@article {1378,
	title = {Avinosol, a meroterpenoid-nucleoside conjugate with antiinvasion activity isolated from the marine sponge Dysidea sp},
	journal = {Organic Letters},
	volume = {8},
	number = {17},
	year = {2006},
	note = {ISI Document Delivery No.: 072EJTimes Cited: 10Cited Reference Count: 18Diaz-Marrero, Ana R. Austin, Pamela Van Soest, Rob Matainaho, Teatulohi Roskelley, Calvin D. Roberge, Michel Andersen, Raymond J.},
	month = {Aug},
	pages = {3749-3752},
	type = {Article},
	abstract = {The new meroterpenoids avinosol (1),3 {\textquoteright}-aminoavarone (2), and 3 {\textquoteright}-phenethylaminoavarone (3) have been isolated from the marine sponge Dysidea sp. collected in Papua New Guinea, and their structures were elucidated by analysis of spectroscopic data. Avinosol (1), which is apparently the first example of a naturally occurring meroterpenoid-nucleoside conjugate, showed antiinvasion activity in a cell-based assay.},
	keywords = {ANTI-INVASION, AVAROL, INHIBITOR, KINASE, MIGRATION, PROTEOLYSIS, SESQUITERPENE QUINONES, STRESS FIBERS, STRONGYLOPHORINE-26, TUMOR-CELL INVASION},
	isbn = {1523-7060},
	url = {<Go to ISI>://000239655500033},
	author = {Diaz-Marrero, A. R. and Austin, P. and Van Soest, R. and Matainaho, T. and Roskelley, C. D. and Roberge, M. and Andersen, R. J.}
}
@article {1127,
	title = {Structural and mechanistic analysis of sialic acid synthase NeuB from Neisseria meningitidis in complex with Mn2+ phosphoenolpyruvate, and N-acetylmannosaminitol},
	journal = {Journal of Biological Chemistry},
	volume = {280},
	number = {5},
	year = {2005},
	note = {ISI Document Delivery No.: 897DJTimes Cited: 19Cited Reference Count: 58},
	month = {Feb},
	pages = {3555-3563},
	type = {Article},
	abstract = {In Neisseria meningitidis and related bacterial pathogens, sialic acids play critical roles in mammalian cell immunity evasion and are synthesized by a conserved enzymatic pathway that includes sialic acid synthase (NeuB, SiaC, or SynC). NeuB catalyzes the condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine, directly forming N-acetylneuraminic acid (or sialic acid). In this paper we report the development of a coupled assay to monitor NeuB reaction kinetics and an O-18-labeling study that demonstrates the synthase operates via a C-O bond cleavage mechanism. We also report the first structure of a sialic acid synthase, that of NeuB, revealing a unique domain-swapped homodimer architecture consisting of a (beta/alpha)(8) barrel (TIM barrel)type fold at the N-terminal end and a domain with high sequence identity and structural similarity to the ice binding type III antifreeze proteins at the C-terminal end of the enzyme. We have determined the structures of NeuB in the malate-bound form and with bound PEP and the substrate analog N-acetylmannosaminitol to 1.9 and 2.2 Angstrom resolution, respectively. Typical of other TIM barrel proteins, the active site of NeuB is located in a cavity at the C-terminal end of the barrel; however, the positioning of the swapped antifreeze-like domain from the adjacent monomer provides key residues for hydrogen bonding with substrates in the active site of NeuB, a structural feature that leads to distinct modes of substrate binding from other PEP-utilizing enzymes that lack an analogous antifreeze-like domain. Our observation of a direct interaction between a highly ordered manganese and the N-acetylmannosaminitol in the NeuB active site also suggests an essential role for the ion as an electrophilic catalyst that activates the N-acetylmannosamine carbortyl to the addition of PEP.},
	keywords = {3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE SYNTHASE, 3-DEOXY-D-MANNO-OCTULOSONATE-8-PHOSPHATE SYNTHASE, ACETYLNEURAMINIC ACID, BISUBSTRATE, CAMPYLOBACTER-JEJUNI, CATALYTIC MECHANISM, CELL GLYCOSYLATION, ENZYMATIC SYNTHESIS, ESCHERICHIA-COLI, INHIBITOR, KDO8P SYNTHASE},
	isbn = {0021-9258},
	url = {<Go to ISI>://000226983900053},
	author = {Gunawan, J. and Simard, D. and Gilbert, M. and Lovering, A. L. and Wakarchuk, W. W. and Tanner, M. E. and Strynadka, N. C. J.}
}
@article {543,
	title = {Motuporamines, anti-invasion and anti-angiogenic alkaloids from the marine sponge Xestospongia exigua (Kirkpatrick): Isolation, structure elucidation, analogue synthesis, and conformational analysis},
	journal = {Journal of Organic Chemistry},
	volume = {67},
	number = {1},
	year = {2002},
	note = {ISI Document Delivery No.: 509MHTimes Cited: 32Cited Reference Count: 28},
	month = {Jan},
	pages = {245-258},
	type = {Article},
	abstract = {Extracts of the sponge Xestospongia exigua collected in Papua New Guinea were positive in a new assay for anti-invasion activity. Bioassay-guided fractionation led to the identification of the three known motuporamines A (1), B (2), and C (3) along with the new motuporamines D (4), E (5), and F (6) and a mixture of G, H, and 1 (15). Motuporamines A (1), B (2), and C (3) and the mixture of G, H, and 1 (15) were responsible for the anti-invasion activity of the crude extract. Motuporamine C (3) has also been found to be anti-angiogenic. A series of analogues of the motuporamines have been synthesized and evaluated for anti-invasive activity. These SAR results revealed that a saturated 15-membered cyclic amine fused to the natural motuporamine diamine side chain (13) represented the optimal structure for anti-invasive activity in this family. Single-crystal X-ray diffraction analysis of one of the analogues 20 showed that in the solid state its 16-membered macrocyclic amine fragment adopted the [4444] quadrangular conformation predicted by calculations to be the lowest energy conformation for the corresponding cycloalkane, cyclobexadecane. These data along with literature X-ray data and conformational analysis for derivatives of azacyclotridecane have been used as precedents for predicting the lowest energy ring conformations of other motuporamines. The SAR data from the natural and synthetic motuporamines have been combined with the conformational analyses to provide an outline of the functionality and shape required for activity in this family of alkaloids and to design a new analogue 49 that showed good anti-invasion activity.},
	keywords = {A-C, CANCER, INHIBITOR, METASTASIS, METATHESIS, TUMOR-GROWTH},
	isbn = {0022-3263},
	url = {<Go to ISI>://000173151200039},
	author = {Williams, D. E. and Craig, K. S. and Patrick, B. and McHardy, L. M. and Van Soest, R. and Roberge, M. and Andersen, R. J.}
}
@article {4557,
	title = {Catalytic acid/base residues of glutamate racemase},
	journal = {Biochemistry},
	volume = {38},
	number = {13},
	year = {1999},
	note = {ISI Document Delivery No.: 182QZTimes Cited: 43Cited Reference Count: 37},
	month = {Mar},
	pages = {4106-4113},
	type = {Article},
	abstract = {Glutamate racemase is a cofactor-independent enzyme that employs two active-site cysteine residues as acid/base catalysts during the interconversion of glutamate enantiomers, In a given reaction direction, a thiolate from one of the cysteines abstracts the alpha-proton, and the other cysteine thiol delivers a proton to the opposite face of the resulting carbanionic intermediate. This paper reports that the C73S and C184S mutants are still capable of racemizing glutamate with specificity constants about 10(3)-fold lower than those of the wild-type enzyme, A "one-base requiring" reaction, the elimination of water from N-hydroxyglutamate, has been used to deduce which thiol acts as the base for a given enantiomer. With D-N-hydroxyglutamate the C73S mutant is a much poorer catalyst than wild-type enzyme, whereas the C184S mutant is a somewhat better catalyst. This trend was reversed with L-N-hydroxyglutamate, suggesting that Cys73 is responsible for the deprotonation of D-glutamate and Cys184 is responsible for the deprotonation of L-glutamate. In addition, with C73S the V-max/K-M isotope effect on D-glutamate racemization was greater than that seen with wild-type enzyme, whereas the isotope effect with L-glutamate had decreased. The results were reversed with the C184S mutant. This is interpreted as being due to an asymmetry in the free energy profiles that is induced upon mutation, with the deprotonation step involving a serine becoming the more cleanly rate-determining of the two. These results support the above assignment and the notion that a carbanionic intermediate is formed during catalysis.},
	keywords = {BACILLUS-STEAROTHERMOPHILUS, DIAMINOPIMELATE EPIMERASE, ENERGETICS, ESCHERICHIA-COLI, INHIBITOR, IRREVERSIBLE, L-ALANINE, MANDELATE RACEMASE, MECHANISM, PROLINE RACEMASE, PURIFICATION},
	isbn = {0006-2960},
	url = {<Go to ISI>://000079510800031},
	author = {Glavas, S. and Tanner, M. E.}
}
@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 {4167,
	title = {Glucose-lowering properties of vanadium compounds: Comparison of coordination complexes with maltol or kojic acid as ligands},
	journal = {Journal of Inorganic Biochemistry},
	volume = {68},
	number = {2},
	year = {1997},
	note = {ISI Document Delivery No.: YA963Times Cited: 72Cited Reference Count: 44},
	month = {Nov},
	pages = {109-116},
	type = {Article},
	abstract = {Bis(kojato)oxovanadium(IV) [abbreviated VO(ka)(2)], a close chemical analog of the insulin-mimetic lead compound bis(maltolato) oxovanadium (IV) - abbreviated BMOV or VO(ma)(2) - is reported and its reaction chemistry and insulin-mimetic properties are presented. VO(ka)(2) [log K-1 = 7.61(10), log K-2 = 6.89(6), log beta(2) = 14.50(16)] has a reaction chemistry which directly parallels that of VO(ma)(2). In aqueous solution it is more slowly oxidized by molecular oxygen to [VO2(ka)(2)](-) than is VO(ma)(2) to [VO2(ma)(2)](-). Variable pH electrochemistry and variable pH V-51 NMR of solutions of VO(Ka)(2) are presented and contrasted with the corresponding results for VO(ma)(2). Time course studies (24 hr) in Sn-diabetic rats following the oral or ip administration of VO(ka)(2), VO(ma)(2), VO2+ (vanadyl) as vanadyl sulfate (VOSO4), and [VO2(ma)(2)](-) as its [NH4](+) salt have been performed, as have chronic oral studies comparing VO(ka)(2) and VO(ma)(2) over a six week period. lit all studies, the most potent form of vanadium was the neutrally charged water soluble, complex VO(ma)(2). (C) 1997 Elsevier Science Inc.},
	keywords = {ALUMINUM(III), BIOINORGANIC CHEMISTRY, BIS(MALTOLATO)OXOVANADIUM(IV) BMOV, DIABETIC RATS, INHIBITOR, INSULIN MIMETIC AGENT, ISOLATED RAT ADIPOCYTES, LABILE, METABOLISM, OXOVANADATES, VANADATE},
	isbn = {0162-0134},
	url = {<Go to ISI>://A1997YA96300005},
	author = {Yuen, V. G. and Caravan, P. and Gelmini, L. and Glover, N. and McNeill, J. H. and Setyawati, I. A. and Zhou, Y. and Orvig, Chris}
}
@article {3851,
	title = {Ferintoic acids A and B, new cyclic hexapeptides from the freshwater cyanobacterium Microcystis aeruginosa},
	journal = {Journal of Natural Products},
	volume = {59},
	number = {6},
	year = {1996},
	note = {ISI Document Delivery No.: UT658Times Cited: 23Cited Reference Count: 30},
	month = {Jun},
	pages = {570-575},
	type = {Article},
	abstract = {The cyclic hexapeptides ferintoic acids A (1) and B (2) have been isolated from cells of Microcystis aeruginosa harvested during a natural bloom of the toxic cyanobacterium. The structures of 1 and 2 were determined by a combination of spectroscopic analysis and chemical degradation.},
	keywords = {AMINO-ACIDS, BLUE-GREEN-ALGA, INHIBITOR, LR, PEPTIDE, PHASE, PROTEIN PHOSPHATASES, SPONGE THEONELLA SP, TOXIN},
	isbn = {0163-3864},
	url = {<Go to ISI>://A1996UT65800004},
	author = {Williams, D. E. and Craig, M. and Holmes, C. F. B. and Andersen, R. J.}
}
@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.}
}
