@article {1489,
	title = {Crystal structures of protein phosphatase-1 bound to motuporin and dihydromicrocystin-LA: Elucidation of the mechanism of enzyme inhibition by cyanobacterial toxins},
	journal = {Journal of Molecular Biology},
	volume = {356},
	number = {1},
	year = {2006},
	note = {ISI Document Delivery No.: 007AFTimes Cited: 17Cited Reference Count: 42},
	month = {Feb},
	pages = {111-120},
	type = {Article},
	abstract = {The microcystins and nodularins are tumour promoting hepatotoxins that are responsible for global adverse human health effects and wildlife fatalities in countries where drinking water supplies contain cyanobacteria. The toxins function by inhibiting broad specificity Ser/Thr protein phosphatases in the host cells, thereby disrupting signal transduction pathways. A previous crystal structure of a microcystin bound to the catalytic subunit of protein phosphatase-1 (PP-1c) showed distinct changes in the active site region when compared with protein phosphatase-1 structures bound to other toxins. We have elucidated the crystal structures of the cyanotoxins, motuporin (nodularin-V) and dihydromicrocystin-LA bound to human protein phosphatase-1c (gamma isoform). The atomic structures of these complexes reveal the structural basis for inhibition of protein phosphatases by these toxins. Comparisons of the structures of the cyanobacterial toxin:phosphatase complexes explain the biochemical mechanism by which microcystins but not nodularins permanently modify their protein phosphatase targets by covalent addition to an active site cysteine residue. (c) 2005 Elsevier Ltd. All rights reserved.},
	keywords = {CATALYTIC SUBUNIT, COMPLEX, crystal structure, cyanobacteria, IN-VIVO, microcystin, MICROCYSTIN-LR, MOLECULAR-MECHANISMS, nodularin, POTENT, PROGRAM, TUMOR-PROMOTER, TYPE-1},
	isbn = {0022-2836},
	url = {<Go to ISI>://000234938600010},
	author = {Maynes, J. T. and Luu, H. A. and Cherney, M. M. and Andersen, R. J. and Williams, D. and Holmes, C. F. B. and James, M. N. G.}
}
@article {558,
	title = {An NMR approach to structural proteomics},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {99},
	number = {4},
	year = {2002},
	note = {ISI Document Delivery No.: 524UKTimes Cited: 109Cited Reference Count: 28},
	month = {Feb},
	pages = {1825-1830},
	type = {Article},
	abstract = {The influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural proteomics of small proteins using NMR spectroscopy. Over 500 small proteins from several organisms were cloned, expressed, purified, and evaluated by NMIR. Although there was variability among proteomes, overall 20\% of these proteins were found to be readily amenable to NMR structure determination. NMIR sample preparation was centralized in one facility, and a distributive approach was used for NMR data collection and analysis. Twelve structures are reported here as part of this approach, which allowed us to infer putative functions for several conserved hypothetical proteins.},
	keywords = {ASSIGNMENTS, CATH, DOMAIN, PROGRAM, PROTEINS, SPECTRA},
	isbn = {0027-8424},
	url = {<Go to ISI>://000174031100016},
	author = {Yee, A. and Chang, X. Q. and Pineda-Lucena, A. and Wu, B. and Semesi, A. and Le, B. and Ramelot, T. and Lee, G. M. and Bhattacharyya, S. and Gutierrez, P. and Denisov, A. and Lee, C. H. and Cort, J. R. and Kozlov, G. and Liao, J. and Finak, G. and Chen, L. and Wishart, D. and Lee, W. and McIntosh, L. P. and Gehring, K. and Kennedy, M. A. and Edwards, A. M. and Arrowsmith, C. H.}
}
@article {7283,
	title = {COMPLEXATION OF IRON WITH THE ORALLY ACTIVE DECORPORATION DRUG-L1 (3-HYDROXY-1,2-DIMETHYL-4-PYRIDINONE)},
	journal = {Clinical Chemistry},
	volume = {38},
	number = {4},
	year = {1992},
	note = {ISI Document Delivery No.: HN921Times Cited: 18Cited Reference Count: 37},
	month = {Apr},
	pages = {562-565},
	type = {Note},
	abstract = {{The stability constants for the Fe(III) complexes of the orally active iron decorporation drug L1 (3-hydroxy-1,2-dimethyl-4-pyridinone) have been determined by potentiometric titration [glass electrode, 25.0-degrees-C},
	keywords = {2-DIMETHYL-3-HYDROXYPYRID-4-ONE L1, aluminum, CHELATOR 1, CHEMISTRY, DESFERRIOXAMINE, EQUILIBRIUM, gallium, HETEROAROMATIC CHELATORS, IRON OVERLOAD, IRON-BINDING DRUGS, LONG-TERM TRIAL, MOBILIZATION, POTENTIOMETRIC TITRATION, PROGRAM},
	isbn = {0009-9147},
	url = {<Go to ISI>://A1992HN92100022},
	author = {Kline, M. A. and Orvig, Chris}
}
