@article {2658,
	title = {Composition of secondary alcohols, ketones, alkanediols, and ketols in Arabidopsis thaliana cuticular waxes},
	journal = {Journal of Experimental Botany},
	volume = {60},
	number = {6},
	year = {2009},
	note = {ISI Document Delivery No.: 437ZCTimes Cited: 0Cited Reference Count: 25Wen, Miao Jetter, Reinhard},
	month = {Apr},
	pages = {1811-1821},
	type = {Article},
	abstract = {Arabidopsis wax components containing secondary functional groups were examined (i) to test the biosynthetic relationship between secondary alcohols and ketols and (ii) to determine the regiospecificity and substrate preference of the enzyme involved in ketol biosynthesis. The stem wax of Arabidopsis wild type contained homologous series of C-27 to C-31 secondary alcohols (2.4 mu g cm(-2)) and C-28 to C-30 ketones (6.0 mu g cm(-2)) dominated by C-29 homologues. In addition, compound classes containing two secondary functional groups were identified as C-29 diols (similar to 0.05 mu g cm(-2)) and ketols (similar to 0.16 mu g cm(-2)). All four compound classes showed characteristic isomer distributions, with functional groups located between C-14 and C-16. In the mah1 mutant stem wax, diols and ketols could not be detected, while the amounts of secondary alcohols and ketones were drastically reduced. In two MAH1-overexpressing lines, equal amounts of C-29 and C-31 secondary alcohols were detected. Based on the comparison of homologue and isomer compositions between the different genotypes, it can be concluded that biosynthetic pathways lead from alkanes to secondary alcohols, and via ketones or diols to ketols. It seems plausible that MAH1 is the hydroxylase enzyme involved in all these conversions in Arabidopsis thaliana.},
	keywords = {BRASSICA-OLERACEA, chain lengths, CHROMATOGRAPHY, cytochrome P450, ECERIFERUM MUTANTS, EPICUTICULAR WAXES, fatty acid derivatives, GAS, HYDROXYLATION, LEAF WAXES, LEAVES, MAH1, MASS SPECTROMETRY, neutral lipids, plant surface composition, RESISTANT, ULTRASTRUCTURE, wax},
	isbn = {0022-0957},
	url = {<Go to ISI>://000265524400023},
	author = {Wen, M. and Jetter, R.}
}
@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.}
}
