PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 11917024-0 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 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 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 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