PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19718030-4 2009 Mannose-expressing Mycobacterium tuberculosis and human immunodeficiency virus type 1 (HIV-1) induced the recruitment of effector proteins to the DC-SIGN signalosome to activate Raf-1, whereas fucose-expressing pathogens such as Helicobacter pylori actively dissociated the KSR1-CNK-Raf-1 complex from the DC-SIGN signalosome. Mannose 0-7 CD209 molecule Homo sapiens 146-153 19892432-2 2010 The dendritic cell-specific intercellular adhesion molecule 3 grabbing nonintegrin (DC-SIGN) is a calcium-dependent carbohydrate-binding protein with specificity for mannose-containing glycoconjugates and fucose-containing Lewis antigens. Mannose 166-173 CD209 molecule Homo sapiens 84-91 19892432-3 2010 Mannosylated moieties of the mycobacterial cell wall, such as mannose-capped lipoarabinomannan (manLAM) or higher-order phosphatidylinositol-mannosides (PIMs) of Mtb, were previously shown to bind to DC-SIGN on immature dendritic cells and macrophage subpopulations. Mannose 62-69 CD209 molecule Homo sapiens 200-207 19879650-1 2010 DC-SIGN (dendritic cell-specific ICAM-3-grabbing non-integrin) is a myeloid pathogen-attachment factor C-type lectin which recognizes mannose- and fucose-containing oligosaccharide ligands on clinically relevant pathogens. Mannose 134-141 CD209 molecule Homo sapiens 0-7 19879650-1 2010 DC-SIGN (dendritic cell-specific ICAM-3-grabbing non-integrin) is a myeloid pathogen-attachment factor C-type lectin which recognizes mannose- and fucose-containing oligosaccharide ligands on clinically relevant pathogens. Mannose 134-141 CD209 molecule Homo sapiens 9-61 19718030-4 2009 Mannose-expressing Mycobacterium tuberculosis and human immunodeficiency virus type 1 (HIV-1) induced the recruitment of effector proteins to the DC-SIGN signalosome to activate Raf-1, whereas fucose-expressing pathogens such as Helicobacter pylori actively dissociated the KSR1-CNK-Raf-1 complex from the DC-SIGN signalosome. Mannose 0-7 CD209 molecule Homo sapiens 306-313 19264337-5 2009 Several carbohydrate-binding agents (CBAs), such as the plant lectins HHA, GNA (mannose-specific) and UDA (N-acetylglucosamine-specific), inhibited dose-dependently the binding of DENV and subsequently viral replication in Raji/DC-SIGN(+) cells (EC(50): 0.1-2.2 microM). Mannose 80-87 CD209 molecule Homo sapiens 228-235 19722841-3 2009 DC-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) is a pattern recognition receptor with a broad pathogen recognition specificity as a result of its affinity for mannose and fucose carbohydrates. Mannose 189-196 CD209 molecule Homo sapiens 0-66 19722841-3 2009 DC-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) is a pattern recognition receptor with a broad pathogen recognition specificity as a result of its affinity for mannose and fucose carbohydrates. Mannose 189-196 CD209 molecule Homo sapiens 68-75 19021579-7 2008 CLRs such as DC-SIGN (DC-specific intracellular adhesion molecule-3 grabbing non-integrin) recognizes high-mannose-containing structures and Lewis antigens (Le(x), Le(y), Le(b) and Le(a)), whereas the CLR MGL (macrophage galactose/N-acetylgalactosamine-specific C-type lectin) recognizes GalNAc. Mannose 107-114 CD209 molecule Homo sapiens 13-20 19021579-7 2008 CLRs such as DC-SIGN (DC-specific intracellular adhesion molecule-3 grabbing non-integrin) recognizes high-mannose-containing structures and Lewis antigens (Le(x), Le(y), Le(b) and Le(a)), whereas the CLR MGL (macrophage galactose/N-acetylgalactosamine-specific C-type lectin) recognizes GalNAc. Mannose 107-114 CD209 molecule Homo sapiens 22-89 17522223-1 2007 Human immunodeficiency virus type 1 (HIV-1) envelope (gp120) binding to DC-SIGN, a C-type lectin that can facilitate HIV infection in cis and in trans, is largely dependent on high-mannose-content moieties. Mannose 181-188 CD209 molecule Homo sapiens 72-79 18772280-0 2008 Mutation in the DC-SIGN cytoplasmic triacidic cluster motif markedly attenuates receptor activity for phagocytosis and endocytosis of mannose-containing ligands by human myeloid cells. Mannose 134-141 CD209 molecule Homo sapiens 16-23 17913713-8 2007 The substantial expression of high mannose and complex type N-glycans terminated with Lewisx and Lewisy sequences suggests that sperm glycoproteins are highly decorated with ligands for DC-SIGN. Mannose 35-42 CD209 molecule Homo sapiens 186-193 17150970-1 2007 The dendritic cell surface receptor DC-SIGN and the closely related endothelial cell receptor DC-SIGNR specifically recognize high mannose N-linked carbohydrates on viral pathogens. Mannose 131-138 CD209 molecule Homo sapiens 36-43 17348701-6 2007 These results emphasize the possibility to conjugate mannose at position 6, allowing the incorporation of hydrophobic groups at the anomeric position to interact with hydrophobic residues in the carbohydrate recognition domain of DC-SIGN, increasing binding affinities. Mannose 53-60 CD209 molecule Homo sapiens 230-237 17150970-4 2007 The molecular basis of this enhancement has been investigated by determining crystal structures of DC-SIGN bound to a synthetic six-mannose fragment of a high mannose N-linked oligosaccharide, Manalpha1-2Manalpha1-3[Manalpha1-2Manalpha1-6]Manalpha1-6Man and to the disaccharide Manalpha1-2Man. Mannose 132-139 CD209 molecule Homo sapiens 99-106 12653690-2 2003 DC-SIGN (dendritic cell-specific ICAM-grabbing non-integrin, where ICAM is intercellular adhesion molecule) is a recently described mannose-specific C-type lectin expressed by dendritic cells. Mannose 132-139 CD209 molecule Homo sapiens 0-7 16616922-0 2006 Mannose hyperbranched dendritic polymers interact with clustered organization of DC-SIGN and inhibit gp120 binding. Mannose 0-7 CD209 molecule Homo sapiens 81-88 16616922-2 2006 Surface plasmon resonance has been used to study the affinity of a glycodendritic polymer with 32 mannoses, to DC-SIGN. Mannose 98-106 CD209 molecule Homo sapiens 111-118 16092920-2 2005 We have previously shown that M. tuberculosis binds to human monocyte-derived dendritic cells mostly through the C-type lectin DC-SIGN (dendritic-cell-specific intercellular molecule-3-grabbing non-integrin)/CD209, and we have suggested that DC-SIGN may discriminate between mycobacterial species through recognition of the mannose-capping residues on the lipoglycan lipoarabinomannan of the bacterial envelope. Mannose 324-331 CD209 molecule Homo sapiens 127-134 16092920-2 2005 We have previously shown that M. tuberculosis binds to human monocyte-derived dendritic cells mostly through the C-type lectin DC-SIGN (dendritic-cell-specific intercellular molecule-3-grabbing non-integrin)/CD209, and we have suggested that DC-SIGN may discriminate between mycobacterial species through recognition of the mannose-capping residues on the lipoglycan lipoarabinomannan of the bacterial envelope. Mannose 324-331 CD209 molecule Homo sapiens 136-206 16092920-5 2005 We propose that M. tuberculosis recognition by DC-SIGN relies on both a potential difference of accessibility of lipoarabinomannan in its envelope and, more probably, on the binding of additional ligands, possibly including lipomannan, mannose-capped arabinomannan, as well as the mannosylated 19 kDa and 45 kDa [Apa (alanine/proline-rich antigen)] glycoproteins. Mannose 236-243 CD209 molecule Homo sapiens 47-54 14581539-1 2003 C-type lectins such as DC-SIGN and L-SIGN, which bind mannose-enriched carbohydrate modifications of host and pathogen proteins, have been shown to bind glycoproteins of several viruses and facilitate either cis or trans infection. Mannose 54-61 CD209 molecule Homo sapiens 23-30 12653690-2 2003 DC-SIGN (dendritic cell-specific ICAM-grabbing non-integrin, where ICAM is intercellular adhesion molecule) is a recently described mannose-specific C-type lectin expressed by dendritic cells. Mannose 132-139 CD209 molecule Homo sapiens 9-59 26580315-0 2016 STD NMR and molecular modelling insights into interaction of novel mannose-based ligands with DC-SIGN. Mannose 67-74 CD209 molecule Homo sapiens 94-101 30251341-2 2018 Mannose-binding C-type lectins, which primarily include mannose receptor (MR, CD206) and dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN), are highly expressed on various cancer cells, endothelial cells, macrophages, and dendritic cells (DCs), which make them attractive targets for therapeutic effect. Mannose 0-7 CD209 molecule Homo sapiens 89-168 30251341-2 2018 Mannose-binding C-type lectins, which primarily include mannose receptor (MR, CD206) and dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN), are highly expressed on various cancer cells, endothelial cells, macrophages, and dendritic cells (DCs), which make them attractive targets for therapeutic effect. Mannose 0-7 CD209 molecule Homo sapiens 170-177 34652144-5 2021 In this study, we report on the discovery of a new class of potent glycomimetic DC-SIGN antagonists from a focused library of triazole-based mannose analogues. Mannose 141-148 CD209 molecule Homo sapiens 80-87 34061468-4 2021 Here, we demonstrate that mannose-functionalized poly- l -lysine glycoconjugates efficiently inhibit the attachment of viral glycoproteins to DC-SIGN-presenting cells with picomolar affinity. Mannose 26-33 CD209 molecule Homo sapiens 142-149 31466401-5 2019 High-mannose glycans are the natural ligands of dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN), a dendritic cell associated C-type lectin receptor (CLR), which has the ability to efficiently internalize its cargo and direct it to both major histocompatibility complex (MHC)-I and MHC-II pathways for the induction of CD8+ and CD4+ T cell responses, respectively. Mannose 5-12 CD209 molecule Homo sapiens 48-127 31466401-5 2019 High-mannose glycans are the natural ligands of dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN), a dendritic cell associated C-type lectin receptor (CLR), which has the ability to efficiently internalize its cargo and direct it to both major histocompatibility complex (MHC)-I and MHC-II pathways for the induction of CD8+ and CD4+ T cell responses, respectively. Mannose 5-12 CD209 molecule Homo sapiens 129-136 30344001-2 2018 Starting from libraries of 108 mannose-conjugated peptides, we identified glycopeptides that exhibited up to a 650-fold increase in multivalent binding affinity for DC-SIGN, which is also preserved in cells. Mannose 31-38 CD209 molecule Homo sapiens 165-172 28824637-4 2017 These glycans interact with mannose-specific lectins, especially with dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN). Mannose 28-35 CD209 molecule Homo sapiens 70-149 28824637-4 2017 These glycans interact with mannose-specific lectins, especially with dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN). Mannose 28-35 CD209 molecule Homo sapiens 151-158 26985831-11 2016 Modification of the complex heterotrimeric pili of a model probiotic and microbiota isolate with mannose and fucose is of importance for the functional interaction with the host immune lectin receptor DC-SIGN on human dendritic cells. Mannose 97-104 CD209 molecule Homo sapiens 201-208 26580315-1 2016 Study of interaction of mannose-based ligands with receptor DC-SIGN using high resolution NMR in combination with molecular modelling showed that four alpha-d-mannoside ligands interact with the binding site predominantly through the mannose moiety. Mannose 24-31 CD209 molecule Homo sapiens 60-67 26580315-1 2016 Study of interaction of mannose-based ligands with receptor DC-SIGN using high resolution NMR in combination with molecular modelling showed that four alpha-d-mannoside ligands interact with the binding site predominantly through the mannose moiety. Mannose 234-241 CD209 molecule Homo sapiens 60-67 26146546-8 2014 DC interactions with mannose conjugates were found to be calcium dependent and could be inhibited via anti-DC-SIGN antibodies. Mannose 21-28 CD209 molecule Homo sapiens 107-114 26611567-4 2016 DC-SIGN binds mannose or fucose-containing carbohydrates from viral proteins such as the HIV envelope glycoprotein gp120. Mannose 14-21 CD209 molecule Homo sapiens 0-7 24134734-3 2013 We have shown that, even as single molecules, these compounds efficiently target mannose-binding lectins, such as DC-specific ICAM-3-grabbing nonintegrin (DC-SIGN) important for HIV-1 transmission. Mannose 81-88 CD209 molecule Homo sapiens 155-162 25121780-2 2014 DC-SIGN mediates interactions among dendritic cells, pathogens, and a variety of epithelia, myeloid cells, and endothelia by binding to high mannose residues on pathogenic invaders or fucosylated residues on the membranes of other immune cells. Mannose 141-148 CD209 molecule Homo sapiens 0-7 24556146-0 2014 Monovalent mannose-based DC-SIGN antagonists: targeting the hydrophobic groove of the receptor. Mannose 11-18 CD209 molecule Homo sapiens 25-32 24556146-3 2014 We report the design and synthesis of d-mannose-based DC-SIGN antagonists bearing diaryl substituted 1,3-diaminopropanol or glycerol moieties incorporated to target the hydrophobic groove of the receptor. Mannose 38-47 CD209 molecule Homo sapiens 54-61 24134734-9 2013 We present an interaction model between DC-SIGN and conjugates-either single molecules, micelles, or polymers-that highlights that the most effective interactions by dynamic micelles involve both mannose heads and lipid chains. Mannose 196-203 CD209 molecule Homo sapiens 40-47 22871093-1 2012 Mannose-binding lectins, such as dendritic cell-specific ICAM-3-grabbing non-integrin (DC-SIGN), are expressed at the surface of human dendritic cells (DCs) that capture and transmit human immunodeficiency virus type-1 (HIV-1) to CD4(+) cells. Mannose 0-7 CD209 molecule Homo sapiens 33-85 23417900-0 2013 Selective targeting of dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) with mannose-based glycomimetics: synthesis and interaction studies of bis(benzylamide) derivatives of a pseudomannobioside. Mannose 117-124 CD209 molecule Homo sapiens 23-101 23417900-0 2013 Selective targeting of dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) with mannose-based glycomimetics: synthesis and interaction studies of bis(benzylamide) derivatives of a pseudomannobioside. Mannose 117-124 CD209 molecule Homo sapiens 103-110 23417900-1 2013 Dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) and Langerin are C-type lectins of dendritic cells (DCs) that share a specificity for mannose and are involved in pathogen recognition. Mannose 175-182 CD209 molecule Homo sapiens 0-78 23417900-1 2013 Dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) and Langerin are C-type lectins of dendritic cells (DCs) that share a specificity for mannose and are involved in pathogen recognition. Mannose 175-182 CD209 molecule Homo sapiens 80-87 23417900-5 2013 We show here for the first time that glycomimetics based on a mannose anchor can be tuned to selectively inhibit DC-SIGN over Langerin. Mannose 62-69 CD209 molecule Homo sapiens 113-120 22982058-3 2012 In this study, the binding of glycoproteins with specific high-mannose or human N- and O-linked glycan structures to DC-SIGN was tested. Mannose 63-70 CD209 molecule Homo sapiens 117-124 22982058-4 2012 Proteins with humanized N-glycans including Man5 structures and O-glycans (up to as many as 24) with single mannose chain length showed DC-SIGN binding that was comparable to that measured for a CHO-produced IgG1 which lacks O-linked mannose. Mannose 108-115 CD209 molecule Homo sapiens 136-143 22871093-1 2012 Mannose-binding lectins, such as dendritic cell-specific ICAM-3-grabbing non-integrin (DC-SIGN), are expressed at the surface of human dendritic cells (DCs) that capture and transmit human immunodeficiency virus type-1 (HIV-1) to CD4(+) cells. Mannose 0-7 CD209 molecule Homo sapiens 87-94 22257062-7 2012 Based on the fact that DCSIGN binds mannose- and fucose-based oligo- and polysaccharides, their structural mimics have been designed and proved to inhibit pathogen-DC-SIGN interaction. Mannose 36-43 CD209 molecule Homo sapiens 23-29 22257062-7 2012 Based on the fact that DCSIGN binds mannose- and fucose-based oligo- and polysaccharides, their structural mimics have been designed and proved to inhibit pathogen-DC-SIGN interaction. Mannose 36-43 CD209 molecule Homo sapiens 164-171 20363321-5 2010 Upon DC-SIGN engagement by mannose- or fucose-containing oligosaccharides, the latter leads to a tailored Toll-like receptor signalling, resulting in an altered DC-cytokine profile and skewing of Th1/Th2 responses. Mannose 27-34 CD209 molecule Homo sapiens 5-12 22102941-6 2011 DC-SIGN, a mannose-binding C-type lectin expressed on cells in the mucosal tissue of the rectum, uterus and cervix, facilitates early HIV-1 infection after sexual transmission. Mannose 11-18 CD209 molecule Homo sapiens 0-7 21540232-4 2011 In this side-by-side study DC-SIGN was found to preferentially bind internal mannose residues of high-mannose-type saccharides and the fucose-containing blood-type antigens H, A, B, Le(a), Le(b) Le(x), Le(y), sialyl-Le(a) as well as sulfatated derivatives of Le(a) and Le(x). Mannose 77-84 CD209 molecule Homo sapiens 27-34 21540232-4 2011 In this side-by-side study DC-SIGN was found to preferentially bind internal mannose residues of high-mannose-type saccharides and the fucose-containing blood-type antigens H, A, B, Le(a), Le(b) Le(x), Le(y), sialyl-Le(a) as well as sulfatated derivatives of Le(a) and Le(x). Mannose 102-109 CD209 molecule Homo sapiens 27-34