PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11395522-1	2001	Cet1, the RNA triphosphatase component of the yeast mRNA capping apparatus, catalyzes metal-dependent gamma-phosphate hydrolysis within the hydrophilic interior of an eight-strand beta barrel (the "triphosphate tunnel"), which rests upon a globular protein core (the "pedestal").	triphosphoric acid	198-210	polynucleotide 5'-phosphatase	Saccharomyces cerevisiae S288C	0-4	
16809816-4	2006	The Cet1 active site is unusually complex and located within a topologically closed hydrophilic beta-barrel (the triphosphate tunnel).	triphosphoric acid	113-125	polynucleotide 5'-phosphatase	Saccharomyces cerevisiae S288C	4-8	
11279161-1	2001	Cet1, the RNA triphosphatase component of the yeast mRNA capping apparatus, catalyzes metal-dependent gamma phosphate hydrolysis within the hydrophilic interior of a topologically closed 8-strand beta barrel (the "triphosphate tunnel").	triphosphoric acid	214-226	polynucleotide 5'-phosphatase	Saccharomyces cerevisiae S288C	0-4	
11279098-2	2001	The active site of Cet1 resides within a topologically closed hydrophilic beta-barrel (the triphosphate tunnel) that is supported by a globular hydrophobic core.	triphosphoric acid	91-103	polynucleotide 5'-phosphatase	Saccharomyces cerevisiae S288C	19-23	
10589681-2	1999	The 2.05 A crystal structure of yeast RNA triphosphatase Cet1p reveals a novel active site fold whereby an eight-stranded beta barrel forms a topologically closed triphosphate tunnel.	triphosphoric acid	163-175	polynucleotide 5'-phosphatase	Saccharomyces cerevisiae S288C	57-62	
9710603-3	1998	Purified recombinant Cet1 catalyzes hydrolysis of the gamma phosphate of triphosphate-terminated RNA at a rate of 1 s-1.	triphosphoric acid	73-85	polynucleotide 5'-phosphatase	Saccharomyces cerevisiae S288C	21-25	
9345280-6	1997	The purified recombinant CET1 gene product, Cet1, exhibited an RNA 5"-triphosphatase activity which specifically removed the gamma-phosphate from the triphosphate-terminated RNA substrate, but not from nucleoside triphosphates, confirming the identity of the gene.	triphosphoric acid	150-162	polynucleotide 5'-phosphatase	Saccharomyces cerevisiae S288C	25-29	
9345280-6	1997	The purified recombinant CET1 gene product, Cet1, exhibited an RNA 5"-triphosphatase activity which specifically removed the gamma-phosphate from the triphosphate-terminated RNA substrate, but not from nucleoside triphosphates, confirming the identity of the gene.	triphosphoric acid	150-162	polynucleotide 5'-phosphatase	Saccharomyces cerevisiae S288C	44-48	
9852075-1	1998	Saccharomyces cerevisiae Cet1p catalyzes the first step of mRNA capping, the hydrolysis of the gamma phosphate of triphosphate-terminated RNA to form a 5" diphosphate end.	triphosphoric acid	114-126	polynucleotide 5'-phosphatase	Saccharomyces cerevisiae S288C	25-30