@article {4070,
	title = {Stereospecific assignment of the NH2 resonances from the primary amides of asparagine and glutamine side chains in isotopically labeled proteins},
	journal = {Journal of Biomolecular Nmr},
	volume = {9},
	number = {3},
	year = {1997},
	note = {ISI Document Delivery No.: XF937Times Cited: 18Cited Reference Count: 33},
	month = {Apr},
	pages = {306-312},
	type = {Article},
	abstract = {An HMQC-based pulse scheme is presented for the stereospecific assignment of asparagine and glutamine side-chain amide protons. The approach makes use of the recently developed quantitative-J correlation spectroscopy [Bar, A. et al. (1994) Methods Enzymol., 239, 79-105] to distinguish the E and Z primary amide protons and, as such, eliminates the need for assignments derived from more time-consuming and potentially ambiguous NOE methods. An application of this method to a uniformly N-15,C-13-labeled cellulose-binding domain is presented. When used in combination with a NOESY-HSQC experiment, the predominant chi(2) dihedral angles of two asparagine side chains in this protein can also be defined.},
	keywords = {ANGLE, BACKBONE AMIDE, C-13 MAGNETIZATION, dihedral, EXCITATION, H-1, HMQC spectroscopy, LARGER PROTEINS, N-15, NMR, primary amide, SATURATION, SPECTRA, SPECTROSCOPY, STEREOSPECIFIC ASSIGNMENT},
	isbn = {0925-2738},
	url = {<Go to ISI>://A1997XF93700008},
	author = {McIntosh, L. P. and Brun, E. and Kay, L. E.}
}
@article {3819,
	title = {Structural coupling of the inhibitory regions flanking the ETS domain of murine Ets-1},
	journal = {Protein Science},
	volume = {5},
	number = {2},
	year = {1996},
	note = {ISI Document Delivery No.: TU724Times Cited: 46Cited Reference Count: 66},
	month = {Feb},
	pages = {296-309},
	type = {Article},
	abstract = {Several members of the ets gene family of transcription factors show negative regulation of DNA binding by intramolecular interactions. A structural mechanism for this auto-inhibition is investigated using a 161-residue N-terminal deletion mutant of murine Ets-1, Ets-1 Delta N280. This protein shows a similar reduced affinity for DNA as native Ets-1 because it contains the ETS domain in context of the flanking amino- and carboxy-terminal regions that together mediate repression of DNA binding. The secondary structure of Ets-1 Delta N280 was determined using NMR chemical shift, NOE, J coupling, and amide hydrogen exchange information. In addition to the winged helix-turn-helix ETS domain, Ets-1 Delta N280 contains two alpha-helices in the amino-terminal inhibitory region and one alpha-helix in the carboxy-terminal inhibitory region. Chemical shift comparisons were made between this protein and an activated form of Ets-1 lacking the amino-terminal inhibitory region. The spectral differences demonstrate that the amino- and carboxy-terminal inhibitory sequences are structurally coupled to one another, thus explaining the observation that both regions are required for the repression of DNA binding. Furthermore, these data show that the inhibitory sequences also interact directly with the first helix of the intervening ETS domain, thereby providing a pathway for the repression of DNA binding. These results lead to a model of an inhibitory module in Ets-1 composed of both the amino- and carboxy-terminal regions interfaced with the ETS domain. This establishes the structural framework for understanding the intramolecular inhibition of Ets-1 DNA binding.},
	keywords = {3-DIMENSIONAL NMR-SPECTROSCOPY, allosteric, ASSIGNMENT, CRYSTAL-STRUCTURE, DNA binding, DNA-BINDING MOTIF, ETS domain, Ets-1 and Ets-2, FACTORS, H-1, INHIBITION, INTRAMOLECULAR, LARGER PROTEINS, N-15 NMR, NMR, protein structure, SPECTRA, transcription, V-ETS, winged helix-turn-helix},
	isbn = {0961-8368},
	url = {<Go to ISI>://A1996TU72400014},
	author = {Skalicky, J. J. and Donaldson, L. W. and Petersen, J. M. and Graves, B. J. and McIntosh, L. P.}
}
@article {7186,
	title = {CONTIGNASTEROL, A HIGHLY OXYGENATED STEROID WITH THE UNNATURAL 14-BETA CONFIGURATION FROM THE MARINE SPONGE PETROSIA-CONTIGNATA THIELE, 1899},
	journal = {Journal of Organic Chemistry},
	volume = {57},
	number = {2},
	year = {1992},
	note = {ISI Document Delivery No.: HA466Times Cited: 56Cited Reference Count: 18},
	month = {Jan},
	pages = {525-528},
	type = {Article},
	abstract = {Contignasterol (1), a highly oxygenated steroid with the {\textquoteright}{\textquoteright}unnatural{\textquoteright}{\textquoteright} 14-beta proton configuration and a cyclic hemiacetal functionality in its side chain, has been isolated from the marine sponge Petrosia contignata. The structure of contignasterol was elucidated via spectroscopic studies of its tetraacetate 2 and its reduction product pentaacetate 5. Contignasterol (1) is the first example of a naturally occurring steroid with the {\textquoteright}{\textquoteright}unnatural{\textquoteright}{\textquoteright} 14-beta proton configuration.},
	keywords = {C-13 ASSIGNMENTS, H-1, NMR-SPECTROSCOPY},
	isbn = {0022-3263},
	url = {<Go to ISI>://A1992HA46600024},
	author = {Burgoyne, D. L. and Andersen, R. J. and Allen, T. M.}
}
@article {7080,
	title = {RUBROLIDES-A-H, METABOLITES OF THE COLONIAL TUNICATE RITTERELLA-RUBRA},
	journal = {Journal of Organic Chemistry},
	volume = {56},
	number = {22},
	year = {1991},
	note = {ISI Document Delivery No.: GM576Times Cited: 53Cited Reference Count: 25},
	month = {Oct},
	pages = {6275-6280},
	type = {Article},
	abstract = {Rubrolides A (1) to H (8), a new family of biologically active tunicate metabolites, have been isolated from Ritterella rubra. The structures of the rubrolides were solved by a combination of spectroscopic analysis and chemical interconversions. Rubrolides B (2) and H (8) represent some of the first chlorinated metabolites known from tunicates. The rubrolides are potent in vitro antibiotics and they show moderate but selective inhibition of protein phosphatases 1 and 2A.},
	keywords = {C-13 ASSIGNMENTS, CARIBBEAN TUNICATE, ECTEINASCIDIA-TURBINATA, H-1, MARINE NATURAL-PRODUCTS, NMR, SIGILLINOIDES},
	isbn = {0022-3263},
	url = {<Go to ISI>://A1991GM57600012},
	author = {Miao, S. C. and Andersen, R. J.}
}
@article {7083,
	title = {TRITERPENOID GLYCOSIDES FROM THE NORTHEASTERN PACIFIC MARINE SPONGE XESTOSPONGIA-VANILLA},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {69},
	number = {9},
	year = {1991},
	note = {ISI Document Delivery No.: GH861Times Cited: 7Cited Reference Count: 13},
	month = {Sep},
	pages = {1352-1364},
	type = {Article},
	abstract = {Isoxestovanin A (6), xestovanin B (7), xestovanin C (8), dehydroxestovanin A (9), epidehydroxestovanin A (10), dehydroxestovanin C (11), and secodehydroxestovanin A (12), seven new triterpenoid glycosides, have been isolated from the Northeastern Pacific sponge Xestospongia vanilla. The structures of the metabolites were determined by a combination of spectroscopic analysis and chemical degradation. The aglycone of 6 has the new isoxestovanane triterpenoid carbon skeleton. Compounds 7, 8, and 11 are the first X. vanilla triterpenoid glycosides known to contain three monosaccharide subunits.},
	keywords = {C-13 ASSIGNMENTS, GLYCOSIDE, H-1, NMR, SPONGE, SUGARS, TRITERPENOID, XESTOSPONGIA},
	isbn = {0008-4042},
	url = {<Go to ISI>://A1991GH86100003},
	author = {Morris, S. A. and Northcote, P. T. and Andersen, R. J.}
}
