PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2732208-1 1989 One of the characteristic features of the asparagine-linked sugar chains of human chorionic gonadotropin (hCG) is that their sialic acid residues occur exclusively as the Neu5Ac alpha 2----3Gal group. N-Acetylneuraminic Acid 171-177 chorionic gonadotropin subunit beta 5 Homo sapiens 106-109 2732208-1 1989 One of the characteristic features of the asparagine-linked sugar chains of human chorionic gonadotropin (hCG) is that their sialic acid residues occur exclusively as the Neu5Ac alpha 2----3Gal group. N-Acetylneuraminic Acid 125-136 chorionic gonadotropin subunit beta 5 Homo sapiens 106-109 2732208-2 1989 In order to determine whether this sialic acid linkage is important for the functional role played by the sugar moiety of hCG or not, isomeric hCG containing the Neu5Ac alpha 2----6Gal group was prepared and its hormonal activity in vitro was investigated. N-Acetylneuraminic Acid 162-168 chorionic gonadotropin subunit beta 5 Homo sapiens 143-146 2448402-5 1987 After treatment with sialidase, both hCG alpha and PU alpha were shifted to the basic region, indicating that they contained terminal sialic acid residues. N-Acetylneuraminic Acid 134-145 chorionic gonadotropin subunit beta 5 Homo sapiens 37-40 2464369-9 1988 Isoelectric focusing of the HeLa and hCG subunits demonstrated that the tumor protein had a lower pI (4.7-5.5 compared to 6.5-7.8), and removal of sialic acid by mild acid hydrolysis did not entirely eliminate this difference. N-Acetylneuraminic Acid 147-158 chorionic gonadotropin subunit beta 5 Homo sapiens 37-40 2462932-3 1988 Using hCG, asialo-hCG (A-hCG) and DG-hCG, we have shown that removal of sugars internal to sialic acid is required to produce these specific antibodies. N-Acetylneuraminic Acid 91-102 chorionic gonadotropin subunit beta 5 Homo sapiens 6-9 2462932-3 1988 Using hCG, asialo-hCG (A-hCG) and DG-hCG, we have shown that removal of sugars internal to sialic acid is required to produce these specific antibodies. N-Acetylneuraminic Acid 91-102 chorionic gonadotropin subunit beta 5 Homo sapiens 18-21 2462932-3 1988 Using hCG, asialo-hCG (A-hCG) and DG-hCG, we have shown that removal of sugars internal to sialic acid is required to produce these specific antibodies. N-Acetylneuraminic Acid 91-102 chorionic gonadotropin subunit beta 5 Homo sapiens 18-21 2462932-3 1988 Using hCG, asialo-hCG (A-hCG) and DG-hCG, we have shown that removal of sugars internal to sialic acid is required to produce these specific antibodies. N-Acetylneuraminic Acid 91-102 chorionic gonadotropin subunit beta 5 Homo sapiens 18-21 3794447-11 1986 of 75,000 to 100,000, which is present in crude hCG but different from genuine hCG, has potent immunosuppressive effects and that sialic acid residues in the substance(s) are related to the manifestation of these effects. N-Acetylneuraminic Acid 130-141 chorionic gonadotropin subunit beta 5 Homo sapiens 48-51 3036467-1 1987 The present studies were undertaken to delineate the role of sialic acid residues in the two subunits of hCG in relation to its hormonal activity. N-Acetylneuraminic Acid 61-72 chorionic gonadotropin subunit beta 5 Homo sapiens 105-108 3036467-2 1987 Sialic acid was removed by treatment of the individual subunits or intact hCG with insolubilized neuraminidase. N-Acetylneuraminic Acid 0-11 chorionic gonadotropin subunit beta 5 Homo sapiens 74-77 3036467-7 1987 In a TSH receptor assay in human thyroid membranes, loss of sialic acid from either one or both hCG subunits resulted in enhancement of binding affinity; the rank order of decreasing potency was asialo-hCG, alpha-as beta, as alpha-beta. N-Acetylneuraminic Acid 60-71 chorionic gonadotropin subunit beta 5 Homo sapiens 96-99 3036467-12 1987 In all cases, sialic acid in the beta-subunit of hCG appears to have a predominant role in these effects. N-Acetylneuraminic Acid 14-25 chorionic gonadotropin subunit beta 5 Homo sapiens 49-52 7320438-6 1981 The significant difference was that while sialic acid was undetectable in hCG-choriocarcinoma approximately 8.5% of sialic acid was found in hCG-normal pregnancy and hCG-hydatidiform mole. N-Acetylneuraminic Acid 116-127 chorionic gonadotropin subunit beta 5 Homo sapiens 141-144 3003212-3 1985 PNA is highly specific for the terminal carbohydrate linkage Gal beta-(1----3)-Gal NAc which is only exposed to hCG when the O-serine linked oligosaccharide of its unique beta-CTP region is deficient in sialic acid. N-Acetylneuraminic Acid 203-214 chorionic gonadotropin subunit beta 5 Homo sapiens 112-115 7320438-6 1981 The significant difference was that while sialic acid was undetectable in hCG-choriocarcinoma approximately 8.5% of sialic acid was found in hCG-normal pregnancy and hCG-hydatidiform mole. N-Acetylneuraminic Acid 116-127 chorionic gonadotropin subunit beta 5 Homo sapiens 141-144 17585415-4 2007 The thyrotropic potency and thereby the degree of cross reactivity of hCG is determined by several factors, such as content of sialic acid or lack of the C-terminal tail. N-Acetylneuraminic Acid 127-138 chorionic gonadotropin subunit beta 5 Homo sapiens 70-73 10447009-5 1999 Molecular variants of hCG with increased thyrotropic potency include basic molecules with reduced sialic acid content, truncated molecules lacking the C-terminal tail, or molecules in which the 47-48 peptide bond in the beta-subunit loop is nicked. N-Acetylneuraminic Acid 98-109 chorionic gonadotropin subunit beta 5 Homo sapiens 22-25 14967177-4 2004 hCG molecules may vary in sialic acid content; this changes the acidity of the molecule. N-Acetylneuraminic Acid 26-37 chorionic gonadotropin subunit beta 5 Homo sapiens 0-3 16094462-1 2005 The microheterogeneity property of hCG with regards to its sialic acid contents resulted in variable mobility of the glycoprotein in SDS-PAGE. N-Acetylneuraminic Acid 59-70 chorionic gonadotropin subunit beta 5 Homo sapiens 35-38 9349585-6 1997 Indeed, removal of the sialic acid or carbohydrate residues from native hCG transformed it into a thyroid stimulator that elicited a maximal response in terms of iodide uptake, organification and T3 secretion by human thyroid follicles as high as TSH and almost twice as high as native hCG. N-Acetylneuraminic Acid 23-34 chorionic gonadotropin subunit beta 5 Homo sapiens 72-75 9580152-5 1998 The results indicate that the loss of sialic acid from the hCG molecule slightly increases the binding activity to LH receptors and results in steroidogenic activity with an increased ED50. N-Acetylneuraminic Acid 38-49 chorionic gonadotropin subunit beta 5 Homo sapiens 59-62 9349585-6 1997 Indeed, removal of the sialic acid or carbohydrate residues from native hCG transformed it into a thyroid stimulator that elicited a maximal response in terms of iodide uptake, organification and T3 secretion by human thyroid follicles as high as TSH and almost twice as high as native hCG. N-Acetylneuraminic Acid 23-34 chorionic gonadotropin subunit beta 5 Homo sapiens 286-289 9349585-9 1997 hCG, and to a greater extent ds-hCG and dg-hCG, inhibited, as did TSH, gamma-interferon-induced human leukocyte antigen-DR (HLA-DR) expression in human thyrocytes, again reflecting the intrinsic thyrotropic activity of native hCG and its variants depleted of sialic acid or carbohydrate residues. N-Acetylneuraminic Acid 259-270 chorionic gonadotropin subunit beta 5 Homo sapiens 0-3 9349585-9 1997 hCG, and to a greater extent ds-hCG and dg-hCG, inhibited, as did TSH, gamma-interferon-induced human leukocyte antigen-DR (HLA-DR) expression in human thyrocytes, again reflecting the intrinsic thyrotropic activity of native hCG and its variants depleted of sialic acid or carbohydrate residues. N-Acetylneuraminic Acid 259-270 chorionic gonadotropin subunit beta 5 Homo sapiens 32-35 9349585-9 1997 hCG, and to a greater extent ds-hCG and dg-hCG, inhibited, as did TSH, gamma-interferon-induced human leukocyte antigen-DR (HLA-DR) expression in human thyrocytes, again reflecting the intrinsic thyrotropic activity of native hCG and its variants depleted of sialic acid or carbohydrate residues. N-Acetylneuraminic Acid 259-270 chorionic gonadotropin subunit beta 5 Homo sapiens 32-35 9349585-9 1997 hCG, and to a greater extent ds-hCG and dg-hCG, inhibited, as did TSH, gamma-interferon-induced human leukocyte antigen-DR (HLA-DR) expression in human thyrocytes, again reflecting the intrinsic thyrotropic activity of native hCG and its variants depleted of sialic acid or carbohydrate residues. N-Acetylneuraminic Acid 259-270 chorionic gonadotropin subunit beta 5 Homo sapiens 32-35 9349585-11 1997 The study was conducted in a serum-free culture system of human thyroid follicles and shows that removal of the sialic acid or carbohydrate residues from native hCG transform hCG variants into thyroid stimulating superagonists. N-Acetylneuraminic Acid 112-123 chorionic gonadotropin subunit beta 5 Homo sapiens 161-164 9349585-11 1997 The study was conducted in a serum-free culture system of human thyroid follicles and shows that removal of the sialic acid or carbohydrate residues from native hCG transform hCG variants into thyroid stimulating superagonists. N-Acetylneuraminic Acid 112-123 chorionic gonadotropin subunit beta 5 Homo sapiens 175-178 7867650-3 1995 hCG derivatives were obtained by enzymic removal of the alpha 3-linked sialic acid residues followed by alpha 6-sialylation, alpha 3-galactosylation or alpha 3-fucosylation of uncovered Gal beta 1-->4GlcNAc (LacNAc) termini, or alpha 3-sialylation of Gal beta 1-->3GalNAc sequences. N-Acetylneuraminic Acid 71-82 chorionic gonadotropin subunit beta 5 Homo sapiens 0-3 8625917-7 1996 Analyses for sulfate and sialic acid contents demonstrated that pituitary hCG contained both sulfate and sialic acid. N-Acetylneuraminic Acid 25-36 chorionic gonadotropin subunit beta 5 Homo sapiens 74-77 8625917-7 1996 Analyses for sulfate and sialic acid contents demonstrated that pituitary hCG contained both sulfate and sialic acid. N-Acetylneuraminic Acid 105-116 chorionic gonadotropin subunit beta 5 Homo sapiens 74-77 8777139-3 1996 We modified N-acetylneuraminic acid (NeuAc) on the oligosaccharide moieties of hCG, and determined the effect on its biological activity by measuring hormone-stimulated adenylyl cyclase. N-Acetylneuraminic Acid 12-35 chorionic gonadotropin subunit beta 5 Homo sapiens 79-82 8777139-3 1996 We modified N-acetylneuraminic acid (NeuAc) on the oligosaccharide moieties of hCG, and determined the effect on its biological activity by measuring hormone-stimulated adenylyl cyclase. N-Acetylneuraminic Acid 37-42 chorionic gonadotropin subunit beta 5 Homo sapiens 79-82 8777139-4 1996 Treating hCG with sodium periodate to remove two carbon atoms from NeuAc or quantitatively removing NeuAc from hCG reduced its biological activity by 36% and 50%, respectively. N-Acetylneuraminic Acid 67-72 chorionic gonadotropin subunit beta 5 Homo sapiens 9-12 8777139-4 1996 Treating hCG with sodium periodate to remove two carbon atoms from NeuAc or quantitatively removing NeuAc from hCG reduced its biological activity by 36% and 50%, respectively. N-Acetylneuraminic Acid 100-105 chorionic gonadotropin subunit beta 5 Homo sapiens 111-114 8777139-5 1996 The galactose residues of asialo-hCG were reacted with NeuAc-hydrazone or a hydrazone of the oligosaccharide from the ganglioside GM1 (Gal(beta 1-3)GalNAc(beta 1-4) [NeuAc(alpha 2-3)]Gal(beta 1-4)Glc). N-Acetylneuraminic Acid 55-60 chorionic gonadotropin subunit beta 5 Homo sapiens 33-36 8777139-7 1996 These results suggest that several structural aspects of NeuAc including carbon side chain, an intact ring structure, and the position of NeuAc relative to other carbohydrate residues are important for full biological activity of hCG. N-Acetylneuraminic Acid 57-62 chorionic gonadotropin subunit beta 5 Homo sapiens 230-233 8777139-7 1996 These results suggest that several structural aspects of NeuAc including carbon side chain, an intact ring structure, and the position of NeuAc relative to other carbohydrate residues are important for full biological activity of hCG. N-Acetylneuraminic Acid 138-143 chorionic gonadotropin subunit beta 5 Homo sapiens 230-233 8563483-13 1995 Basic hCG isoforms with lower sialic acid content extracted from hydatidiform moles were more potent in activating adenylate cyclase, and showed high bioactivity/immunoactivity (B/I) ratio in CHO cells expressing human TSH receptors. N-Acetylneuraminic Acid 30-41 chorionic gonadotropin subunit beta 5 Homo sapiens 6-9 7803516-0 1994 Role of sialic acid residues in the in vitro superactivity of human choriogonadotropin (hCG) in rat Leydig cells. N-Acetylneuraminic Acid 8-19 chorionic gonadotropin subunit beta 5 Homo sapiens 88-91 7584519-0 1995 Crude urinary human chorionic gonadotropin contains variant forms of HCG with low sialic acid content that exhibit an increased thyrotropic activity in CHO cells expressing the human TSH receptor. N-Acetylneuraminic Acid 82-93 chorionic gonadotropin subunit beta 5 Homo sapiens 69-72 7803516-4 1994 The removal of sialic acid residues with neuraminidase dramatically diminished hCG stimulating activity without impairing its receptor binding activity but the S/B ratio for asialo-hCG never reached values lower than 1. N-Acetylneuraminic Acid 15-26 chorionic gonadotropin subunit beta 5 Homo sapiens 79-82 7803516-6 1994 Sialic acid residues in the Asn beta 30 carbohydrate chains of hLH and hCG appear to be responsible for their superactivity in the in vitro stimulation of testosterone secretion by rat Leydig cells. N-Acetylneuraminic Acid 0-11 chorionic gonadotropin subunit beta 5 Homo sapiens 71-74 1606356-8 1992 1H-NMR spectroscopy (400 MHz) of the glycan chains, alpha 6-sialylated in vitro, showed that the enzyme highly prefers the galactosyl residue at the Gal beta 1----4GlcNAc beta 1----2-Man alpha 1----3Man branch for attachment of the first mol of sialic acid into the diantennary glycans of desialylated hCG. N-Acetylneuraminic Acid 245-256 chorionic gonadotropin subunit beta 5 Homo sapiens 302-305 7689955-11 1993 Nicking of the putative amphipathic helix loop, hCG beta 38-57, apparently renders the hormone significantly less hydrophobic despite the equal molar content of sialic acid. N-Acetylneuraminic Acid 161-172 chorionic gonadotropin subunit beta 5 Homo sapiens 48-51 8499763-2 1993 Because most of the information on the structure-function relation of hCG as a thyroid stimulator has been derived from in vitro experiments, the present studies were undertaken to assess the role of its sialic acid residues in the expression of its thyrotropic activity in vivo. N-Acetylneuraminic Acid 204-215 chorionic gonadotropin subunit beta 5 Homo sapiens 70-73 1397383-13 1992 Sialic acid content in choriocarcinoma hCG was extremely lower compared to that in normal hCG. N-Acetylneuraminic Acid 0-11 chorionic gonadotropin subunit beta 5 Homo sapiens 39-42 8157712-10 1994 The difference in pI of each hCG isoform was attributable to the extent of sialylation; basic hCG isoforms contained less sialic acid by immunological detection using lectins. N-Acetylneuraminic Acid 122-133 chorionic gonadotropin subunit beta 5 Homo sapiens 94-97 1606356-3 1992 Initial rates of sialic acid incorporation into the desialylated glycans of hCG alpha and hCG beta in the heterodimer were higher with the alpha-subunit. N-Acetylneuraminic Acid 17-28 chorionic gonadotropin subunit beta 5 Homo sapiens 76-79 1846577-3 1991 The removal of sialic acid from either one or both subunits sharply increased the [125I]bovine TSH binding-inhibiting activity of hCG in the receptor assay. N-Acetylneuraminic Acid 15-26 chorionic gonadotropin subunit beta 5 Homo sapiens 130-133 1691720-5 1990 The mature alpha- and beta-subunits, secreted by BeWo cells as well as subunits of urinary hCG which are usually used as a standard hCG secreted by normal placental cells, were sensitive to neuraminidase treatment indicating that these subunits have terminal sialic acid(s). N-Acetylneuraminic Acid 259-270 chorionic gonadotropin subunit beta 5 Homo sapiens 91-94