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Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-130 Sentence denotes The role of a single N-linked glycosylation site for a functional epitope of herpes simplex virus type 1 envelope glycoprotein gC.
T1 0-130 Sentence denotes The role of a single N-linked glycosylation site for a functional epitope of herpes simplex virus type 1 envelope glycoprotein gC.
T1 0-130 Sentence denotes The role of a single N-linked glycosylation site for a functional epitope of herpes simplex virus type 1 envelope glycoprotein gC.
TextSentencer_T2 131-436 Sentence denotes A monoclonal antibody, B1C1, binding to an epitope of antigenic site II of the herpes simplex virus type 1 (HSV-1) glycoprotein gC-1, is a potent inhibitor of two important biological functions of gC-1: its binding to cell surface heparan sulfate and its binding to the receptor for complement factor C3b.
T2 131-436 Sentence denotes A monoclonal antibody, B1C1, binding to an epitope of antigenic site II of the herpes simplex virus type 1 (HSV-1) glycoprotein gC-1, is a potent inhibitor of two important biological functions of gC-1: its binding to cell surface heparan sulfate and its binding to the receptor for complement factor C3b.
T2 131-436 Sentence denotes A monoclonal antibody, B1C1, binding to an epitope of antigenic site II of the herpes simplex virus type 1 (HSV-1) glycoprotein gC-1, is a potent inhibitor of two important biological functions of gC-1: its binding to cell surface heparan sulfate and its binding to the receptor for complement factor C3b.
TextSentencer_T3 437-614 Sentence denotes Here, we have analyzed a B1C1-resistant HSV-1 variant (HSV-12762/B1C1B4.2), obtained after passage of wild type HSV-1 (HSV-12762) in the presence of high concentrations of B1C1.
T3 437-614 Sentence denotes Here, we have analyzed a B1C1-resistant HSV-1 variant (HSV-12762/B1C1B4.2), obtained after passage of wild type HSV-1 (HSV-12762) in the presence of high concentrations of B1C1.
T3 437-614 Sentence denotes Here, we have analyzed a B1C1-resistant HSV-1 variant (HSV-12762/B1C1B4.2), obtained after passage of wild type HSV-1 (HSV-12762) in the presence of high concentrations of B1C1.
TextSentencer_T4 615-802 Sentence denotes The transport of newly synthesized mutant gC-1 to the cell surface was comparable to that of wild type glycoprotein, but no binding of surface-associated mutant gC-1 to B1C1 was detected.
T4 615-802 Sentence denotes The transport of newly synthesized mutant gC-1 to the cell surface was comparable to that of wild type glycoprotein, but no binding of surface-associated mutant gC-1 to B1C1 was detected.
T4 615-802 Sentence denotes The transport of newly synthesized mutant gC-1 to the cell surface was comparable to that of wild type glycoprotein, but no binding of surface-associated mutant gC-1 to B1C1 was detected.
TextSentencer_T5 803-879 Sentence denotes However, mutant and wild type gC-1 bound equally well to other site II Mabs.
T5 803-879 Sentence denotes However, mutant and wild type gC-1 bound equally well to other site II Mabs.
T5 803-947 Sentence denotes However, mutant and wild type gC-1 bound equally well to other site II Mabs. Attachment of wild type but not mutant virus was inhibited by B1C1.
TextSentencer_T6 880-947 Sentence denotes Attachment of wild type but not mutant virus was inhibited by B1C1.
T6 880-947 Sentence denotes Attachment of wild type but not mutant virus was inhibited by B1C1.
TextSentencer_T7 948-1119 Sentence denotes Sequencing of the mutant gC-1 gene revealed only one nucleotide change, resulting in replacement of Thr150 by an Ile, in turn destroying an N-glycosylation site at Asn148.
T6 948-1119 Sentence denotes Sequencing of the mutant gC-1 gene revealed only one nucleotide change, resulting in replacement of Thr150 by an Ile, in turn destroying an N-glycosylation site at Asn148.
T7 948-1119 Sentence denotes Sequencing of the mutant gC-1 gene revealed only one nucleotide change, resulting in replacement of Thr150 by an Ile, in turn destroying an N-glycosylation site at Asn148.
TextSentencer_T8 1120-1258 Sentence denotes Loss of one complex type N-linked glycan was confirmed by endoglycosidase digestion and subsequent SDS-polyacrylamide gel electrophoresis.
T7 1120-1258 Sentence denotes Loss of one complex type N-linked glycan was confirmed by endoglycosidase digestion and subsequent SDS-polyacrylamide gel electrophoresis.
T8 1120-1258 Sentence denotes Loss of one complex type N-linked glycan was confirmed by endoglycosidase digestion and subsequent SDS-polyacrylamide gel electrophoresis.
TextSentencer_T9 1259-1442 Sentence denotes Circular dichroism analysis of purified gC-1 from cells infected with mutant or wild type virus did not reveal any difference in secondary structure between mutant and wild type gC-1.
T8 1259-1442 Sentence denotes Circular dichroism analysis of purified gC-1 from cells infected with mutant or wild type virus did not reveal any difference in secondary structure between mutant and wild type gC-1.
T9 1259-1442 Sentence denotes Circular dichroism analysis of purified gC-1 from cells infected with mutant or wild type virus did not reveal any difference in secondary structure between mutant and wild type gC-1.
TextSentencer_T10 1443-1583 Sentence denotes It was not possible to obtain a B1C1-resistant phenotype by nucleotide-directed mutagenesis of gC-1 where Asn148 was changed to a glutamine.
T9 1443-1583 Sentence denotes It was not possible to obtain a B1C1-resistant phenotype by nucleotide-directed mutagenesis of gC-1 where Asn148 was changed to a glutamine.
T10 1443-1583 Sentence denotes It was not possible to obtain a B1C1-resistant phenotype by nucleotide-directed mutagenesis of gC-1 where Asn148 was changed to a glutamine.
TextSentencer_T11 1584-1721 Sentence denotes These data demonstrated that the threonine of the glycosylation site and not the N-linked glycan in itself was essential for B1C1 binding
T10 1584-1721 Sentence denotes These data demonstrated that the threonine of the glycosylation site and not the N-linked glycan in itself was essential for B1C1 binding
T11 1584-1721 Sentence denotes These data demonstrated that the threonine of the glycosylation site and not the N-linked glycan in itself was essential for B1C1 binding