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Oxysterol binding protein is an intracellular protein that is believed to transport sterols from lysosomes to the nucleus where the sterol down-regulates the genes for the LDL receptor, HMG-CoA reductase, and HMG synthetase [provided by RefSeq, Jul 2008].. Zusätzlich bieten wir Ihnen Oxysterol Binding Protein Antikörper (67) und Oxysterol Binding Protein Kits (4) und viele weitere Produktgruppen zu diesem Protein an.
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Study identified an OSBP- and FAN (zeige NSMAF Proteine)-mediated sterol requirement in Drosophila spermatogenesis
the component proteins of the machinery, OSBP, VAP (zeige F10 Proteine), SAC1 (zeige SACM1L Proteine), and PITPNB (zeige PITPNB Proteine), are all essential host factors for AiV (zeige ANXA4 Proteine) replication. Importantly, the machinery is directly recruited to the RNA replication sites through previously unknown interactions of VAP (zeige F10 Proteine)/OSBP/SAC1 (zeige SACM1L Proteine) with the AiV (zeige ANXA4 Proteine) proteins and with ACBD3 (zeige Acbd3 Proteine).
results demonstrate that Sac1 (zeige SACM1L Proteine) expression in either the ER or Golgi apparatus has a minimal impact on the PI-4P that regulates OSBP activity or recruitment to contact sites
Cholesterol transfer, PI4P consumption, and control of membrane lipid order by endogenous OSBP have been described.
Data suggest that OSBP shifts the distribution of phosphatidylinositol 4-phosphate upon localization to endoplasmic reticulum-Golgi contact sites.
Our results identify OspB as a regulator of mTORC1 and mTORC1-dependent cell proliferation early during S. flexneri infection and establish a role for IQGAP1 (zeige IQGAP1 Proteine) in mTORC1 signaling
These results suggest that poliovirus proteins modulate PI4KB (zeige PI4KB Proteine) activity and provide PI4P for recruitment of OSBP to accumulate unesterified cholesterol on virus-induced membrane structure for formation of a virus replication complex.
OSBP-mediated back transfer of phosphatidylinositol 4-phosphate might coordinate the transfer of other lipid species at the endoplasmic reticulum-Golgi interface.
OSBP is required for efficient replication of intracellular S. Typhimurium.
Data indicate that phosphorylation on two serine-rich motifs, S381-S391 (site 1) and S192, S195, S200 (site 2), specifically controls oxysterol-binding protein (OSBP) activity at the endoplasmic reticulum (ER).
PKD (zeige PRKD1 Proteine) negatively regulates HCV secretion/release by attenuating OSBP and CERT (zeige COL4A3BP Proteine) functions by phosphorylation inhibition. This study identifies the key role of the Golgi components in the HCV maturation process.
OSBP may be a target and downstream effector of miR (zeige MLXIP Proteine)-124 for regulating neurite outgrowth and elongation.
Partitioning of Osbp between the endoplasmic reticulum and the Golgi apparatus is regulated by Vapa (zeige VAPA Proteine).
OSBP opposes the activity of LXR (zeige NR1H3 Proteine) by negatively regulating ABCA1 (zeige ABCA1 Proteine) activity in the cytoplasm by sterol-binding domain-dependent protein destabilization
Oxysterol-binding protein is required for the perinuclear localization of intra-Golgi v-SNAREs.
Oxysterol binding protein is an intracellular protein that is believed to transport sterols from lysosomes to the nucleus where the sterol down-regulates the genes for the LDL receptor, HMG-CoA reductase, and HMG synthetase
, oxysterol binding protein
, oxysterol-binding protein
, oxysterol-binding protein 1