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PubMed:1983782 JSONTXT 50 Projects

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Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-113 Sentence denotes Intracellular accumulation of the cellular prion protein after mutagenesis of its Asn-linked glycosylation sites.
T1 0-113 Sentence denotes Intracellular accumulation of the cellular prion protein after mutagenesis of its Asn-linked glycosylation sites.
T1 0-113 Sentence denotes Intracellular accumulation of the cellular prion protein after mutagenesis of its Asn-linked glycosylation sites.
TextSentencer_T2 114-300 Sentence denotes The cellular isoform of the prion protein (PrPC) is a sialoglycoprotein bound almost exclusively on the external surface of the plasma membrane by a glycosyl phosphatidylinositol anchor.
T2 114-300 Sentence denotes The cellular isoform of the prion protein (PrPC) is a sialoglycoprotein bound almost exclusively on the external surface of the plasma membrane by a glycosyl phosphatidylinositol anchor.
T2 114-300 Sentence denotes The cellular isoform of the prion protein (PrPC) is a sialoglycoprotein bound almost exclusively on the external surface of the plasma membrane by a glycosyl phosphatidylinositol anchor.
TextSentencer_T3 301-495 Sentence denotes The deduced amino acid sequence of Syrian hamster PrPC identifies two potential sites for the addition of Asn-linked carbohydrates at amino acids 181-183 (Asn-Ile-Thr) and 197-199 (Asn-Phe-Thr).
T3 301-495 Sentence denotes The deduced amino acid sequence of Syrian hamster PrPC identifies two potential sites for the addition of Asn-linked carbohydrates at amino acids 181-183 (Asn-Ile-Thr) and 197-199 (Asn-Phe-Thr).
T3 301-495 Sentence denotes The deduced amino acid sequence of Syrian hamster PrPC identifies two potential sites for the addition of Asn-linked carbohydrates at amino acids 181-183 (Asn-Ile-Thr) and 197-199 (Asn-Phe-Thr).
TextSentencer_T4 496-719 Sentence denotes We have altered these sites by replacing the threonine residues with alanine and expressed the mutant proteins transiently in CV1 cells utilizing a mutagenesis vector with the T7 promoter located upstream from the PrP gene.
T4 496-719 Sentence denotes We have altered these sites by replacing the threonine residues with alanine and expressed the mutant proteins transiently in CV1 cells utilizing a mutagenesis vector with the T7 promoter located upstream from the PrP gene.
T4 496-719 Sentence denotes We have altered these sites by replacing the threonine residues with alanine and expressed the mutant proteins transiently in CV1 cells utilizing a mutagenesis vector with the T7 promoter located upstream from the PrP gene.
TextSentencer_T5 720-802 Sentence denotes The T7 RNA polymerase was supplied by infection with a recombinant vaccinia virus.
T5 720-802 Sentence denotes The T7 RNA polymerase was supplied by infection with a recombinant vaccinia virus.
T5 720-802 Sentence denotes The T7 RNA polymerase was supplied by infection with a recombinant vaccinia virus.
TextSentencer_T6 803-938 Sentence denotes The 3 mutant proteins (PrPAla183, PrPAla199 and PrPAla183/199) have a reduced relative molecular weight compared to wild-type (wt) PrP.
T6 803-938 Sentence denotes The 3 mutant proteins (PrPAla183, PrPAla199 and PrPAla183/199) have a reduced relative molecular weight compared to wild-type (wt) PrP.
T6 803-938 Sentence denotes The 3 mutant proteins (PrPAla183, PrPAla199 and PrPAla183/199) have a reduced relative molecular weight compared to wild-type (wt) PrP.
TextSentencer_T7 939-1111 Sentence denotes Deglycosylation as well as synthesis in the presence of tunicamycin reduced the relative molecular weight of all the PrP species to that of the double mutant PrPAla183/199.
T7 939-1111 Sentence denotes Deglycosylation as well as synthesis in the presence of tunicamycin reduced the relative molecular weight of all the PrP species to that of the double mutant PrPAla183/199.
T7 939-1111 Sentence denotes Deglycosylation as well as synthesis in the presence of tunicamycin reduced the relative molecular weight of all the PrP species to that of the double mutant PrPAla183/199.
TextSentencer_T8 1112-1311 Sentence denotes Our results indicate that both single-site mutant prion proteins are glycosylated at non-mutated sites and they suggest that both potential sites for Asn-linked glycosylation are utilized in wt PrPC.
T8 1112-1311 Sentence denotes Our results indicate that both single-site mutant prion proteins are glycosylated at non-mutated sites and they suggest that both potential sites for Asn-linked glycosylation are utilized in wt PrPC.
T8 1112-1311 Sentence denotes Our results indicate that both single-site mutant prion proteins are glycosylated at non-mutated sites and they suggest that both potential sites for Asn-linked glycosylation are utilized in wt PrPC.
TextSentencer_T9 1312-1457 Sentence denotes Immunofluorescence studies demonstrate that while wt PrPC localizes to the cell surface, all the mutant PrP molecules accumulate intracellularly.
T9 1312-1457 Sentence denotes Immunofluorescence studies demonstrate that while wt PrPC localizes to the cell surface, all the mutant PrP molecules accumulate intracellularly.
T9 1312-1457 Sentence denotes Immunofluorescence studies demonstrate that while wt PrPC localizes to the cell surface, all the mutant PrP molecules accumulate intracellularly.
TextSentencer_T10 1458-1605 Sentence denotes The site of accumulation of PrPAla183 is probably prior to the mid-Golgi stack since this protein does not acquire resistance to endoglycosidase H.
T10 1458-1605 Sentence denotes The site of accumulation of PrPAla183 is probably prior to the mid-Golgi stack since this protein does not acquire resistance to endoglycosidase H.
T10 1458-1781 Sentence denotes The site of accumulation of PrPAla183 is probably prior to the mid-Golgi stack since this protein does not acquire resistance to endoglycosidase H. Whether the intracellular locations of the mutant PrPC species are the same as those identified for the scrapie isoform of the prion protein (PrPSc) remains to be established.
TextSentencer_T11 1606-1781 Sentence denotes Whether the intracellular locations of the mutant PrPC species are the same as those identified for the scrapie isoform of the prion protein (PrPSc) remains to be established.
T11 1606-1781 Sentence denotes Whether the intracellular locations of the mutant PrPC species are the same as those identified for the scrapie isoform of the prion protein (PrPSc) remains to be established.