@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.}
}
@article {3478,
	title = {MODULATION OF TRANSCRIPTION FACTOR ETS-1 DNA-BINDING - DNA-INDUCED UNFOLDING OF AN ALPHA-HELIX},
	journal = {Science},
	volume = {269},
	number = {5232},
	year = {1995},
	note = {ISI Document Delivery No.: RX194Times Cited: 143Cited Reference Count: 49},
	month = {Sep},
	pages = {1866-1869},
	type = {Article},
	abstract = {Conformational changes, including local protein folding, play important roles in protein-DNA interactions. Here, studies of the transcription factor Ets-1 provided evidence that local protein unfolding also can accompany DNA binding. Circular dichroism and partial proteolysis showed that the secondary structure of the Ets-1 DNA-binding domain is unchanged in the presence of DNA. In contrast, DNA allosterically induced the unfolding of an cr helix that lies within a flanking region involved in the negative regulation of DNA binding. These findings suggest a structural basis for the intramolecular inhibition of DNA binding and a mechanism for the cooperative partnerships that are common features of many eukaryotic transcription factors.},
	keywords = {BASIC REGION, CRYSTAL-STRUCTURE, DOMAIN, FAMILY, GCN4, INDUCED CONFORMATIONAL CHANGE, PROTEIN-KINASES, REPRESSOR, SEQUENCE, SUBUNITS},
	isbn = {0036-8075},
	url = {<Go to ISI>://A1995RX19400036},
	author = {Petersen, J. M. and Skalicky, J. J. and Donaldson, L. W. and McIntosh, L. P. and Alber, T. and Graves, B. J.}
}
