@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 {1299,
	title = {Neopetrosiamides, peptides from the marine sponge Neopetrosia sp that inhibit amoeboid invasion by human tumor cells},
	journal = {Organic Letters},
	volume = {7},
	number = {19},
	year = {2005},
	note = {ISI Document Delivery No.: 964DETimes Cited: 11Cited Reference Count: 19},
	month = {Sep},
	pages = {4173-4176},
	type = {Article},
	abstract = {Neopetrosiamdes A (1) and B (2), two diastereomeric tricyclic peptides that inhibit amoeboid invasion of human tumor cells, have been isolated from the marine sponge Neopetrosia sp. collected in Papua New Guinea. The structures of the neopetrosiamides were elucidated by analysis of MS and NMR data and confirmed by chemical degradation.},
	keywords = {ANTI-INVASION, MIGRATION, PAPUA-NEW-GUINEA, PROLINE, PROTEOLYSIS, STRONGYLOPHORINE-26},
	isbn = {1523-7060},
	url = {<Go to ISI>://000231858100028},
	author = {Williams, D. E. and Austin, P. and Diaz-Marrero, A. R. and Van Soest, R. and Matainaho, T. and Roskelley, C. D. and Roberge, M. and Andersen, R. J.}
}
@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 {727,
	title = {The photochemistry of trans-1,4,4,4-tetraphenylbut-2-en-1-one: A highly efficient aryl migration (type B) enone photorearrangement},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {81},
	number = {6},
	year = {2003},
	note = {ISI Document Delivery No.: 706UATimes Cited: 0Cited Reference Count: 18},
	month = {Jun},
	pages = {705-708},
	type = {Article},
	abstract = {Photolysis of trans-1,4,4,4-tetraphenylbut-2-en-1-one (3) in acetonitrile or benzene leads to trans-cis isomerization (7) along with rearrangement to trans-1 -benzoyl-2,2,3-triphenylcyclopropane(8). Formation of the latter product represents a new example of the aryl migration (type B) enone photorearrangement reaction first reported by Zimmerman and co-workers for 4,4-diphenylcyclohex-2-en-1-one (1). The quantum yield in the case of enone 3 (0.4) is approximately 10 times greater than that for 4,4,-diphenylcyclohex-2-en-1-one, a result that is ascribed to steric acceleration of phenyl migration from the triphenylmethyl group plus greater resonance stabilization of the intermediate biradical.},
	keywords = {aryl migration, ASYMMETRIC INDUCTION, di-pi-methane, enone, EXPLORATORY ORGANIC PHOTOCHEMISTRY, MECHANISM, MIGRATION, PHENYL, PHOTOCHEMISTRY, PHOTOCYCLIZATION, REARRANGEMENT, STATE},
	isbn = {0008-4042},
	url = {<Go to ISI>://000184472400035},
	author = {Scheffer, J. R. and Vishnumurthy, K.}
}
@article {5179,
	title = {Inhibition of tumor cell invasion and angiogenesis by motuporamines},
	journal = {Cancer Research},
	volume = {61},
	number = {18},
	year = {2001},
	note = {ISI Document Delivery No.: 474LKTimes Cited: 41Cited Reference Count: 26},
	month = {Sep},
	pages = {6788-6794},
	type = {Article},
	abstract = {Tissue invasion is an important determinant of angiogenesis and metastasis and constitutes an attractive target for cancer therapy. We have developed an assay to identify agents that inhibit invasion by mechanisms other than inhibition of cell attachment or cytotoxicity. A screen of marine sponge extracts identified motuporamines as micromolar inhibitors of invasion of basement membrane gels by MDA-231 breast carcinoma, PC-3 prostate carcinoma, and U-87 and U-251 glioma cells. Motuporamine C inhibits cell migration in monolayer cultures and impairs actin-mediated membrane ruffling at the leading edge of lamellae. Motuporamine C also reduces beta1-integrin activation, raising the possibility that it interferes with "inside-out" signaling to integrins. In addition, motuporamine C inhibits angiogenesis in an in vitro sprouting assay with human endothelial cells and an in vivo chick chorioallantoic membrane assay. The motuporamines show little or no toxicity or inhibition of cell proliferation, and they are structurally simple and easy to synthesize, making them attractive drug candidates.},
	keywords = {CANCER, GTPASES, INTEGRINS, MIGRATION},
	isbn = {0008-5472},
	url = {<Go to ISI>://000171108400030},
	author = {Roskelley, C. D. and Williams, D. E. and McHardy, L. M. and Leong, K. G. and Troussard, A. and Karsan, A. and Andersen, R. J. and Dedhar, S. and Roberge, M.}
}
