PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
116899-4	1979	The enzymic properties of another neuraminidase-treated Kasahara-variant enzyme such as inhibitions by L-phenylalanine, L-homoarginine, L-tryptophan, and L-leucine, effects of inorganic phosphate, urea, and sodium dodecyl sulfate, heat stability, and the reactivity with concanavalin-A are consistent with those of Kasahara isoenzyme.	Tryptophan	136-148	neuraminidase 1	Homo sapiens	34-47	
10462487-9	1999	Functional significance of the spectral data was derived from the known structure of influenza neuraminidase, where a tyrosinate ion is involved in the stabilization of the transition-state carbonium ion, and a tryptophan residue is involved in the binding of the acetyl moiety of the substrate.	Tryptophan	211-221	neuraminidase 1	Homo sapiens	95-108	
11702224-7	2001	DNA analysis of the family showed that both the proband and the third sibling had a novel homozygous nonsense point mutation at nucleotide 87 in exon 1 of the alpha-N-acetyl-neuraminidase (neu1) gene causing a substitution of tryptophan at codon 29 by a termination codon (W29X).	Tryptophan	226-236	neuraminidase 1	Homo sapiens	174-187	
11702224-7	2001	DNA analysis of the family showed that both the proband and the third sibling had a novel homozygous nonsense point mutation at nucleotide 87 in exon 1 of the alpha-N-acetyl-neuraminidase (neu1) gene causing a substitution of tryptophan at codon 29 by a termination codon (W29X).	Tryptophan	226-236	neuraminidase 1	Homo sapiens	189-193	
4343930-0	1972	Effect of tryptophan modification on the activity of bacterial and viral neuraminidase.	Tryptophan	10-20	neuraminidase 1	Homo sapiens	73-86	
29483296-4	2018	Furthermore, the N-terminal domain of NanH was hypothesised and proved to be capable of binding to a range of sialoglycans and non-sialylated derivatives with Kd in the micromolar range, as determined by steady-state tryptophan fluorescence spectroscopy, but it has no catalytic activity in isolation from the active site.	Tryptophan	217-227	neuraminidase 1	Homo sapiens	38-42