@article {2137,
	title = {Synthesis and Enzymatic Incorporation of Modified Deoxyadenosine Triphosphates},
	journal = {European Journal of Organic Chemistry},
	number = {29},
	year = {2008},
	note = {ISI Document Delivery No.: 365YXTimes Cited: 7Cited Reference Count: 35Lam, Curtis Hipolito, Christopher Perrin, David M.},
	month = {Oct},
	pages = {4915-4923},
	type = {Article},
	abstract = {Several deoxyadenosine triphosphates containing modifications at the 8-position have been synthesized. Suitably protected 8-bromodeoxyadenosines were coupled with five imidazole-containing moieties by nucleophilic aromatic substitution or Sonagashira coupling to give modified nucleosides that were then triphosphorylated. Incorporation assays were performed for these modified residues with many commercially available DNA polymerases, and it was found that two of the modified dATPs could be effectively taken up as substrates by Sequenase V2.0. These two residues are candidates for substrates in combinatorial selections in the search for improved catalysis from DNAzymes. ((C) Wiley-VCH Verlag GmbH \& Co. KGaA, 69451 Weinheim, Germany, 2008)},
	keywords = {AMINO-ACID, bioorganic chemistry, CATALYTIC REPERTOIRE, CLEAVING DNA ENZYME, DERIVATIVES, DNA, ENZYMES, FUNCTIONALITIES, HETEROCYCLES, IN-VITRO SELECTION, NUCLEIC-ACIDS, nucleotides, OLIGONUCLEOTIDES, PCR, POLYMERASES, SELEX},
	isbn = {1434-193X},
	url = {<Go to ISI>://000260447200009},
	author = {Lam, C. and Hipolito, C. and Perrin,David M.}
}
@article {940,
	title = {Covalent Schiff base catalysis and turnover by a DNAzyme: A M2+ independent AP-endonuclease mimic},
	journal = {Journal of the American Chemical Society},
	volume = {126},
	number = {13},
	year = {2004},
	note = {ISI Document Delivery No.: 809LBTimes Cited: 44Cited Reference Count: 117},
	month = {Apr},
	pages = {4145-4156},
	type = {Review},
	abstract = {A DNAzyme, synthetically modified with both primary amines and imidazoles, is found to act as a M2+ -independent AP lyase-endonuclease. In the course of the cleavage reaction, this DNAzyme forms a covalent Schiff base intermediate with an abasic site on a complementary oligodeoxyribonucleotide. This intermediate, which is inferred from NaCNBH3 trapping as well as cyanide inhibition, does not evidently accumulate because the second step, dehydrophosphorylative elimination, is fast compared to Schiff base formation. The 5{\textquoteright}-product that remains linked to the catalyst hydrolyzes slowly to regenerate free catalyst. The use of duly modified DNAzymes to perform Schiff base catalysis demonstrates the value of modified nucleotides for enhancing the catalytic repertoire of nucleic acids. This work suggests that DNAzymes will be capable of catalyzing aldol condensation reactions.},
	keywords = {ALDEHYDIC ABASIC, APURINIC SITES, BETA-ELIMINATION, DIVALENT METAL-ION, FUNCTIONALITIES, IMIDAZOLYL, IN-VITRO SELECTION, NUCLEIC-ACIDS, RNA CLEAVAGE, SITES, TETRAHYMENA RIBOZYME, THERMOSTABLE DNA-POLYMERASES},
	isbn = {0002-7863},
	url = {<Go to ISI>://000220637100042},
	author = {May, J. P. and Ting, R. and Lermer, L. and Thomas, J. M. and Roupioz, Y. and Perrin,David M.}
}
@article {430,
	title = {Toward an RNaseA mimic: a DNAzyme with imidazoles and cationic amines},
	journal = {Journal of the American Chemical Society},
	volume = {124},
	number = {34},
	year = {2002},
	note = {ISI Document Delivery No.: 586GJTimes Cited: 41Cited Reference Count: 52},
	month = {Aug},
	pages = {9960-9961},
	type = {Article},
	keywords = {CATALYTIC REPERTOIRE, CATIONS, CLEAVING DNA ENZYME, FUNCTIONALITIES, HAMMERHEAD, IN-VITRO SELECTION, MONOVALENT, NUCLEIC-ACIDS, RIBOZYME, SEQUENCE-SPECIFIC CLEAVAGE, SITE-SPECIFIC CLEAVAGE},
	isbn = {0002-7863},
	url = {<Go to ISI>://000177576000001},
	author = {Lermer, L. and Roupioz, Y. and Ting, R. and Perrin,David M.}
}
