@article {2561,
	title = {Functional Cell-Based Screening and Saturation Transfer Double-Difference NMR Have Identified Haplosamate A as a Cannabinoid Receptor Agonist},
	journal = {Acs Chemical Biology},
	volume = {4},
	number = {2},
	year = {2009},
	note = {ISI Document Delivery No.: 410WNTimes Cited: 1Cited Reference Count: 19Pereira, Alban Pfeifer, Tom A. Grigliatti, Thomas A. Andersen, Raymond J.},
	month = {Feb},
	pages = {139-144},
	type = {Article},
	abstract = {A marine natural product extract library has been screened with a functional cell-based G-protein coupled receptor assay to find compounds capable of binding the human cannabinoid receptors CB1 and CB2. The methanol extract of the marine sponge Dasychalina fragilis collected in Papua New Guinea was active in the assay. Bioassay guided fractionation of the extract identified the phosphorylated sterol sulfate haplosamate A(1) as a cannabinoid receptor agonist. The high water solubility of haplosamate A(1) allowed exploration of its binding interactions with the human cannabinoid recepors in whole insect cells by means of saturation transfer double-difference NMR spectroscopy. This technique confirmed that haplosamate A(1) binds selectively to these receptors.},
	keywords = {DOCKING, ENDOCANNABINOID SYSTEM, inhibitors, INTEGRIN ALPHA(IIB)BETA(3), LIGAND-BINDING, PEPTIDE, PROTEIN, SPECTROSCOPY, STD-NMR},
	isbn = {1554-8929},
	url = {<Go to ISI>://000263609100008},
	author = {Pereira, A. and Pfeifer, T. A. and Grigliatti, T. A. and Andersen, R. J.}
}
@article {1545,
	title = {Characterization of de novo four-helix bundles by molecular dynamics simulations},
	journal = {Proteins-Structure Function and Bioinformatics},
	volume = {64},
	number = {3},
	year = {2006},
	note = {ISI Document Delivery No.: 064QITimes Cited: 5Cited Reference Count: 34Scott, Walter R. P. Seo, Emily Huttunen, Heidi Wallhorn, Diana Sherman, John C. Straus, Suzana K.},
	month = {Aug},
	pages = {719-729},
	type = {Article},
	abstract = {We have investigated the structure and dynamics of three cavitand-based four-helix bundles (caviteins) by computer simulation. In these systems, designed de novo, each of the four helices contain the identical basis sequence EELLKKLEELLKKG (N1). Each cavitein consists of a rigid macrocycle (cavitand) with four aryl linkages, to each of which is connected an NI peptide by means of a linker peptide. The three caviteins studied here differ only in the linker peptide, which consist of one, two, or three glycine residues. Previous experimental work has shown that these systems exhibit very different behavior in terms of stability and oligomerization states despite the small differences in the linker peptide. Given that to date no three-dimensional structure is available for these caviteins, we have undertaken a series of molecular dynamics (MD) simulations in explicit water to try to rationalize the large differences in the experimentally observed behavior of these systems. Our results provide insight, for the first time, into why and how the cavitein with a single glycine linker forms dimers. In addition, our results indicate why although the two- and three-glycine-linked caviteins have similar stabilities, they have different native-like characteristics: the cavitein with three glycines can form a supercoiled helix, whereas the one with two glycines cannot. These findings may provide a useful guide in the rational de novo design of novel proteins with finely tunable structures and functions in the future.},
	keywords = {caviteins, de novo four-helix bundle, DESIGN, DOMAIN, HELICAL BUNDLES, molecular dynamics simulations, PEPTIDE, PROTEIN DESIGN, PROTEINS, STATE, SYSTEM, TASP, template-assembled synthetic protein},
	isbn = {0887-3585},
	url = {<Go to ISI>://000239103800014},
	author = {Scott, W. R. P. and Seo, E. and Huttunen, H. and Wallhorn, D. and Sherman, J. C. and Straus, S. K.}
}
@article {4500,
	title = {Design of proteins using rigid organic macrocycles as scaffolds},
	journal = {Bioorganic \& Medicinal Chemistry},
	volume = {7},
	number = {1},
	year = {1999},
	note = {ISI Document Delivery No.: 173QETimes Cited: 21Cited Reference Count: 39},
	month = {Jan},
	pages = {23-27},
	type = {Article},
	abstract = {We have designed and synthesized new three-helix template-assembled synthetic proteins (TASPs) 1a-c. The template was the rigid cyclotribenzylene (CTB) macrocycle 2, which has C-3 symmetry. Thiol moieties on the CTB template were used to link cysteine-containing peptide strands 3a-c via disulfide bonds. With designed peptide strands of 15 and 18 residues in length, the structure of TASPs 1a-c were determined to be helical in water according to circular dichroism (CD) spectroscopy. The helicities of TASPs la-e were unchanged over large ranges of pH (2-12) and salt concentrations (0-2 M KCl). TASPs 1a-c were also extremely resistant to chemical denaturants: it requires a guanidine hydrochloride (GnHCl) concentration of 7.4 M for TASPs 1a-c to lose 50\% of their helicity. The major force for stabilization of TASPs 1a-c is the hydrophobic bundling of the helices. (C) 1999 Elsevier Science Ltd. All rights reserved.},
	keywords = {4-HELIX BUNDLE PROTEIN, ASSEMBLED SYNTHETIC PROTEINS, CHEMOSELECTIVE LIGATION, CONSTRUCTION, CROSS-LINKING, CRYSTAL-STRUCTURE, cyclotribenzylene, de novo protein, DE-NOVO PROTEINS, HELICAL BUNDLES, HELICAL PROTEIN, PEPTIDE, TASP, TEMPLATE},
	isbn = {0968-0896},
	url = {<Go to ISI>://000078990600004},
	author = {Causton, A. S. and Sherman, J. C.}
}
@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 {3342,
	title = {EFFICIENT COUPLING OF AMINO-ACID DERIVATIVES TO RIGID ORGANIC SCAFFOLDS - MODEL SYNTHESES FOR DE-NOVO PROTEINS},
	journal = {Tetrahedron},
	volume = {51},
	number = {32},
	year = {1995},
	note = {ISI Document Delivery No.: RM784Times Cited: 34Cited Reference Count: 42},
	month = {Aug},
	pages = {8719-8732},
	type = {Article},
	abstract = {We describe the coupling of amino acid derivatives to four different rigid organic macrocycles. The couplings were achieved in high yields, which augurs well for the coupling of polypeptides to the rigid macrocycles to create a new family of de novo proteins. We discuss the structure of the model compounds based on the hydrogen bonding patterns that are evident from their NMR and IR spectra.},
	keywords = {BUNDLE PROTEIN, DESIGN, PEPTIDE, TASP},
	isbn = {0040-4020},
	url = {<Go to ISI>://A1995RM78400004},
	author = {Gibb, B. C. and Mezo, A. R. and Causton, A. S. and Fraser, J. R. and Tsai, F. C. S. and Sherman, J. C.}
}
@article {3343,
	title = {PROTOTYPE FOR A NEW FAMILY OF DE-NOVO PROTEINS},
	journal = {Tetrahedron Letters},
	volume = {36},
	number = {42},
	year = {1995},
	note = {ISI Document Delivery No.: RZ295Times Cited: 24Cited Reference Count: 30},
	month = {Oct},
	pages = {7587-7590},
	type = {Article},
	abstract = {We report the design, synthesis, and preliminary structural analysis of a four-helix bundle affixed to a rigid organic macrocycle.},
	keywords = {ASSEMBLED SYNTHETIC PROTEINS, CAVITANDS, CHANNEL, DESIGN, HOST GUEST COMPLEXATION, MOLECULAR, PEPTIDE, TASP, TOPOLOGY, VESSELS},
	isbn = {0040-4039},
	url = {<Go to ISI>://A1995RZ29500004},
	author = {Gibb, B. C. and Mezo, A. R. and Sherman, J. C.}
}
@article {2932,
	title = {THE ISOLATION OF MAJUSCULAMIDE-C FROM THE SPONGE PTILOCAULIS-TRACHYS COLLECTED IN ENEWETAK AND DETERMINATION OF THE ABSOLUTE-CONFIGURATION OF THE 2-METHYL-3-AMINOPENTANOIC ACID RESIDUE},
	journal = {Journal of Natural Products},
	volume = {56},
	number = {4},
	year = {1993},
	note = {ISI Document Delivery No.: KX568Times Cited: 19Cited Reference Count: 24},
	month = {Apr},
	pages = {545-551},
	type = {Article},
	abstract = {Majusculamide C [1], a cyclic depsipeptide metabolite of the blue-green alga Lyngbya majuscula, has been isolated from the sponge Ptilocaulis trachys collected at Enewetak Atoll in the Marshall Islands. The absolute configuration of the novel beta amino acid 2-methyl-3-aminopentanoic acid (MAP), a component of the structure of 1, has been determined to be 2S,3R.},
	keywords = {AMINO-ACIDS, BIOACTIVE MARINE METABOLITES, CYCLIC DEPSIPEPTIDE, CYCLODEPSIPEPTIDES, LYNGBYA-MAJUSCULA, PEPTIDE, THEONELLA SP},
	isbn = {0163-3864},
	url = {<Go to ISI>://A1993KX56800015},
	author = {Williams, D. E. and Burgoyne, D. L. and Rettig, S. J. and Andersen, R. J. and Fathiafshar, Z. R. and Allen, T. M.}
}
@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.}
}
@article {7216,
	title = {MOTUPORIN, A POTENT PROTEIN PHOSPHATASE INHIBITOR ISOLATED FROM THE PAPUA-NEW-GUINEA SPONGE THEONELLA-SWINHOEI GRAY},
	journal = {Tetrahedron Letters},
	volume = {33},
	number = {12},
	year = {1992},
	note = {ISI Document Delivery No.: HJ784Times Cited: 131Cited Reference Count: 15},
	month = {Mar},
	pages = {1561-1564},
	type = {Article},
	abstract = {Motuporin (1), a cyclic pentapeptide that is a potent protein phosphatase-1 inhibitor and cytotoxin, has been isolated from the marine sponge Theonella swinhoei collected in Papua New Guinea. The structure of motuporin was elucidated by spectroscopic analysis and chemical degradation.},
	keywords = {BIOACTIVE MARINE METABOLITES, MICROCYSTIS-AERUGINOSA, PEPTIDE, TOXIN},
	isbn = {0040-4039},
	url = {<Go to ISI>://A1992HJ78400009},
	author = {De Silva, E. D. and Williams, D. E. and Andersen, R. J. and Klix, H. and Holmes, C. F. B. and Allen, T. M.}
}
@article {7287,
	title = {PSEUDOAXINELLIN, A CYCLIC HEPTAPEPTIDE ISOLATED FROM THE PAPUA-NEW-GUINEA SPONGE PSEUDOAXINELLA-MASSA},
	journal = {Tetrahedron Letters},
	volume = {33},
	number = {23},
	year = {1992},
	note = {ISI Document Delivery No.: HX160Times Cited: 18Cited Reference Count: 21},
	month = {Jun},
	pages = {3269-3272},
	type = {Article},
	abstract = {Pseudoaxinellin (1), a new cyclic heptapeptide, has been isolated from the marine sponge Pseudoaxinella massa collected in Papua New Guinea. The structure of 1 was solved by spectroscopic analysis and chemical degradation. Pseudoaxinellin is the first cyclic heptapeptide reported from a marine source. One of the amide bonds in 1 is cis.},
	keywords = {AMINO-ACIDS, BIOACTIVE MARINE METABOLITES, PEPTIDE, THEONELLA},
	isbn = {0040-4039},
	url = {<Go to ISI>://A1992HX16000005},
	author = {Kong, F. M. and Burgoyne, D. L. and Andersen, R. J. and Allen, T. M.}
}
