PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11562482-1 2001 Peptide:N-glycanase (PNGase) cleaves oligosaccharide chains from glycopeptides and glycoproteins. Oligosaccharides 37-52 N-glycanase 1 Homo sapiens 0-19 11562482-1 2001 Peptide:N-glycanase (PNGase) cleaves oligosaccharide chains from glycopeptides and glycoproteins. Oligosaccharides 37-52 N-glycanase 1 Homo sapiens 21-27 10764604-6 2000 Following release by peptide N-glycanase (PNGase) digestion and purification by ultrafiltration, oligosaccharides can be characterized by a high-resolution oligosaccharide mapping technique using the same equipment employed for composition analysis. Oligosaccharides 97-113 N-glycanase 1 Homo sapiens 21-40 10764604-6 2000 Following release by peptide N-glycanase (PNGase) digestion and purification by ultrafiltration, oligosaccharides can be characterized by a high-resolution oligosaccharide mapping technique using the same equipment employed for composition analysis. Oligosaccharides 97-113 N-glycanase 1 Homo sapiens 42-48 10764604-6 2000 Following release by peptide N-glycanase (PNGase) digestion and purification by ultrafiltration, oligosaccharides can be characterized by a high-resolution oligosaccharide mapping technique using the same equipment employed for composition analysis. Oligosaccharides 97-112 N-glycanase 1 Homo sapiens 21-40 10764604-6 2000 Following release by peptide N-glycanase (PNGase) digestion and purification by ultrafiltration, oligosaccharides can be characterized by a high-resolution oligosaccharide mapping technique using the same equipment employed for composition analysis. Oligosaccharides 97-112 N-glycanase 1 Homo sapiens 42-48 10764604-7 2000 Oligosaccharide mapping can be applied to the entire hormone, individual subunits, or individual glycosylation sites by varying PNGase digestion conditions or substrates. Oligosaccharides 0-15 N-glycanase 1 Homo sapiens 128-134 10764604-8 2000 Oligosaccharide release by PNGase is readily monitored by SDS-PAGE. Oligosaccharides 0-15 N-glycanase 1 Homo sapiens 27-33 7797502-2 1995 L-929 PNGase was found to bind strongly with oligosaccharides having triomannosido-N,N"-diacetyl-chitobiosyl (Man3GlcNAc2) structure (Kd = approximately 10 microM). Oligosaccharides 45-61 N-glycanase 1 Homo sapiens 6-12 9881748-0 1998 Reproducible and sensitive determination of charged oligosaccharides from haptoglobin by PNGase F digestion and HPAEC/PAD analysis: glycan composition varies with disease. Oligosaccharides 52-68 N-glycanase 1 Homo sapiens 89-95 7797502-5 1995 Oligosaccharides having Man3GlcNAc2 structure were also shown to be strong inhibitors for the PNGase-catalyzed reaction (Ki = approximately 10 microM). Oligosaccharides 0-16 N-glycanase 1 Homo sapiens 94-100 7797502-7 1995 Enzyme kinetic studies showed that the mechanism of inhibition by the oligosaccharides and Man3 fits well with a model wherein two inhibitor binding sites reside on L-929 PNGase. Oligosaccharides 70-86 N-glycanase 1 Homo sapiens 171-177 7891293-2 1994 Using high-performance anion exchange chromatography with pulsed amperometric detection (HPAEC/PAD), we have analyzed the PNGase F released oligosaccharides of several IgG preparations including human polyclonal IgG, a humanized monoclonal IgG (MAb M115), and a murine monoclonal IgG (MAb MY9-6) derived respectively from serum, hybridoma cultures, and ascites fluid. Oligosaccharides 140-156 N-glycanase 1 Homo sapiens 122-128 3092742-2 1986 The oligosaccharides were segregated first according to class, using endo-beta-N-acetylglucosaminidase H (Endo H) to release the high mannose species, and then with peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase (PNGase F), which provided a complete array of complex oligosaccharide chains. Oligosaccharides 4-20 N-glycanase 1 Homo sapiens 224-230 7535137-2 1994 The unique properties of L-929 PNGase are that the enzyme had a high affinity to the substrate glycopeptide (e.g. Km = 114 microM for fetuin derived glycopentapeptide) and that the PNGase-catalysed reaction is strongly inhibited by the released free oligosaccharides but not by the free peptides formed, suggesting that L-929 PNGase is able to bind to a certain type of carbohydrate chain. Oligosaccharides 250-266 N-glycanase 1 Homo sapiens 31-37 7535137-2 1994 The unique properties of L-929 PNGase are that the enzyme had a high affinity to the substrate glycopeptide (e.g. Km = 114 microM for fetuin derived glycopentapeptide) and that the PNGase-catalysed reaction is strongly inhibited by the released free oligosaccharides but not by the free peptides formed, suggesting that L-929 PNGase is able to bind to a certain type of carbohydrate chain. Oligosaccharides 250-266 N-glycanase 1 Homo sapiens 181-187 7535137-2 1994 The unique properties of L-929 PNGase are that the enzyme had a high affinity to the substrate glycopeptide (e.g. Km = 114 microM for fetuin derived glycopentapeptide) and that the PNGase-catalysed reaction is strongly inhibited by the released free oligosaccharides but not by the free peptides formed, suggesting that L-929 PNGase is able to bind to a certain type of carbohydrate chain. Oligosaccharides 250-266 N-glycanase 1 Homo sapiens 181-187 8060671-4 1993 The commercial Endo F-peptide N-glycosidase/glycanyl amidase (PNGase) mixture readily cleaved high mannose and complex oligosaccharides (neutral and sialyated) with common core alpha 1-6 linked fucose found in porcine thyroglobulin including the trimannosyl-chitobiose core structure. Oligosaccharides 119-135 N-glycanase 1 Homo sapiens 20-60 8060671-4 1993 The commercial Endo F-peptide N-glycosidase/glycanyl amidase (PNGase) mixture readily cleaved high mannose and complex oligosaccharides (neutral and sialyated) with common core alpha 1-6 linked fucose found in porcine thyroglobulin including the trimannosyl-chitobiose core structure. Oligosaccharides 119-135 N-glycanase 1 Homo sapiens 62-68 3092742-2 1986 The oligosaccharides were segregated first according to class, using endo-beta-N-acetylglucosaminidase H (Endo H) to release the high mannose species, and then with peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase (PNGase F), which provided a complete array of complex oligosaccharide chains. Oligosaccharides 4-19 N-glycanase 1 Homo sapiens 224-230 3092742-10 1986 Thus, by employing a variation of this method, it was possible to confirm the location of fucose in the core of PNGase F-released hybrid oligosaccharides by the subsequent release with Endo H of the disaccharide, fucosyl-N-acetylglucosamine. Oligosaccharides 137-153 N-glycanase 1 Homo sapiens 112-118 23474886-5 2013 Furthermore, PNGase is found to play important roles in the ER-associated degradation pathway of glycoproteins.Recent studies of the glycosidases in Bifidobacteria have revealed that GNB/LNB pathway, which uniquely exist in this bacteria, works for the expression of Bifidus factor activity of human milk oligosaccharides, an important topic in the baby nutrition. Oligosaccharides 305-321 N-glycanase 1 Homo sapiens 13-19 29550355-4 2018 Urine oligosaccharide analysis was included as part of a routine evaluation for possible biomarkers in patients with confirmed NGLY1-CDDG. Oligosaccharides 6-21 N-glycanase 1 Homo sapiens 127-132 29550355-5 2018 During the qualitative review of oligosaccharide profiles by an experienced laboratory director an abnormal analyte with a proposed structure of Neu5Ac1Hex1GlcNAc1-Asn was identified in NGLY1-CDDG patient urine samples. Oligosaccharides 33-48 N-glycanase 1 Homo sapiens 186-191 29550355-9 2018 Urine oligosaccharide screening by MALDI-TOF MS can identify individuals with NGLY1-CDDG. Oligosaccharides 6-21 N-glycanase 1 Homo sapiens 78-83 27567076-1 2016 Peptide:N-glycanase (NGLY1) is an enzyme responsible for cleaving oligosaccharide moieties from misfolded glycoproteins to enable their proper degradation. Oligosaccharides 66-81 N-glycanase 1 Homo sapiens 0-19 27567076-1 2016 Peptide:N-glycanase (NGLY1) is an enzyme responsible for cleaving oligosaccharide moieties from misfolded glycoproteins to enable their proper degradation. Oligosaccharides 66-81 N-glycanase 1 Homo sapiens 21-26 26872155-8 2016 The PNGase F coated magnetic beads offered comparable deglycosylation level to the conventional in-solution based method in 10-min reaction times for the model glycoproteins of immunoglobulin G (mostly neutral carbohydrates), ribonuclease B (high mannose type sugars), and fetuin (highly sialylated oligosaccharides) with the special features of easy removal of the enzyme from the reaction mixture and reusability. Oligosaccharides 299-315 N-glycanase 1 Homo sapiens 4-10 16848760-3 2006 The free oligosaccharides released by PNGase are known to be further catabolized by a cytosolic alpha-mannosidase, although the gene encoding this enzyme has not been identified unequivocally. Oligosaccharides 9-25 N-glycanase 1 Homo sapiens 38-44 21979948-3 2011 Glycoproteins bearing this motif bind Yos9p and are dislocated into the cytoplasm and then deglycosylated by peptide N-glycanase (Png1p) to yield free oligosaccharides (fOS). Oligosaccharides 151-167 N-glycanase 1 Homo sapiens 109-128 21979948-3 2011 Glycoproteins bearing this motif bind Yos9p and are dislocated into the cytoplasm and then deglycosylated by peptide N-glycanase (Png1p) to yield free oligosaccharides (fOS). Oligosaccharides 151-167 N-glycanase 1 Homo sapiens 130-135 16848760-8 2006 The oligosaccharide processing in the cytosol by PNGase, endo-beta-N-acetylglucosaminidase and alpha-mannosidase may represent the common "non-lysosomal" catabolic pathway for N-glycans in animal cells, although the molecular mechanism as well as the functional importance of such processes remains to be determined. Oligosaccharides 4-19 N-glycanase 1 Homo sapiens 49-55 16131661-10 2005 The structures of N-linked oligosaccharides were elucidated from the MS/MS spectra of glycopeptides and exoglycosidase sequencing of PNGase A-released oligosaccharides. Oligosaccharides 27-43 N-glycanase 1 Homo sapiens 133-139