PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17084501-1	2007	Polynucleotide phosphorylase (PNPase) is a phosphate-dependent 3" to 5" exonuclease widely diffused among bacteria and eukaryotes.	Phosphates	43-52	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	0-28	
17084501-1	2007	Polynucleotide phosphorylase (PNPase) is a phosphate-dependent 3" to 5" exonuclease widely diffused among bacteria and eukaryotes.	Phosphates	43-52	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	30-36	
31995710-7	2020	Furthermore, we show that PNPase localizes predominantly into the coacervate phase and that its depolymerization activity in high-phosphate buffer causes coacervate degradation.	Phosphates	130-139	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	26-32	
18083836-0	2008	Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts.	Phosphates	111-120	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	22-50	
18083836-0	2008	Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts.	Phosphates	111-120	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	52-58	
10222010-3	1999	At the moment, only radioisotopic methods are available for assaying PNPase in crude extracts; these involve incubating [32P]phosphate and poly(A) in the presence of the enzyme, separating [32P]phosphate from [32P]ADP, and quantifying ADP by scintillation counting.	Phosphates	125-134	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	69-75	
24770417-4	2014	Here, we demonstrated that a fraction of the SUV3 PNPase complex interacts with mitochondrial polyadenylation polymerase (mtPAP) under low mitochondrial matrix inorganic phosphate (Pi) conditions.	Phosphates	160-179	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	50-56	
23319881-2	2012	The archaeal exosome is functionally similar to bacterial polynucleotide phosphorylase (PNPase) and RNase PH enzymes as it uses inorganic phosphate (Pi) to processively cleave RNA substrates releasing nucleoside diphosphates.	Phosphates	128-147	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	58-86	
23319881-2	2012	The archaeal exosome is functionally similar to bacterial polynucleotide phosphorylase (PNPase) and RNase PH enzymes as it uses inorganic phosphate (Pi) to processively cleave RNA substrates releasing nucleoside diphosphates.	Phosphates	128-147	polyribonucleotide nucleotidyltransferase 1	Homo sapiens	88-94