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Steady-state kinetic analysis revealed that PKN1 (zeige PKN1 Proteine)-3 follows a sequential ordered Bi-Bi (zeige CACNA1A Proteine) kinetic mechanism, where peptide substrate binding is preceded by ATP binding. This kinetic mechanism was confirmed by additional kinetic studies for product inhibition and affinity of small molecule inhibitors.
PKN2 knockdown in vitro decreased insulin-stimulated glucose uptake, incorporation into glyco (zeige PRKAA1 Proteine)gen, and oxidation. Thus, PKN2 alters key signaling pathways and transcriptional networks to regulate glucose and lipid metabolism.
Helicobacter pylori CagA (zeige S100A8 Proteine) interacts with PRK2 and inhibits its kinase activity.
TXA2 (zeige TBXA2R Proteine)-mediated neoplastic responses in prostate adenocarcinoma PC-3 (zeige PCSK1 Proteine) cells occur through a PRK1 (zeige PKN1 Proteine)/PRK2-dependent mechanism.
findings demonstrate that Yersinia enterocolitica rYopM interacts with RSK1 (zeige RPS6KA1 Proteine) and PRK2 following cell-penetration
Regulation of protein kinase C-related (zeige PKN1 Proteine) protein kinase 2 (PRK2) by an intermolecular PRK2-PRK2 interaction mediated by Its N-terminal domain.
these findings suggest that Hsp90 (zeige HSP90 Proteine) plays a critical role in the regulation of HCV RNA polymerase phosphorylation via the PDK1 (zeige PDK1 Proteine)-PRK2 signaling pathway.
PKN (zeige PKN1 Proteine) isoforms are not simply redundant in supporting migration, but appear to be linked through isoform specific regulatory domain properties to selective upstream signals. It
Rho binding is essential for PRK2 function and facilitates PRK2 recruitment to junctions. Kinase-dead PRK2 acts as a dominant-negative mutant and prevents apical junction formation.
Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases.
In mature skeletal muscle, in vivo PKN2 knockdown decreased glucose uptake and increased AMPK (zeige PRKAA1 Proteine) phosphorylation. Thus, PKN2 alters key signaling pathways and transcriptional networks to regulate glucose and lipid metabolism.
Mechanistically, Yersinia pseudotuberculosis YopM recruits and activates the mouse host kinases PRK1 (zeige PKN1 Proteine) and PRK2 to negatively regulate pyrin (zeige MEFV Proteine) by phosphorylation.
PKN2 formed complexes with Cdo (zeige CDO1 Proteine), APPL1 (zeige APPL1 Proteine) and AKT (zeige AKT1 Proteine) via its C-terminal region and this interaction appeared to be important for induction of AKT (zeige AKT1 Proteine) activity as well as myoblast differentiation.
To unravel the in vivo physiological function of PKN2, we targeted the PKN2 gene. Constitutive disruption of the mouse PKN2 gene resulted in growth retardation and lethality before embryonic day (E) 10.5. PKN2(-/-) embryo did not undergo axial turning and showed insufficient closure of the neural tube.Mouse embryonic fibroblasts (MEFs) derived from PKN2(-/-) embryos at E9.5 failed to grow.
Yersinia pseudotuberculosis mutants expressing YopM proteins unable to interact with either RSK1 (zeige RPS6KA1 Proteine) or PRK2 were defective for virulence in this assay, indicating that both interaction domains are important for YopM to promote pathogenesis.
phospholipid-regulated protein kinase, phosphorylates ribosomal protein S6\; may play a role in hepatic regulation
, cardiolipin-activated protein kinase Pak2
, protein kinase C-like 2
, protein-kinase C-related kinase 2
, serine/threonine-protein kinase N2
, serine/threonine kinase 7
, p140 kinase
, protease-activated kinase 2
, protein kinase N2
, protein kinase C-related kinase 2
, serine/threonine-protein kinase N2-like