PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25226389-13	2014	In human cells, targeted one-base deletion was undetectable, and dTMP>dCMP were the next preferred nucleotides inserted opposite Z. siRNA knockdown of Rev1 or pol zeta established that both these polymerases are vital for AP-site bypass, as demonstrated by 36-67% reduction in bypass efficiency.	Deoxycytidine Monophosphate	73-77	REV1 DNA directed polymerase	Homo sapiens	154-158	
11917024-0	2002	Response of human REV1 to different DNA damage: preferential dCMP insertion opposite the lesion.	Deoxycytidine Monophosphate	61-65	REV1 DNA directed polymerase	Homo sapiens	18-22	
24366879-5	2014	The pre-steady-state rate constant of deoxycytidine monophosphate (dCMP) insertion opposite the first tetrad-guanine by hRev1 is ~56% as fast as that observed for non-G4 DNA substrates.	Deoxycytidine Monophosphate	38-65	REV1 DNA directed polymerase	Homo sapiens	120-125	
24366879-5	2014	The pre-steady-state rate constant of deoxycytidine monophosphate (dCMP) insertion opposite the first tetrad-guanine by hRev1 is ~56% as fast as that observed for non-G4 DNA substrates.	Deoxycytidine Monophosphate	67-71	REV1 DNA directed polymerase	Homo sapiens	120-125	
20726503-8	2010	dCMP and dTMP were most frequently inserted by hPol iota, and only dCMP was inserted by Rev1.	Deoxycytidine Monophosphate	67-71	REV1 DNA directed polymerase	Homo sapiens	88-92	
12584190-6	2003	The in vitro results also suggested the involvement of pol iota and/or REV1 in inserting correct dCMP opposite alpha-OH-PdG during error-free synthesis.	Deoxycytidine Monophosphate	97-101	REV1 DNA directed polymerase	Homo sapiens	71-75	
12044876-2	2002	We show that purified REV1 protein inserts dCMP opposite template G, A, T and C, and dGMP and dTMP opposite template G in the presence of magnesium, while in the presence of manganese the specificity for dCMP was found to be relaxed and the REV1 protein acquired the ability to insert dCMP, dGMP, dAMP and dTMP opposite templates G, A, T, and C. Kinetic analysis provided evidence for high affinity for dCTP with template G, suggesting that the REV1 protein is specialized for dCTP and template G.	Deoxycytidine Monophosphate	43-47	REV1 DNA directed polymerase	Homo sapiens	22-26	
12044876-2	2002	We show that purified REV1 protein inserts dCMP opposite template G, A, T and C, and dGMP and dTMP opposite template G in the presence of magnesium, while in the presence of manganese the specificity for dCMP was found to be relaxed and the REV1 protein acquired the ability to insert dCMP, dGMP, dAMP and dTMP opposite templates G, A, T, and C. Kinetic analysis provided evidence for high affinity for dCTP with template G, suggesting that the REV1 protein is specialized for dCTP and template G.	Deoxycytidine Monophosphate	204-208	REV1 DNA directed polymerase	Homo sapiens	22-26	
12044876-2	2002	We show that purified REV1 protein inserts dCMP opposite template G, A, T and C, and dGMP and dTMP opposite template G in the presence of magnesium, while in the presence of manganese the specificity for dCMP was found to be relaxed and the REV1 protein acquired the ability to insert dCMP, dGMP, dAMP and dTMP opposite templates G, A, T, and C. Kinetic analysis provided evidence for high affinity for dCTP with template G, suggesting that the REV1 protein is specialized for dCTP and template G.	Deoxycytidine Monophosphate	204-208	REV1 DNA directed polymerase	Homo sapiens	22-26	
11917024-3	2002	Lacking a 3"-->5" proofreading exonuclease activity, purified human REV1 exhibited a DNA polymerase activity on a repeating template G sequence, but catalyzed nucleotide insertion with 6-fold lower efficiency opposite a template A and 19-27-fold lower efficiency opposite a template T or C. Furthermore, dCMP insertion was greatly preferred regardless of the specific template base.	Deoxycytidine Monophosphate	307-311	REV1 DNA directed polymerase	Homo sapiens	71-75	
11917024-4	2002	Human REV1 inserted a dCMP efficiently opposite a template 8-oxoguanine, (+)-trans-anti-benzo[a]pyrene-N2-dG, (-)-trans-anti-benzo[a]pyrene-N2-dG and 1,N6-ethenoadenine adducts, very inefficiently opposite an acetylaminofluorene-adducted guanine, but was unresponsive to a template TT dimer or TT (6-4) photoproduct.	Deoxycytidine Monophosphate	22-26	REV1 DNA directed polymerase	Homo sapiens	6-10	
11917024-6	2002	By combining the dCMP insertion activity of human REV1 with the extension synthesis activity of human polymerase kappa, bypass of the trans-anti-benzo[a]pyrene-N2-dG adducts and the 1,N6-ethenoadenine lesion was achieved by the two-polymerase two-step mechanism.	Deoxycytidine Monophosphate	17-21	REV1 DNA directed polymerase	Homo sapiens	50-54	
11917024-7	2002	These results suggest that human REV1 is a specialized DNA polymerase that may contribute to dCMP insertion opposite many types of DNA damage during lesion bypass.	Deoxycytidine Monophosphate	93-97	REV1 DNA directed polymerase	Homo sapiens	33-37	
10536157-7	1999	We show that the human REV1 protein is a dCMP transferase that specifically inserts a dCMP residue opposite a DNA template G. In addition, the human REV1 transferase is able to efficiently and specifically insert a dCMP opposite a DNA template apurinic/apyrimidinic (AP) site or a uracil residue.	Deoxycytidine Monophosphate	41-45	REV1 DNA directed polymerase	Homo sapiens	23-27	
10536157-7	1999	We show that the human REV1 protein is a dCMP transferase that specifically inserts a dCMP residue opposite a DNA template G. In addition, the human REV1 transferase is able to efficiently and specifically insert a dCMP opposite a DNA template apurinic/apyrimidinic (AP) site or a uracil residue.	Deoxycytidine Monophosphate	41-45	REV1 DNA directed polymerase	Homo sapiens	149-153	
10536157-7	1999	We show that the human REV1 protein is a dCMP transferase that specifically inserts a dCMP residue opposite a DNA template G. In addition, the human REV1 transferase is able to efficiently and specifically insert a dCMP opposite a DNA template apurinic/apyrimidinic (AP) site or a uracil residue.	Deoxycytidine Monophosphate	86-90	REV1 DNA directed polymerase	Homo sapiens	23-27	
10536157-7	1999	We show that the human REV1 protein is a dCMP transferase that specifically inserts a dCMP residue opposite a DNA template G. In addition, the human REV1 transferase is able to efficiently and specifically insert a dCMP opposite a DNA template apurinic/apyrimidinic (AP) site or a uracil residue.	Deoxycytidine Monophosphate	86-90	REV1 DNA directed polymerase	Homo sapiens	149-153	
11278384-8	2001	Therefore, the molecular mechanism of the dCMP transfer reaction of the REV1S protein and maybe also the REV1 protein might be the same as that of the dNTP transfer reaction of the translesion DNA polymerases.	Deoxycytidine Monophosphate	42-46	REV1 DNA directed polymerase	Homo sapiens	72-76