@article {2389,
	title = {Cytotoxicity of the traditional chinese medicine (TCM) plumbagin in its copper chemistry},
	journal = {Dalton Transactions},
	number = {48},
	year = {2009},
	note = {ISI Document Delivery No.: 527IETimes Cited: 3Cited Reference Count: 96Chen, Zhen-Feng Tan, Ming-Xiong Liu, Li-Min Liu, Yan-Cheng Wang, Heng-Shan Yang, Bin Peng, Yan Liu, Hua-Gang Liang, Hong Orvig, Chris},
	pages = {10824-10833},
	type = {Article},
	abstract = {The anticancer traditional Chinese medicine (TCM), plumbagin (PLN), was isolated from Plumbago Zeylanica. Reaction of plumbagin with Cu-II salt, afforded [Cu(PLN)(2)]center dot 2H(2)O (1). With 2,2{\textquoteright}-bipyridine (bipy) as a co-ligand, PLN reacts with Cu-II to give [Cu(PLN)(bipy)(H2O)](2)(NO3)(2)center dot 4H(2)O (2). 1 and 2 were characterized by elemental analysis, IR, ESI-MS spectra. Their crystal structures were determined by single crystal X-ray diffraction methods. The in vitro cytotoxicity of PLN, 1 and 2 against seven human tumour cell lines was assayed. The metal-based compounds exhibit enhanced cytotoxicity vs. that of free PLN, suggesting that these compounds display synergy in the combination of metal ions with PLN. The binding properties of PLN, 1 and 2 to DNA were investigated through UV-vis, fluorescence, CD spectra, and gel mobility shift assay, which indicated that 1 and 2 were non-covalent binding and mainly intercalated the neighboring base pairs of DNA. PLN, 1 and 2 exhibit inhibition activity to topoisomerase I (TOPO I), but 1 and 2 were more effective than PLN.},
	keywords = {BIOLOGICAL-ACTIVITY, CALF-THYMUS DNA, CANCER-CELLS, CRYSTAL-STRUCTURE, DNA CLEAVAGE ACTIVITY, IRON(II) COMPLEXES, METAL-COMPLEXES, N-PROPYL-NORFLOXACIN, PLATINUM ANTICANCER AGENTS, TOPOISOMERASE-I},
	isbn = {1477-9226},
	url = {<Go to ISI>://000272359900024},
	author = {Chen, Z. F. and Tan, M. X. and Liu, L. M. and Liu, Y. C. and Wang, H. S. and Yang, B. and Peng, Y. and Liu, H. G. and Liang, H. and Orvig, Chris}
}
@article {4600,
	title = {Methylarsenicals and arsinothiols are potent inhibitors of mouse liver thioredoxin reductase},
	journal = {Chemical Research in Toxicology},
	volume = {12},
	number = {10},
	year = {1999},
	note = {ISI Document Delivery No.: 248DFTimes Cited: 114Cited Reference Count: 64},
	month = {Oct},
	pages = {924-930},
	type = {Article},
	abstract = {Thioredoxin reductase (TR, EC 1.6.4.5) was purified 5800-fold from the livers of adult male B6C3F1 mice. The estimated molecular mass of the purified protein was about 57 kDa, The activity of the purified enzyme was monitored by the NADPH-dependent reduction of 5,5{\textquoteright}-dithiobis(2-nitrobenzoic acid) (DTNB); this activity was fully inhibited by 1 mu M aurothioglucose. Arsenicals and arsinothiols, complexes of As-III-containing compounds with L-cysteine or glutathione, were tested as inhibitors of the DTNB reductase activity of the purified enzyme. Pentavalent arsenicals were much less potent inhibitors than trivalent arsenicals. Among all the arsenicals, CH3AsIII was the most potent inhibitor of TR. CH3AsIII was found to be a competitive inhibitor of the reduction of DTNB (K-i similar to 100 nM) and a noncompetitive inhibitor of the oxidation of NADPH. The inhibition of TR by CH3AsIII was time-dependent and could not be reversed by the addition of a dithiol-containing molecule, 2,3-dimercaptosuccinic acid, to the reaction mixture. The inhibition of TR by CH3AsIII required the simultaneous presence of NADPH in the reaction mixture. However, unlike other pyridine nucleotide disulfide oxidoreductases, there was no evidence that mouse liver TR was inactivated by exposure to NADPH. Treatment with CH3AsIII did not increase the NADPH oxidase activity of the purified enzyme. Thus, CH3AsIII, a putative intermediate in the pathway for the biomethylation of As, is a potent and irreversible inhibitor of an enzyme involved in the response of the cell to oxidative stress.},
	keywords = {ARSENATE REDUCTASE, CANCER-CELLS, ENDOTHELIAL-CELLS, ESCHERICHIA-COLI, GLUTATHIONE-REDUCTASE, KAPPA-B ACTIVATION, LIPOAMIDE DEHYDROGENASE, MAMMALIAN THIOREDOXIN, MULTI-ENZYME COMPLEX, RABBIT ERYTHROCYTES},
	isbn = {0893-228X},
	url = {<Go to ISI>://000083259500008},
	author = {Lin, S. and Cullen, W. R. and Thomas, D. J.}
}
