@article {2525,
	title = {Detection and assignment of phosphoserine and phosphothreonine residues by C-13-P-31 spin-echo difference NMR spectroscopy},
	journal = {Journal of Biomolecular Nmr},
	volume = {43},
	number = {1},
	year = {2009},
	note = {ISI Document Delivery No.: 379QKTimes Cited: 0Cited Reference Count: 31McIntosh, Lawrence P. Kang, Hyun-Seo Okon, Mark Nelson, Mary L. Graves, Barbara J. Brutscher, Bernhard},
	month = {Jan},
	pages = {31-37},
	type = {Article},
	abstract = {A simple NMR method is presented for the identification and assignment of phosphorylated serine and threonine residues in C-13- or C-13/N-15-labeled proteins. By exploiting modest (similar to 5 Hz) 2- and 3-bond C-13-P-31 scalar couplings, the aliphatic H-1-C-13 signals from phosphoserines and phosphothreonines can be detected selectively in a P-31 spin-echo difference constant time H-1-C-13 HSQC spectrum. Inclusion of the same P-31 spin-echo element within the C-13 frequency editing period of an intraHNCA or HN(CO)CA experiment allows identification of the amide H-1(N) and N-15 signals of residues (i) for which C-13(alpha)(i) or C-13(alpha)(i - 1), respectively, are coupled to a phosphate. Furthermore, P-31 resonance assignments can be obtained by applying selective low power cw P-31 decoupling during the spin-echo period. The approach is demonstrated using a PNT domain containing fragment of the transcription factor Ets-1, phosphorylated in vitro at Thr38 and Ser41 with the MAP kinase ERK2.},
	keywords = {ASSIGNMENT, CENTER-DOT-OP, CONSTANT-TIME, Ets-1, MAP kinase, NUCLEIC-ACIDS, OP HYDROGEN-BONDS, P-31-C-13 scalar coupling, Phosphoprotein, PHOSPHORYLATION, POINTED DOMAIN, PROTEIN, QUANTITATIVE J-CORRELATION, RESONANCE, SCALAR COUPLINGS, TRANSCRIPTION FACTOR},
	isbn = {0925-2738},
	url = {<Go to ISI>://000261411100004},
	author = {McIntosh, L. P. and Kang, H. S. and Okon, M. and Nelson, M. L. and Graves, B. J. and Brutscher, B.}
}
@article {2438,
	title = {A DNAzyme with Three Protein-Like Functional Groups: Enhancing Catalytic Efficiency of M2+-Independent RNA Cleavage},
	journal = {Chembiochem},
	volume = {10},
	number = {12},
	year = {2009},
	note = {ISI Document Delivery No.: 487MWTimes Cited: 5Cited Reference Count: 76Hollenstein, Marcel Hipolito, Christopher J. Lam, Curtis H. Perrin, David M.},
	month = {Aug},
	pages = {1988-1992},
	type = {Article},
	keywords = {BEACON SENSOR, biology, CLEAVING DNA ENZYME, CYTOSOLIC FREE MAGNESIUM, DEOXYRIBOZYMES, DNAzymes, enzyme catalysis, EVOLUTION, HAIRPIN RIBOZYME, HIGH-DENSITY, IN-VITRO SELECTION, ION, nucleic acids, NUCLEIC-ACIDS, RNAse A mimics, synthetic},
	isbn = {1439-4227},
	url = {<Go to ISI>://000269279700012},
	author = {Hollenstein, M. and Hipolito, C. J. and Lam, C. H. and Perrin,David M.}
}
@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 {1007,
	title = {High affinity DNAzyme-based ligands for transition metal cations - a prototype sensor for Hg2+},
	journal = {Organic \& Biomolecular Chemistry},
	volume = {2},
	number = {3},
	year = {2004},
	note = {ISI Document Delivery No.: 776YCTimes Cited: 32Cited Reference Count: 47},
	month = {Feb},
	pages = {307-312},
	type = {Article},
	abstract = {Inspired by recent interest in DNAzymes as transition metal ion sensors, a survey of the effects of various transition metals on the intramolecular cleavage rate of an imidazole modified, M2+-independent, self-cleaving "9(25)-11" DNA is reported. In particular, 9(25)-11 activity was strongly inhibited by Hg2+ (K-d(APP) = 110 +/- 9 nM). It is postulated that the affinity and selectivity of 9(25)-11 for Hg2+ stems from the fact that this synthetically modified DNAzyme contains imidazoles. This study demonstrates the utility of modified nucleotides in developing DNAzyme sensors for metals ions, especially those for which unmodified nucleic acids might not serve as inherently good ligands.},
	keywords = {2-STEP MECHANISM, BIOSENSOR, CATALYTIC REPERTOIRE, CLEAVING DNA ENZYME, IMIDAZOLYL FUNCTIONALITIES, MERCURIC ION, MERCURY(II), NUCLEIC-ACIDS, NUCLEOSIDES, SELECTION},
	isbn = {1477-0520},
	url = {<Go to ISI>://000189146100008},
	author = {Thomas, J. M. and Ting, R. and Perrin,David M.}
}
@article {1016,
	title = {Selection and characterization of DNAzymes with synthetically appended functionalities: A case of a synthetic RNaseA mimic},
	journal = {Pure and Applied Chemistry},
	volume = {76},
	number = {7-8},
	year = {2004},
	note = {ISI Document Delivery No.: 855WQTimes Cited: 1Cited Reference Count: 7039th IUPAC Congress/86th Conference of the Canadian-Society-for-ChemistryAUG 10-15, 2003Ottawa, CANADACanadian Soc Chem, Natl Res Council Canada, Int Union Pure \& Appl Chem},
	month = {Jul-Aug},
	pages = {1571-1577},
	type = {Proceedings Paper},
	abstract = {We have been interested in merging synthetic nucleotide chemistry with combinatorial selection of DNAzymes to deliver a more complete (and complex) chemical complement to the catalytic repertoire of nucleic acids. Thus we ask, what do modified dNTPs really bring to nucleic acids in terms of an increased repertoire? In asking this question, we have looked first at conditions, and more recently for reaction classes where nucleic acids are found to be catalytically inefficient, deficient, or at least to date, seemingly incapable of certain functions. A case of this is M2+-independent ribophosphodiester hydrolysis at physiological pH and low ionic strength where nucleic acids exhibit especially low rate constants for self-cleavage and seem to be incapable of turnover.},
	keywords = {CATALYTIC, CLEAVING DNA ENZYME, DIVALENT METAL-ION, IMIDAZOLYL FUNCTIONALITIES, IN-VITRO SELECTION, MONOVALENT CATIONS, NUCLEIC-ACIDS, NUCLEOSIDE 5{\textquoteright}-TRIPHOSPHATES, REPERTOIRE, SEQUENCE-SPECIFIC CLEAVAGE, SITE-SPECIFIC CLEAVAGE},
	isbn = {0033-4545},
	url = {<Go to ISI>://000224006000028},
	author = {Ting, R. and Lermer, L. and Thomas, J. and Roupioz, Y. and Perrin,David M.}
}
@article {1017,
	title = {Substrate specificity and kinetic framework of a DNAzyme with an expanded chemical repertoire: a putative RNaseA mimic that catalyzes RNA hydrolysis independent of a divalent metal cation},
	journal = {Nucleic Acids Research},
	volume = {32},
	number = {22},
	year = {2004},
	note = {ISI Document Delivery No.: 887METimes Cited: 24Cited Reference Count: 71},
	pages = {6660-6672},
	type = {Article},
	abstract = {This work addresses the binding, cleavage and dissociation rates for the substrate and products of a synthetic RNaseA mimic that was combinatorially selected using chemically modified nucleoside triphosphates. This trans-cleaving DNAzyme, 9(25)-11t, catalyzes sequence-specific ribophosphodiester hydrolysis in the total absence of a divalent metal cation, and in low ionic strength at pH 7.5 and in the presence of EDTA. It is the first such sequence capable of multiple turnover. 9(25)-11t consists of 31 bases, 18 of which form a catalytic domain containing 4 imidazole and 6 allylamino modified nucleotides. This sequence cleaves the 15 nt long substrate, S1, at one embedded ribocytosine at the eighth position to give a 5{\textquoteright}-product terminating in a 2{\textquoteright},3{\textquoteright}-phosphodiester and a 3{\textquoteright}-product terminating in a 5{\textquoteright}-OH. Under single turnover conditions at 24degreesC, 9(25)-11t displays a maximum first-order rate constant, k(cat), of 0.037 min(-1) and a catalytic efficiency, k(cat)/K-m, of 5.3 x 10(5) M-1 min(-1). The measured value of k(cat) under catalyst excess conditions agrees with the value of k(cat) observed for steady-state multiple turnover, implying that slow product release is not rate limiting with respect to multiple turnover. The substrate specificity of 9(25)-11t was gauged in terms of k(cat) values for substrate sequence variants. Base substitutions on the scissile ribose and at the two bases immediately downstream decrease k(cat) values by a factor of 4 to 250, indicating that 9(25)-11t displays significant sequence specificity despite the lack of an apparent Watson-Crick base-pairing scheme for recognition.},
	keywords = {CATIONS, CLEAVING DNA ENZYME, CYTOSOLIC FREE MAGNESIUM, HAIRPIN RIBOZYME CLEAVAGE, HAMMERHEAD, IMIDAZOLYL FUNCTIONALITIES, IN-VITRO SELECTION, MONOVALENT, NUCLEIC-ACIDS, NUCLEOSIDE TRIPHOSPHATES, SEQUENCE-SPECIFIC CLEAVAGE},
	isbn = {0305-1048},
	url = {<Go to ISI>://000226309400036},
	author = {Ting, R. and Thomas, J. M. and Lermer, L. and Perrin,David M.}
}
@article {429,
	title = {Incorporation of 8-histaminyldeoxyadenosine [8-(2-(4-imidazolyl)ethylamino)-2 {\textquoteright}-deoxyriboadenosine] into oligodeoxyribonucleotides by solid phase phosphoramidite coupling},
	journal = {Nucleosides Nucleotides \& Nucleic Acids},
	volume = {21},
	number = {10},
	year = {2002},
	note = {ISI Document Delivery No.: 622CATimes Cited: 5Cited Reference Count: 37},
	pages = {651-664},
	type = {Article},
	abstract = {The 3{\textquoteright} phosphoramidite of 8-histaminyl deoxyadenosine has been prepared and successfully incorporated into a short oligodeoxyribonucleotide. The synthetic methodology leading to this preparation is given and the implications for developing new DNAzymes as well as probing unusual nucleic acid structures are discussed.},
	keywords = {BEARING IMIDAZOLE, CATALYTIC REPERTOIRE, CLEAVAGE, DERIVATIVES, DNA, IMIDAZOLYL FUNCTIONALITIES, NUCLEIC-ACIDS, OLIGONUCLEOTIDES, RIBONUCLEASES, RNA},
	isbn = {1525-7770},
	url = {<Go to ISI>://000179627900003},
	author = {Lermer, L. and Hobbs, J. 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.}
}
@article {4554,
	title = {Computational prediction of the enantioselectivity of a solid-state photoreaction},
	journal = {Organic Letters},
	volume = {1},
	number = {8},
	year = {1999},
	note = {ISI Document Delivery No.: 281QKTimes Cited: 8Cited Reference Count: 26},
	month = {Oct},
	pages = {1279-1281},
	type = {Article},
	abstract = {[GRAPHICS] To better understand the forces controlling chemical reactions in crystals, the absolute asymmetric photorearrangement of 4-m-chlorobenzyloxy-2-pyridone leading to the corresponding enantiomerically enriched (78\% ee) beta-lactam was modeled computationally using a flexible minilattice consisting of a central reactant and 20 nearest and 72 next-nearest neighbors. The computational results predicted a preference for formation of the (R,R)-enantiomer, and this was verified experimentally by absolute configuration correlation studies.},
	keywords = {ABSOLUTE ASYMMETRIC-SYNTHESIS, CRYSTAL LATTICES, FORCE-FIELD, MEDIA, MODEL, MOLECULAR MECHANICS, NUCLEIC-ACIDS, PHOTOCHEMISTRY, PROTEINS},
	isbn = {1523-7060},
	url = {<Go to ISI>://000085172100037},
	author = {Garcia-Garibay, M. A. and Houk, K. N. and Keating, A. E. and Cheer, C. J. and Leibovitch, M. and Scheffer, J. R. and Wu, L. C.}
}
