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Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-148 Sentence denotes Cloning and characterization of mammalian UDP-glucose glycoprotein: glucosyltransferase and the development of a specific substrate for this enzyme.
T1 0-148 Sentence denotes Cloning and characterization of mammalian UDP-glucose glycoprotein: glucosyltransferase and the development of a specific substrate for this enzyme.
T1 0-148 Sentence denotes Cloning and characterization of mammalian UDP-glucose glycoprotein: glucosyltransferase and the development of a specific substrate for this enzyme.
TextSentencer_T2 149-436 Sentence denotes The endoplasmic reticulum enzyme UDP-glucose glycoprotein:glucosyltransferase (UGGT) has the unique property of recognizing incompletely folded glycoproteins and, if they carry an N -linked Man(9)GlcNAc(2)oligosaccharide, of catalyzing the addition of a glucose residue from UDP-glucose.
T2 149-436 Sentence denotes The endoplasmic reticulum enzyme UDP-glucose glycoprotein:glucosyltransferase (UGGT) has the unique property of recognizing incompletely folded glycoproteins and, if they carry an N -linked Man(9)GlcNAc(2)oligosaccharide, of catalyzing the addition of a glucose residue from UDP-glucose.
T2 149-436 Sentence denotes The endoplasmic reticulum enzyme UDP-glucose glycoprotein:glucosyltransferase (UGGT) has the unique property of recognizing incompletely folded glycoproteins and, if they carry an N -linked Man(9)GlcNAc(2)oligosaccharide, of catalyzing the addition of a glucose residue from UDP-glucose.
TextSentencer_T3 437-559 Sentence denotes Using peptide sequence information, we have isolated the complete cDNA of rat liver UGGT and expressed it in insect cells.
T3 437-559 Sentence denotes Using peptide sequence information, we have isolated the complete cDNA of rat liver UGGT and expressed it in insect cells.
T3 437-559 Sentence denotes Using peptide sequence information, we have isolated the complete cDNA of rat liver UGGT and expressed it in insect cells.
TextSentencer_T4 560-686 Sentence denotes The cDNA specifies an open reading frame which codes for a protein of 1527 residues including an 18 amino acid signal peptide.
T4 560-686 Sentence denotes The cDNA specifies an open reading frame which codes for a protein of 1527 residues including an 18 amino acid signal peptide.
T4 560-686 Sentence denotes The cDNA specifies an open reading frame which codes for a protein of 1527 residues including an 18 amino acid signal peptide.
TextSentencer_T5 687-793 Sentence denotes The protein has a C-terminal tetrapeptide (HEEL) characteristic of endoplasmic reticulum luminal proteins.
T5 687-793 Sentence denotes The protein has a C-terminal tetrapeptide (HEEL) characteristic of endoplasmic reticulum luminal proteins.
T5 687-793 Sentence denotes The protein has a C-terminal tetrapeptide (HEEL) characteristic of endoplasmic reticulum luminal proteins.
TextSentencer_T6 794-954 Sentence denotes The purified recombinant enzyme shows the same preference for unfolded polypeptides with N -linked Man(9)GlcNAc(2)glycans as the enzyme purified from rat liver.
T6 794-954 Sentence denotes The purified recombinant enzyme shows the same preference for unfolded polypeptides with N -linked Man(9)GlcNAc(2)glycans as the enzyme purified from rat liver.
T6 794-954 Sentence denotes The purified recombinant enzyme shows the same preference for unfolded polypeptides with N -linked Man(9)GlcNAc(2)glycans as the enzyme purified from rat liver.
TextSentencer_T7 955-1158 Sentence denotes A genetically engineered Saccharomyces cerevisiae strain capable of producing glyco-proteins with Man(9)GlcNAc(2)core oligosaccharides was constructed and secreted acid phosphatase (G0-AcP) was purified.
T7 955-1158 Sentence denotes A genetically engineered Saccharomyces cerevisiae strain capable of producing glyco-proteins with Man(9)GlcNAc(2)core oligosaccharides was constructed and secreted acid phosphatase (G0-AcP) was purified.
T7 955-1158 Sentence denotes A genetically engineered Saccharomyces cerevisiae strain capable of producing glyco-proteins with Man(9)GlcNAc(2)core oligosaccharides was constructed and secreted acid phosphatase (G0-AcP) was purified.
TextSentencer_T8 1159-1309 Sentence denotes G0-AcP was used as an acceptor glycoprotein for UGGT and found to be a better substrate than the previously used soybean agglutinin and thyroglobulin.
T8 1159-1309 Sentence denotes G0-AcP was used as an acceptor glycoprotein for UGGT and found to be a better substrate than the previously used soybean agglutinin and thyroglobulin.
T8 1159-1309 Sentence denotes G0-AcP was used as an acceptor glycoprotein for UGGT and found to be a better substrate than the previously used soybean agglutinin and thyroglobulin.
TextSentencer_T9 1310-1372 Sentence denotes Recombinant rat UGGT has a K (m) of 44 microM for UDP-glucose.
T9 1310-1372 Sentence denotes Recombinant rat UGGT has a K (m) of 44 microM for UDP-glucose.
T9 1310-1372 Sentence denotes Recombinant rat UGGT has a K (m) of 44 microM for UDP-glucose.
TextSentencer_T10 1373-1532 Sentence denotes A proteolytic fragment of UGGT was found to retain enzymatic activity thus localizing the catalytic site of the enzyme to the C-terminal 37 kDa of the protein.
T10 1373-1532 Sentence denotes A proteolytic fragment of UGGT was found to retain enzymatic activity thus localizing the catalytic site of the enzyme to the C-terminal 37 kDa of the protein.
T10 1373-1532 Sentence denotes A proteolytic fragment of UGGT was found to retain enzymatic activity thus localizing the catalytic site of the enzyme to the C-terminal 37 kDa of the protein.
TextSentencer_T11 1533-1709 Sentence denotes Using site-directed mutagenesis and photoaffinity labeling, we have identified residues D1334, D1336, Q1429, and N1433 to be necessary for the catalytic activity of the enzyme.
T11 1533-1709 Sentence denotes Using site-directed mutagenesis and photoaffinity labeling, we have identified residues D1334, D1336, Q1429, and N1433 to be necessary for the catalytic activity of the enzyme.
T11 1533-1709 Sentence denotes Using site-directed mutagenesis and photoaffinity labeling, we have identified residues D1334, D1336, Q1429, and N1433 to be necessary for the catalytic activity of the enzyme.