@article {2546,
	title = {Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {106},
	number = {33},
	year = {2009},
	note = {ISI Document Delivery No.: 484WETimes Cited: 5Cited Reference Count: 30Nag, Shalini Ma, Qing Wang, Hui Chumnarnsilpa, Sakesit Lee, Wei Lin Larsson, Marten Kannan, Balakrishnan Hernandez-Valladarez, Maria Burtnick, Leslie D. Robinson, Robert C.},
	month = {Aug},
	pages = {13713-13718},
	type = {Article},
	abstract = {Gelsolin consists of six homologous domains (G1-G6), each containing a conserved Ca-binding site. Occupation of a subset of these sites enables gelsolin to sever and cap actin filaments in a Ca-dependent manner. Here, we present the structures of Ca-free human gelsolin and of Ca-bound human G1-G3 in a complex with actin. These structures closely resemble those determined previously for equine gelsolin. However, the G2 Ca-binding site is occupied in the human G1-G3/actin structure, whereas it is vacant in the equine version. In-depth comparison of the Ca-free and Ca-activated, actin-bound human gelsolin structures suggests G2 and G6 to be cooperative in binding Ca2+ and responsible for opening the G2-G6 latch to expose the F-actin-binding site on G2. Mutational analysis of the G2 and G6 Ca-binding sites demonstrates their interdependence in maintaining the compact structure in the absence of calcium. Examination of Ca binding by G2 in human G1-G3/actin reveals that the Ca2+ locks the G2-G3 interface. Thermal denaturation studies of G2-G3 indicate that Ca binding stabilizes this fragment, driving it into the active conformation. The G2 Ca-binding site is mutated in gelsolin from familial amyloidosis (Finnish-type) patients. This disease initially proceeds through protease cleavage of G2, ultimately to produce a fragment that forms amyloid fibrils. The data presented here support a mechanism whereby the loss of Ca binding by G2 prolongs the lifetime of partially activated, intermediate conformations in which the protease cleavage site is exposed.},
	keywords = {actin, AMYLOIDOGENESIS, biosynthesis, calcium, calcium activated, calcium dependent, FAMILIAL AMYLOIDOSIS, IDENTIFICATION, PLASMA GELSOLIN, PROTEIN, SITE, TERMINAL HALF, TIRF},
	isbn = {0027-8424},
	url = {<Go to ISI>://000269078700018},
	author = {Nag, S. and Ma, Q. and Wang, H. and Chumnarnsilpa, S. and Lee, W. L. and Larsson, M. and Kannan, B. and Hernandez-Valladarez, M. and Burtnick, L. D. and Robinson, R. C.}
}
@article {2510,
	title = {The Engineering of Bacteria Bearing Azido-Pseudaminic Acid-Modified Flagella},
	journal = {Chembiochem},
	volume = {10},
	number = {8},
	year = {2009},
	note = {ISI Document Delivery No.: 452SMTimes Cited: 3Cited Reference Count: 24Liu, Feng Aubry, Annie J. Schoenhofen, Ian C. Logan, Susan M. Tanner, Martin E.},
	month = {May},
	pages = {1317-1320},
	type = {Article},
	keywords = {4, 6-DEHYDRATASE, azides, biosynthesis, C. jejuni, CAMPYLOBACTER-JEJUNI, cell surfaces, flagella, FUNCTIONAL-CHARACTERIZATION, HELICOBACTER-PYLORI, IDENTIFICATION, METABOLISM, PATHWAY, PROTEINS, PseB, reaction, Staudinger, UDP-N-ACETYLGLUCOSAMINE},
	isbn = {1439-4227},
	url = {<Go to ISI>://000266561500009},
	author = {Liu, F. and Aubry, A. J. and Schoenhofen, I. C. and Logan, S. M. and Tanner, M. E.}
}
@article {2660,
	title = {Pyrodysinoic Acid Derivatives from the Marine Sponge Dysidea robusta},
	journal = {Journal of Natural Products},
	volume = {72},
	number = {9},
	year = {2009},
	note = {ISI Document Delivery No.: 507LSTimes Cited: 1Cited Reference Count: 30Williams, David E. Marques, Suzi O. Hajdu, Eduardo Peixinho, Solange Andersen, Raymond J. Berlinck, Roberto G. S.},
	month = {Sep},
	pages = {1691-1694},
	type = {Article},
	abstract = {Three new nitrogen-containing terpenes related to pyrodysinoic acid (1) have been isolated from the sponge Dysidea robusta collected in Brazil. Isopyrodysinoic acid (2), 13-hydroxyisopyrodysinoic acid (3), and pyrodysinoic acid B (4) were obtained from the crude extract of D. robusta and identified by analysis of spectroscopic data. Pyrodysinoic acid B (4) is the first furodysin or furodysinin sesquiterpene derivative with a trans junction between the two six-membered rings of the 1,2,3,4,4a,7,8,8a-octahydro-1,1,6-trimethylnaphthalene moiety.},
	keywords = {AMINO-ACID, biosynthesis, CELLULAR-ORIGIN, DENDROLASIN, DYSIHERBAINE, GENUS DYSIDEA, HERBACEA, METABOLITES, NATURAL-PRODUCTS, SESQUITERPENES},
	isbn = {0163-3864},
	url = {<Go to ISI>://000270855600026},
	author = {Williams, D. E. and Marques, S. O. and Hajdu, E. and Peixinho, S. and Andersen, R. J. and Berlinck, R. G. S.}
}
@article {2305,
	title = {Cladoniamides A-G, tryptophan-derived alkaloids produced in culture by Streptomyces uncialis},
	journal = {Organic Letters},
	volume = {10},
	number = {16},
	year = {2008},
	note = {ISI Document Delivery No.: 335LWTimes Cited: 6Cited Reference Count: 10Williams, David E. Davies, Julian Patrick, Brian O. Bottriell, Helen Tarling, Tamsin Roberge, Michel Andersen, Raymond J.},
	month = {Aug},
	pages = {3501-3504},
	type = {Article},
	abstract = {Cladoniamides A-G (3-9) have been isolated from cultures of Streptomyces uncialis, and their structures have been elucidated by a combination of spectroscopic analysis and an X-ray diffraction analysis of cladoniamide A (3). The cladoniamides have unprecedented rearranged and degraded alkaloid skeletons with putative biogenetic origins from indolocarbazole precursors. Cladoniamide G (9) is cytotoxic to MCF-7 cells in vitro at 10 mu g/mL.},
	keywords = {biosynthesis, CHROMOPYRROLIC ACID, REBECCAMYCIN},
	isbn = {1523-7060},
	url = {<Go to ISI>://000258293100031},
	author = {Williams, D. E. and Davies, J. and Patrick, B. O. and Bottriell, H. and Tarling, T. and Roberge, M. and Andersen, R. J.}
}
@article {2235,
	title = {Sintokamides A to E, Chlorinated Peptides from the Sponge Dysidea sp that Inhibit Transactivation of the N-Terminus of the Androgen Receptor in Prostate Cancer Cells},
	journal = {Organic Letters},
	volume = {10},
	number = {21},
	year = {2008},
	note = {ISI Document Delivery No.: 367EETimes Cited: 10Cited Reference Count: 23Sadar, Marianne D. Williams, David E. Mawji, Nasrin R. Patrick, Brian O. Wikanta, Thamrin Chasanah, Ekowati Irianto, Hari Eko Van Soest, Rob Andersen, Raymond J.},
	month = {Nov},
	pages = {4947-4950},
	type = {Article},
	abstract = {The new chlorinated peptides sintokamides A to E (1-5) have been isolated from specimens of the marine sponge Dysidea sp. collected in Indonesia. Their structures were elucidated by a combination of spectroscopic and single-crystal X-ray diffraction analyses. Sintokamide A (1) is an inhibitor of N-terminus transactivation of the androgen receptor in prostate cancer cells.},
	keywords = {AMINO-ACID, BARBAMIDE, biosynthesis, CYANOBACTERIUM, DOMAIN, HERBACEA, METABOLITES},
	isbn = {1523-7060},
	url = {<Go to ISI>://000260534500060},
	author = {Sadar, M. D. and Williams, D. E. and Mawji, N. R. and Patrick, B. O. and Wikanta, T. and Chasanah, E. and Irianto, H. E. and Van Soest, R. and Andersen, R. J.}
}
@article {1234,
	title = {Efficient chemoenzymatic synthesis of ADP-D-glycero-beta-D-manno-heptose and a mechanistic study of ADP-L-glycero-D-manno-heptose 6-epimerase},
	journal = {Organic Letters},
	volume = {7},
	number = {12},
	year = {2005},
	note = {ISI Document Delivery No.: 932SSTimes Cited: 10Cited Reference Count: 21},
	month = {Jun},
	pages = {2457-2460},
	type = {Article},
	abstract = {[GRAPHICS] A chemoenzymatic synthesis of ADP-D-glycero-\&beta;-D-manno-heptose (ADP-D,D-Hep) is described in which D,D-Hep 7-phosphate is converted to ADP-D,D-Hep by two biosynthetic enzymes. This strategy allows access to the 6"-deuterated analogue, which upon incubation with the epimerase showed complete retention of the isotopic label at the 6"-position. This provides evidence for a direct oxidation mechanism in which the hydride initially transferred to the NADP(+) cofactor is subsequently returned to the same carbon in a nonstereospecific manner.},
	keywords = {biosynthesis, CARBON, D-MANNOHEPTOSE 6-EPIMERASE, EPIMERIZATION, PATHWAY},
	isbn = {1523-7060},
	url = {<Go to ISI>://000229574300042},
	author = {Read, J. A. and Ahmed, R. A. and Tanner, M. E.}
}
@article {1279,
	title = {The enzymes of sialic acid biosynthesis},
	journal = {Bioorganic Chemistry},
	volume = {33},
	number = {3},
	year = {2005},
	note = {ISI Document Delivery No.: 931CJTimes Cited: 36Cited Reference Count: 59},
	month = {Jun},
	pages = {216-228},
	type = {Review},
	abstract = {The sialic acids are a family of nine carbon a-keto acids that play a wide variety of biological roles in nature. In mammals, they are found at the distal ends of cell surface glycoconjugates, and thus are major determinants of cellular recognition and adhesion events. In certain strains of pathogenic bacteria, they are found in capsular polysaccharides that mask the organism from the immune system by mimicking the exterior of a mammalian cell. This review outlines recent developments in the understanding of the two main enzymes responsible for the biosynthesis of the sialic acid, N-acetylneuraminic acid. The first, a hydrolyzing UDP-N-acetyl-glucosamine 2-epimerase, generates N-acetylmannosamine and UDP from UDP-N-acetylglucosamine. The second, sialic acid synthase, generates either N-acetylneuraminic acid (bacteria) or N-acetylneuraminic acid 9-phosphate (mammals) in a condensation reaction with phosphoenolpyruvate. An emphasis is placed on an understanding of the mechanistic and structural features of these enzymes. (c) 2005 Elsevier Inc. All rights reserved.},
	keywords = {2-EPIMERASE/N-ACETYLMANNOSAMINE KINASE, BIFUNCTIONAL KEY ENZYME, biosynthesis, ESCHERICHIA-COLI K1, FIRST 2, KDO8P SYNTHASE, MECHANISM, N-ACETYLGLUCOSAMINE 2-EPIMERASE, N-acetylmannosamine, N-ACETYLNEURAMINIC ACID, NEISSERIA-MENINGITIDIS, PHOSPHATE, phosphoenolpyruvate, RAT-LIVER, sialic acid synthase, STEPS, SYNTHASE GENE, UDP-GlcNAc 2-epimerase},
	isbn = {0045-2068},
	url = {<Go to ISI>://000229463100007},
	author = {Tanner, M. E.}
}
@article {950,
	title = {Identification and mechanism of a bacterial hydrolyzing UDP-N-acetylglucosamine 2-epimerase},
	journal = {Biochemistry},
	volume = {43},
	number = {44},
	year = {2004},
	note = {ISI Document Delivery No.: 868UVTimes Cited: 13Cited Reference Count: 38},
	month = {Nov},
	pages = {14290-14298},
	type = {Article},
	abstract = {This paper reports the first identification of a fully functional hydrolyzing UDP-N-acetylglucosamine 2-epimerase from a bacterial source. The epimerase (known as SiaA or NeuC from Neisseria meningitidis MC58 group B is shown to catalyze the conversion of UDP-GlcNAc into ManNAc and UDP in the first step of sialic acid (N-acetylneuraminic acid) biosynthesis. The mechanism is proposed to involve an anti elimination of UDP to form 2-acetamidoglucal as an intermediate, followed by the syn addition of water. The observation that the alpha-anomer of ManNAc is the true product and that solvent deuterium is incorporated at C-2 is consistent with this mechanism. The use of the O-18-labeled substrate confirms that the overall hydrolysis reaction proceeds via cleavage of the C-O bond. Furthermore, the putative intermediate 2-acetamidoglucal is shown to serve as a catalytically competent substrate and is enzymatically hydrated to give ManNAc exclusively. Isotope effect studies show that cleavage of the C-H bond is not rate limiting during catalysis. Mutagenesis studies show that three active site carboxylate residues are crucial for catalysis. In two of the mutants that were studied (E122Q and D131N), 2-acetamidoglucal was released from the active site during catalysis, providing direct evidence that the enzyme is capable of catalyzing the anti elimination of UDP from UDP-GlcNAc.},
	keywords = {2-EPIMERASE/N-ACETYLMANNOSAMINE, biosynthesis, CELL-INTERACTIONS, ENZYME, ESCHERICHIA-COLI K1, KINASE, POLYSIALIC ACID, PURIFICATION, RAT-LIVER, SIALIC-ACID, STEREOCHEMISTRY},
	isbn = {0006-2960},
	url = {<Go to ISI>://000224939400045},
	author = {Murkin, A. S. and Chou, W. K. and Wakarchuk, W. W. and Tanner, M. E.}
}
@article {760,
	title = {Trisphaerolide A, a novel polyketide from the Dominican sponge Erylus trisphaerus},
	journal = {Journal of Natural Products},
	volume = {66},
	number = {4},
	year = {2003},
	note = {ISI Document Delivery No.: 673CVTimes Cited: 4Cited Reference Count: 14},
	month = {Apr},
	pages = {561-563},
	type = {Article},
	abstract = {The structure of trisphaerolide A (1), a mildly cytotoxic metabolite isolated from extracts of the marine sponge Erylus trisphaerus collected in Dominica, has been elucidated by detailed analysis of spectroscopic data. Trisphaerolide A (1) has a putative polyketide biogenesis, incorporating a rare variant on the standard pathway, which involves the addition of methyl branches arising from C-2 carbons of acetate units to chain carbons that arise from C-1 of acetate units.},
	keywords = {biosynthesis, CELL-CYCLE, DNA-DAMAGE CHECKPOINT, INHIBITION, ISOGRANULATIMIDE},
	isbn = {0163-3864},
	url = {<Go to ISI>://000182562800025},
	author = {van Altena, I. and Van Soest, R. and Roberge, M. and Andersen, R. J.}
}
@article {338,
	title = {De Novo terpenoid biosynthesis by the dendronotid nudibranch Melibe leonina},
	journal = {Chemoecology},
	volume = {12},
	number = {4},
	year = {2002},
	note = {ISI Document Delivery No.: 635GATimes Cited: 6Cited Reference Count: 23},
	pages = {199-202},
	type = {Article},
	abstract = {Stable isotope feeding studies using [1,2-C-13(2)]-sodium acetate have demonstrated that 2,6-dimetbyl-5-heptenal (1), a putative defensive allomone, is made by the Dendronotid nudibranch Melibe leonina via de novo biosynthesis.},
	keywords = {biosynthesis, CADLINA-LUTEOMARGINATA, chemical, CHEMICAL DEFENSE, defense nudibranch, DORID-NUDIBRANCHS, ECOLOGY, ISOTOPE INCORPORATION EVIDENCE, OPISTHOBRANCH MOLLUSK, ORIGIN, terpenoid, TRIOPHAMINE},
	isbn = {0937-7409},
	url = {<Go to ISI>://000180389600006},
	author = {Barsby, T. and Linington, R. G. and Andersen, R. J.}
}
@article {5208,
	title = {Sugar nucleotide-modifying enzymes},
	journal = {Current Organic Chemistry},
	volume = {5},
	number = {2},
	year = {2001},
	note = {ISI Document Delivery No.: 411FKTimes Cited: 12Cited Reference Count: 170},
	month = {Feb},
	pages = {169-192},
	type = {Review},
	abstract = {Sugar nucleotides serve as the activated forms of carbohydrates that are used in a wide range of biosynthetic pathways. Instead of building up the sugar nucleotide from the free sugar itself, nature often chooses to modify the "donor" portion of a pre-existing sugar nucleotide in a biosynthetically efficient manner. In doing so a rich variety of catalytic strategies are employed and this review focuses on recent mechanistic and structural studies of the sugar nucleotide-modifying enzymes. The review is organized around the types of reactions catalyzed and contains the following sections: Epimerases/Mutases/Decarboxylases, Eliminations and Substitutions, Oxidation and Reduction, and Substitutions on the Periphery of Sugar Nucleotides.},
	keywords = {4, 6-DEHYDRATASE, 6-DIDEOXYHEXOSES, ACETYLGLUCOSAMINE 2-EPIMERASE/N-ACETYLMANNOSAMINE, ACETYLNEURAMINIC ACID, biosynthesis, CYTIDINE DIPHOSPHATE 3, D-GLUCOSE, ESCHERICHIA-COLI K-12, FIRST 2, GDP-FUCOSE SYNTHETASE, KINASE, N-ACETYLGLUCOSAMINE, SITE-DIRECTED MUTAGENESIS, STEPS, UDP-GALACTOSE 4-EPIMERASE},
	isbn = {1385-2728},
	url = {<Go to ISI>://000167487300004},
	author = {Tanner, M. E.}
}
@article {4273,
	title = {Covalent adduct formation with a mutated enzyme: Evidence for a thioester intermediate in the reaction catalyzed by UDP-glucose dehydrogenase},
	journal = {Journal of the American Chemical Society},
	volume = {120},
	number = {26},
	year = {1998},
	note = {ISI Document Delivery No.: ZZ420Times Cited: 15Cited Reference Count: 23},
	month = {Jul},
	pages = {6613-6614},
	type = {Article},
	keywords = {ALDEHYDE DEHYDROGENASE, biosynthesis, GENE, GROUP-A, HYALURONIC-ACID SYNTHESIS, INSERTION, MOLECULAR CHARACTERIZATION, MUTATIONS, PNEUMONIAE, STREPTOCOCCI, TYPE-3 CAPSULAR POLYSACCHARIDE},
	isbn = {0002-7863},
	url = {<Go to ISI>://000074727600028},
	author = {Ge, X. and Campbell, R. E. and van de Rijn, I. and Tanner, M. E.}
}
@article {3982,
	title = {Massetolides A-H, antimycobacterial cyclic depsipeptides produced by two pseudomonads isolated from marine habitats},
	journal = {Journal of Natural Products},
	volume = {60},
	number = {3},
	year = {1997},
	note = {ISI Document Delivery No.: WP603Times Cited: 52Cited Reference Count: 16},
	month = {Mar},
	pages = {223-229},
	type = {Article},
	abstract = {Massetolides A-H (1-8), novel cyclic depsipetides, and the known compound viscosin (9) have been isolated from cultures of two Pseudomonas sp. isolated from a marine alga and a marine tube worm, respectively. Massetolide A (1) and viscosin (9) exhibit in vitro antimicrobial activity against Mycobacterium tuberculosis and Mycobacterium avium-intracellulare. Precursor-directed biosynthesis has been used to generate unnatural massetolides 11-13 incorporating nonprotein amino acids.},
	keywords = {BACTERIA, biosynthesis, METABOLITES},
	isbn = {0163-3864},
	url = {<Go to ISI>://A1997WP60300006},
	author = {Gerard, J. and Lloyd, R. and Barsby, T. and Haden, P. and Kelly, M. T. and Andersen, R. J.}
}
@article {3805,
	title = {Enzymatic formation and release of a stable glycal intermediate: The mechanism of the reaction catalyzed by UDP-N-acetylglucosamine 2-epimerase},
	journal = {Journal of the American Chemical Society},
	volume = {118},
	number = {12},
	year = {1996},
	note = {ISI Document Delivery No.: UC380Times Cited: 19Cited Reference Count: 25},
	month = {Mar},
	pages = {3033-3034},
	type = {Article},
	keywords = {ACID, BACTERIOPHAGE-N4 ADSORPTION, biosynthesis, enterobacterial common antigen, ESCHERICHIA-COLI, MUTANTS, POSITIONAL ISOTOPE EXCHANGE, SEQUENCE},
	isbn = {0002-7863},
	url = {<Go to ISI>://A1996UC38000035},
	author = {Sala, R. F. and Morgan, P. M. and Tanner, M. E.}
}
@article {3680,
	title = {Loloatin B, a cyclic decapeptide antibiotic produced in culture by a tropical marine bacterium},
	journal = {Tetrahedron Letters},
	volume = {37},
	number = {40},
	year = {1996},
	note = {ISI Document Delivery No.: VK223Times Cited: 13Cited Reference Count: 11},
	month = {Sep},
	pages = {7201-7204},
	type = {Article},
	abstract = {Loloatin B (I), a novel cyclic decapeptide antibiotic with potent gram positive activity, is produced in culture by a Bacillus sp. isolated from the tissues of a marine worm collected in Papua New Guinea. Copyright (C) 1996 Elsevier Science Ltd},
	keywords = {biosynthesis, ISOLATE, METABOLITES},
	isbn = {0040-4039},
	url = {<Go to ISI>://A1996VK22300012},
	author = {Gerard, J. and Haden, P. and Kelly, M. T. and Andersen, R. J.}
}
@article {3682,
	title = {Stable isotope incorporation evidence for a polyacetate origin of the acyl residues in triophamine, a diacylguanidine metabolite obtained from the dorid nudibranch Triopha catalinae},
	journal = {Chemical Communications},
	number = {20},
	year = {1996},
	note = {ISI Document Delivery No.: VP467Times Cited: 11Cited Reference Count: 16},
	month = {Oct},
	pages = {2377-2378},
	type = {Article},
	abstract = {Biosynthetic feeding experiments with sodium [1,2-(13)-C-2]-acetate have shown that the acyl residues of triophamine 1 are formed de novo in Triopha catalinae from five intact acetate units.},
	keywords = {biosynthesis, DEFENSE, MARINE NATURAL-PRODUCTS, MOLLUSKS},
	isbn = {1359-7345},
	url = {<Go to ISI>://A1996VP46700036},
	author = {Graziani, E. I. and Andersen, R. J.}
}
@article {2732,
	title = {ACANTHENE-A TO ACANTHENE-C - A-CHLORO, ISOTHIOCYANATE, FORMAMIDE SESQUITERPENE TRIAD ISOLATED FROM THE NORTHEASTERN PACIFIC MARINE SPONGE ACANTHELLA SP AND THE DORID NUDIBRANCH CADLINA-LUTEOMARGINATA},
	journal = {Tetrahedron},
	volume = {49},
	number = {21},
	year = {1993},
	note = {ISI Document Delivery No.: LD386Times Cited: 21Cited Reference Count: 19},
	month = {May},
	pages = {4503-4510},
	type = {Article},
	abstract = {Acanthenes A (1) and B (2), two new eudesmane sesquiterpenoids, have been isolated from the marine sponge Acanthella. Acandthene C (3), the formamide analog of 1 and 2, has been isolated from the nudibranch Cadlina luteomarginata which feeds on Acanthella. The structures of 1 to 3 were solved by analysis of spectroscopic data. Acanthene A (1) appears to represent the first example of the co-occurrence a chloro sesquiterpenoid analog of sponge isothiocyanate, formamide or isonitrile sesquiterpenoids.},
	keywords = {AXINELLA-CANNABINA, biosynthesis, NITROGENOUS SESQUITERPENES},
	isbn = {0040-4020},
	url = {<Go to ISI>://A1993LD38600006},
	author = {Burgoyne, D. L. and Dumdei, E. J. and Andersen, R. J.}
}
@article {7393,
	title = {REGIOSELECTIVE AND STEREOSELECTIVE DIELS-ALDER REACTIONS OF UNSYMMETRICAL 1,2-DISUBSTITUTED VINYL SULFONES WITH A MONOVINYLPORPHYRIN},
	journal = {New Journal of Chemistry},
	volume = {16},
	number = {5},
	year = {1992},
	note = {ISI Document Delivery No.: JK625Times Cited: 2Cited Reference Count: 15},
	month = {May},
	pages = {537-539},
	type = {Note},
	abstract = {A study of the Diels-Alder reactions of several 1,2-disubstituted vinyl sulfones with a beta-methyl-beta{\textquoteright}-monovinylporphyrin shows that the cycloadditions are highly regioselective and that stereochemical control can be manipulated by replacing a carboxyl ester group by a cyano group or by changing the geometry of the dienophile.},
	keywords = {biosynthesis, ROUTE},
	isbn = {1144-0546},
	url = {<Go to ISI>://A1992JK62500003},
	author = {Yonhin, P. and Wijesekera, T. P. and Dolphin, D.}
}
