@article {1148,
	title = {Ceratamines, structurally simple microtubule-stabilizing antimitotic agents with unusual cellular effects},
	journal = {Cancer Research},
	volume = {65},
	number = {8},
	year = {2005},
	note = {ISI Document Delivery No.: 916ZFTimes Cited: 14Cited Reference Count: 9},
	month = {Apr},
	pages = {3040-3043},
	type = {Article},
	abstract = {Ceratamine A and ceratamine B are heterocyclic alkaloids recently identified in a screen for compounds that arrest cells in mitosis. Treatment of breast carcinoma MCF-7 cells causes a concentration-dependent block of cell cycle progression exclusively at mitosis. In vitro studies with purified tubulin indicate that the ceratamines directly stimulate microtubule polymerization in the absence of microtubule-associated proteins. Cells treated with ceratamines show a dense perinuclear microtubule network in interphase and multiple pillar-like tubulin structures in mitotic cells. The ceratamines do not compete with paclitaxel for binding to microtubules in vitro. Unlike other microtubule-stabilizing agents, the ceratamines have simple structures with no chiral centers, making them attractive drug leads.},
	keywords = {BIND, CELLS, RESISTANT, TAXOID SITE, TUBULIN},
	isbn = {0008-5472},
	url = {<Go to ISI>://000228424800012},
	author = {Karjala, G. and Chan, Q. and Manzo, E. and Andersen, R. J. and Roberge, N.}
}
@article {1032,
	title = {Boneratamides A-C, new sesquiterpenoids isolated from the marine sponge Axinyssa aplysinoides},
	journal = {Journal of Natural Products},
	volume = {67},
	number = {10},
	year = {2004},
	note = {ISI Document Delivery No.: 865MRTimes Cited: 4Cited Reference Count: 14},
	month = {Oct},
	pages = {1752-1754},
	type = {Article},
	abstract = {Three new sesquiterpenoids, boneratamides A (1)-C (3), have been isolated as their methyl esters 4-6 from extracts of the marine sponge Axinyssa aplysinoides collected in Indonesia. The structures of methyl esters 4-6 were elucidated by analysis of spectroscopic data and confirmed by single-crystal X-ray diffraction analysis of 4.},
	keywords = {AGENT, ANALOGS, BINDING, HEMIASTERLIN, NATURAL-PRODUCTS, PACLITAXEL, TUBULIN},
	isbn = {0163-3864},
	url = {<Go to ISI>://000224707700025},
	author = {Williams, D. E. and Patrick, B. O. and Tahir, A. and Van Soest, R. and Roberge, M. and Andersen, R. J.}
}
@article {769,
	title = {Spirastrellolide A, an antimitotic macrolide isolated from the Caribbean Marine Sponge Spirastrella Coccinea},
	journal = {Journal of the American Chemical Society},
	volume = {125},
	number = {18},
	year = {2003},
	note = {ISI Document Delivery No.: 675FLTimes Cited: 52Cited Reference Count: 14},
	month = {May},
	pages = {5296-5297},
	type = {Article},
	keywords = {AGENTS, PACLITAXEL, PEPTIDES, TUBULIN},
	isbn = {0002-7863},
	url = {<Go to ISI>://000182682700025},
	author = {Williams, D. E. and Roberge, M. and Van Soest, R. and Andersen, R. J.}
}
@article {701,
	title = {Synthesis and antimitotic/cytotoxic activity of hemiasterlin analogues},
	journal = {Journal of Natural Products},
	volume = {66},
	number = {2},
	year = {2003},
	note = {ISI Document Delivery No.: 652JHTimes Cited: 45Cited Reference Count: 37},
	month = {Feb},
	pages = {183-199},
	type = {Article},
	abstract = {The antimitotic sponge tripeptide hemiasterlin (1) and a number of structural analogues have been synthesized and evaluated in cell-based assays for both cytotoxic and antimitotic activity in order to explore the SAR for this promising anticancer drug lead. One synthetic analogue, SPA110 (8), showed more potent in vitro cytotoxicty and antimitotic activity than the natural product hemiasterlin (1), and consequently it has been subjected to thorough preclinical evaluation and targeted for clinical evaluation. The details of the synthesis of hemiasterlin (1) and the analogues and a discussion of how their biological activities vary with their structures are presented in this paper.},
	keywords = {(-)-HEMIASTERLIN, AGENTS, ALPHA-AMINO-ACIDS, ASYMMETRIC-SYNTHESIS, AZIDATION, CYTOTOXIC PEPTIDES, ELEUTHEROBIN, TRIPEPTIDE, TUBULIN},
	isbn = {0163-3864},
	url = {<Go to ISI>://000181375700005},
	author = {Nieman, J. A. and Coleman, J. E. and Wallace, D. J. and Piers, E. and Lim, L. Y. and Roberge, M. and Andersen, R. J.}
}
@article {5024,
	title = {Synthetic transformations of eleutherobin reveal new features of its microtubule-stabilizing pharmacophore},
	journal = {Journal of the American Chemical Society},
	volume = {123},
	number = {35},
	year = {2001},
	note = {ISI Document Delivery No.: 467XNTimes Cited: 21Cited Reference Count: 13},
	month = {Sep},
	pages = {8632-8633},
	type = {Article},
	keywords = {AGENTS, COMMON PHARMACOPHORE, PACLITAXEL, TAXOL, TUBULIN},
	isbn = {0002-7863},
	url = {<Go to ISI>://000170729200037},
	author = {Britton, R. and De Silva, E. D. and Bigg, C. M. and McHardy, L. M. and Roberge, M. and Andersen, R. J.}
}
@article {4775,
	title = {Antimitotic diterpenes from Erythropodium caribaeorum test pharmacophore models for microtubule stabilization},
	journal = {Organic Letters},
	volume = {2},
	number = {3},
	year = {2000},
	note = {ISI Document Delivery No.: 282UXTimes Cited: 36Cited Reference Count: 17},
	month = {Feb},
	pages = {257-260},
	type = {Article},
	abstract = {[GRAPHICS] Six new antimitotic diterpenes, 2-7, have been isolated from the Caribbean octocoral Erythropodium caribaeorum, Structural variations encountered in this group of natural products test recently proposed pharmacophore models for microtubule stabilizing compounds.},
	keywords = {AGENTS, ELEUTHEROBIN, TAXOL, TUBULIN},
	isbn = {1523-7060},
	url = {<Go to ISI>://000085238900007},
	author = {Cinel, B. and Roberge, M. and Behrisch, H. and van Ofwegen, L. P. and Castro, C. B. and Andersen, R. J.}
}
@article {3876,
	title = {Cytotoxic peptides hemiasterlin, hemiasterlin A and hemiasterlin B induce mitotic arrest and abnormal spindle formation},
	journal = {Cancer Chemotherapy and Pharmacology},
	volume = {39},
	number = {3},
	year = {1997},
	note = {ISI Document Delivery No.: VZ251Times Cited: 66Cited Reference Count: 17},
	month = {Jan},
	pages = {223-226},
	type = {Article},
	abstract = {Purpose: Hemiasterlin, hemiasterlin A and hemiasterlin B are newly isolated cytotoxic tripeptides with potential as antitumor drugs. We wished to determine their mechanism of cytotoxicity. Methods: We studied their effect on cell survival, cell cycle progression, and microtubule morphology in MCF-7 human mammary carcinoma cells. Results: At the nanomolar concentrations at which they were cytotoxic, the peptides induced arrest in mitotic metaphase. Hemiasterlin A produced abnormal mitotic spindles like those produced by the microtubule inhibitors taxol, nocodazole and vinblastine at low concentrations. At high concentrations hemiasterlin A did not cause microtubule bundling like taxol, but caused microtubule depolymerization like nocodazole and vinblastine. Conclusions: The hemiasterlins probably exert their cytotoxic effect by inhibiting spindle microtubule dynamics.},
	keywords = {CANCER, COLCHICINE SITE, FOSTRIECIN, INHIBITION, microtubules, mitosis, NATURAL-PRODUCTS, OKADAIC ACID, PHOSPHATASE-2A, PODOPHYLLOTOXIN, TAXOL, TUBULIN, VINBLASTINE, VINCA DOMAIN},
	isbn = {0344-5704},
	url = {<Go to ISI>://A1997VZ25100008},
	author = {Anderson, H. J. and Coleman, J. E. and Andersen, R. J. and Roberge, M.}
}
