@article {2663,
	title = {A Carboxy-Terminal Affinity Tag for the Purification and Mass Spectrometric Characterization of Integral Membrane Proteins},
	journal = {Journal of Proteome Research},
	volume = {8},
	number = {5},
	year = {2009},
	note = {ISI Document Delivery No.: 441BWTimes Cited: 3Cited Reference Count: 22Wong, Julie P. Reboul, Emmanuelle Molday, Robert S. Kast, Juergen},
	month = {May},
	pages = {2388-2396},
	type = {Article},
	abstract = {G-protein-coupled receptors (GPCRs) and other structurally and functionally related membrane proteins represent particularly attractive targets for drug discovery. Integral membrane proteins are often difficult to purify from native contexts, and lack of sufficient quantities hampers subsequent structural and functional proteomic studies. We describe here an optimized enrichment strategy involving a membrane protein-compatible 1D4 affinity tag that is derived from the carboxy-terminal nine amino residues of bovine rhodopsin, and its corresponding tag-specific, high-affinity monoclonal antibody. When two GPCRs as well as two related ATP binding cassette (ABC) transporters are expressed in their functional forms in human cell lines, we have shown that a single detergent and wash condition can be employed for the purification of all said membrane proteins. Subsequent in-gel digestion with trypsin and mass spectrometric peptide analysis resulted in high sequence coverage for the ABC transporters ABCA1-1D4 and ABCA4-1D4. In contrast, digestion by various enzymatic combinations was necessary to obtain the best sequence coverage for affinity-enriched GPCRs CXCR4-1D4 and CCR5-1D4 as compared against other entries in an annotated spectrum library. Furthermore, specific enzyme combinations were necessary to produce suitable peptides for deducing N-glycosylation sites on CXCR4. Our results demonstrate that the 1D4-tag enrichment strategy is a versatile tool for the characterization of integral membrane proteins that can be employed for functional proteomic studies.},
	keywords = {1D4 affinity tag, 2-DIMENSIONAL, annotated spectrum libraries, ATP binding cassette transporters, BINDING, ELECTROPHORESIS, EXPRESSION, G-protein-coupled, membrane protein enrichment, N-LINKED GLYCOSYLATION, PROTEOMICS, proteotypic peptides, RECEPTOR, RECEPTORS, RHODOPSIN, ROD OUTER SEGMENTS, SITES, SYNTHETIC PEPTIDES, Tandem mass spectrometry},
	isbn = {1535-3893},
	url = {<Go to ISI>://000265745300025},
	author = {Wong, J. P. and Reboul, E. and Molday, R. S. and Kast, J.}
}
@article {1603,
	title = {The anti-invasive compound motuporamine C is a robust stimulator of neuronal growth cone collapse},
	journal = {Neuroscience},
	volume = {139},
	number = {4},
	year = {2006},
	note = {ISI Document Delivery No.: 044SBTimes Cited: 7Cited Reference Count: 41},
	pages = {1263-1274},
	type = {Article},
	abstract = {Neuronal outgrowth is a fundamental process for normal development of the nervous system. Despite recent advances, the molecular mechanisms governing neuronal motility are still poorly understood. To provide insight into the intracellular signaling mechanisms required for neuronal outgrowth, we have characterized the effects of a compound previously identified for its anti-motility effects on transformed cells. We show that this compound, motuporamine C, acts as a robust inhibitor of chick neurite outgrowth in a dose-dependent fashion. Furthermore, in the presence of motuporamine C, growth cone collapse is observed, followed by neurite retraction. After removal, growth cones re-extend lamellipodial and filopodial processes and re-establish motility. Neurons exposed to motuporamine C exhibit a significant upregulation of active Rho-GTP. Additionally, effector-blocking experiments using Rho and Rho-associated kinase inhibitors indicate that the Rho pathway plays a critical role in motuporamine C-mediated growth cone collapse. Thus, we have characterized a novel anti-motility compound that has a robust inhibitory effect on neuronal outgrowth and involves signaling through the Rho-Rho kinase collapse pathway. Due to these robust effects, motuporamine C may serve as a valuable tool in further examining the intracellular mechanisms associated with growth cone motility. (c) 2006 IBRO. Published by Elsevier Ltd. All rights reserved.},
	keywords = {ACTIN STRESS FIBERS, ADP-RIBOSYLATION, AXONAL GROWTH, BINDING PROTEIN-RHO, collapse, development, FOCAL ADHESIONS, growth cone, IN-VIVO, KINASE-ACTIVITY, LYSOPHOSPHATIDIC ACID, motuporamine, NEURITE RETRACTION, outgrowth, RECEPTORS, Rho GTPase},
	isbn = {0306-4522},
	url = {<Go to ISI>://000237691600009},
	author = {To, K. C. W. and Loh, K. T. and Roskelley, C. D. and Andersen, R. J. and O{\textquoteright}Connor, T. P.}
}
@article {1116,
	title = {Synthesis, structure, and computational studies of soluble conjugated multidentate macrocycles},
	journal = {J. Org. Chem.},
	volume = {70},
	number = {20},
	year = {2005},
	note = {ISI Document Delivery No.: 968MOTimes Cited: 47Cited Reference Count: 67},
	month = {Sep},
	pages = {7936-7946},
	type = {Article},
	abstract = {<p>Conjugated, shape-persistent macrocycles based on [3 + 3] Schiff-base condensation are of interest for supramolecular materials. In an effort to develop new discotic liquid crystals based on these compounds, a series of macrocycles with peripheral alkoxy groups of varying length have been prepared. The synthesis and mechanism of formation have been probed by isolation of oligomeric intermediates. A single-crystal X-ray diffraction study of one macrocycle revealed a nonplanar, strongly hydrogen-bonded structure. To our surprise, even with very long substituents, the macrocycles were not liquid crystalline. This has been rationalized by ab initio calculations that indicate the macrocycles are undergoing rotation of the dibydroxydiiminobenzene rings that may not allow a stable discotic liquid crystalline phase. These results provide new insight into the formation and properties of these large macrocycles and may provide guidance to developing stable liquid crystalline materials in the future.</p>},
	keywords = {CHEMISTRY, CRYSTAL-STRUCTURE, cyclodextrin, LIGANDS, LIQUID-CRYSTAL, METAL-COMPLEXES, porphyrins, RECEPTORS, SCHIFF-BASE MACROCYCLES, SHAPE-PERSISTENT MACROCYCLES, supramolecular},
	isbn = {0022-3263},
	url = {<Go to ISI>://000232166800015},
	author = {Gallant, A. J. and J. K.-H. Hui and Zahariev, F. E. and Y. A. Wang* and M. J. MacLachlan*}
}
@article {4647,
	title = {The structures of the neurotrophin 4 homodimer and the brain-derived neurotrophic factor/neurotrophin 4 heterodimer reveal a common Trk-binding site},
	journal = {Protein Science},
	volume = {8},
	number = {12},
	year = {1999},
	note = {ISI Document Delivery No.: 266RPTimes Cited: 24Cited Reference Count: 45},
	month = {Dec},
	pages = {2589-2597},
	type = {Article},
	abstract = {The neurotrophins are growth factors that are involved in the development and survival of neurons. Neurotrophin release by a target tissue results in neuron growth along the neurotrophin concentration gradient, culminating in the eventual innervation of the target tissue. These activities are mediated through trk cell surface receptors. We have determined the structures of the heterodimer formed between brain-derived neurotrophic factor (BDNF) and neurotrophin 4 (NT4), as well as the structure of homodimer of NT4. We also present the structure of the Neurotrophin 3 homodimer, which is refined to higher resolution than previously published. These structures provide the first views of the architecture of the NT4 protomer. Comparison of the surface of a model of the BDNF homodimer with the structures of the neurotrophin homodimers reveals common features that may be important in the binding between the neurotrophins and their receptors. In particular, there exists an analogous region on the surface of each neurotrophin that is likely to be involved in trk receptor binding. Variations in sequence on the periphery of this common region serve to confer trk receptor specificity.},
	keywords = {BDNF, CELLS, CRYSTAL-STRUCTURE, CRYSTALLOGRAPHY, DIFFERENTIATION, nerve growth factor, NERVE GROWTH-FACTOR, NGF, PURIFICATION, RECEPTOR, RECEPTORS, RECOGNITION, SPECIFICITY},
	isbn = {0961-8368},
	url = {<Go to ISI>://000084314100005},
	author = {Robinson, R. C. and Radziejewski, C. and Spraggon, G. and Greenwald, J. and Kostura, M. R. and Burtnick, L. D. and Stuart, D. I. and Choe, S. and Jones, E. Y.}
}
