PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17698664-6 2007 The data demonstrated that the Ser-->Asp amino acid substitution at position 466 in the haemagglutinin-neuraminidase protein resulted in decreased receptor binding and neuraminidase activity, the Ala/Thr-->Thr selection in the fusion protein resulted in decreased fusion activity, and the Ile-->Val substitution in the polymerase resulted in increased replicative/transcriptional activity. Threonine 203-206 neuraminidase 1 Homo sapiens 106-119 6608726-2 1984 After neuraminidase treatment, the O-linked carbohydrate is susceptible to digestion with an endoglycosidase (endo-beta-N-acetylgalactosaminidase) that cleaves glycans with the structure Gal(beta 1----3)-GalNAc-Ser/Thr, and sialic acid can be added back to this core oligosaccharide by specific sialyltransferases. Threonine 215-218 neuraminidase 1 Homo sapiens 6-19 17698664-6 2007 The data demonstrated that the Ser-->Asp amino acid substitution at position 466 in the haemagglutinin-neuraminidase protein resulted in decreased receptor binding and neuraminidase activity, the Ala/Thr-->Thr selection in the fusion protein resulted in decreased fusion activity, and the Ile-->Val substitution in the polymerase resulted in increased replicative/transcriptional activity. Threonine 212-215 neuraminidase 1 Homo sapiens 106-119 7685769-4 1993 Neuraminidase and O-glycanase digestion followed by sodium dodecyl sulfate polyacrylamide and isoelectric focusing gel electrophoreses distinguished two possible carbohydrate structures attached at Thr-133: structure A, NeuNAc-Gal-beta(1,3)-GalNAc-O-Thr; and structure B, NeuNAc-Gal-beta(1,3)-[NeuNAc]-GalNAc-O-Thr. Threonine 198-201 neuraminidase 1 Homo sapiens 0-13 35582490-11 2022 One substitution, threonine (T) 135 to serine (S) in neuraminidase (NA), was only detected in an IAV isolate from a contact-exposed piglet. Threonine 18-27 neuraminidase 1 Homo sapiens 53-66 2160449-5 1990 The Mr of the inhibitor was reduced by treatment with neuraminidase, O-glycanase, and also with glycopeptidase-A, suggesting that the inhibitor has both Asn-linked and Ser/Thr-linked carbohydrate chains. Threonine 172-175 neuraminidase 1 Homo sapiens 54-67