842) and VEGFA (zeige VEGFA Proteine) (rs699947) were the most statistically significant variants associated in hypoxia pathway analysis.
PIASgamma-dependent modification of tomosyn-1 (zeige STXBP5 Proteine) with SUMO-2 (zeige SUMO2 Proteine)/3 presents a novel mechanism to adapt secretory strength to the dynamic synaptic environment.
SUMOylation of RXRalpha (zeige RXRA Proteine) is significantly enhanced through PIAS4-mediated activity.
High reactive oxygen speciesinduces oxidation and ubiquitin-mediated degradation of PIASgamma, thereby disrupting PIASgamma-IKKgamma (zeige IKBKG Proteine) cross talk.
Data suggest that PIASy exhibits a SIM (zeige SIM2 Proteine) (SUMO-interacting motif) in addition to the SIM (zeige SIM2 Proteine) identified in homologous proteins in other species; both SIMs are located near C terminus of PIASy, and both are required for full ligase activity of PIASy; hydrophobic core residues of the new SIM (zeige SIM2 Proteine) are essential in binding to SUMO-3 (zeige SUMO3 Proteine). (PIASy = protein inhibitors of activated STAT (zeige STAT1 Proteine) y; SUMO-3 (zeige SUMO3 Proteine) = small ubiquitin-like modifier 3 (zeige SUMO3 Proteine))
The Xenopus PIAS (zeige PIAS1 Proteine) genes are expressed throughout early development and have overlapping and distinct expression patterns, with, for example, strong expression of PIAS4 in the neural and neural crest derivatives.
XPIASy functions as an essential negative regulator of the XSmad2 (zeige SMAD2 Proteine) pathway to ensure proper mesoderm induction at the appropriate time and in the appropriate region.
Data show that the Rod/Zw10 (zeige ZW10 Proteine) complex interacts with the first 47 residues of PIASy which are important for mitotic SUMOylation, and that depletion of Rod compromises the centromeric localization of PIASy and SUMO2 (zeige SUMO2 Proteine)/3 in mitosis.
a PIAS4 homologue (zfPIAS4a) from the zebrafish model that shares many conserved structural hallmarks with the human and mammal PIAS4 proteins was successfully identified
Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway, the Wnt pathway and the steroid hormone signaling pathway. Involved in gene silencing. Promotes PARK7 sumoylation. In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations.
protein inhibitor of activated STAT, 4
, protein inhibitor of activated STAT protein 4
, E3 SUMO-protein ligase PIAS4-like
, e3 SUMO-protein ligase PIAS4-like
, E3 SUMO-protein ligase PIAS4
, protein inhibitor of activated STAT PIASy
, protein inhibitor of activated STAT protein gamma
, protein inhibitor of activated STAT protein PIASy
, zinc finger, MIZ-type containing 6
, protein inhibitor of activated STAT 4