PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29483298-0	2018	Hydrolytic activity of human Nudt16 enzyme on dinucleotide cap analogs and short capped oligonucleotides.	Dinucleoside Phosphates	46-58	nudix hydrolase 16	Homo sapiens	29-35	
29483298-4	2018	The present study focuses on hNudt16 and its hydrolytic activity toward dinucleotide cap analogs and short capped oligonucleotides.	Dinucleoside Phosphates	72-84	nudix hydrolase 16	Homo sapiens	29-36	
29483298-5	2018	We performed a screening assay for potential dinucleotide and oligonucleotide substrates for hNudt16.	Dinucleoside Phosphates	45-57	nudix hydrolase 16	Homo sapiens	93-100	
29483298-6	2018	Our data indicate that dinucleotide cap analogs and capped oligonucleotides containing guanine base in the first transcribed nucleotide are more susceptible to enzymatic digestion by hNudt16 than their counterparts containing adenine.	Dinucleoside Phosphates	23-35	nudix hydrolase 16	Homo sapiens	183-190	
29483298-7	2018	Furthermore, unmethylated dinucleotides (GpppG and ApppG) and respective oligonucleotides (GpppG-16nt and GpppA-16nt) were hydrolyzed by hNudt16 with greater efficiency than were m7GpppG and m7GpppG-16nt.	Dinucleoside Phosphates	26-39	nudix hydrolase 16	Homo sapiens	137-144	
29483298-8	2018	In conclusion, we found that hNudt16 hydrolysis of dinucleotide cap analogs and short capped oligonucleotides displayed a broader spectrum specificity than is currently known.	Dinucleoside Phosphates	51-63	nudix hydrolase 16	Homo sapiens	29-36