PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28386256-7 2017 In particular, the sialic acid residues present on gp120 can bind Siglec-7 on natural killer and monocytes/macrophages and Siglec-1 on monocytes/macrophages and dendritic cells. N-Acetylneuraminic Acid 19-30 sialic acid binding Ig like lectin 1 Homo sapiens 123-131 29266251-3 2018 In this study, micro-array data identified the upregulation of sialic acid-binding immunoglobulin-type lectin 1 (Siglec-1) in human RSV-infected infants. N-Acetylneuraminic Acid 63-74 sialic acid binding Ig like lectin 1 Homo sapiens 113-121 28742001-2 2017 Porcine sialoadhesin [pSn, also known as sialic acid-binding immunoglobulin-type lectin (Siglec-1)] and porcine CD163 (pCD163) have been identified as the most important host entry mediators that can fully coordinate PRRSV infection into macrophages. N-Acetylneuraminic Acid 41-52 sialic acid binding Ig like lectin 1 Homo sapiens 8-20 23822217-4 2013 Our laboratory has identified porcine sialoadhesin expressed on Kupffer cells as the lectin responsible for binding N-acetylneuraminic acid on the surface of the hRBC. N-Acetylneuraminic Acid 116-139 sialic acid binding Ig like lectin 1 Homo sapiens 38-50 26370074-1 2015 Siglec-1 (sialoadhesin, CD169) is a surface receptor on human cells that mediates trans-enhancement of HIV-1 infection through recognition of sialic acid moieties in virus membrane gangliosides. N-Acetylneuraminic Acid 142-153 sialic acid binding Ig like lectin 1 Homo sapiens 10-22 26370074-1 2015 Siglec-1 (sialoadhesin, CD169) is a surface receptor on human cells that mediates trans-enhancement of HIV-1 infection through recognition of sialic acid moieties in virus membrane gangliosides. N-Acetylneuraminic Acid 142-153 sialic acid binding Ig like lectin 1 Homo sapiens 24-29 28258691-3 2017 CD169 is a Siglec that may function as an adhesion molecule and a facilitator of the recognition and internalization of sialic acid decorated apoptotic bodies and exosomes derived from tumors. N-Acetylneuraminic Acid 120-131 sialic acid binding Ig like lectin 1 Homo sapiens 0-5 26370074-1 2015 Siglec-1 (sialoadhesin, CD169) is a surface receptor on human cells that mediates trans-enhancement of HIV-1 infection through recognition of sialic acid moieties in virus membrane gangliosides. N-Acetylneuraminic Acid 142-153 sialic acid binding Ig like lectin 1 Homo sapiens 0-8 23740482-1 2013 Porcine sialoadhesin (pSn; a sialic acid-binding lectin) and porcine CD163 (pCD163) are molecules that facilitate infectious entry of porcine reproductive and respiratory syndrome virus (PRRSV) into alveolar macrophages. N-Acetylneuraminic Acid 29-40 sialic acid binding Ig like lectin 1 Homo sapiens 8-20 22526486-2 2012 Sialoadhesin is a macrophage adhesion molecule containing 17 extracellular immunoglobulin-like domains, and is an I-type lectin which binds to sialic acid ligands expressed on hematopoietic cells. N-Acetylneuraminic Acid 143-154 sialic acid binding Ig like lectin 1 Homo sapiens 0-12 23610394-4 2013 CD169 is known as sialoadhesin (Sn), a macrophage-specific adhesion and endocytic receptor of the siglec family that recognizes sialic acid containing glycans as ligands. N-Acetylneuraminic Acid 128-139 sialic acid binding Ig like lectin 1 Homo sapiens 0-5 23610394-4 2013 CD169 is known as sialoadhesin (Sn), a macrophage-specific adhesion and endocytic receptor of the siglec family that recognizes sialic acid containing glycans as ligands. N-Acetylneuraminic Acid 128-139 sialic acid binding Ig like lectin 1 Homo sapiens 18-30 23610394-4 2013 CD169 is known as sialoadhesin (Sn), a macrophage-specific adhesion and endocytic receptor of the siglec family that recognizes sialic acid containing glycans as ligands. N-Acetylneuraminic Acid 128-139 sialic acid binding Ig like lectin 1 Homo sapiens 32-34 22958948-3 2012 Sialoadhesin, a macrophage restricted lectin that binds sialic acid, was originally described as a sheep erythrocyte binding receptor. N-Acetylneuraminic Acid 56-67 sialic acid binding Ig like lectin 1 Homo sapiens 0-12 22958948-10 2012 These data support the hypothesis that porcine sialoadhesin is a xenogeneic receptor that mediates porcine macrophage binding of human erythrocytes in a sialic acid-dependent manner. N-Acetylneuraminic Acid 153-164 sialic acid binding Ig like lectin 1 Homo sapiens 47-59 22396535-6 2012 Sialylation-dependent ligand recognition is also a property of SIGLEC1, a member of the sialic acid-binding Ig-like lectins. N-Acetylneuraminic Acid 88-99 sialic acid binding Ig like lectin 1 Homo sapiens 63-70 22450957-3 2012 Sialoadhesin is a major macrophage receptor that specifically recognizes sialic acid, an abundant component of host glycoconjugates but which can also be found on several human pathogens. N-Acetylneuraminic Acid 73-84 sialic acid binding Ig like lectin 1 Homo sapiens 0-12 21359217-3 2011 Originally, sialoadhesin was characterized as a lymphocyte adhesion molecule, though recently its involvement in internalization of sialic acid carrying pathogens was shown, suggesting that sialoadhesin is an endocytic receptor. N-Acetylneuraminic Acid 132-143 sialic acid binding Ig like lectin 1 Homo sapiens 12-24 23271952-6 2012 Here we show that the sialic acid-binding Ig-like lectin 1 (Siglec-1, CD169), which is highly expressed on mature DCs, specifically binds HIV-1 and vesicles carrying sialyllactose. N-Acetylneuraminic Acid 22-33 sialic acid binding Ig like lectin 1 Homo sapiens 60-68 21359217-3 2011 Originally, sialoadhesin was characterized as a lymphocyte adhesion molecule, though recently its involvement in internalization of sialic acid carrying pathogens was shown, suggesting that sialoadhesin is an endocytic receptor. N-Acetylneuraminic Acid 132-143 sialic acid binding Ig like lectin 1 Homo sapiens 190-202 21359217-9 2011 Together, these data expand sialoadhesin functionality and show that it can function as an endocytic receptor, a feature that cannot only be misused by sialic acid carrying pathogens, but that may also be used for specific targeting of toxins or antigens to sialoadhesin-expressing macrophages. N-Acetylneuraminic Acid 152-163 sialic acid binding Ig like lectin 1 Homo sapiens 28-40 20084110-0 2010 The M/GP(5) glycoprotein complex of porcine reproductive and respiratory syndrome virus binds the sialoadhesin receptor in a sialic acid-dependent manner. N-Acetylneuraminic Acid 125-136 sialic acid binding Ig like lectin 1 Homo sapiens 98-110 19285339-6 2010 The specificity of sialic acid binding membrane-anchored lectins, siglecs-1, -5, -7, -8 and -9 was determined using this methodology. N-Acetylneuraminic Acid 19-30 sialic acid binding Ig like lectin 1 Homo sapiens 66-94 20084110-6 2010 The soluble sialoadhesin could bind PRRSV in a sialic acid-dependent manner and could neutralize PRRSV infection of macrophages, thereby confirming the role of sialoadhesin as an essential PRRSV receptor on macrophages. N-Acetylneuraminic Acid 47-58 sialic acid binding Ig like lectin 1 Homo sapiens 12-24 20084110-8 2010 The interaction was found to be dependent on the sialic acid binding capacity of sialoadhesin and on the presence of sialic acids on GP(5). N-Acetylneuraminic Acid 49-60 sialic acid binding Ig like lectin 1 Homo sapiens 81-93 17137591-2 2007 Previously reported structures of the N-terminal domain of the Siglec sialoadhesin (SnD1) in complex with various sialic acid analogs revealed the structural template for sialic acid binding. N-Acetylneuraminic Acid 114-125 sialic acid binding Ig like lectin 1 Homo sapiens 70-82 18414664-5 2008 Using a stringent binding assay, sialoadhesin-expressing monocytes adsorbed HIV-1 through interaction with the sialic acid residues on the viral envelope glycoprotein gp120. N-Acetylneuraminic Acid 111-122 sialic acid binding Ig like lectin 1 Homo sapiens 33-45 18056365-9 2007 Interestingly, the binding of the LacNAc-specific lectins galectin-3 and -8 increased during maturation and up-regulation of sialic acid expression by mDC correlated with an increased binding of siglec-1, -2, and -7. N-Acetylneuraminic Acid 125-136 sialic acid binding Ig like lectin 1 Homo sapiens 195-215 17567703-0 2007 Porcine arterivirus attachment to the macrophage-specific receptor sialoadhesin is dependent on the sialic acid-binding activity of the N-terminal immunoglobulin domain of sialoadhesin. N-Acetylneuraminic Acid 100-111 sialic acid binding Ig like lectin 1 Homo sapiens 67-79 17567703-0 2007 Porcine arterivirus attachment to the macrophage-specific receptor sialoadhesin is dependent on the sialic acid-binding activity of the N-terminal immunoglobulin domain of sialoadhesin. N-Acetylneuraminic Acid 100-111 sialic acid binding Ig like lectin 1 Homo sapiens 172-184 17567703-1 2007 The sialic acid-binding lectin sialoadhesin (Sn) is a macrophage-restricted receptor for porcine reproductive and respiratory syndrome virus (PRRSV). N-Acetylneuraminic Acid 4-15 sialic acid binding Ig like lectin 1 Homo sapiens 31-43 18808170-2 2008 In this paper, we have examined this question using antibodies directed to Sialoadhesin (Sn), a macrophage-restricted adhesion molecule that mediates sialic acid dependent binding to different cells. N-Acetylneuraminic Acid 150-161 sialic acid binding Ig like lectin 1 Homo sapiens 75-87 18808170-2 2008 In this paper, we have examined this question using antibodies directed to Sialoadhesin (Sn), a macrophage-restricted adhesion molecule that mediates sialic acid dependent binding to different cells. N-Acetylneuraminic Acid 150-161 sialic acid binding Ig like lectin 1 Homo sapiens 89-91 17137591-2 2007 Previously reported structures of the N-terminal domain of the Siglec sialoadhesin (SnD1) in complex with various sialic acid analogs revealed the structural template for sialic acid binding. N-Acetylneuraminic Acid 171-182 sialic acid binding Ig like lectin 1 Homo sapiens 70-82 16732727-1 2006 Soluble siglecs-1, -4, -5, -6, -7, -8, -9, and -10 were probed with polyacrylamide glycoconjugates in which: 1) the Neu5Ac residue was substituted by a sulfate group (Su); 2) glycoconjugates contained both Su and Neu5Ac; 3) sialoglycoconjugates contained a tyrosine-O-sulfate residue. N-Acetylneuraminic Acid 116-122 sialic acid binding Ig like lectin 1 Homo sapiens 8-50 15254181-3 2004 In rodents and humans, sialoadhesin, or Siglec-1, has been described as a macrophage-restricted molecule and to specifically bind sialic acid moieties. N-Acetylneuraminic Acid 130-141 sialic acid binding Ig like lectin 1 Homo sapiens 23-35 15488769-1 2004 Sialoadhesin is a sialic acid-binding immunoglobulin-like lectin (Siglec), expressed on subsets of macrophages. N-Acetylneuraminic Acid 18-29 sialic acid binding Ig like lectin 1 Homo sapiens 0-12 15488769-3 2004 The N-terminal sialoadhesin domain can mediate sialic acid-binding on its own. N-Acetylneuraminic Acid 47-58 sialic acid binding Ig like lectin 1 Homo sapiens 15-27 15254181-3 2004 In rodents and humans, sialoadhesin, or Siglec-1, has been described as a macrophage-restricted molecule and to specifically bind sialic acid moieties. N-Acetylneuraminic Acid 130-141 sialic acid binding Ig like lectin 1 Homo sapiens 40-48 14698884-7 2004 The data reveal that sialoadhesin mainly recognizes the N-acetyl neuraminic acid and a small part of the galactose moiety of 1. N-Acetylneuraminic Acid 56-80 sialic acid binding Ig like lectin 1 Homo sapiens 21-33 12523830-4 2003 The sialopeptide libraries were screened against the recombinant binding domain (SnD1) of a sialic acid binding Ig-like protein, sialoadhesin (Siglec-1). N-Acetylneuraminic Acid 92-103 sialic acid binding Ig like lectin 1 Homo sapiens 129-141 14575475-3 2003 These newly constructed bioactive sialic acid-based structures were differentially recognized by sialoadhesin, a mammalian macrophage sialic acid binding protein. N-Acetylneuraminic Acid 34-45 sialic acid binding Ig like lectin 1 Homo sapiens 97-109 14575475-3 2003 These newly constructed bioactive sialic acid-based structures were differentially recognized by sialoadhesin, a mammalian macrophage sialic acid binding protein. N-Acetylneuraminic Acid 134-145 sialic acid binding Ig like lectin 1 Homo sapiens 97-109 14575475-5 2003 Modulating the interaction between sialoadhesin and its sialic acid ligands has important implications in immunobiology. N-Acetylneuraminic Acid 56-67 sialic acid binding Ig like lectin 1 Homo sapiens 35-47 12737821-0 2003 Structure-guided design of sialic acid-based Siglec inhibitors and crystallographic analysis in complex with sialoadhesin. N-Acetylneuraminic Acid 27-38 sialic acid binding Ig like lectin 1 Homo sapiens 109-121 12737821-2 2003 The crystal structure of the N-terminal immunoglobulin-like domain of the Siglec sialoadhesin (SnD1) in complex with 2,3-sialyllactose has informed the design of sialic acid analogs (sialosides) that bind Siglecs with significantly enhanced affinities and specificities. N-Acetylneuraminic Acid 162-173 sialic acid binding Ig like lectin 1 Homo sapiens 81-93 12523830-4 2003 The sialopeptide libraries were screened against the recombinant binding domain (SnD1) of a sialic acid binding Ig-like protein, sialoadhesin (Siglec-1). N-Acetylneuraminic Acid 92-103 sialic acid binding Ig like lectin 1 Homo sapiens 143-151 10499918-5 1999 Similar to other sialoadhesin molecules, p75/AIRM1 appears to mediate sialic acid-dependent ligand recognition. N-Acetylneuraminic Acid 70-81 sialic acid binding Ig like lectin 1 Homo sapiens 17-29 10722703-5 2000 Human siglec-1 (sialoadhesin) strongly prefers Neu5Ac over Neu5Gc. N-Acetylneuraminic Acid 47-53 sialic acid binding Ig like lectin 1 Homo sapiens 6-14 10722703-5 2000 Human siglec-1 (sialoadhesin) strongly prefers Neu5Ac over Neu5Gc. N-Acetylneuraminic Acid 47-53 sialic acid binding Ig like lectin 1 Homo sapiens 16-28 10608819-1 1999 Extended glycoconjugate binding specificities of three sialic acid-dependent immunoglobulin-like family member lectins (siglecs), myelin-associated glycoprotein (MAG), Schwann cell myelin protein (SMP), and sialoadhesin, were compared by measuring siglec-mediated cell adhesion to immobilized gangliosides. N-Acetylneuraminic Acid 55-66 sialic acid binding Ig like lectin 1 Homo sapiens 207-219 10610356-4 1999 Sn-Fc was found to bind specifically and in a sialic acid-dependent manner to the breast cancer cell lines MCF-7, T47.D and BT-20 both in solid- and solution-phase binding assays. N-Acetylneuraminic Acid 46-57 sialic acid binding Ig like lectin 1 Homo sapiens 0-2 11133773-1 2001 Sialoadhesin is a macrophage-restricted cellular interaction molecule and a prototypic member of the Siglec family of sialic acid binding immunoglobulin (Ig)-like lectins. N-Acetylneuraminic Acid 118-129 sialic acid binding Ig like lectin 1 Homo sapiens 0-12 11133773-5 2001 A recombinant protein consisting of the first 4 N-terminal domains of human sialoadhesin fused to the Fc region of human IgG1 mediated sialic acid-dependent binding with a specificity similar to its mouse counterpart, preferring sialic acid in the alpha2,3 glycosidic linkage over the alpha2,6 linkage. N-Acetylneuraminic Acid 135-146 sialic acid binding Ig like lectin 1 Homo sapiens 76-88 11133773-5 2001 A recombinant protein consisting of the first 4 N-terminal domains of human sialoadhesin fused to the Fc region of human IgG1 mediated sialic acid-dependent binding with a specificity similar to its mouse counterpart, preferring sialic acid in the alpha2,3 glycosidic linkage over the alpha2,6 linkage. N-Acetylneuraminic Acid 229-240 sialic acid binding Ig like lectin 1 Homo sapiens 76-88 10577497-4 1999 Sn is a prototypical member of the siglec family of sialic acid binding proteins, which includes CD22, myelin-associated glycoprotein, CD33, and siglec-5. N-Acetylneuraminic Acid 52-63 sialic acid binding Ig like lectin 1 Homo sapiens 0-2 10577497-6 1999 The sialic acid binding region of siglecs is localized within the membrane-distal, amino-terminal domain and in the case of Sn, it has been characterized in atomic detail by X-ray crystallography, nuclear magnetic resonance, and site-directed mutagenesis. N-Acetylneuraminic Acid 4-15 sialic acid binding Ig like lectin 1 Homo sapiens 124-126 9949167-0 1999 Sialylation of the sialic acid binding lectin sialoadhesin regulates its ability to mediate cell adhesion. N-Acetylneuraminic Acid 19-30 sialic acid binding Ig like lectin 1 Homo sapiens 46-58 10393093-4 1999 The resonances corresponding to the methyl protons within the N-acetyl moiety of sialic acid undergo upfield shifting and broadening during titrations, reflecting an interaction of this group with Trp2 in sialoadhesin as observed in co-crystals of the terminal domain with bound ligand. N-Acetylneuraminic Acid 81-92 sialic acid binding Ig like lectin 1 Homo sapiens 205-217 9949167-1 1999 The macrophage-specific cell surface receptor sialoadhesin, which is a member of the newly recognized family of sialic acid binding lectins called siglecs, binds glycoprotein and glycolipid ligands containing a2-3-linked sialic acid on the surface of several leukocyte subsets. N-Acetylneuraminic Acid 112-123 sialic acid binding Ig like lectin 1 Homo sapiens 46-58 9949167-1 1999 The macrophage-specific cell surface receptor sialoadhesin, which is a member of the newly recognized family of sialic acid binding lectins called siglecs, binds glycoprotein and glycolipid ligands containing a2-3-linked sialic acid on the surface of several leukocyte subsets. N-Acetylneuraminic Acid 221-232 sialic acid binding Ig like lectin 1 Homo sapiens 46-58 9201997-1 1997 Sialic acid linkage and substructure requirements for binding of myelin-associated glycoprotein, Schwann cell myelin protein, and sialoadhesin. N-Acetylneuraminic Acid 0-11 sialic acid binding Ig like lectin 1 Homo sapiens 130-142 9298693-3 1997 These proteins, collectively known as the sialoadhesin family, are able to mediate sialic acid-dependent binding with distinct specificities for both the type of sialic acid and its linkage to subterminal sugars. N-Acetylneuraminic Acid 83-94 sialic acid binding Ig like lectin 1 Homo sapiens 42-54 9298693-3 1997 These proteins, collectively known as the sialoadhesin family, are able to mediate sialic acid-dependent binding with distinct specificities for both the type of sialic acid and its linkage to subterminal sugars. N-Acetylneuraminic Acid 162-173 sialic acid binding Ig like lectin 1 Homo sapiens 42-54 2050106-5 1991 To investigate the specificity for sialic acid, we studied the interaction of sialoadhesin with derivatized human erythrocytes, glycoproteins, and glycolipids. N-Acetylneuraminic Acid 35-46 sialic acid binding Ig like lectin 1 Homo sapiens 78-90 8981082-3 1996 More recently, the Sialoadhesin family of sialic acid-dependent adhesion molecules was defined within the superfamily of immunoglobulin-like molecules. N-Acetylneuraminic Acid 42-53 sialic acid binding Ig like lectin 1 Homo sapiens 19-31 8530048-3 1995 These molecules establish a distinct family of sialic acid-dependent adhesion molecules, the sialoadhesin family. N-Acetylneuraminic Acid 47-58 sialic acid binding Ig like lectin 1 Homo sapiens 93-105 9068613-6 1997 Particular attention is focused on the recently evolving information about sialic acid recognition by certain C-type lectins (the selectins), I-type lectins (e.g., CD22 and sialoadhesin), and a complement regulatory protein (the H protein). N-Acetylneuraminic Acid 75-86 sialic acid binding Ig like lectin 1 Homo sapiens 173-185 9070454-0 1997 Expression, crystallization, and preliminary X-ray analysis of a sialic acid-binding fragment of sialoadhesin in the presence and absence of ligand. N-Acetylneuraminic Acid 65-76 sialic acid binding Ig like lectin 1 Homo sapiens 97-109 7718872-2 1995 It shares sequence similarity with sialoadhesin, CD22, and the myelin-associated glycoprotein, which constitute the Sialoadhesin family of sialic acid-dependent cell adhesion molecules. N-Acetylneuraminic Acid 139-150 sialic acid binding Ig like lectin 1 Homo sapiens 35-47 7718872-2 1995 It shares sequence similarity with sialoadhesin, CD22, and the myelin-associated glycoprotein, which constitute the Sialoadhesin family of sialic acid-dependent cell adhesion molecules. N-Acetylneuraminic Acid 139-150 sialic acid binding Ig like lectin 1 Homo sapiens 116-128 7533044-0 1994 Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily. N-Acetylneuraminic Acid 77-88 sialic acid binding Ig like lectin 1 Homo sapiens 0-12 7533044-2 1994 Apart from the selectins, the only well-characterized vertebrate sialic acid-dependent adhesion molecules are CD22 and sialoadhesin; CD22 is a member of the immunoglobulin superfamily that is expressed by B lymphocytes and sialoadhesin is a macrophage receptor. N-Acetylneuraminic Acid 65-76 sialic acid binding Ig like lectin 1 Homo sapiens 119-131 7533044-2 1994 Apart from the selectins, the only well-characterized vertebrate sialic acid-dependent adhesion molecules are CD22 and sialoadhesin; CD22 is a member of the immunoglobulin superfamily that is expressed by B lymphocytes and sialoadhesin is a macrophage receptor. N-Acetylneuraminic Acid 65-76 sialic acid binding Ig like lectin 1 Homo sapiens 223-235 35378756-10 2022 Here we show that CD169, a macrophage- specific sialic-acid binding lectin, facilitates abortive SARS-CoV-2 infection of macrophages that results in innate immune sensing of viral replication intermediates and production of proinflammatory responses. N-Acetylneuraminic Acid 48-59 sialic acid binding Ig like lectin 1 Homo sapiens 18-23 34539981-1 2021 CD169/Siglec1/sialoadhesin, a sialic acid-binding immunoglobulin-like lectin, is mainly expressed in metallophilic macrophages in the marginal zone of the spleen and in macrophages in the subcapsular sinus and medulla of lymph nodes. N-Acetylneuraminic Acid 30-41 sialic acid binding Ig like lectin 1 Homo sapiens 0-5 34539981-1 2021 CD169/Siglec1/sialoadhesin, a sialic acid-binding immunoglobulin-like lectin, is mainly expressed in metallophilic macrophages in the marginal zone of the spleen and in macrophages in the subcapsular sinus and medulla of lymph nodes. N-Acetylneuraminic Acid 30-41 sialic acid binding Ig like lectin 1 Homo sapiens 6-13 34539981-1 2021 CD169/Siglec1/sialoadhesin, a sialic acid-binding immunoglobulin-like lectin, is mainly expressed in metallophilic macrophages in the marginal zone of the spleen and in macrophages in the subcapsular sinus and medulla of lymph nodes. N-Acetylneuraminic Acid 30-41 sialic acid binding Ig like lectin 1 Homo sapiens 14-26