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Sin1, Rictor, Trc and target of rapamycin (TOR), components of the TOR complex 2 (TORC2), are required for dendritic tiling of class IV da neurons
SIN1 interacted and co-located with PKC zeta by pleckstrin homology (PH) domain. Downregulation of SIN1 severely impaired PKC zeta translocation and phosphorylation induced by insulin.
SIN1 plays an important role in breast cancer.
In colorectal cancer tissues, the Sin1 protein but not mRNA was significantly upregulated while Pdcd4 protein was downregulated, suggesting that loss of Pdcd4 might correlate with Sin1 protein level but not mRNA level in colorectal cancer.
SIN1 plays an important role in non-small cell lung cancer; SIN1 is a potential biomarker and a promising target in the treatment of NSCLC
This study provides evidence that Sin1, a known element of the mammalian target of rapamycin complex 2 (mTORC2), is required for Interferon-gamma-induced phosphorylation and activation of AKT and that such activation mediates downstream regulation of mTORC1 and its effectors.
Intracellular localization of mTORC2 component, mSin1, contributes to regulation of Akt phosphorylation.
Akt phosphorylates SIN1 at T86, enhancing mTORC2 kinase activity, which leads to phosphorylation of Akt S473 by mTORC2, thereby catalyzing full activation of Akt.
MAPKAP1 may represent a novel anti-infection and anti-fibrogenesis genomic locus in chronic schistosomiasis japonica.
mitogen-activated protein kinase associated protein 1 rs10118570 may be an important protective factor for developing better management strategies in lung squamous cell carcinoma.
DNA-PKcs-mTORC2(SIN1) association is required for UVB-induced Akt Ser-473 phosphorylation and cell survival.
Estradiol and mTORC2 cooperate to enhance prostaglandin biosynthesis and tumorigenesis in TSC2-deficient lymphangioleiomyomatosis cells.
results reveal a Sin1-phosphorylation-dependent mTORC2 regulation, providing a potential molecular mechanism by which mutations in the mTORC1-S6K-Sin1 signalling axis might cause aberrant hyper-activation of the mTORC2-Akt pathway
NBS1 interacts with the mTOR/Rictor/SIN1 complex through the a.a. 221-402 domain and contributes to the activation of Akt activity.
SIN1 plays an important role in hepatocellular carcinoma invasion and metastasis by facilitating epithelial-mesenchymal transition.
structures show that the C-termini of Avo1 and Sin1 both have the pleckstrin homology (PH) domain fold
mSIN1 protein mediates SGK1 protein interaction with mTORC2 protein complex and is required for selective activation of the epithelial sodium channel
There is an increased mitochondrial dependence upon mTORC2 dependent cell growth due to PTEN loss
Results demonstrate that Sin1 transcripts can use alternative polyadenylation signals and describe a number of Sin1 splice variants that potentially encode functionally different isoforms.
The human Sin1 proteins form a complex with Jun N-terminal kinase.
A novel MEKK2-interacting protein, Mip1, that regulates MEKK2 dimerization and activation by forming a complex with inactive and nonphosphorylated MEKK2, was identified.
This gene encodes a protein that is highly similar to the yeast SIN1 protein, a stress-activated protein kinase. Alternatively spliced transcript variants encoding distinct isoforms have been described. Alternate polyadenylation sites as well as alternate 3' UTRs have been identified for transcripts of this gene.
, Stress-activated protein kinase [SAPK]-interacting protein
, stress-activated map kinase-interacting protein 1
, mitogen-activated protein kinase associated protein 1
, Target of rapamycin complex 2 subunit MAPKAP1
, target of rapamycin complex 2 subunit MAPKAP1-like
, MEKK2-interacting protein 1
, SAPK-interacting protein 1
, TORC2 subunit MAPKAP1
, mitogen-activated protein kinase 2-associated protein 1
, ras inhibitor MGC2745
, stress-activated map kinase interacting protein 1
, stress-activated protein kinase-interacting 1
, target of rapamycin complex 2 subunit MAPKAP1
, mitogen activated protein kinase associated protein 1
, SAPK interacting protein