@article {2147,
	title = {Identification of the wax ester synthase/acyl-coenzyme A: Diacylglycerol acyltransferase WSD1 required for stem wax ester biosynthesis in Arabidopsis},
	journal = {Plant Physiology},
	volume = {148},
	number = {1},
	year = {2008},
	note = {ISI Document Delivery No.: 344SMTimes Cited: 16Cited Reference Count: 52Li, Fengling Wu, Xuemin Lam, Patricia Bird, David Zheng, Huanquan Samuels, Lacey Jetter, Reinhard Kunst, Ljerka},
	month = {Sep},
	pages = {97-107},
	type = {Article},
	abstract = {Wax esters are neutral lipids composed of aliphatic alcohols and acids, with both moieties usually long-chain (C-16 and C-18) or very-long-chain (C-20 and longer) carbon structures. They have diverse biological functions in bacteria, insects, mammals, and terrestrial plants and are also important substrates for a variety of industrial applications. In plants, wax esters are mostly found in the cuticles coating the primary shoot surfaces, but they also accumulate to high concentrations in the seed oils of a few plant species, including jojoba (Simmondsia chinensis), a desert shrub that is the major commercial source of these compounds. Here, we report the identification and characterization of WSD1, a member of the bifunctional wax ester synthase/diacylglycerol acyltransferase gene family, which plays a key role in wax ester synthesis in Arabidopsis (Arabidopsis thaliana) stems, as first evidenced by severely reduced wax ester levels of in the stem wax of wsd1 mutants. In vitro assays using protein extracts from Escherichia coli expressing WSD1 showed that this enzyme has a high level of wax synthase activity and approximately 10-fold lower level of diacylglycerol acyltransferase activity. Expression of the WSD1 gene in Saccharomyces cerevisiae resulted in the accumulation of wax esters, but not triacylglycerol, indicating that WSD1 predominantly functions as a wax synthase. Analyses of WSD1 expression revealed that this gene is transcribed in flowers, top parts of stems, and leaves. Fully functional yellow fluorescent protein-tagged WSD1 protein was localized to the endoplasmic reticulum, demonstrating that biosynthesis of wax esters, the final products of the alcohol-forming pathway, occurs in this subcellular compartment.},
	keywords = {ABC, CLONING, CONDENSING ENZYME, ELONGATION, GENE-EXPRESSION, PLANT CUTICULAR WAXES, SURFACES, THALIANA, TRANSFORMATION, TRANSGENIC ARABIDOPSIS, TRANSPORTER},
	isbn = {0032-0889},
	url = {<Go to ISI>://000258947600010},
	author = {Li, F. and Wu, X. and Lam, P. and Bird, D. and Zheng, H. and Samuels, L. and Jetter, R. and Kunst, L.}
}
@article {697,
	title = {Activation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin},
	journal = {Febs Letters},
	volume = {552},
	number = {2-3},
	year = {2003},
	note = {ISI Document Delivery No.: 726DKTimes Cited: 15Cited Reference Count: 23},
	month = {Sep},
	pages = {82-85},
	type = {Article},
	abstract = {Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 resolution in the presence of Ca2+ ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca2+ sites occupied. Neither actin nor the type-1 Ca2+, which normally is sandwiched between actin and G4, is required to achieve this conformation. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.},
	keywords = {actin, calcium-activation, COMPLEX, DOMAINS, F-ACTIN, gelsolin, PLASMA GELSOLIN, REGULATORY PROTEIN, TRANSFORMATION},
	isbn = {0014-5793},
	url = {<Go to ISI>://000185583000002},
	author = {Narayan, K. and Chumnarnsilpa, S. and Choe, H. and Irobi, E. and Urosev, D. and Lindberg, U. and Schutt, C. E. and Burtnick, L. D. and Robinson, R. C.}
}
@article {572,
	title = {New okadaic acid analogues from the marine sponge Merriamum oxeato and their effect on mitosis},
	journal = {Journal of Natural Products},
	volume = {66},
	number = {6},
	year = {2003},
	note = {ISI Document Delivery No.: 695CYTimes Cited: 4Cited Reference Count: 25},
	month = {Jun},
	pages = {838-843},
	type = {Article},
	abstract = {Inhibitors of the G2 DNA damage checkpoint can selectively sensitize cancer cells with impaired p53 tumor suppressor activity to killing by DNA-damaging drugs or ionizing radiation and have been proposed as a promising therapeutic strategy. An extract from the Northeastern Pacific marine sponge Merriamum. oxeato showed G2 checkpoint inhibitory activity, and fractionation identified the known dinoflagellate toxin dinophysistoxin 1 (1) and the two novel analogues 27-O-acetylokadaic acid (2) and 27-O-acetyldinophysistoxin 1 (3) as the active compounds. The mixture of 1, 2, and 3 was extremely potent at inhibiting the G2 checkpoint (IC50 = 1 ng/mL) and cellular protein Ser/Thr phosphatases (IC50 = 1 ng/mL), and it radiosensitized MCF-7 breast cancer cells expressing mutated p53 at all concentrations tested. However, the mixture of 1, 2, and 3 was also very toxic to cells not exposed to DNA damage (IC50 = 1 ng/mL), making these compounds poor candidates for therapeutic agents to augment the effectiveness of DNA-damaging therapies.},
	keywords = {CELL-CYCLE CHECKPOINTS, DNA-DAMAGE CHECKPOINT, ELUCIDATION, INHIBITION, ISOGRANULATIMIDE, P53, PROTEIN-KINASES, TRANSFORMATION},
	isbn = {0163-3864},
	url = {<Go to ISI>://000183814600019},
	author = {Britton, R. and Roberge, M. and Brown, C. and Van Soest, R. and Andersen, R. J.}
}
