@article {2660,
	title = {Pyrodysinoic Acid Derivatives from the Marine Sponge Dysidea robusta},
	journal = {Journal of Natural Products},
	volume = {72},
	number = {9},
	year = {2009},
	note = {ISI Document Delivery No.: 507LSTimes Cited: 1Cited Reference Count: 30Williams, David E. Marques, Suzi O. Hajdu, Eduardo Peixinho, Solange Andersen, Raymond J. Berlinck, Roberto G. S.},
	month = {Sep},
	pages = {1691-1694},
	type = {Article},
	abstract = {Three new nitrogen-containing terpenes related to pyrodysinoic acid (1) have been isolated from the sponge Dysidea robusta collected in Brazil. Isopyrodysinoic acid (2), 13-hydroxyisopyrodysinoic acid (3), and pyrodysinoic acid B (4) were obtained from the crude extract of D. robusta and identified by analysis of spectroscopic data. Pyrodysinoic acid B (4) is the first furodysin or furodysinin sesquiterpene derivative with a trans junction between the two six-membered rings of the 1,2,3,4,4a,7,8,8a-octahydro-1,1,6-trimethylnaphthalene moiety.},
	keywords = {AMINO-ACID, biosynthesis, CELLULAR-ORIGIN, DENDROLASIN, DYSIHERBAINE, GENUS DYSIDEA, HERBACEA, METABOLITES, NATURAL-PRODUCTS, SESQUITERPENES},
	isbn = {0163-3864},
	url = {<Go to ISI>://000270855600026},
	author = {Williams, D. E. and Marques, S. O. and Hajdu, E. and Peixinho, S. and Andersen, R. J. and Berlinck, R. G. S.}
}
@article {2235,
	title = {Sintokamides A to E, Chlorinated Peptides from the Sponge Dysidea sp that Inhibit Transactivation of the N-Terminus of the Androgen Receptor in Prostate Cancer Cells},
	journal = {Organic Letters},
	volume = {10},
	number = {21},
	year = {2008},
	note = {ISI Document Delivery No.: 367EETimes Cited: 10Cited Reference Count: 23Sadar, Marianne D. Williams, David E. Mawji, Nasrin R. Patrick, Brian O. Wikanta, Thamrin Chasanah, Ekowati Irianto, Hari Eko Van Soest, Rob Andersen, Raymond J.},
	month = {Nov},
	pages = {4947-4950},
	type = {Article},
	abstract = {The new chlorinated peptides sintokamides A to E (1-5) have been isolated from specimens of the marine sponge Dysidea sp. collected in Indonesia. Their structures were elucidated by a combination of spectroscopic and single-crystal X-ray diffraction analyses. Sintokamide A (1) is an inhibitor of N-terminus transactivation of the androgen receptor in prostate cancer cells.},
	keywords = {AMINO-ACID, BARBAMIDE, biosynthesis, CYANOBACTERIUM, DOMAIN, HERBACEA, METABOLITES},
	isbn = {1523-7060},
	url = {<Go to ISI>://000260534500060},
	author = {Sadar, M. D. and Williams, D. E. and Mawji, N. R. and Patrick, B. O. and Wikanta, T. and Chasanah, E. and Irianto, H. E. and Van Soest, R. and Andersen, R. J.}
}
@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 {459,
	title = {Control of enantioselectivity in the photochemical conversion of alpha-oxoamides into beta-lactam derivatives},
	journal = {Organic Letters},
	volume = {4},
	number = {9},
	year = {2002},
	note = {ISI Document Delivery No.: 545XYTimes Cited: 19Cited Reference Count: 34},
	month = {May},
	pages = {1443-1446},
	type = {Article},
	abstract = {[GRAPHIC] Several approaches to asymmetric induction in the alpha-oxoamide (1) to beta-lactam (2) photorearrangement are described. Best results are obtained via irradiation of ionic and covalent chiral auxiliary-containing reactants in the crystalline state and in the interior supercages of zeolites.},
	keywords = {AMINO-ACID, ASYMMETRIC INDUCTION, CATION-PI INTERACTIONS, CRYSTALLINE STATE, GAS-PHASE, GEOMETRIC REQUIREMENTS, II, PHOTOCYCLIZATION, REACTIONS, SOLID-STATE PHOTOCHEMISTRY, ZWITTERIONS},
	isbn = {1523-7060},
	url = {<Go to ISI>://000175243900009},
	author = {Natarajan, A. and Wang, K. and Ramamurthy, V. and Scheffer, J. R. and Patrick, B.}
}
@article {4447,
	title = {Pre-steady state kinetic analysis of an enzymatic reaction monitored by time-resolved electrospray ionization mass spectrometry},
	journal = {Biochemistry},
	volume = {37},
	number = {21},
	year = {1998},
	note = {ISI Document Delivery No.: ZR717Times Cited: 73Cited Reference Count: 53},
	month = {May},
	pages = {7664-7669},
	type = {Article},
	abstract = {For the first time, the new technique of time-resolved electrospray ionization mass spectrometry (ESI-MS) has been used to accurately measure the pre-steady state kinetics of an enzymatic reaction by monitoring a transient enzyme intermediate. The enzyme used to illustrate this approach, Bacillus circulans xylanase, is a retaining glycosidase that hydrolyzes xylan or beta-xylobiosides through a double-displacement mechanism involving a covalent xylobiosyl-enzyme intermediate. A low steady state level of this intermediate formed during the hydrolysis of 2,5-dinitrophenyl beta-D-xylobioside was detected by time-resolved ESI-MS. The low concentration of this intermediate and its rate of formation did not permit pre-steady state kinetic analysis. By contrast, the covalent intermediate accumulates fully when the Tyr80Phe mutant hydrolyzes the same substrate. Using time-resolved ESI-MS, the pre-steady state kinetic parameters for the formation of the covalent intermediate in the mutant xylanase have been determined. The kinetic data are in agreement with those determined by monitoring the release of 2,5-dinitrophenol with stopped-flow W-vis spectroscopy. This demonstrates that time-resolved ESI-MS can be used to accurately monitor the pre-steady state kinetics of enzymatic reactions, with the advantage of identifying transient enzyme intermediates by their mass.},
	keywords = {ACTIVE-SITE NUCLEOPHILE, AMINO-ACID, BACILLUS-CIRCULANS XYLANASE, beta-glucosidase, CELLULASES, CYTOCHROME-C, GAS-PHASE, IDENTIFICATION, inhibitors, MECHANISMS},
	isbn = {0006-2960},
	url = {<Go to ISI>://000074006700002},
	author = {Zechel, D. L. and Konermann, L. and Withers, S. G. and Douglas, D. J.}
}
@article {3800,
	title = {Secondary structure and NMR assignments of Bacillus circulans xylanase},
	journal = {Protein Science},
	volume = {5},
	number = {6},
	year = {1996},
	note = {ISI Document Delivery No.: UP617Times Cited: 23Cited Reference Count: 74},
	month = {Jun},
	pages = {1118-1135},
	type = {Article},
	abstract = {Bacillus circulans xylanase (BCX) is a member of the family of low molecular weight endo-beta-(1,4)-xylanases. The main-chain H-1, C-13, and N-15 resonances of this 20.4-kDa enzyme were assigned using heteronuclear NMR experiments recorded on a combination of selectively and uniformly labeled protein samples. Using chemical shift, NOE, J coupling, and amide hydrogen exchange information, 14 beta-strands, arranged in a network of three beta-sheets, and a single cy-helix were identified in BCX. The NMR-derived secondary structure and beta-sheet topology agree closely with that observed in the crystal structure of this protein. The H-N of Ile 118 has a strongly upfield-shifted resonance at 4.03 ppm, indicative of a potential amide-aromatic hydrogen bond to the indole ring of Trp 71. This interaction, which is conserved in all low molecular weight xylanases of known structure, may play an important role in establishing the active site conformation of these enzymes. Following hen egg white and bacteriophage T4 lysozymes, B. circulans xylanase represents the third family of beta-glycanases for which extensive NMR assignments have been reported. These assignments provide the background for detailed studies of the mechanism of carbohydrate recognition and hydrolysis by this bacterial xylanase.},
	keywords = {amide-aromatic hydrogen bond, AMINO-ACID, ASSIGNMENTS, BACKBONE AMIDE, beta-glycanase, C-13-LABELED PROTEINS, C-ALPHA, chemical shift index, CHEMICAL-SHIFTS, COUPLING-CONSTANTS, LARGER PROTEINS, NMR, NUCLEAR-MAGNETIC-RESONANCE, SECONDARY STRUCTURE, SIDE-CHAIN RESONANCES, SOLVENT, SUPPRESSION, XYLANASE},
	isbn = {0961-8368},
	url = {<Go to ISI>://A1996UP61700014},
	author = {Plesniak, L. A. and Wakarchuk, W. W. and McIntosh, L. P.}
}
@inbook {3468,
	title = {VANADIUM COMPOUNDS AS INSULIN MIMICS},
	booktitle = {Metal Ions in Biological Systems, Vol 31},
	series = {Metal Ions in Biological Systems},
	volume = {31},
	year = {1995},
	note = {ISI Document Delivery No.: BD60ZTimes Cited: 106Cited Reference Count: 126Review270 MADISON AVE, NEW YORK, NY 10016},
	pages = {575-594},
	publisher = {Marcel Dekker},
	organization = {Marcel Dekker},
	address = {New York},
	keywords = {AMINO-ACID, ANTIOXIDANT STATUS, BLOOD-GLUCOSE, GLYCOGEN-SYNTHASE, INSULINOMIMETIC AGENTS, LEVELS, ORAL VANADYL, RECEPTOR TYROSINE KINASE, SKELETAL-MUSCLE, STREPTOZOTOCIN-DIABETIC RATS, VANADATE TREATMENT},
	isbn = {0161-5149},
	url = {<Go to ISI>://A1995BD60Z00017},
	author = {Orvig, Chris and Thompson, K. H. and Battell, M. and McNeill, J. H.}
}
