"58362" . "1433-7851" . "1"^^ . . "7-Aryl-7-deazaadenine 2 '-Deoxyribonucleoside Triphosphates (dNTPs): Better Substrates for DNA Polymerases than dATP in Competitive Incorporations" . "RIV/00216208:11310/14:10271951!RIV15-MSM-11310___" . . . . "Hocek, Michal" . "I, P(GBP206/12/G151)" . "http://dx.doi.org/10.1002/anie.201404742" . "10.1002/anie.201404742" . . . "29" . . . "4"^^ . "7-Aryl-7-deazaadenine 2 '-Deoxyribonucleoside Triphosphates (dNTPs): Better Substrates for DNA Polymerases than dATP in Competitive Incorporations" . "7-Aryl-7-deazaadenine 2 '-Deoxyribonucleoside Triphosphates (dNTPs): Better Substrates for DNA Polymerases than dATP in Competitive Incorporations"@en . "Kielkowski, Pavel" . . . "7-Aryl-7-deazaadenine 2 '-Deoxyribonucleoside Triphosphates (dNTPs): Better Substrates for DNA Polymerases than dATP in Competitive Incorporations"@en . "Angewandte Chemie - International Edition" . . . "[4602A9F9CDBA]" . . "53" . "11310" . "DE - Spolkov\u00E1 republika N\u011Bmecko" . . "A series of 7-substituted 7-deazaadenine and 5-substituted cytosine 2'-deoxyribonucleoside triphosphates (dNTPs) were tested for their competitive incorporations (in the presence of dATP and dCTP) into DNA by several DNA polymerases by using analysis based on cleavage by restriction endonucleases. 7-Aryl-7-deazaadenine dNTPs were more efficient substrates than dATP because of their higher affinity for the active site of the enzyme, as proved by kinetic measurements and calculations."@en . "000339564800025" . "RIV/00216208:11310/14:10271951" . "nucleotides; nucleoside triphosphates; kinetics; enzymes; DNA"@en . . "Fanfrl\u00EDk, Jind\u0159ich" . "A series of 7-substituted 7-deazaadenine and 5-substituted cytosine 2'-deoxyribonucleoside triphosphates (dNTPs) were tested for their competitive incorporations (in the presence of dATP and dCTP) into DNA by several DNA polymerases by using analysis based on cleavage by restriction endonucleases. 7-Aryl-7-deazaadenine dNTPs were more efficient substrates than dATP because of their higher affinity for the active site of the enzyme, as proved by kinetic measurements and calculations." . "3"^^ . . . .