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PI4KIIIbeta interaction with the VHS domain of GGA2 (Montrer GGA2 Protéines) affected PI4KIIIbeta localization.
several disordered regions of PI4KB become protected from proteolytical degradation upon 14-3-3 (Montrer YWHAQ Protéines) binding.
esults show that Aichi virus 3A protein activates the lipid kinase activity of PI4KIIIb,which activation is sensitized by the protein ACBD3 (Montrer Acbd3 Protéines). The interfaces between PI4KIIIbeta-ACBD3 (Montrer Acbd3 Protéines) and ACBD3 (Montrer Acbd3 Protéines)-3A were mapped with hydrogen-deuterium exchange mass spectrometry.
The results showed that, in contrast to the enteroviruses and the cardioviruses, foot-and-mouth disease virus replication does not require PI4KIII (PI4KIIIalpha and PI4KIIIbeta), and phosphatidylinositol 4-phosphate levels do not increase in foot-and-mouth disease virus-infected cells and phosphatidylinositol 4-phosphate is not seen at replication organelles.
Data show that ACBD3 (Montrer Acbd3 Protéines) can recruit PI4KB to model membranes as well as redirect PI4KB to cellular membranes where it is not naturally found. Also, results show that ACBD3 (Montrer Acbd3 Protéines) regulates the enzymatic activity of PI4KB kinase through membrane recruitment rather than allostery.
Analysis reveals novel aspects of the PI4KIIIb-Rab11 complex and determines binding and catalytic sites of the kinase.
PI4KIIIbeta likely plays a role in breast oncogenesis and that cooperation between Rab11a (Montrer RAB11A Protéines) and PI4KIIIbeta represents a novel Akt (Montrer AKT1 Protéines) activation pathway.
Although human rhinovirus 3A protein was previously shown to interact with ACBD3 (Montrer Acbd3 Protéines), these data suggest that PI4KIIIbeta recruitment occurred independently of both GBF1 and ACBD3 (Montrer Acbd3 Protéines).
Authors found that NS5A and PI4KB competed for association of acyl-coenzyme A (Montrer SOAT2 Protéines) binding domain containing protein 3 (Montrer HSPB3 Protéines) (ACBD3 (Montrer Acbd3 Protéines)), which inhibited hepatitis C virus replication.
These results suggest that poliovirus proteins modulate PI4KB activity and provide PI4P for recruitment of OSBP (Montrer OSBP Protéines) to accumulate unesterified cholesterol on virus-induced membrane structure for formation of a virus replication complex.
findings reveal a novel signalling pathway involved in development of the semicircular canal system, and suggest a previously unrecognized role for NCS-1 (Montrer NCS1 Protéines) in mitochondrial function via its association with several mitochondrial proteins.
Depolarization increases phosphatidylinositol (PI) 4,5-bisphosphate level and KCNQ currents through PI 4-kinase mechanisms
Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol- 1,4,5,-trisphosphate (PIP) (By similarity).
phosphatidylinositol 4-kinase, catalytic, beta polypeptide
, phosphatidylinositol 4-kinase, catalytic, beta
, phosphatidylinositol 4-kinase beta
, PtdIns 4-kinase beta
, phosphatidylinositol 4-kinase beta-like
, phosphatidylinositol 4-kinase, wortmannin-sensitive
, type III phosphatidylinositol 4-kinase beta
, catalytic phosphatidylinositol 4-kinase beta
, ptdIns 4-kinase beta
, phosphatidylinositol 4-kinase III beta