PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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	
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	
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	203-206	neuraminidase 1	Homo sapiens	106-119	
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