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Our results demonstrate that SR-BI functions as an oncogene (show RAB1A Proteins) and promotes progression of clear cell renal cell carcinoma (show MOK Proteins) (ccRCC). SR-BI may serve as a potential prognostic biomarker and therapeutic target for ccRCC.
SCARB1 gene polymorphisms may serve as a potential predictor of treatment responses in chronic hepatitis C patients receiving interferon (show IFNA Proteins)-based therapy
The S112F single amino acid mutation in SR-BI inhibited the infectivity of hepatitis C virus derived from cell culture in a cell culture model by downregulating the expression of the SR-BI protein.
The cell surface receptor SR-BI (scavenger receptor class B member 1), is essential for hepatitis C virus (HCV) entry into hepatocytes. Variations in the gene coding this receptor influence infectivity and viral load. We analyzed these variations to gain a better understanding of inter-individual differences over the course of HCV infection.
The SCARB1AA genotype decreased cardiovascular risk and carrying GA genotype and G allele increased the risk of CAD. AA genotype carriers had higher levels of big-sized HDL (show HSD11B1 Proteins) subfraction.
These findings provide new insights into the role of SR-B1 in cellular cholesterol homeostasis and suggest molecular links between SR-B1-dependent lipid sensing and cell cholesterol and lipid droplet dynamics
Liposomes modified with both apolipoproteins A-I and E were internalized in HepG2 cells in FBS (show FBXO8 Proteins)-depleted culture medium at the same levels as unmodified liposomes in FBS (show FBXO8 Proteins)-containing culture medium, which indicates that apolipoproteins A-I and E were the major serum components involved in liposomal binding to SR-B1 or LDLR (show LDLR Proteins) (or both).
Here we show that inhibition of SR-B1 reduced cell survival, migration and invasion, and cholesterol content in NB cell lines. Additionally analysis of SR-B1 levels in NB patient biopsies using the R2: Genomics Analysis and Visualization Platform showed that high SR-B1 expression correlated with decreased overall and event-free survival.
the cigarette smoke (CS)-induced loss of SRB1 induced an alteration of sebocytes lipid content, also demonstrated by cholesterol quantification in SRB1 siRNA experiments. In conclusion, exposure to CS, induced SRB1 post-translational modifications in sebocytes and this might affect sebocytes/skin functionality
SR-BI-triggered autophagy promoted co-elimination of apoptotic immune cells and dead bacteria but barely influenced bacterial sequestration and survival or inflammasome activation, thus exclusively counteracting damage inflicted by immune responses.
Overexpression of miR-24 inhibited SR-B1 expression by directly targeting SR-B1 3' UTR and repressed high density lipoprotein uptake and steroidogenesis in steroidogenic cells.
These data suggest that a moderate amount of alcohol plays a novel role in reverse cholesterol transport, mainly mediated by PPARgamma (show PPARG Proteins) and SR-B1.
To investigate the pharmacokinetics (PKs) and pharmacodynamics (PDs (show SLC26A4 Proteins)) for ION-353382, an antisense oligonucleotide (ASO) targeting scavenger receptor class B type I (SRB1) mRNA, using alpha-2-macroglobulin (A2M (show A2M Proteins)), murinoglobulin double-knockout (DKO), and wild-type mice
Rutaecarpine was identified to be a candidate that protected ApoE (show APOE Proteins)(-/-) mice from developing atherosclerosis through preferentially promoting activities of ABCA1 (show ABCA1 Proteins) and SR-BI within RCT (show FOXE3 Proteins).
SR-B1 is a silica receptor associated with canonical inflammasome activation.
Our results suggest that LPA-enhanced foam cell formation is mediated by LPA1 (show LPAR1 Proteins)/3 -AKT (show AKT1 Proteins) activation and subsequent SRBI expression.
Results show the first high-resolution structure of the C-terminal transmembrane domain of SR-BI. This region of SR-BI harbors a leucine zipper dimerization motif, which when mutated impairs the ability of the receptor to bind HDL (show HSD11B1 Proteins) and mediate cholesterol delivery.
Carboxy-terminal deletion of SR-BI reduced receptor levels in liver and steroidogenic tissues (adrenal cortex, ovary, testicular Leydig cells) and induced hypercholesterolemia.
Luteinization causes upregulation of SR-BI expression, its posttranslational maturation by glycosylation, and insertion into luteal cell membranes.
Aortic endothelial cells transcytose high-density lipoproteins by mechanisms that involve either SR-BI or ABCG1 (show ABCG1 Proteins) but not ABCA1 (show ABCA1 Proteins).
The protein encoded by this gene is a plasma membrane receptor for high density lipoprotein cholesterol (HDL). The encoded protein mediates cholesterol transfer to and from HDL. In addition, this protein is a receptor for hepatitis C virus glycoprotein E2. Two transcript variants encoding different isoforms have been found for this gene.
scavenger receptor class B member 1
, scavenger receptor class B, member 1
, scavenger receptor class B type I
, high density lipoprotein receptor SR-BI
, CD36 and LIMPII analogous 1
, CD36 antigen (collagen type I receptor, thrombospondin receptor)-like 1
, scavenger receptor class B type III
, HDL QTL 1
, scavenger receptor class B1
, CD36 antigen (collagen type I receptor thrombospondin receptor)-like 1 (scavanger receptor class B type 1)
, scavanger receptor class B type 1
, CD36 antigen (collagen type I receptor, thrombospondin receptor-like 1)