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Nectin-1 promotes chlamydial infection in the female genital tract but does not appear to contribute to rectal infection in male mice.
nectin-1 regulates the neuronal activities in the CA3 (show CA3 Proteins) region of the hippocampus.
Novel type of cell adhesion apparatus is mediated by Nectin-1 and Nectin-4 (show PVRL4 Proteins). It's implicated in prolactin receptor (show PRLR Proteins) signaling for mammary gland development.
These results indicate that the nectin-1 spots regulate the branching of mitral cell dendrites in the deep sub-lamina of the EPL and suggest that the nectin-1 spots are required for odor information processing in the olfactory bulb.
Results indicate that the nectin-1 spots constitute a novel adhesion apparatus that tethers mitral cell dendrites in a dendritic meshwork structure of the developing mouse olfactory bulb
results demonstrate a role for both nectin-1 and HVEM (show TNFRSF14 Proteins) as receptors and suggest a further receptor which appears much less efficient.
Pvrl1 is a bona fide target gene of the transcription factor p63 (show CKAP4 Proteins), whereas Pvrl4 (show PVRL4 Proteins) regulation is linked to epidermal differentiation and is under Irf6 (show IRF6 Proteins)
In summary, herpes simplex virus 1 entry into epidermis was shown to strongly depend on the presence of nectin-1, but the restricted presence of HVEM (show TNFRSF14 Proteins) can potentially replace nectin-1 as a receptor.
This study demonstrated that nectin1- and nectin3 (show PVRL3 Proteins)-mediated interactions between Cajal-Retzius cells cells and migrating neurons are critical for radial migration
PRR1 nectin-1 plays a role in the formation of intimal thickening after carotid artery ligation.
In a transgenic mouse line with high expression of nectin-1Ig, significant protection from the infection with 30 and 300 MLD50 was observed .
nectin-1 is expressed in human hair follicles and there is a p63 (show RPE65 Proteins)-responsive element in the NECTIN1 promoter
The viral entry receptor Nectin-1 is also internalized during HSV-1 infection in a Cbl (show CBL Proteins)-dependent mechanism, and that increases the opportunity of the virus to spread to uninfected cells.
HSV gD is able to disrupt intercellular homophilic trans-interaction of nectin-1 and induce a rapid redistribution of nectin-1 from cell junctions.
PVRL1 variants make a contribution to non syndromic Cleft Lip with/without Cleft palate in Turkish patients.
PDZD11 forms a complex with nectin-1 and nectin-3 (show PVRL3 Proteins), and its PDZ domain interacts directly with the PDZ-binding motif of nectin-1.
mutations in exons 2 and 5 of PVRL1, and T334A, A391T, G1183A in the alpha-spliced transcript, and G1082T in the beta-spliced transcript do not participate in the development of non-syndromic cleft of the lip and/or palate in patients from Guangdong.
data suggests that E-cadherin regulates assembly of nectin junctions through alpha-catenin-induced remodeling of the actin cytoskeleton around the cadherin clusters.
The results showed that the interface between the BV gD and nectin-1 molecule is not geometrically complementary.
These data provided solid structural and functional evidence that herpes simplex virus 1 and herpes simplex virus 2 gD proteins recognize nectin-1 via the same binding mode.
Contribution of the second and third Ig-like domains of nectin-1 was analysed by generating transgenic mice expressing the entire ectodomain of nectin-1 fused to the porcine Fc portion.
Results demonstrate that a soluble form of the first domain of porcine nectin-1 is able to exert a significant antiviral effect against pseudorabies virus infection.
This gene encodes an adhesion protein that plays a role in the organization of adherens junctions and tight junctions in epithelial and endothelial cells. The protein is a calcium(2+)-independent cell-cell adhesion molecule that belongs to the immunoglobulin superfamily and has 3 extracellular immunoglobulin-like loops, a single transmembrane domain (in some isoforms), and a cytoplasmic region. This protein acts as a receptor for glycoprotein D (gD) of herpes simplex viruses 1 and 2 (HSV-1, HSV-2), and pseudorabies virus (PRV) and mediates viral entry into epithelial and neuronal cells. Mutations in this gene cause cleft lip and palate/ectodermal dysplasia 1 syndrome (CLPED1) as well as non-syndromic cleft lip with or without cleft palate (CL/P). Alternative splicing results in multiple transcript variants encoding proteins with distinct C-termini.
poliovirus receptor-related 1 (herpesvirus entry mediator C; nectin)
, herpesvirus entry mediator C
, poliovirus receptor related protein
, poliovirus receptor-related protein 1
, nectin 2
, poliovirus receptor-related 1 (herpesvirus entry mediator C)
, Poliovirus receptor-related protein 1
, poliovirus receptor-related 1
, herpes virus entry mediator C
, nectin-1 alpha
, nectin-1 delta
, poliovirus receptor-related 1 (herpesvirus entry mediator C
, ectodermal dysplasia 4 (Margarita Island type)
, herpesvirus Ig-like receptor
, nectin 1
, poliovirus receptor-like 1