@article {2661,
	title = {Rolloamides A and B, Cytotoxic Cyclic Heptapeptides Isolated from the Caribbean Marine Sponge Eurypon laughlini},
	journal = {Journal of Natural Products},
	volume = {72},
	number = {7},
	year = {2009},
	note = {ISI Document Delivery No.: 479MVTimes Cited: 3Cited Reference Count: 14Williams, David E. Yu, Ker Behrisch, Hans W. Van Soest, Rob Andersen, Raymond J.},
	month = {Jul},
	pages = {1253-1257},
	type = {Article},
	abstract = {Two cyclic heptapeptides, rolloamides A (1) and B (2), have been isolated from the Dominican marine sponge Eurypon laughlini. The structures of 1 and 2 were elucidated by a combination of spectroscopic analyses and chemical degradation. Rolloamide A (1), which was found to exist as two distinct conformers in C5D5N, exhibits growth suppressive activity against a panel of histologically diverse cancer cell lines.},
	keywords = {NATURAL-PRODUCTS, OCTAPEPTIDE, PEPTIDES, PORIFERA, PROLINE, STYLOTELLA-AURANTIUM},
	isbn = {0163-3864},
	url = {<Go to ISI>://000268664500006},
	author = {Williams, D. E. and Yu, K. and Behrisch, H. W. and Van Soest, R. and Andersen, R. J.}
}
@article {1300,
	title = {Dominicin, a cyclic octapeptide, and laughine, a bromopyrrole alkaloid, isolated from the Caribbean marine sponge Eurypon laughlini},
	journal = {Journal of Natural Products},
	volume = {68},
	number = {3},
	year = {2005},
	note = {ISI Document Delivery No.: 910JPTimes Cited: 15Cited Reference Count: 9},
	month = {Mar},
	pages = {327-330},
	type = {Article},
	abstract = {Dominicin, a new cyclic peptide, and the new bromopyrrole alkaloid laughine (4) have been isolated from the marine sponge Eurypon laughlini collected in Dominica. The structures of 1 and 4 were determined by a combination of spectroscopic analysis and chemical degradation. Single-crystal X-ray diffraction analysis confirmed the structure of dominicin (1).},
	keywords = {NATURAL-PRODUCTS, PROLINE},
	isbn = {0163-3864},
	url = {<Go to ISI>://000227927700004},
	author = {Williams, D. E. and Patrick, B. O. and Behrisch, H. W. and Van Soest, R. and Roberge, M. and Andersen, R. J.}
}
@article {1299,
	title = {Neopetrosiamides, peptides from the marine sponge Neopetrosia sp that inhibit amoeboid invasion by human tumor cells},
	journal = {Organic Letters},
	volume = {7},
	number = {19},
	year = {2005},
	note = {ISI Document Delivery No.: 964DETimes Cited: 11Cited Reference Count: 19},
	month = {Sep},
	pages = {4173-4176},
	type = {Article},
	abstract = {Neopetrosiamdes A (1) and B (2), two diastereomeric tricyclic peptides that inhibit amoeboid invasion of human tumor cells, have been isolated from the marine sponge Neopetrosia sp. collected in Papua New Guinea. The structures of the neopetrosiamides were elucidated by analysis of MS and NMR data and confirmed by chemical degradation.},
	keywords = {ANTI-INVASION, MIGRATION, PAPUA-NEW-GUINEA, PROLINE, PROTEOLYSIS, STRONGYLOPHORINE-26},
	isbn = {1523-7060},
	url = {<Go to ISI>://000231858100028},
	author = {Williams, D. E. and Austin, P. and Diaz-Marrero, A. R. and Van Soest, R. and Matainaho, T. and Roskelley, C. D. and Roberge, M. and Andersen, R. J.}
}
@article {5082,
	title = {Active site residues of glutamate racemase},
	journal = {Biochemistry},
	volume = {40},
	number = {21},
	year = {2001},
	note = {ISI Document Delivery No.: 436GCTimes Cited: 44Cited Reference Count: 38},
	month = {May},
	pages = {6199-6204},
	type = {Article},
	abstract = {Glutamate racemase, MurI, catalyzes the interconversion of glutamate enantiomers in a cofactor-independent fashion and provides bacteria with a source of D-Glu for use in peptidoglycan biosynthesis. The enzyme uses a "two-base" mechanism involving a deprotonation of the substrate at the ct-position to form an anionic intermediate, followed by a reprotonation in the opposite stereochemical sense. In the Lactobacillus fermenti enzyme, Cys73 is responsible for the deprotonation of D-glutamate, and Cys184 is responsible for the deprotonation of L-glutamate; however, very little is known about the roles of other active site residues. This work describes the preparation of four mutants in which strictly conserved residues containing ionizable side chains were modified (D10N, D36N, E152Q, and H186N). During the course of this research, the structural analysis of a crystallized glutamate racemase indicated that three of these residues (D10, E152, and H186) are in the active site of the enzyme [Hwang, K. Y., Cho, C.-S., Kim, S. S., Sung, H.-C., Yu, Y. G., and Cho, Y. (1999) Nat. Struct. Biol. 6, 422-426]. Two of the mutants, D10N and H186N, displayed a marked decrease in the values of k(cat), but not K-M, and are therefore implicated as important catalytic residues. Further analysis of the primary kinetic isotope effects observed with a-deuterated substrates showed that a significant asymmetry was introduced into the free energy profile by these two mutations. This is interpreted as evidence that the mutated residues normally assist the catalytic thiols in acting as bases (D10 with C73 and H186 with C184). An alternate possibility is that the residues may serve to stabilize the carbanionic intermediate in the racemization reaction.},
	keywords = {AMINO-ACID RACEMASE, AQUIFEX PYROPHILUS, CARBON ACIDS, ENZYME-CATALYZED REACTIONS, ESCHERICHIA-COLI, INFLUENZAE DIAMINOPIMELATE EPIMERASE, IRREVERSIBLE INHIBITOR, MANDELATE RACEMASE, PROLINE, PROTON ABSTRACTION, RACEMASE},
	isbn = {0006-2960},
	url = {<Go to ISI>://000168927300002},
	author = {Glavas, S. and Tanner, M. E.}
}
