PubMed:8381673 JSONTXT

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":469,"end":476},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"}],"text":"Selective modification of Sendai virus hemagglutinin neuraminidase by pyridoxal 5'-phosphate: evidence for an allosteric modulation of neuraminidase activity.\nIncubation of Sendai virus with pyridoxal 5'-phosphate (PLP) causes inhibition of hemolytic activity, a slight reduction of hemagglutinating activity, and an increase in neuraminidase activity. The effects on hemagglutination and neuraminidase are prevented by the presence in the incubation mixture of sialyl lactose, a substrate of hemagglutinin-neuraminidase. Incubation with PLP of the water-soluble enzymatic domain of the neuraminidase has no effect on enzymatic activity, while the allosteric inhibition (Dallocchio et al. (1991) Biochem. Int. 25, 663-668) disappears. Both virus-bound and solubilized neuraminidase are selectively modified by PLP at the lysine-553. Our data suggest that PLP inactivates a previously undetected inhibitory site on the viral neuraminidase, and that a physiological effector is present on the viral envelope."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":469,"end":476},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G15541SE"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G15541SE"}],"text":"Selective modification of Sendai virus hemagglutinin neuraminidase by pyridoxal 5'-phosphate: evidence for an allosteric modulation of neuraminidase activity.\nIncubation of Sendai virus with pyridoxal 5'-phosphate (PLP) causes inhibition of hemolytic activity, a slight reduction of hemagglutinating activity, and an increase in neuraminidase activity. The effects on hemagglutination and neuraminidase are prevented by the presence in the incubation mixture of sialyl lactose, a substrate of hemagglutinin-neuraminidase. Incubation with PLP of the water-soluble enzymatic domain of the neuraminidase has no effect on enzymatic activity, while the allosteric inhibition (Dallocchio et al. (1991) Biochem. Int. 25, 663-668) disappears. Both virus-bound and solubilized neuraminidase are selectively modified by PLP at the lysine-553. Our data suggest that PLP inactivates a previously undetected inhibitory site on the viral neuraminidase, and that a physiological effector is present on the viral envelope."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":997,"end":1005},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0031975"}],"text":"Selective modification of Sendai virus hemagglutinin neuraminidase by pyridoxal 5'-phosphate: evidence for an allosteric modulation of neuraminidase activity.\nIncubation of Sendai virus with pyridoxal 5'-phosphate (PLP) causes inhibition of hemolytic activity, a slight reduction of hemagglutinating activity, and an increase in neuraminidase activity. The effects on hemagglutination and neuraminidase are prevented by the presence in the incubation mixture of sialyl lactose, a substrate of hemagglutinin-neuraminidase. Incubation with PLP of the water-soluble enzymatic domain of the neuraminidase has no effect on enzymatic activity, while the allosteric inhibition (Dallocchio et al. (1991) Biochem. Int. 25, 663-668) disappears. Both virus-bound and solubilized neuraminidase are selectively modified by PLP at the lysine-553. Our data suggest that PLP inactivates a previously undetected inhibitory site on the viral neuraminidase, and that a physiological effector is present on the viral envelope."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":26,"end":38},"obj":"Organism"},{"id":"T2","span":{"begin":173,"end":185},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"11191"},{"id":"A2","pred":"db_id","subj":"T2","obj":"11191"}],"text":"Selective modification of Sendai virus hemagglutinin neuraminidase by pyridoxal 5'-phosphate: evidence for an allosteric modulation of neuraminidase activity.\nIncubation of Sendai virus with pyridoxal 5'-phosphate (PLP) causes inhibition of hemolytic activity, a slight reduction of hemagglutinating activity, and an increase in neuraminidase activity. The effects on hemagglutination and neuraminidase are prevented by the presence in the incubation mixture of sialyl lactose, a substrate of hemagglutinin-neuraminidase. Incubation with PLP of the water-soluble enzymatic domain of the neuraminidase has no effect on enzymatic activity, while the allosteric inhibition (Dallocchio et al. (1991) Biochem. Int. 25, 663-668) disappears. Both virus-bound and solubilized neuraminidase are selectively modified by PLP at the lysine-553. Our data suggest that PLP inactivates a previously undetected inhibitory site on the viral neuraminidase, and that a physiological effector is present on the viral envelope."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":158},"obj":"Sentence"},{"id":"T2","span":{"begin":159,"end":352},"obj":"Sentence"},{"id":"T3","span":{"begin":353,"end":521},"obj":"Sentence"},{"id":"T4","span":{"begin":522,"end":734},"obj":"Sentence"},{"id":"T5","span":{"begin":735,"end":832},"obj":"Sentence"},{"id":"T6","span":{"begin":833,"end":1006},"obj":"Sentence"}],"text":"Selective modification of Sendai virus hemagglutinin neuraminidase by pyridoxal 5'-phosphate: evidence for an allosteric modulation of neuraminidase activity.\nIncubation of Sendai virus with pyridoxal 5'-phosphate (PLP) causes inhibition of hemolytic activity, a slight reduction of hemagglutinating activity, and an increase in neuraminidase activity. The effects on hemagglutination and neuraminidase are prevented by the presence in the incubation mixture of sialyl lactose, a substrate of hemagglutinin-neuraminidase. Incubation with PLP of the water-soluble enzymatic domain of the neuraminidase has no effect on enzymatic activity, while the allosteric inhibition (Dallocchio et al. (1991) Biochem. Int. 25, 663-668) disappears. Both virus-bound and solubilized neuraminidase are selectively modified by PLP at the lysine-553. Our data suggest that PLP inactivates a previously undetected inhibitory site on the viral neuraminidase, and that a physiological effector is present on the viral envelope."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":26,"end":38},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":173,"end":185},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"11191"},{"id":"A2","pred":"db_id","subj":"T2","obj":"11191"}],"text":"Selective modification of Sendai virus hemagglutinin neuraminidase by pyridoxal 5'-phosphate: evidence for an allosteric modulation of neuraminidase activity.\nIncubation of Sendai virus with pyridoxal 5'-phosphate (PLP) causes inhibition of hemolytic activity, a slight reduction of hemagglutinating activity, and an increase in neuraminidase activity. The effects on hemagglutination and neuraminidase are prevented by the presence in the incubation mixture of sialyl lactose, a substrate of hemagglutinin-neuraminidase. Incubation with PLP of the water-soluble enzymatic domain of the neuraminidase has no effect on enzymatic activity, while the allosteric inhibition (Dallocchio et al. (1991) Biochem. Int. 25, 663-668) disappears. Both virus-bound and solubilized neuraminidase are selectively modified by PLP at the lysine-553. Our data suggest that PLP inactivates a previously undetected inhibitory site on the viral neuraminidase, and that a physiological effector is present on the viral envelope."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":997,"end":1005},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0031975"}],"text":"Selective modification of Sendai virus hemagglutinin neuraminidase by pyridoxal 5'-phosphate: evidence for an allosteric modulation of neuraminidase activity.\nIncubation of Sendai virus with pyridoxal 5'-phosphate (PLP) causes inhibition of hemolytic activity, a slight reduction of hemagglutinating activity, and an increase in neuraminidase activity. The effects on hemagglutination and neuraminidase are prevented by the presence in the incubation mixture of sialyl lactose, a substrate of hemagglutinin-neuraminidase. Incubation with PLP of the water-soluble enzymatic domain of the neuraminidase has no effect on enzymatic activity, while the allosteric inhibition (Dallocchio et al. (1991) Biochem. Int. 25, 663-668) disappears. Both virus-bound and solubilized neuraminidase are selectively modified by PLP at the lysine-553. Our data suggest that PLP inactivates a previously undetected inhibitory site on the viral neuraminidase, and that a physiological effector is present on the viral envelope."}