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CD209 encodes a transmembrane receptor and is often referred to as DC-SIGN because of its expression on the surface of dendritic cells and macrophages. Zusätzlich bieten wir Ihnen CD209 Molecule Antikörper (537) und CD209 Molecule Kits (9) und viele weitere Produktgruppen zu diesem Protein an.
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These findings indicate that DC-SIGN plays an important role in Japanese encephalitis virus transmission from dendritic cells to T cells and provide insight into how Japanese encephalitis virus exploits the migratory and antigen-presenting capabilities of dendritic cells to gain access to lymph nodes for dissemination and persistence in the host.
this study shows that DC-SIGN expression in Hofbauer cells may play an important role in immune tolerance in fetal chorionic villi during the development of preeclampsia
The DC-SIGN -336G/A polymorphism significantly affects dengue hemorrhagic fever and dengue fever incidence with the effect more pronounced in certain analyzed patient subgroups (Meta-Analysis).
The results suggest that DC-SIGN SNPs rs7252229, rs4804803, and rs735240 may influence nasopharyngeal carcinoma risk in the Chinese population.
Polymorphism of CD209 and TLR3 (zeige TLR3 Proteine) genes in populations of North Eurasia
searched for the relationship between single nucleotide polymorphism in the promoter region of the CD209, IL-10, IL-28 and 32 base pair deletion in CCR5 coding region (Delta 32) with the human predisposition to development of various clinical presentations of tick-borne encephalitis
These results show that DC-SIGN and TLR-4 (zeige TLR4 Proteine) interactions regulate inflammatory responses in renal tubular epithelial cells and participate in AKI pathogenesis.
1,25(OH)2D3 suppressed the DCSIGN expression in Mycobacterium tuberculosis infected onocytes/macrophages.
Studied the association of CD209 promoter haplotypes with risk of HIV-1 infection in a cohort of Spanish male intravenous drug users (IDU) infected with hepatitis C virus (HCV).
Upon gp120 (zeige ITIH4 Proteine) binding to DC-SIGN, cellular NF-kappaB (zeige NFKB1 Proteine) signaling was triggered, leading to the induction of matrix metalloproteinases, which subsequently degraded tight junction proteins and disrupted the blood-retinal barrier integrity.
The development and use of CD209 to characterize the phenotype of CD209 expressing cells in bovine blood using flow cytometry is reported.
a DC-SIGN-like molecule expressed specifically by bovine DC. This molecule may play an important role in the infection of bovine (DC) cells with M. bovis.
DC-SIGN+ cells showed a clear differential distribution in the decidua in the first 2 weeks of pregnancy, being found only adjacent to the implantation site
DC-SIGN expression in mesenteric lymph nodes is significantly downregulated in simian immunodeficiency virus-infected pig-tailed macaques.
The cloning and characterization of the cDNA and gene encoding porcine DC-SIGN (pDC (zeige PDC Proteine)-SIGN)is reported. The results will help better understand the biological role(s) of DC-SIGN family in innate immunity during the evolutionary process.
identification and functional characterization of DC-SIGN/CD209 molecule in zebrafish
M. scrofulaceum induces a semimature DC phenotype that is characterized by PD-L2 (zeige PDCD1LG2 Proteine) over-expression and elevated synthesis of IL-10 (zeige IL10 Proteine), most likely through TLR4 (zeige TLR4 Proteine) and Raf-1 (zeige RAF1 Proteine) signaling pathway-dependent DC-SIGN stimulation.
results suggested that podocytes in lupus nephritis can exert dendritic cell-like function through their expression of DC-SIGN, which may be involved in immune and inflammatory responses of renal tissues
High-resolution crystal structures of the SIGN-R1 carbohydrate recognition domain show 2 binding sites allowing SIGNR1 (zeige CD209B Proteine) to simultaneously bind both immune glycoproteins and microbial polysaccharide components.
Data suggest that serum amyloid P (SAP (zeige APCS Proteine)) activates CD209 DC-SIGN to regulate the innate immune system differently from C-reactive protein (CRP (zeige CRP Proteine)), and that DC-SIGN is a target for antifibrotics.
Intestinal enterocytes regulate tissue-associated immune compartments under the control of DC-SIGN in inflammatory bowel disease.
In vivo T cell activation induces the formation of CD209(+) PDL-2 (zeige PDCD1LG2 Proteine)(+) dendritic cells.
CD209a expression on dendritic cells is critical for the development of pathogenic Th17 cell responses in murine schistosomiasis.
CD209a is activated in macrophages by LECT2 (zeige LECT2 Proteine).
The neck region of the C-type lectin DC-SIGN regulates its surface spatiotemporal organization and virus-binding capacity on antigen-presenting cells
interactions between the CRD (zeige CRX Proteine) of DC-SIGN and the extracellular matrix and/or cis (zeige CISH Proteine) interactions with transmembrane scaffolding protein(s) play an essential role in organizing these microdomains
This gene encodes a transmembrane receptor and is often referred to as DC-SIGN because of its expression on the surface of dendritic cells and macrophages. The encoded protein is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses with a large impact on public health. The protein is organized into three distinct domains: an N-terminal transmembrane domain, a tandem-repeat neck domain and C-type lectin carbohydrate recognition domain. The extracellular region consisting of the C-type lectin and neck domains has a dual function as a pathogen recognition receptor and a cell adhesion receptor by binding carbohydrate ligands on the surface of microbes and endogenous cells. The neck region is important for homo-oligomerization which allows the receptor to bind multivalent ligands with high avidity. Variations in the number of 23 amino acid repeats in the neck domain of this protein are rare but have a significant impact on ligand binding ability. This gene is closely related in terms of both sequence and function to a neighboring gene (GeneID 10332\; often referred to as L-SIGN). DC-SIGN and L-SIGN differ in their ligand-binding properties and distribution. Alternative splicing results in multiple variants.
C-type lectin domain family 4 member L
, C-type lectin domain family 4, member L
, CD209 antigen
, HIV gpl20-binding protein
, dendritic cell-specific ICAM-3-grabbing non-integrin 1
, dendritic cell-specific intracellular adhesion molecules (ICAM)-3 grabbing non-integrin
, CD209-like protein
, dendritic cell-specific ICAM-3 grabbing non-integrin
, C-type lectin domain family 4, member M
, DC-SIGN protein
, putative mannose-binding C-type lectin
, CD209 antigen-like protein A
, dendritic cell-specific ICAM-3-grabbing non-integrin
, CD209 antigen-like protein C
, CD209c antigen
, Dendritic cell-specific ICAM-3-grabbing non-integrin 1
, dendritic cell-specific ICAM-3 grabbing nonintegrin