PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27251370-5 2016 These effects were accompanied by decreased level of T cell surface sialoglycosphingolipid (ganglioside) GM1 that is regulated by the endogenous neuraminidase in response to viral challenge. G(M1) Ganglioside 105-108 neuraminidase 1 Homo sapiens 145-158 1704123-7 1990 However, the functional cholera toxin receptor ganglioside Gm1 is resistant to neuraminidase treatment and periodate oxidation. G(M1) Ganglioside 59-62 neuraminidase 1 Homo sapiens 79-92 24434060-8 2014 Neurons treated with neuraminidase exhibited an increase in GM1 content, a loss in poly-sialoganglioside content, and a decrease in PMCA activity that was greater than that produced by d-PDMP treatment. G(M1) Ganglioside 60-63 neuraminidase 1 Homo sapiens 21-34 1697781-3 1990 The binding of 125I-labeled CT to neuraminidase-treated human type B erythrocytes was effectively inhibited by ganglioside GM1, but not by porcine gastric mucin with both A and H determinants (hog A + H), blood group specific lectins, and other substances at the highest concentrations used. G(M1) Ganglioside 123-126 neuraminidase 1 Homo sapiens 34-47 2280488-2 1990 The binding of 125I-labeled CT to neuraminidase-treated human type B erythrocytes was most effectively inhibited by ganglioside GM1 among different inhibitors used. G(M1) Ganglioside 128-131 neuraminidase 1 Homo sapiens 34-47 2280488-4 1990 On the other hand, hemagglutination of neuraminidase-treated human type B erythrocytes by CT was inhibited by lactose, galactose, hog A + H, bovine salivary mucin, porcine thyroglobulin, and fetuin, whereas that was not effectively inhibited by ganglioside GM1 at the highest concentration. G(M1) Ganglioside 245-260 neuraminidase 1 Homo sapiens 39-52 2182380-2 1990 The binding of 125I-labeled LTh-B to neuraminidase-treated human type B erythrocytes was most effectively inhibited by ganglioside GM1. G(M1) Ganglioside 131-134 neuraminidase 1 Homo sapiens 37-50 2182380-6 1990 These results suggest that the predominant binding substance for LTh-B on neuraminidase-treated human type B erythrocytes is ganglioside GM1, but indicate that the interaction of LTh-B with ganglioside GM1 is different in hemagglutination. G(M1) Ganglioside 137-140 neuraminidase 1 Homo sapiens 74-87 2182380-6 1990 These results suggest that the predominant binding substance for LTh-B on neuraminidase-treated human type B erythrocytes is ganglioside GM1, but indicate that the interaction of LTh-B with ganglioside GM1 is different in hemagglutination. G(M1) Ganglioside 125-140 neuraminidase 1 Homo sapiens 74-87 2670153-2 1989 The binding of 125I-labeled LTp to neuraminidase-treated human type A erythrocytes was most effectively inhibited by ganglioside GM1. G(M1) Ganglioside 129-132 neuraminidase 1 Homo sapiens 35-48 2547442-6 1989 These findings suggest that the predominant binding substance on neuraminidase-treated human type B erythrocytes for the LTc-B is ganglioside GM1 and that the combining site of LTc-B may be specific for the terminal disaccharide (galactose-N-acetyl-D-galactosamine)-linked portion of ganglioside GM1. G(M1) Ganglioside 142-145 neuraminidase 1 Homo sapiens 65-78 2547442-6 1989 These findings suggest that the predominant binding substance on neuraminidase-treated human type B erythrocytes for the LTc-B is ganglioside GM1 and that the combining site of LTc-B may be specific for the terminal disaccharide (galactose-N-acetyl-D-galactosamine)-linked portion of ganglioside GM1. G(M1) Ganglioside 296-299 neuraminidase 1 Homo sapiens 65-78 3947670-6 1986 Furthermore, the activity of GQ1b was completely abolished by neuraminidase treatment, which converted GQ1b to GM1, so we examined other molecular species of gangliosides having a common gangliotetraose backbone but linked differently with two to four sialic acids (i.e., GD1a, GD1b, GT1a, GT1b, GQ1b and GQ1c). G(M1) Ganglioside 111-114 neuraminidase 1 Homo sapiens 62-75 3086209-5 1986 Fibroblasts from different types of galactosialidosis, a recessive disease associated with a coexistent beta-galactosidase/neuraminidase deficiency all showed degradation of ingested GM1. G(M1) Ganglioside 183-186 neuraminidase 1 Homo sapiens 123-136 2649154-2 1989 The binding of 125I-labeled LTp to neuraminidase-treated human type A erythrocytes was most effectively inhibited by ganglioside GM1 among inhibitors used. G(M1) Ganglioside 117-132 neuraminidase 1 Homo sapiens 35-48 2649154-5 1989 On the other hand, hemagglutination of neuraminidase-treated human type A erythrocytes by LTp was inhibited by methyl alpha-D-galactopyranoside, galactose, melibiose and some glycoproteins, but not effectively inhibited by ganglioside GM1 at the highest concentration used. G(M1) Ganglioside 223-238 neuraminidase 1 Homo sapiens 39-52 2649154-7 1989 Although these findings show that there may be fundamental differences between interactions with ganglioside GM1 in hemagglutination compared to interactions with ganglioside GM1 in binding, the predominant binding substance for LTp on neuraminidase-treated human type A erythrocytes is suggested to be ganglioside GM1. G(M1) Ganglioside 175-178 neuraminidase 1 Homo sapiens 236-249 7172413-3 1982 Neuraminidase treatments caused a time- and dose-related release of sialic acid from the cells and enhanced the stimulatory effect of cholera toxin on basal and TPA-induced ODC activities as much as the monosialoganglioside GM1. G(M1) Ganglioside 224-227 neuraminidase 1 Homo sapiens 0-13 4072495-1 1985 In this work the possibility of using neuraminidase for increasing the content of ganglioside GM1 in the mixture of gangliosides used for the sensitization of erythrocytes has been studied. G(M1) Ganglioside 82-97 neuraminidase 1 Homo sapiens 38-51 6435528-10 1984 When SAP-1 from GM1 gangliosidosis liver was treated sequentially with neuraminidase, beta-galactosidase, and endoglycosidase D, almost all of it was converted to the forms found in control human liver. G(M1) Ganglioside 16-19 neuraminidase 1 Homo sapiens 71-84 6171919-6 1981 Pretreatment of lymphocytes from spleen, thymus and lymph node with neuraminidase resulted in subsequent reactivity of 80-90% of these cells with anti-asialo GM1 anti-bodies. G(M1) Ganglioside 158-161 neuraminidase 1 Homo sapiens 68-81 6171919-7 1981 A smaller increase in asialo GM1 detection after neuraminidase treatment was seen with bone-marrow cells (65%). G(M1) Ganglioside 29-32 neuraminidase 1 Homo sapiens 49-62 7014713-11 1980 The data indicated that the number of cryptic GM1 and/or higher gangliosides exposed by neuraminidase in the cell membrane varied during cell differentiation and was directly related to specific cell types. G(M1) Ganglioside 46-49 neuraminidase 1 Homo sapiens 88-101 6257300-1 1980 Hydrolysis of ganglioside GM1 by Sendai virus neuraminidase. G(M1) Ganglioside 14-29 neuraminidase 1 Homo sapiens 46-59 6257300-2 1980 The action of neuraminidase of influenza A virus, Sendai virus and Newcastle disease virus particles on bovine brain ganglioside GM1 and the properties of Sendai virus neuraminidase for GM1 were studied. G(M1) Ganglioside 129-132 neuraminidase 1 Homo sapiens 14-27 6257300-2 1980 The action of neuraminidase of influenza A virus, Sendai virus and Newcastle disease virus particles on bovine brain ganglioside GM1 and the properties of Sendai virus neuraminidase for GM1 were studied. G(M1) Ganglioside 186-189 neuraminidase 1 Homo sapiens 168-181 6257300-5 1980 The apparent Km of Sendai virus neuraminidase for GM1 hydrolysis was found to be 2.67 x 10(-4) M and the optimum pH was 5.6. G(M1) Ganglioside 50-53 neuraminidase 1 Homo sapiens 32-45 6257300-8 1980 In the absence of the surfactant, Sendai virus neuraminidase hydrolyzed GM1 more efficiently than Arthobacter ureafaciens neuraminidase which has been reported recently as being an adequate enzyme to hydrolyze ganglioside GM1 as a substrate. G(M1) Ganglioside 72-75 neuraminidase 1 Homo sapiens 47-60 6257300-8 1980 In the absence of the surfactant, Sendai virus neuraminidase hydrolyzed GM1 more efficiently than Arthobacter ureafaciens neuraminidase which has been reported recently as being an adequate enzyme to hydrolyze ganglioside GM1 as a substrate. G(M1) Ganglioside 72-75 neuraminidase 1 Homo sapiens 122-135 6257300-8 1980 In the absence of the surfactant, Sendai virus neuraminidase hydrolyzed GM1 more efficiently than Arthobacter ureafaciens neuraminidase which has been reported recently as being an adequate enzyme to hydrolyze ganglioside GM1 as a substrate. G(M1) Ganglioside 222-225 neuraminidase 1 Homo sapiens 47-60 6257300-8 1980 In the absence of the surfactant, Sendai virus neuraminidase hydrolyzed GM1 more efficiently than Arthobacter ureafaciens neuraminidase which has been reported recently as being an adequate enzyme to hydrolyze ganglioside GM1 as a substrate. G(M1) Ganglioside 222-225 neuraminidase 1 Homo sapiens 122-135 658424-0 1978 Susceptibility of ganglioside GM1 to a new bacterial neuraminidase. G(M1) Ganglioside 30-33 neuraminidase 1 Homo sapiens 53-66