@article {2277,
	title = {Phosphorylation of U24 from Human Herpes Virus type 6 (HHV-6) and its potential role in mimicking myelin basic protein (MBP) in multiple sclerosis},
	journal = {Febs Letters},
	volume = {582},
	number = {18},
	year = {2008},
	note = {ISI Document Delivery No.: 332UKTimes Cited: 2Cited Reference Count: 31Tait, Andrew R. Straus, Suzana K.},
	month = {Aug},
	pages = {2685-2688},
	type = {Article},
	abstract = {Myelin basic protein (MBP) from multiple sclerosis ( MS) patients contains lower levels of phosphorylation at Thr97 than normal individuals. The significance of phosphorylation at this site is not fully understood, but it is proposed to play a role in the normal functioning of MBP. Human Herpesvirus Type 6 encodes the protein U24, which has tentatively been implicated in the pathology of MS. U24 shares a 7 amino acid stretch encompassing the Thr97 phosphorylation site of MBP: PRTPPPS. We demonstrate using a combination of mass spectrometry, thin layer chromatography and autoradiography, that U24 can be phosphorylated at the equivalent threonine. Phospho-U24 may confound signalling or other pathways in which phosphorylated MBP may participate, precipitating a pathological process.},
	keywords = {BINDING, EXPRESSION, HUMAN-HERPESVIRUS-6, IDENTIFICATION, KINASE, MEMBRANE MICRODOMAINS, mimicry, myelin, PHOSPHORYLATION, POSTTRANSLATIONAL MODIFICATIONS, SITE, T-ANTIGEN, U24},
	isbn = {0014-5793},
	url = {<Go to ISI>://000258108400002},
	author = {Tait, A. R. and Straus, S. K.}
}
@article {1378,
	title = {Avinosol, a meroterpenoid-nucleoside conjugate with antiinvasion activity isolated from the marine sponge Dysidea sp},
	journal = {Organic Letters},
	volume = {8},
	number = {17},
	year = {2006},
	note = {ISI Document Delivery No.: 072EJTimes Cited: 10Cited Reference Count: 18Diaz-Marrero, Ana R. Austin, Pamela Van Soest, Rob Matainaho, Teatulohi Roskelley, Calvin D. Roberge, Michel Andersen, Raymond J.},
	month = {Aug},
	pages = {3749-3752},
	type = {Article},
	abstract = {The new meroterpenoids avinosol (1),3 {\textquoteright}-aminoavarone (2), and 3 {\textquoteright}-phenethylaminoavarone (3) have been isolated from the marine sponge Dysidea sp. collected in Papua New Guinea, and their structures were elucidated by analysis of spectroscopic data. Avinosol (1), which is apparently the first example of a naturally occurring meroterpenoid-nucleoside conjugate, showed antiinvasion activity in a cell-based assay.},
	keywords = {ANTI-INVASION, AVAROL, INHIBITOR, KINASE, MIGRATION, PROTEOLYSIS, SESQUITERPENE QUINONES, STRESS FIBERS, STRONGYLOPHORINE-26, TUMOR-CELL INVASION},
	isbn = {1523-7060},
	url = {<Go to ISI>://000239655500033},
	author = {Diaz-Marrero, A. R. and Austin, P. and Van Soest, R. and Matainaho, T. and Roskelley, C. D. and Roberge, M. and Andersen, R. J.}
}
@article {1271,
	title = {Modulation of the G(2) cell cycle checkpoint by sesquiterpene lactones psilostachyins A and C isolated from the common ragweed Ambrosia artemisiifolia},
	journal = {Planta Medica},
	volume = {71},
	number = {10},
	year = {2005},
	note = {ISI Document Delivery No.: 985TLTimes Cited: 8Cited Reference Count: 30},
	month = {Oct},
	pages = {938-943},
	type = {Article},
	abstract = {A phenotypic cell-based assay for inhibitors of the G(2) DNA damage checkpoint was used to screen plant extracts from the US National Cancer Institute Natural Products Repository. It revealed activity in a methanol extract from the common ragweed Ambrosia artemisiifolia. Assay-guided fractionation led to the identification of the sesquiterpene lactones psilostachyins A and C as novel checkpoint inhibitors. Elimination of their alpha,beta-unsaturated carbonyl group caused a loss of activity, suggesting that the compounds can bind covalently to target proteins through Michael addition. Psilostachyins A and C also blocked cells in mitosis and caused the formation of aberrant microtubule spindles. However, the compounds did not interfere with microtubule polymerization in vitro. The related sesquiterpene lactones psilostachyin 13, paulitin and isopaulitin were also isolated from the same extract but showed no checkpoint inhibition. The identification of the target(s) of psilostachyins A and C may provide further insight into the signalling pathways involved in cell cycle arrest and mitotic progression.},
	keywords = {Ambrosia artemisiffolia, CAFFEINE, CANCER, cell cycle, checkpoint, CHK1, DILACTONE, DNA-DAMAGE CHECKPOINT, G(2) phase, INHIBITION, KINASE, MCF-7 CELLS, mitosis, P53, PROTEIN, UCN-01},
	isbn = {0032-0943},
	url = {<Go to ISI>://000233401400009},
	author = {Sturgeon, C. M. and Craig, K. and Brown, C. and Rundle, N. T. and Andersen, R. J. and Roberge, M.}
}
@article {1198,
	title = {Strongylophorine-26, a Rho-dependent inhibitor of tumor cell invasion that reduces actin stress fibers and induces nonpolarized lamellipodial extensions},
	journal = {Molecular Cancer Therapeutics},
	volume = {4},
	number = {5},
	year = {2005},
	note = {ISI Document Delivery No.: 926DETimes Cited: 6Cited Reference Count: 37},
	month = {May},
	pages = {772-778},
	type = {Article},
	abstract = {Strongylophorine-26, a new meroditerpenoid, was recently identified as an inhibitor of cancer cell invasion. This study was undertaken to characterize its mechanism of action. We find that strongylophorine-26 inhibits the motility of MDA-MB-231 breast carcinoma cells on a plastic surface. Upon addition of strongylophorine-26, rapid cell contraction and depolarization occurred, followed by spreading and flattening of the entire cell. Treated cells exhibited increased membrane ruffling throughout and extended lamellipodia in all directions. Strongylophorine-26 induced a decrease in actin stress fibers, a dramatic increase in the size and number of focal adhesions, and the appearance of a dense meshwork of actin filaments around the cell periphery. Strongylophorine-26 caused a transient activation of the small GTPase Rho and treatment with the Rho inhibitor C3 exoenzyme abrogated the anti-invasive activity of strongylophorine-26. These effects are distinct from those of many motility and angiogenesis inhibitors that seem to act by a common mechanism involving the induction of actin stress fibers. This difference in mechanism of action sets strongylophorine-26 apart as an experimental anticancer agent and indicates that pharmacologic inhibition of cell migration may be achieved by mechanisms not involving the stabilization of actin stress fibers.},
	keywords = {ACTIVATION, ANGIOGENESIS, CYTOSKELETON, FAMILY, FOCAL ADHESIONS, KINASE, MIGRATION, MOTILITY, PROTEIN, SMALL GTPASE},
	isbn = {1535-7163},
	url = {<Go to ISI>://000229102300009},
	author = {McHardy, L. M. and Warabi, K. and Andersen, R. J. and Roskelley, C. D. and Roberge, M.}
}
@article {950,
	title = {Identification and mechanism of a bacterial hydrolyzing UDP-N-acetylglucosamine 2-epimerase},
	journal = {Biochemistry},
	volume = {43},
	number = {44},
	year = {2004},
	note = {ISI Document Delivery No.: 868UVTimes Cited: 13Cited Reference Count: 38},
	month = {Nov},
	pages = {14290-14298},
	type = {Article},
	abstract = {This paper reports the first identification of a fully functional hydrolyzing UDP-N-acetylglucosamine 2-epimerase from a bacterial source. The epimerase (known as SiaA or NeuC from Neisseria meningitidis MC58 group B is shown to catalyze the conversion of UDP-GlcNAc into ManNAc and UDP in the first step of sialic acid (N-acetylneuraminic acid) biosynthesis. The mechanism is proposed to involve an anti elimination of UDP to form 2-acetamidoglucal as an intermediate, followed by the syn addition of water. The observation that the alpha-anomer of ManNAc is the true product and that solvent deuterium is incorporated at C-2 is consistent with this mechanism. The use of the O-18-labeled substrate confirms that the overall hydrolysis reaction proceeds via cleavage of the C-O bond. Furthermore, the putative intermediate 2-acetamidoglucal is shown to serve as a catalytically competent substrate and is enzymatically hydrated to give ManNAc exclusively. Isotope effect studies show that cleavage of the C-H bond is not rate limiting during catalysis. Mutagenesis studies show that three active site carboxylate residues are crucial for catalysis. In two of the mutants that were studied (E122Q and D131N), 2-acetamidoglucal was released from the active site during catalysis, providing direct evidence that the enzyme is capable of catalyzing the anti elimination of UDP from UDP-GlcNAc.},
	keywords = {2-EPIMERASE/N-ACETYLMANNOSAMINE, biosynthesis, CELL-INTERACTIONS, ENZYME, ESCHERICHIA-COLI K1, KINASE, POLYSIALIC ACID, PURIFICATION, RAT-LIVER, SIALIC-ACID, STEREOCHEMISTRY},
	isbn = {0006-2960},
	url = {<Go to ISI>://000224939400045},
	author = {Murkin, A. S. and Chou, W. K. and Wakarchuk, W. W. and Tanner, M. E.}
}
@article {941,
	title = {The tumor invasion inhibitor dihydromotuporamine C activates RHO, remodels stress fibers and focal adhesions, and stimulates sodium-proton exchange},
	journal = {Cancer Research},
	volume = {64},
	number = {4},
	year = {2004},
	note = {ISI Document Delivery No.: 778MKTimes Cited: 23Cited Reference Count: 45},
	month = {Feb},
	pages = {1468-1474},
	type = {Article},
	abstract = {The motuporamines are macrocyclic alkaloids that inhibit tumor cell invasion by an, as yet, unknown mechanism. A structure-activity study recently identified dihydromotuporamine C (dhMotC) as a highly active and readily synthesized analogue. Here, we show that dhMotC causes subtle cytoskeletal alterations in highly invasive MDA231 breast tumor cells that include an increase in the thickness and number of cytoplasmic actin stress fibers. Experiments with serum-starved Swiss 3T3 fibroblasts showed that micromolar concentrations of dhMotC that inhibit tumor cell invasion induce the formation of new stress fibers and large focal adhesion complexes that are dispersed around the entire cell periphery. dhMotC treatment of Swiss 3T3 cells also initiates a strong, long-lived activation of the small GTP-binding protein Rho, and it stimulates Rho kinase-dependent sodium-proton exchanger activity. Liposome-mediated cell loading of C3 exoenzyme prevents dhMotC-mediated Rho activation and stress fiber formation in 3T3 cells. C3 exoenzyme loading also reestablishes elongated MDA231 breast tumor cell invasion in the presence of dhMotC. Taken together, these results indicate that the ability to activate Rho is one important determinant of the anti-invasive activity of dhMotC.},
	keywords = {ANGIOGENESIS, CANCER, CELL-MIGRATION, FARNESYLTRANSFERASE INHIBITORS, GROWTH, GTP-BINDING PROTEIN, GTPASES, KINASE, MEMBRANE PROTRUSION, PROGRESSION},
	isbn = {0008-5472},
	url = {<Go to ISI>://000189245200037},
	author = {McHardy, L. M. and Sinotte, R. and Troussard, A. and Sheldon, C. and Church, J. and Williams, D. E. and Andersen, R. J. and Dedhar, S. and Roberge, M. and Roskelley, C. D.}
}
@article {480,
	title = {Oligomerization-dependent association of the SAM domains from Schizosaccharomyces pombe Byr2 and Ste4},
	journal = {Journal of Biological Chemistry},
	volume = {277},
	number = {42},
	year = {2002},
	note = {ISI Document Delivery No.: 605EATimes Cited: 21Cited Reference Count: 46},
	month = {Oct},
	pages = {39585-39593},
	type = {Article},
	abstract = {SAM (sterile alpha motif) domains are protein-protein interaction modules found in a large number of regulatory proteins. Byr2 and Ste4 are two SAM domain-containing proteins in the mating pheromone response pathway of the fission yeast, Schizosaccharomyces pombe. Byr2 is a mitogen-activated protein kinase kinase kinase that is regulated by Ste4. Tu et al (Tu, H., Barr, M., Dong, D. L., and Wigler, M. (1997) Mol. Cell. Biol. 17, 5876-5887) showed that the isolated SAM domain of Byr2 binds a fragment of Ste4 that contains both a leucine zipper (Ste4-LZ) domain as well as a SAM domain, suggesting that Byr2-SAM and Ste4-SAM may form a hetero-oligomer. Here, we show that the individual SAM domains of Ste4 and Byr2 are monomeric at low concentrations and bind to each other in a 1:1 stoichiometry with a relatively weak dissociation constant of 56 +/- 3 mum. Inclusion of the Ste4-LZ domain, which determines the oligomeric state of Ste4, has a dramatic effect on binding affinity, however. We find that the Ste4-LZ domain is trimeric and, when included with the Ste4-SAM domain, yields a 3:1 Ste4-LZ-SAM:Byr2-SAM complex with a tight dissociation constant of 19 +/- 4 nm. These results suggest that the Ste4-LZ-SAM protein may recognize multiple binding sites on Byr2-SAM, indicating a new mode of oligomeric organization for SAM domains. The fact that high affinity binding occurs only with the addition of an oligomerization domain suggests that it may be necessary to include ancillary oligomerization modules when searching for binding partners of SAM domains.},
	keywords = {CRYSTAL-STRUCTURE, HUMAN LEUKEMIA, IDENTIFICATION, KINASE, LAC REPRESSOR, PROTEIN-KINASE, RECEPTOR, TEL, TRANSCRIPTION FACTOR, TYROSINE, YEAST},
	isbn = {0021-9258},
	url = {<Go to ISI>://000178662500069},
	author = {Ramachander, R. and Kim, C. A. and Phillips, M. L. and Mackereth, C. D. and Thanos, C. D. and McIntosh, L. P. and Bowie, J. U.}
}
@article {5208,
	title = {Sugar nucleotide-modifying enzymes},
	journal = {Current Organic Chemistry},
	volume = {5},
	number = {2},
	year = {2001},
	note = {ISI Document Delivery No.: 411FKTimes Cited: 12Cited Reference Count: 170},
	month = {Feb},
	pages = {169-192},
	type = {Review},
	abstract = {Sugar nucleotides serve as the activated forms of carbohydrates that are used in a wide range of biosynthetic pathways. Instead of building up the sugar nucleotide from the free sugar itself, nature often chooses to modify the "donor" portion of a pre-existing sugar nucleotide in a biosynthetically efficient manner. In doing so a rich variety of catalytic strategies are employed and this review focuses on recent mechanistic and structural studies of the sugar nucleotide-modifying enzymes. The review is organized around the types of reactions catalyzed and contains the following sections: Epimerases/Mutases/Decarboxylases, Eliminations and Substitutions, Oxidation and Reduction, and Substitutions on the Periphery of Sugar Nucleotides.},
	keywords = {4, 6-DEHYDRATASE, 6-DIDEOXYHEXOSES, ACETYLGLUCOSAMINE 2-EPIMERASE/N-ACETYLMANNOSAMINE, ACETYLNEURAMINIC ACID, biosynthesis, CYTIDINE DIPHOSPHATE 3, D-GLUCOSE, ESCHERICHIA-COLI K-12, FIRST 2, GDP-FUCOSE SYNTHETASE, KINASE, N-ACETYLGLUCOSAMINE, SITE-DIRECTED MUTAGENESIS, STEPS, UDP-GALACTOSE 4-EPIMERASE},
	isbn = {1385-2728},
	url = {<Go to ISI>://000167487300004},
	author = {Tanner, M. E.}
}
@article {3690,
	title = {Characterization of the potent insulin mimetic agent bis(maltolato)oxovanadium(IV) (BMOV) in solution by EPR spectroscopy},
	journal = {Inorganic Chemistry},
	volume = {35},
	number = {22},
	year = {1996},
	note = {ISI Document Delivery No.: VP449Times Cited: 63Cited Reference Count: 48},
	month = {Oct},
	pages = {6507-6512},
	type = {Article},
	abstract = {{Bis(maltolato)oxovanadium(IV) (abbreviated BMOV or VO(ma)(2)) has been characterized by electron paramagnetic resonance (EPR) spectroscopy in CH2Cl2, H2O, MeOH, and pyridine at both room and low temperatures. Spin Hamiltonian parameters for mono- and bis(maltolato)oxovanadium(IV) complexes [VO(ma)](+) (=[VO(ma)(H2O)(n)](+)},
	keywords = {ADIPOCYTES, CHEMISTRY, DIABETIC RATS, ELECTRON-PARAMAGNETIC-RES, FUTURE, GLUCOSE, KINASE, MIMICS, SULFATE, treatment, VANADYL COMPLEXES},
	isbn = {0020-1669},
	url = {<Go to ISI>://A1996VP44900022},
	author = {Hanson, G. R. and Sun, Y. and Orvig, Chris}
}
@article {3827,
	title = {Oxidation kinetics of the potent insulin mimetic agent bis(maltolato)oxovanadium(IV) (BMOV) in water and in methanol},
	journal = {Inorganic Chemistry},
	volume = {35},
	number = {6},
	year = {1996},
	note = {ISI Document Delivery No.: UA169Times Cited: 58Cited Reference Count: 45},
	month = {Mar},
	pages = {1667-1673},
	type = {Article},
	abstract = {{The kinetics of oxidation of bis(maltolato)oxovanadium(IV), BMOV or VO(ma)(2), by dioxygen have been studied by UV-vis spectroscopy in both MeOH and H2O media. The VO(ma)(2):O-2 stoichiometry was 4:1. In aqueous solution, the pH-dependeut rate of the VO(ma)(2)/O-2 reaction to generate cis-[VO2(ma)(2)](-) is attributed to the deprotonation of coordinated H2O, the deprotonated species [VO(ma)(2)(OH)](-) being more easily oxidized (k(OH) = 0.39 M(-1) s(-1), 25 degrees C) than the neutral form VO(ma)(2)(H2O) (k(H2O) = 0.08 M(-1) s(-1), 25 degrees C). The activation parameters for the two second-order reactions in aqueous solution were deduced from variable temperature kinetic measurements. In MeOH, VO(ma)(2) was oxidized by dioxygen to cis-VO(OMe)(ma)(2), whose structure was characterized by single-crystal X-ray diffraction; the crystals were monoclinic, C2/c, with a = 28.103(1) Angstrom},
	keywords = {ANATION, AQUEOUS-SOLUTION, COMPLEXES, CYSTEINE, KINASE, RAT ADIPOCYTES, VANADYL TREATMENT},
	isbn = {0020-1669},
	url = {<Go to ISI>://A1996UA16900042},
	author = {Sun, Y. and James, Brian R. and Rettig, S. J. and Orvig, Chris}
}
@article {3827,
	title = {Oxidation kinetics of the potent insulin mimetic agent bis(maltolato)oxovanadium(IV) (BMOV) in water and in methanol},
	journal = {Inorganic Chemistry},
	volume = {35},
	number = {6},
	year = {1996},
	note = {ISI Document Delivery No.: UA169Times Cited: 58Cited Reference Count: 45},
	month = {Mar},
	pages = {1667-1673},
	type = {Article},
	abstract = {{The kinetics of oxidation of bis(maltolato)oxovanadium(IV), BMOV or VO(ma)(2), by dioxygen have been studied by UV-vis spectroscopy in both MeOH and H2O media. The VO(ma)(2):O-2 stoichiometry was 4:1. In aqueous solution, the pH-dependeut rate of the VO(ma)(2)/O-2 reaction to generate cis-[VO2(ma)(2)](-) is attributed to the deprotonation of coordinated H2O, the deprotonated species [VO(ma)(2)(OH)](-) being more easily oxidized (k(OH) = 0.39 M(-1) s(-1), 25 degrees C) than the neutral form VO(ma)(2)(H2O) (k(H2O) = 0.08 M(-1) s(-1), 25 degrees C). The activation parameters for the two second-order reactions in aqueous solution were deduced from variable temperature kinetic measurements. In MeOH, VO(ma)(2) was oxidized by dioxygen to cis-VO(OMe)(ma)(2), whose structure was characterized by single-crystal X-ray diffraction; the crystals were monoclinic, C2/c, with a = 28.103(1) Angstrom},
	keywords = {ANATION, AQUEOUS-SOLUTION, COMPLEXES, CYSTEINE, KINASE, RAT ADIPOCYTES, VANADYL TREATMENT},
	isbn = {0020-1669},
	url = {<Go to ISI>://A1996UA16900042},
	author = {Sun, Y. and James, Brian R. and Rettig, S. J. and Orvig, Chris}
}
