Synonyms for nectin or Related words with nectin

plexin              neuropilin              alcam              prominin              glypican              podoplanin              ceacam              fzd              rhamm              tetraspanin              desmocollin              desmoglein              nucleolin              endosialin              syndecan              neuropilins              gpnmb              emilin              upar              tgfrii              lamr              siglec              sialomucin              tetraspan              plzf              mortalin              decysin              magea              cxadr              claudin              zyxin              mesothelin              caix              ephrin              tnfrsf              anxa              lilrb              tnfreceptor              contactin              attractin              ectodomains              hveb              podxl              cubilin              neurofascin              msln              rptp              filamin              plakophilin              caveolin             

Examples of "nectin"
So far four nectins have been identified in humans, namely nectin-1, nectin-2, nectin-3 and nectin-4. These four family members have also been found in most other well studied mammals. Also, five Necls have been identified, these are: Necl-1, Necl-2, Necl-3, Necl-4 and Necl-5.
Nectin-1 and nectin-3 have been shown to be involved in cellular adhesion in some neuronal synapses. Unlike many other cellular adhesion molecules they do not distribute evenly on axonal and dendritic side of the synapse. Instead, Nectin-1 is primarily found on the axonal side and nectin-3 primarily on the dendritic side. Nectin-1 serves as the entry receptor for Herpes Simplex Viruses 1 and 2, binding to the viral envelope glycoprotein gD, and for Pseudorabies Virus.
nectin-3 : PVRL3 (Poliovirus receptor-related 3), CD113 (Cluster of Differentiation 113)
Nectins and Nectin-like molecules (Necl) are families of cellular adhesion molecules involved in Ca-independent cellular adhesion.
nectin-2 : PVRL2 (Poliovirus receptor-related 2), HveB (herpesvirus entry mediator B), CD112 (Cluster of Differentiation 112)
nectin-1 : PVRL1 (Poliovirus receptor-related 1), HveC (herpesvirus entry mediator C), CD111 (Cluster of Differentiation 111)
Poliovirus receptor-related 3 (PVRL3), also known as nectin-3 and CD113, is a human protein of the immunoglobulin superfamily which forms part of adherens junctions.
Poliovirus receptor-related 2 (PVRL2), also known as nectin-2 and CD112 (formerly herpesvirus entry mediator B, HVEB), is a human plasma membrane glycoprotein.
In 2016, researchers found that PLEKHA7 recruits the small PDZ protein PDZD11 to adherens junctions, thus resulting in the stabilisation of nectins at adherens junctions. Knock-out of PLEKHA7 results in the loss of PDZD11 from epithelial adherens junctions, and this is rescued by the introduction of exogenous PLEKHA7. The N-terminal 44 residues of PDZD11 interact with the first WW domain of PLEKHA7. In the absence of either PLEKHA7 or PDZD11, the amount of nectin-3 and nectin-4 detected at junctions is decreased, as well as total nectin levels, through proteasome-mediated degradation. PDZD11 interacts directly with the cytoplasmic PDZ-binding motif of nectins, through its own PDZ domain. Proximity ligation assay shows that PLEKHA7 is associated to nectins in a PDZD11-dependent manner. Nectins are the second major class of transmembrane adhesion molecules at adherens junctions, besides cadherins. Therefore, PLEKHA7lstabilises both cadherins and nectins at AJ.
In addition to catenins and cadherins, PTPmu dephosphorylates PIPKIγ90 and nectin-3 (PVRL3) to stabilize E-cadherin-based adherens junctions. PTPmu also dephosphorylates another cell junction protein, connexin 43. The interaction between connexin 43 and PTPmu increases gap junction communication.
Enfortumab vedotin (ASG-22ME) is an antibody-drug conjugate designed for the treatment of cancer expressing Nectin-4. Enfortumab refers to the monoclonal antibody part, and vedotin refers to the payload drug (MMAE) and the linker.
Recently, it has been found that nectin-4 can be found in the serum of patients suffering from lung cancer. This has led to speculations that this protein might be involved in some developing cancers and might even have a pharmaceutical potential.
Nectins (e.g., PVRL1; MIM 600644) are immunoglobulin-like adhesion molecules that interact with afadin (AF6; MIM 159559). Afadin is an actin filament-binding protein that connects nectins to the actin cytoskeleton. The nectin-afadin system organizes adherens junctions cooperatively with the cadherin (see MIM 192090)-catenin (see MIM 116805) system in epithelial cells.[supplied by OMIM]
The measles virus has two envelope glycoproteins on the viral surface—hemagglutinin (H) and membrane fusion protein (F). These proteins are responsible for host cell binding and invasion. Three receptors for the H protein have been identified to date: complement regulatory molecule CD46, the signaling lymphocyte activation molecule (SLAM) and the cell adhesion molecule Nectin-4.
Campadelli-Fiume's discovery of nectin as the receptor for Herpes Simplex Virus (HSV), is one of her greatest accomplishments. Through her research, she also discovered the triggering activity of receptor- bound gD. In addition to these major discoveries, she uncovered the identity of the gF profusion domain, which provided the first evidence that retargeted HSVs exert anti-tumor activity.
In the chemical synapse PVRL1 interacts with PVRL3 (nectin-3) and both proteins can be found in neuronal tissue already in early stages of brain development as well as in aging brains. Inerestingly the two proteins have been found to localize asymmetrically along the chemical synapse, with PVRL1 primarily on the axonal side and PVRL3 on the dendritic side.
In the case of a herpes virus, initial interactions occur when two viral envelope glycoprotein called glycoprotein C (gC) and glycoprotein B (gB) bind to a cell surface particle called heparan sulfate. Next, the major receptor binding protein, glycoprotein D (gD), binds specifically to at least one of three known entry receptors. These cell receptors include herpesvirus entry mediator (HVEM), nectin-1 and 3-O sulfated heparan sulfate. The nectin receptors usually produce cell-cell adhesion, to provide a strong point of attachment for the virus to the host cell. These interactions bring the membrane surfaces into mutual proximity and allow for other glycoproteins embedded in the viral envelope to interact with other cell surface molecules.
Elfin may be identified with the "Alphin m. Nectin" listed in the "Annals of Ulster" as dying in 693 along with "Bruide m. Bili" (i.e. Bridei III of the Picts). It is possible that this Nectin is Neithon of Alt Clut, an earlier King of Alt Clut, and that the Harleian genealogies have Elfin's pedigree wrong. However, this identification would cause serious incongruities in the dating of the other kings of Alt Clut, as Neithon was the grandfather of Eugein I and is thought to have died around 620. Scholars such as Alfred P. Smyth suggest two Elfins, one the son of Eugein and one the son of Neithon. However, Alan MacQuarrie suggests that there was one Elfin, but that the "Annals of Ulster" have substituted the name of his great-grandfather Neithon for his father Eugein, an error perhaps reflecting importance attached to descent from Neithon.
Poliovirus receptor-related 1 (PVRL1), also known as nectin-1 and CD111 (formerly herpesvirus entry mediator C, HVEC) is a human protein of the immunoglobulin superfamily (IgSF), also considered a member of the nectins. It is a membrane protein with three extracellular immunoglobulin domains, a single transmembrane helix and a cytoplasmic tail. The protein can mediate Ca-independent cellular adhesion further characterizing it as IgSF cell adhesion molecule (IgSF CAM).
All nectins and Necls can form homo-cis dimers, meaning a dimer of two alike molecules on the same cell membrane. Following the homo-dimer formation they can trans-interact in an either heterophilic or homophilic manner. The network of the nectin and Necl trans-interactions has been characterized. Recent structural reports reveal the physical and chemical determinants of homophilic interactions mediated by N-terminal IgV domains. In general, heterophilic interactions among nectins have higher affinity than their respective homophilic interactions.