PubMed:22296330 / 0-427 JSONTXT

{"project":"Allie","denotations":[{"id":"SS1_22296330_1_0","span":{"begin":395,"end":417},"obj":"expanded"},{"id":"SS2_22296330_1_0","span":{"begin":419,"end":422},"obj":"abbr"}],"relations":[{"id":"AE1_22296330_1_0","pred":"abbreviatedTo","subj":"SS1_22296330_1_0","obj":"SS2_22296330_1_0"}],"text":"Transition state analysis of Vibrio cholerae sialidase-catalyzed hydrolyses of natural substrate analogues.\nA series of isotopically labeled natural substrate analogues (phenyl 5-N-acetyl-α-d-neuraminyl-(2→3)-β-d-galactopyranosyl-(1→4)-1-thio-β-d-glucopyranoside; Neu5Acα2,3LacβSPh, and the corresponding 2→6 isomer) were prepared chemoenzymatically in order to characterize, by use of multiple kinetic isotope effect (KIE) mea"}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":29,"end":44},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0015766"}],"text":"Transition state analysis of Vibrio cholerae sialidase-catalyzed hydrolyses of natural substrate analogues.\nA series of isotopically labeled natural substrate analogues (phenyl 5-N-acetyl-α-d-neuraminyl-(2→3)-β-d-galactopyranosyl-(1→4)-1-thio-β-d-glucopyranoside; Neu5Acα2,3LacβSPh, and the corresponding 2→6 isomer) were prepared chemoenzymatically in order to characterize, by use of multiple kinetic isotope effect (KIE) mea"}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":264,"end":270},"obj":"Glycan"},{"id":"T2","span":{"begin":274,"end":277},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A11","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/ G84224TW"},{"id":"A12","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G84224TW"}],"text":"Transition state analysis of Vibrio cholerae sialidase-catalyzed hydrolyses of natural substrate analogues.\nA series of isotopically labeled natural substrate analogues (phenyl 5-N-acetyl-α-d-neuraminyl-(2→3)-β-d-galactopyranosyl-(1→4)-1-thio-β-d-glucopyranoside; Neu5Acα2,3LacβSPh, and the corresponding 2→6 isomer) were prepared chemoenzymatically in order to characterize, by use of multiple kinetic isotope effect (KIE) mea"}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":29,"end":44},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0015766"}],"text":"Transition state analysis of Vibrio cholerae sialidase-catalyzed hydrolyses of natural substrate analogues.\nA series of isotopically labeled natural substrate analogues (phenyl 5-N-acetyl-α-d-neuraminyl-(2→3)-β-d-galactopyranosyl-(1→4)-1-thio-β-d-glucopyranoside; Neu5Acα2,3LacβSPh, and the corresponding 2→6 isomer) were prepared chemoenzymatically in order to characterize, by use of multiple kinetic isotope effect (KIE) mea"}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":29,"end":44},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"666"}],"text":"Transition state analysis of Vibrio cholerae sialidase-catalyzed hydrolyses of natural substrate analogues.\nA series of isotopically labeled natural substrate analogues (phenyl 5-N-acetyl-α-d-neuraminyl-(2→3)-β-d-galactopyranosyl-(1→4)-1-thio-β-d-glucopyranoside; Neu5Acα2,3LacβSPh, and the corresponding 2→6 isomer) were prepared chemoenzymatically in order to characterize, by use of multiple kinetic isotope effect (KIE) mea"}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":107},"obj":"Sentence"}],"text":"Transition state analysis of Vibrio cholerae sialidase-catalyzed hydrolyses of natural substrate analogues.\nA series of isotopically labeled natural substrate analogues (phenyl 5-N-acetyl-α-d-neuraminyl-(2→3)-β-d-galactopyranosyl-(1→4)-1-thio-β-d-glucopyranoside; Neu5Acα2,3LacβSPh, and the corresponding 2→6 isomer) were prepared chemoenzymatically in order to characterize, by use of multiple kinetic isotope effect (KIE) mea"}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":264,"end":270},"obj":"Glycan"},{"id":"T2","span":{"begin":274,"end":277},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A11","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/ G84224TW"},{"id":"A12","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G84224TW"}],"text":"Transition state analysis of Vibrio cholerae sialidase-catalyzed hydrolyses of natural substrate analogues.\nA series of isotopically labeled natural substrate analogues (phenyl 5-N-acetyl-α-d-neuraminyl-(2→3)-β-d-galactopyranosyl-(1→4)-1-thio-β-d-glucopyranoside; Neu5Acα2,3LacβSPh, and the corresponding 2→6 isomer) were prepared chemoenzymatically in order to characterize, by use of multiple kinetic isotope effect (KIE) mea"}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":29,"end":44},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"666"}],"text":"Transition state analysis of Vibrio cholerae sialidase-catalyzed hydrolyses of natural substrate analogues.\nA series of isotopically labeled natural substrate analogues (phenyl 5-N-acetyl-α-d-neuraminyl-(2→3)-β-d-galactopyranosyl-(1→4)-1-thio-β-d-glucopyranoside; Neu5Acα2,3LacβSPh, and the corresponding 2→6 isomer) were prepared chemoenzymatically in order to characterize, by use of multiple kinetic isotope effect (KIE) mea"}