PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10632727-6	2000	Removing either one of the terminal disulfide bonds liberates a similar number of residues and has a similar effect on conformational stability, decreasing the midpoint of the thermal transition by almost 40 degrees C. The disulfide variants catalyze the cleavage of poly(cytidylic acid) with values of kcat/Km that are 2- to 40-fold less than that of wild-type RNase A.	Poly C	267-287	ribonuclease pancreatic	Bos taurus	362-369	
11742128-2	2002	Oligocytidylic acids, ranging from dinucleotides to heptanucleotides, were obtained by RNase A digestion of poly(C).	Poly C	108-115	ribonuclease pancreatic	Bos taurus	87-94	
9724524-6	1998	Wild-type RNase A and the K66A, K7A/R10A, and K7A/R10A/K66A variants were evaluated as catalysts for the cleavage of poly(cytidylic acid) [poly(C)] and for their abilities to bind to single-stranded DNA, a substrate analogue.	Poly C	117-137	ribonuclease pancreatic	Bos taurus	10-17	
9724524-6	1998	Wild-type RNase A and the K66A, K7A/R10A, and K7A/R10A/K66A variants were evaluated as catalysts for the cleavage of poly(cytidylic acid) [poly(C)] and for their abilities to bind to single-stranded DNA, a substrate analogue.	Poly C	139-146	ribonuclease pancreatic	Bos taurus	10-17	
9724524-8	1998	The kcat/Km values for poly(C) cleavage by the K66A, K7A/R10A, and K7A/R10A/K66A variants were 3-fold, 60-fold, and 300-fold lower, respectively, than that of wild-type RNase A.	Poly C	23-30	ribonuclease pancreatic	Bos taurus	169-176	
10504400-11	1999	On the contrary, the activity of the RNase A oligomers, from dimer to pentamer, on yeast RNA and poly(C) (Kunitz assay) is lower than that of monomeric RNase A.	Poly C	97-103	ribonuclease pancreatic	Bos taurus	37-44	
10220316-6	1999	T45G RNase A, which catalyzes the processive cleavage of poly(A) but the distributive cleavage of poly(cytidylic acid) [poly(C)], has the same preference.	Poly C	98-118	ribonuclease pancreatic	Bos taurus	5-12	
10220316-6	1999	T45G RNase A, which catalyzes the processive cleavage of poly(A) but the distributive cleavage of poly(cytidylic acid) [poly(C)], has the same preference.	Poly C	120-127	ribonuclease pancreatic	Bos taurus	5-12	
8844858-6	1996	The free energies with which Y97F, Y97A, and Y97G RNase A bind to the rate-limiting transition state during the cleavage of poly(cytidylic acid) are diminished by 0.74, 3.3, and 3.8 kcal/mol, respectively.	Poly C	124-144	ribonuclease pancreatic	Bos taurus	50-57