PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6165879-7	1981	The presence of polyC during preincubation protected rho+ activity but produced substantial inactivation of rho-115 ATPase.	Poly C	16-21	ATPase	Escherichia coli	116-122	
2451028-9	1988	Poly(rC) and poly(dC) bind to rho competitively and with equal affinity and site size, although poly(rC) is the strongest cofactor for activating rho-dependent ATPase and poly(dC) has no ATPase cofactor activity at all.	Poly C	0-8	ATPase	Escherichia coli	160-166	
6452899-5	1981	The purified rho has an ATPase specific activity of 32 nmol of Pi released min-1 microgram-1 when poly(cytidylic acid) is used as a cofactor, and it functions effectively in termination of T7 DNA transcription.	Poly C	98-118	ATPase	Escherichia coli	24-30	
6165879-9	1981	Concentrations of polyC between 625 ng/ml and 100 micrograms/ml yielded the same extent of rho-115 ATPase inactivation during preincubation at 45 degrees C. Thermal inactivation of rho-115 ATPase by polyC was halted by shifting preincubation temperature from 45 degrees C to 35 degrees C, indicating that polyC-induced destabilization of rho-115 was irreversible.	Poly C	18-23	ATPase	Escherichia coli	99-105	
6165879-9	1981	Concentrations of polyC between 625 ng/ml and 100 micrograms/ml yielded the same extent of rho-115 ATPase inactivation during preincubation at 45 degrees C. Thermal inactivation of rho-115 ATPase by polyC was halted by shifting preincubation temperature from 45 degrees C to 35 degrees C, indicating that polyC-induced destabilization of rho-115 was irreversible.	Poly C	18-23	ATPase	Escherichia coli	189-195	
6165879-9	1981	Concentrations of polyC between 625 ng/ml and 100 micrograms/ml yielded the same extent of rho-115 ATPase inactivation during preincubation at 45 degrees C. Thermal inactivation of rho-115 ATPase by polyC was halted by shifting preincubation temperature from 45 degrees C to 35 degrees C, indicating that polyC-induced destabilization of rho-115 was irreversible.	Poly C	199-204	ATPase	Escherichia coli	189-195