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In the second family, we identified a previously unreported homozygous missense change, c.154T > C (p.Cys52Arg) in the VLDLR gene
VLDLR expression was negatively regulated by miR (show MLXIP Proteins)-200c Colorectal cancer (CRC (show CALR Proteins)) cells and their expression levels were inversely correlated in CRC (show CALR Proteins) patients.
We screened for mutations in RELN (show RELN Proteins) or VLDLR and compared the phenotype of these patients with that of previously reported patients. differences in clinical severity, involvement of the cerebellar hemispheres, together with the severity of the neocortical defect, enables RELN (show RELN Proteins)-mutated patients to be distinguished from VLDLR-mutated patients.
Data suggest that, in the binding of fibrin beta N-domains and the (1-8) peptide fragment of VLDLR (very low density lipoprotein receptor), the second and third Lys (show LYZ Proteins)/Arg clusters in fibrin make major contributions to this interaction while the contribution of the first cluster is moderate.
The presence of reelin (show RELN Proteins) was elevated in junctional areas as in dysplastic nevi. VLDLR presented positive values in 16 cases (16/ 32) and ApoER2 (show LRP8 Proteins) was weak positive in 7 cases.
These results for the first time demonstrated that SalA protected against IS/RP-induced endothelial barrier dysfunction through suppression of VLDL receptor expression
these results suggest that VLDLR functions in vivo as an HCV receptor independent of canonical CD81 (show CD81 Proteins)-mediated HCV entry.
the results obtained indicate that minimal fibrin-binding structures are located within the second and third CR domains of the VLDL receptor and the presence of the fourth CR domain is required for high-affinity binding
The results of this study demonstrated the presence of reelin (show RELN Proteins), its receptors VLDLR and ApoER2 (show LRP8 Proteins) as well as Dab1 (show DAB1 Proteins) in the ENS and might indicate a novel role of the reelin (show RELN Proteins) system in regulating neuronal plasticity and pre-synaptic functions in the ENS.
these results suggested that the miR (show MLXIP Proteins)-135a-VLDLR-p38 (show CRK Proteins) axis may contribute to gallbladder cancer cell proliferation
C-terminal truncation of the reelin (show RELN Proteins) protein disrupts the interaction of reelin (show RELN Proteins) with VLDLR, resulting in abnormal development of the cerebral cortex and hippocampus.
Study showed that the two major VLDLR splice variants have differential activities in regulating Wnt (show WNT2 Proteins) signaling due to their different ectodomain shedding rates, which identified the functional difference of these splice variants.
The absence of PCSK9 (show PCSK9 Proteins) results in a sex- and tissue-specific subcellular distribution of the LDLR (show LDLR Proteins) and VLDLR, which is determined by estradiol levels.
In the retinas of Vldlr(-/-) mice with low fatty acid uptake but high circulating lipid levels, we found that Ffar1 suppresses expression of the glucose transporter Glut1 (show SLC2A1 Proteins)
neuronal stress differentially regulates lipoprotein receptor expression in neurons, with VLDLR upregulation as a common element as a modulator of neuronal Wnt (show WNT2 Proteins) signaling
Subretinal vascularization (SRV) in the Vldlr-/- model is associated with mistargeted neurites and that SRV is preceded by altered retinal vascular development.
VLDLR requires RasGRF1 (show RASGRF1 Proteins)/CaMKII (show CAMK2G Proteins) to alter dendritic spine formation.
This study demonstrated that VLDLR is expressed in distinct spatiotemporal patterns in developing mouse cerebral cortex.
LRP5 (show LRP5 Proteins) signaling is a prerequisite for neovascularization in VLDLR knockout mice. LRP5 (show LRP5 Proteins) may be an effective target for inhibiting intraretinal neovascularization.
these results identify a novel role for the VLDLR as a negative regulator of DC-mediated adaptive immune responses in HDM (show HDAC3 Proteins)-induced allergic airway inflammation.
The low density lipoprotein receptor (LDLR) gene family consists of cell surface proteins involved in receptor-mediated endocytosis of specific ligands. This gene encodes a lipoprotein receptor that is a member of the LDLR family and plays important roles in VLDL-triglyceride metabolism and the reelin signaling pathway. Mutations in this gene cause VLDLR-associated cerebellar hypoplasia. Alternative splicing generates multiple transcript variants encoding distinct isoforms for this gene.
, very low-density lipoprotein receptor
, VTG receptor
, very low density lipoprotein (VLDL)/vitellogenin receptor
, vitellogenin receptor