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Inhibition of PLSCR1 decreased the antiviral activity of IFN against HBV.
Data suggest that PLSCR1 is involved in viral entry; here, herpes simplex viruses activate PLSCR1 and up-regulate flipping of phosphatidylserines and AKT to outside of plasma membrane shortly following HSV-1 or HSV-2 exposure. (PLSCR1 = phospholipid scramblase 1; AKT = proto-oncogene c-Akt)
wogonoside promotes the expression of PLSCR1 and enhances its nuclear translocation and binding to the 1, 4, 5-trisphosphate receptor 1 (IP3R1) promoter in AML patient-derived primary cells. Wogonoside activates IP3R1, in turn, promotes release of Ca(2+) from endoplasmic reticulum, and eventually leads to cell differentiation.
Data indicate heterogeneous expression of phospholipid scramblase 1 (PLSCR1) and suggest its possible implication in the response to anticancer therapies, especially to drugs promoting protective autophagy.
investigate how the polar aspartate residue is accommodated in lipid bilayers containing POPC with and without cholesterol, using all-atom molecular dynamics simulations
Human phospholipid scramblase 1 has five histidine residues and point mutations of histidine residues to alanine in hPLSCR1 resulted in 60 % loss in nuclease activity.
The mechanisms of pH-induced functional activation of hPLSCR1 are described.
directed mutagenesis revealed the importance of c-Myc binding sites from -751 to -756 and -548 to -553 on the promoter of hPLSCR1in transcriptionally regulating the expression of hPLSCR1.
PLSCR1 positively regulates hepatic carcinoma cell proliferation and migration through interacting with midkine
Suggest role for PLSCR1 in negatively regulating trophoblast fusion rather than directly promoting fusion.
PLSCR1 mediates the antiviral activity and anticarcinogenesis against hepatitis B virus by regulating HBx stability.
affinity of SCR for cholesterol-rich domains in membranes
This is the first biochemical evidence to prove the above hypothesis that hPLSCR1 is activated in heavy metal poisoning, which leads to bidirectional transbilayer movement of phospholipids.
The C-terminal transmembrane domain of human phospholipid scramblase 1 is essential for the protein flip-flop activity and Ca(2)-binding.
This is the first report showing the transcriptional regulation of hPLSCR1 expression by Snail TF and its possible implications in cancer progression.
PLSCR1 interacted with ANG in the cell nucleus and regulated rRNA transcription.
hPLSCR1 and PRD-hPLSCR2 showed Ca(2+)-dependent aggregation and scrambling activity
The data are in agreement with the possibility that PLSCR1 is an integral membrane protein.
Phospholipid Scramblase 1, an interferon-regulated gene located at 3q23, is regulated by SnoN/SkiL in ovarian cancer cells.
The C-terminal helix of human PLSCR1 is required for membrane insertion and calcium binding.
PLSCR1 aggravates anaphylactic reactions by increasing Fc epsion RI-dependent mast cell degranulation.
Genetic knockdown of PLSCR1 activity reduces intracellular calcium dysregulation, prevents phosphatidylserine externalization, and enables months-long protection of vector-transduced, transgene-expressing cells from microglial phagocytosis.
Phospholipid scramblase 1 regulates phosphatidylserine exposure in response to oxygen stress, leading to beta2-glycoprotein I and IgM binding and lipid-mediated, inflammatory responses.
Lipopolysaccharide treatment resulted in increased expression of phospholipid scramblase 1(PLSCR-1) and decrease in phospholipid scramblase 4(Plscr4 )messenger RNA demonstrating modulation of PLSCR-1 and PLSCR-4 in lipopolysaccharide-induced preterm birth
Study demonstrates that PLSCR1 is a TLR9-interacting protein that plays an important role in pDC's type 1 IFN responses by regulating TLR9 trafficking to the endosomal compartment.
the capacity of PLSCR1 to augment G-CSF-dependent production of mature neutrophils from myeloid progenitors is unrelated to its reported activities at the endofacial surface of the plasma membrane but does require entry of the protein into the nucleus
deficiency results in normal hemostasis but defective hematopoieetic response to growth factors
mediates phosphatidylserine exposure in sicke cell disease and beta thalassemia
PLSCR1 appears to influence progression of UV-induced apoptosis and could be a point of regulation or intervention during programmed cell death
PLSCR1, which is itself an IFN-stimulated gene-encoded protein, provides a mechanism for amplifying and enhancing the IFN response through increased expression of a select subset of potent antiviral genes
PLSCR1 binds to the promoter region of the IP3R1 gene to enhance its expression
These findings demonstrate a functional interdependence between onzin and PLSCR1.
These data provide evidence that PLSCR1 is a positive intracellular acute phase protein with a tissue-specific mechanism for up-regulation.
may act as a downstream mediator of immune response in IgE receptor signaling\; may transport phospholipids in the plasma membrane
phospholipid scramblase 1
, PL scramblase 1
, ca(2+)-dependent phospholipid scramblase 1
, phospholipid scramblase 2
, erythrocyte phospholipid scramblase
, transplantability-associated protein 1
, PL scramblase 2
, ca(2+)-dependent phospholipid scramblase 2