@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 {1373,
	title = {Recent approaches to the construction of 1-azaspiro[4.5]decanes and related 1-azaspirocycles},
	journal = {Tetrahedron},
	volume = {62},
	number = {15},
	year = {2006},
	note = {ISI Document Delivery No.: 027TBTimes Cited: 25Cited Reference Count: 147},
	month = {Apr},
	pages = {3467-3492},
	type = {Review},
	keywords = {3 degrees carbon center, AROMATIC PI-NUCLEOPHILE, azaspirocyclic ring systems, DIELS-ALDER REACTION, DIPOLAR CYCLOADDITION ROUTES, FORMAL TOTAL-SYNTHESIS, HYPERVALENT, IMMUNOSUPPRESSANT FR901483, IODINE OXIDATION, MARINE ALKALOID LEPADIFORMINE, N-ACYLNITRENIUM IONS, OXIDATIVE RADICAL CYCLIZATION, POTENT, RING-CLOSING METATHESIS, spirocycles},
	isbn = {0040-4020},
	url = {<Go to ISI>://000236437400001},
	author = {Dake, G. R.}
}
@article {1369,
	title = {Synthetic ventures inspired by biosynthetic hypotheses: the evolution of a method for the oxidative amidation of phenols},
	journal = {Tetrahedron},
	volume = {62},
	number = {22},
	year = {2006},
	note = {ISI Document Delivery No.: 045ONTimes Cited: 22Cited Reference Count: 141Ciufolini, Marco A. Canesi, Sylvain Ousmer, Malika Braun, Norbert A.},
	month = {May},
	pages = {5318-5337},
	type = {Review},
	abstract = {We describe the development of a technique for the oxidative conversion of 4-alkyl phenols to derivatives of the corresponding 4-alkyl-4-amino-2,5-cyclohexanediones. This transformation, which was inspired by biogenetic considerations, constitutes a key step in the total syntheses of FR-901483, TAN-1251C, and cylindricine C. (c) 2006 Elsevier Ltd. All rights reserved.},
	keywords = {ALPHA-AMINO-ALDEHYDES, AROMATIC-SUBSTITUTION, ASCIDIAN CLAVELINA-CYLINDRICA, ELECTROPHILIC, HIGH ENANTIOMERIC EXCESS, HYPERVALENT IODINE OXIDATION, IMMUNOSUPPRESSANT FR901483, MANNICH CYCLIZATION APPROACH, MARINE ALKALOIDS, N-ACYLNITRENIUM IONS, NITROGEN HETEROCYCLIC-COMPOUNDS, POTENT, TRICYCLIC},
	isbn = {0040-4020},
	url = {<Go to ISI>://000237751500016},
	author = {Ciufolini,Marco A. and Canesi, S. and Ousmer, M. and Braun, N. A.}
}
@article {4156,
	title = {C-14-Labeled microcystin-LR administered to Atlantic salmon via intraperitoneal injection provides in vivo evidence for covalent binding of microcystin-LR in salmon livers},
	journal = {Toxicon},
	volume = {35},
	number = {6},
	year = {1997},
	note = {ISI Document Delivery No.: XG731Times Cited: 32Cited Reference Count: 18},
	month = {Jun},
	pages = {985-989},
	type = {Article},
	abstract = {The tissue distribution and clearance of radiolabeled microcystin-LR administered to Atlantic salmon via i.p. injection has been re-examined using uniformly C-14-labeled toxin, Significant differences were found to exist between these results and those obtained when fish received an i.p. injection of tritium-labeled dihydromicrocystin-LR. In addition, MeOH liver extracts were assayed by both phosphatase assay and C-14 counts and the results compared with the total levels of incorporation determined by digestion and subsequent C-14 counting of the same liver tissues. An attempt to investigate the metabolism and to document the putative products was also undertaken. It was found that microcystin-LR was extensively metabolized to compounds that are more polar than the parent compound. (C) 1997 Elsevier Science Ltd.},
	keywords = {biotransformation, CHROMATOGRAPHY, DIARRHETIC SHELLFISH TOXINS, DISEASE, IDENTIFICATION, INHIBITOR, POTENT, PROTEIN PHOSPHATASE, TISSUE DISTRIBUTION, TYPE-1},
	isbn = {0041-0101},
	url = {<Go to ISI>://A1997XG73100017},
	author = {Williams, D. E. and Craig, M. and Dawe, S. C. and Kent, M. L. and Andersen, R. J. and Holmes, C. F. B.}
}
@article {3234,
	title = {COMPARISON OF THE SOLUTION STRUCTURES OF MICROCYSTIN-LR AND MOTUPORIN},
	journal = {Nature Structural Biology},
	volume = {2},
	number = {2},
	year = {1995},
	note = {ISI Document Delivery No.: RF665Times Cited: 1Cited Reference Count: 15},
	month = {Feb},
	pages = {114-116},
	type = {Letter},
	abstract = {A comparison of the structures of two cyanobacterial toxins yields insights into how they may inhibit protein phosphatase-1 and -2A and why microcystins but not motuporin may covalently modify their protein phosphatase targets.},
	keywords = {INHIBITOR, nodularin, POTENT, PROTEIN PHOSPHATASES, TOXINS},
	isbn = {1072-8368},
	url = {<Go to ISI>://A1995RF66500006},
	author = {Bagy, J. R. and Sonnichsen, F. D. and Williams, D. and Andersen, R. J. and Sykes, B. D. and Holmes, C. F. B.}
}
@article {2753,
	title = {IDENTIFICATION OF PROTEIN PHOSPHATASE INHIBITORS OF THE MICROCYSTIN CLASS IN THE MARINE-ENVIRONMENT},
	journal = {Toxicon},
	volume = {31},
	number = {11},
	year = {1993},
	note = {ISI Document Delivery No.: MM430Times Cited: 38Cited Reference Count: 28},
	month = {Nov},
	pages = {1407-1414},
	type = {Article},
	abstract = {Toxins produced by marine phytoplankton represent a severe global health hazard to humans that eat seafood and are also responsible for massive natural fish kills in specialized bloom situations. Tumour-promoting hepatotoxins from the freshwater microcystin/nodularin class were identified in Northeastern Pacific Ocean, Eastern Canadian and European mussels for the first time. These hepatotoxins were detected at biologically active levels up to three-fold higher than accepted quarantine levels for the diarrhetic shellfish toxin okadaic acid (OA), based on their activity (in microcystin-LR equivalent units) in a liquid chromatography (LC)-linked protein phosphatase bioassay. The presence of microcystins/nodularins in oceanic shellfish identifies a potentially novel class of intoxication which is also prevalent in other forms of marine aquatic life, namely sponges and fish. The widespread presence of prokaryotic microcystins and nodularins in the marine environment may be indicative of the importance of signal transduction pathways involving potent inhibition of protein phosphatases in early marine eukaryotes.},
	keywords = {DIARRHETIC SHELLFISH TOXINS, HIGHER-PLANTS, LR, nodularin, OKADAIC ACID, POTENT, TYPE-1},
	isbn = {0041-0101},
	url = {<Go to ISI>://A1993MM43000005},
	author = {Chen, D. Z. X. and Boland, M. P. and Smillie, M. A. and Klix, H. and Ptak, C. and Andersen, R. J. and Holmes, C. F. B.}
}
@article {2702,
	title = {NEW NATURAL-PRODUCTS FROM MARINE-INVERTEBRATES},
	journal = {Gazzetta Chimica Italiana},
	volume = {123},
	number = {6},
	year = {1993},
	note = {ISI Document Delivery No.: LL566Times Cited: 3Cited Reference Count: 457TH INTERNATIONAL SYMP ON MARINE NATURAL PRODUCTS ( VII MANAPRO )JUL 05-10, 1992CAPRI, ITALY},
	month = {Jun},
	pages = {293-299},
	type = {Proceedings Paper},
	abstract = {Extracts of marine invertebrates collected in British Columbia and Papua New Guinea have been screened for the presence of cytotoxic and enzyme modulatory metabolites. Chemical examination of several active extracts has resulted in the identification of a number of novel natural products. These include: contignasterol, 2, a steroid having a cis C/D ring junction; pseudaxinellin, 5, a cyclic heptapeptide; trididemnic acids A, 7, and B, 8, two aromatic alkaloids from a tunicate; the rubrolides A, 13, to H, 20, a family of highly halogenated tunicate metabolites; and motuporin, 22, a cyclic pentapeptide that is the first marine representative of the microcystin class of hepatotoxic and tumor-promoting cyclic peptides. Microcystin LR has been found in marine shellfish for the first time and it has been implicated as the cause of a severe liver disease that occurs in netpen reared salmon in British Columbia.},
	keywords = {METABOLITES, microcystin, OKADAIC ACID, PEPTIDE, POTENT, SPONGE THEONELLA SP, TUMOR PROMOTER},
	isbn = {0016-5603},
	url = {<Go to ISI>://A1993LL56600001},
	author = {Andersen, R. J. and Burgoyne, D. L. and Williams, D. E. and Kong, F. M. and De Silva, E. D. and Miao, S. C. and Allen, T. M. and Holmes, C. F. B. and Chen, D. and Kent, M.}
}
