@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 {1577,
	title = {Design of targeting ligands in medicinal inorganic chemistry},
	journal = {Chemical Society Reviews},
	volume = {35},
	number = {6},
	year = {2006},
	note = {ISI Document Delivery No.: 047UHTimes Cited: 58Cited Reference Count: 51},
	pages = {534-544},
	type = {Review},
	abstract = {This tutorial review will highlight recent advances in medicinal inorganic chemistry pertaining to the use of multifunctional ligands for enhanced effect. Ligands that adequately bind metal ions and also include specific targeting features are gaining in popularity due to their ability to enhance the efficacy of less complicated metal-based agents. Moving beyond the traditional view of ligands modifying reactivity, stabilizing specific oxidation states, and contributing to substitution inertness, we will discuss recent work involving metal complexes with multifunctional ligands that target specific tissues, membrane receptors, or endogenous molecules, including enzymes.},
	keywords = {CANCER, COMPLEXES, FLUORESCENCE, GADOLINIUM, IN-VITRO, PARACEST AGENTS, PROTEINS, RECEPTOR, therapy, TRANSPORT},
	isbn = {0306-0012},
	url = {<Go to ISI>://000237903700005},
	author = {Storr, T. and Thompson, K. H. and Orvig, Chris}
}
@article {1392,
	title = {Glucosamine conjugates of tricarbonylcyclopentadienyl rhenium(I) and technetium(I) cores},
	journal = {Inorganic Chemistry},
	volume = {45},
	number = {17},
	year = {2006},
	note = {ISI Document Delivery No.: 073DPTimes Cited: 13Cited Reference Count: 43Ferreira, Cara L. Ewart, Charles B. Bayly, Simon R. Patrick, Brian O. Steele, Jennifer Adam, Michael J. Orvig, Chris},
	month = {Aug},
	pages = {6979-6987},
	type = {Article},
	abstract = {To obtain a Tc-99m glucose conjugate for imaging, double-ligand transfer (DLT) and related reactions were examined for the preparation of CpM(CO)(3) (Cp = cyclopentadienyl; M = Re, Tc) complexes with pendant carbohydrates at Cp. Tricarbonyl {N-(1,3,4,6-tetra-O-acetyl-2-amino-2-deoxy-beta-D-glucopyranose) cyclopentadienyl carboxamide} rhenium(I) (1a) and tricarbonyl {N-(2-amino-2-deoxy-beta-D-glucopyranose) cyclopentadienyl carboxamide} rhenium(I) (2a) were prepared. The compounds were fully characterized by mass spectrometry, elemental analysis, IR, and NMR spectroscopy. Full assignment of the NMR spectra verified the pendant nature of the glucosamine moieties in the solution state and that 2a exists as both anomers. The solid-state structure of 2a was determined by X-ray crystallography, again confirming the pendant nature of the glucosamine, but differing from the solution state in that the, anomer crystallized preferentially (93\%). Compound 2a was determined to be a high-affinity competitive inhibitor (K-i = 330 +/- 70 mu M) of the glucose metabolism enzyme hexokinase, demonstrating that it retains certain biological activity. The Tc-99m analogues 1b and 2b were prepared in moderate radiochemical yields by means of the single-ligand transfer (SLT) route, which is more pertinent to radiopharmaceutical synthesis.},
	keywords = {BIOMOLECULES, COORDINATION, CYCLOPENTADIENYL-TRICARBONYL COMPLEXES, DERIVATIVES, FUNCTIONALIZATION, IN-VITRO, METAL-COMPLEXES, RE-186(I), RECEPTOR, TC-99M},
	isbn = {0020-1669},
	url = {<Go to ISI>://000239723300060},
	author = {Ferreira, C. L. and Ewart, C. B. and Bayly, S. R. and Patrick, B. O. and Steele, J. and Adam,Michael J. and Orvig, Chris}
}
@article {1392,
	title = {Glucosamine conjugates of tricarbonylcyclopentadienyl rhenium(I) and technetium(I) cores},
	journal = {Inorganic Chemistry},
	volume = {45},
	number = {17},
	year = {2006},
	note = {ISI Document Delivery No.: 073DPTimes Cited: 13Cited Reference Count: 43Ferreira, Cara L. Ewart, Charles B. Bayly, Simon R. Patrick, Brian O. Steele, Jennifer Adam, Michael J. Orvig, Chris},
	month = {Aug},
	pages = {6979-6987},
	type = {Article},
	abstract = {To obtain a Tc-99m glucose conjugate for imaging, double-ligand transfer (DLT) and related reactions were examined for the preparation of CpM(CO)(3) (Cp = cyclopentadienyl; M = Re, Tc) complexes with pendant carbohydrates at Cp. Tricarbonyl {N-(1,3,4,6-tetra-O-acetyl-2-amino-2-deoxy-beta-D-glucopyranose) cyclopentadienyl carboxamide} rhenium(I) (1a) and tricarbonyl {N-(2-amino-2-deoxy-beta-D-glucopyranose) cyclopentadienyl carboxamide} rhenium(I) (2a) were prepared. The compounds were fully characterized by mass spectrometry, elemental analysis, IR, and NMR spectroscopy. Full assignment of the NMR spectra verified the pendant nature of the glucosamine moieties in the solution state and that 2a exists as both anomers. The solid-state structure of 2a was determined by X-ray crystallography, again confirming the pendant nature of the glucosamine, but differing from the solution state in that the, anomer crystallized preferentially (93\%). Compound 2a was determined to be a high-affinity competitive inhibitor (K-i = 330 +/- 70 mu M) of the glucose metabolism enzyme hexokinase, demonstrating that it retains certain biological activity. The Tc-99m analogues 1b and 2b were prepared in moderate radiochemical yields by means of the single-ligand transfer (SLT) route, which is more pertinent to radiopharmaceutical synthesis.},
	keywords = {BIOMOLECULES, COORDINATION, CYCLOPENTADIENYL-TRICARBONYL COMPLEXES, DERIVATIVES, FUNCTIONALIZATION, IN-VITRO, METAL-COMPLEXES, RE-186(I), RECEPTOR, TC-99M},
	isbn = {0020-1669},
	url = {<Go to ISI>://000239723300060},
	author = {Ferreira, C. L. and Ewart, C. B. and Bayly, S. R. and Patrick, B. O. and Steele, J. and Adam,Michael J. and Orvig, Chris}
}
@article {1029,
	title = {Pachymoside A - A novel glycolipid isolated from the marine sponge Pachymatisma johnstonia},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {82},
	number = {2},
	year = {2004},
	note = {ISI Document Delivery No.: 802BHTimes Cited: 5Cited Reference Count: 21},
	month = {Feb},
	pages = {102-112},
	type = {Article},
	abstract = {Crude extracts of the North Sea marine sponge Pachymatisma johnstonia showed promising activity in a new assay for inhibitors of bacterial type III secretion. Bioassay-guided fractionation resulted in the isolation of the pachymosides, a new family of sponge glycolipids. A major part of the structural diversity in this family of glycolipids involves increasing degrees of acetylation and differing positions of acetylation on a common pachymoside glycolipid template. All of the metabolites with these variations in acetylation pattern were converted into the same peracetylpachymoside methyl ester (2) for purification and spectroscopic analysis. Pachymoside A (1) is the component of the mixture that has natural acetylation at the eight galactose hydroxyls and at the C-6 hydroxyls of glucose-B and glucose-D. Chemical degradation and transformation in conjunction with extensive analysis of 800 MHz NMR data was used to elucidate the structure of pachymoside A (1).},
	keywords = {BACTERIAL VIRULENCE, ENTEROPATHOGENIC ESCHERICHIA-COLI, glycolipid, GLYCOSPHINGOLIPIDS, HOST-CELLS, III SECRETION, inhibitors, marine sponge, NATURAL-PRODUCTS, Pachymatisma johnstonia, pachymoside, PLAKORTIS-SIMPLEX, PLAKOSIDE, PRENYLATED, RECEPTOR},
	isbn = {0008-4042},
	url = {<Go to ISI>://000220138500006},
	author = {Warabi, K. and Zimmerman, W. T. and Shen, J. K. and Gauthier, A. and Robertson, M. and Finlay, B. B. and Van Soest, R. and Andersen, R. J.}
}
@article {433,
	title = {Caminoside A, an antimicrobial glycolipid isolated from the marine sponge Caminus sphaeroconia},
	journal = {Organic Letters},
	volume = {4},
	number = {23},
	year = {2002},
	note = {ISI Document Delivery No.: 614DUTimes Cited: 21Cited Reference Count: 13},
	month = {Nov},
	pages = {4089-4092},
	type = {Article},
	abstract = {[GRAPHICS] Extracts of the marine sponge Caminus sphaeroconia showed potent activity in a screen for bacterial type III secretion inhibitors. Bioassay guided fractionation of the extract led to the isolation of the novel antimicrobial glycollpid caminoside A (1). The structure of caminoside A was elucidated by analysis of spectroscopic data and chemical degradation.},
	keywords = {ENTEROPATHOGENIC ESCHERICHIA-COLI, HOST-CELLS, PROTEIN, RECEPTOR, SECRETION, SYSTEMS},
	isbn = {1523-7060},
	url = {<Go to ISI>://000179173700026},
	author = {Linington, R. G. and Robertson, M. and Gauthier, A. and Finlay, B. B. and van Soes, R. and Andersen, R. J.}
}
@article {480,
	title = {Oligomerization-dependent association of the SAM domains from Schizosaccharomyces pombe Byr2 and Ste4},
	journal = {Journal of Biological Chemistry},
	volume = {277},
	number = {42},
	year = {2002},
	note = {ISI Document Delivery No.: 605EATimes Cited: 21Cited Reference Count: 46},
	month = {Oct},
	pages = {39585-39593},
	type = {Article},
	abstract = {SAM (sterile alpha motif) domains are protein-protein interaction modules found in a large number of regulatory proteins. Byr2 and Ste4 are two SAM domain-containing proteins in the mating pheromone response pathway of the fission yeast, Schizosaccharomyces pombe. Byr2 is a mitogen-activated protein kinase kinase kinase that is regulated by Ste4. Tu et al (Tu, H., Barr, M., Dong, D. L., and Wigler, M. (1997) Mol. Cell. Biol. 17, 5876-5887) showed that the isolated SAM domain of Byr2 binds a fragment of Ste4 that contains both a leucine zipper (Ste4-LZ) domain as well as a SAM domain, suggesting that Byr2-SAM and Ste4-SAM may form a hetero-oligomer. Here, we show that the individual SAM domains of Ste4 and Byr2 are monomeric at low concentrations and bind to each other in a 1:1 stoichiometry with a relatively weak dissociation constant of 56 +/- 3 mum. Inclusion of the Ste4-LZ domain, which determines the oligomeric state of Ste4, has a dramatic effect on binding affinity, however. We find that the Ste4-LZ domain is trimeric and, when included with the Ste4-SAM domain, yields a 3:1 Ste4-LZ-SAM:Byr2-SAM complex with a tight dissociation constant of 19 +/- 4 nm. These results suggest that the Ste4-LZ-SAM protein may recognize multiple binding sites on Byr2-SAM, indicating a new mode of oligomeric organization for SAM domains. The fact that high affinity binding occurs only with the addition of an oligomerization domain suggests that it may be necessary to include ancillary oligomerization modules when searching for binding partners of SAM domains.},
	keywords = {CRYSTAL-STRUCTURE, HUMAN LEUKEMIA, IDENTIFICATION, KINASE, LAC REPRESSOR, PROTEIN-KINASE, RECEPTOR, TEL, TRANSCRIPTION FACTOR, TYROSINE, YEAST},
	isbn = {0021-9258},
	url = {<Go to ISI>://000178662500069},
	author = {Ramachander, R. and Kim, C. A. and Phillips, M. L. and Mackereth, C. D. and Thanos, C. D. and McIntosh, L. P. and Bowie, J. U.}
}
@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.}
}
@article {3550,
	title = {ADHESION OF MAMMALIAN-CELLS TO A RECOMBINANT ATTACHMENT FACTOR, CBD/RGD, ANALYZED BY IMAGE-ANALYSIS},
	journal = {Biotechnology and Bioengineering},
	volume = {46},
	number = {3},
	year = {1995},
	note = {ISI Document Delivery No.: QR821Times Cited: 16Cited Reference Count: 26},
	month = {May},
	pages = {185-193},
	type = {Article},
	abstract = {A luminance thresholding procedure was developed to quantify cell attachment of a variety of cell lines to CBD/RGD, a hybrid attachment factor comprising a cellulose binding domain and the fibronectin-like RGD attachment peptide. The technique used local thresholding, median filtering, and opening to separate and count cells on each image. Cell lines exhibited three different patterns of attachment to CBD/RGD, depending on whether it was immobilized on polystyrene or cellulose acetate. Vero, COS, HFF, 3T3, 293, and U373 cells attached well to CBD/RGD immobilized on polystyrene or cellulose acetate. CHO, MRC-5, and HEp-2 cells attached to CBD/RGD immobilized on polystyrene, but not to CBD/RGD immobilized on cellulose acetate. BHK and L cells failed to attach to CBD/RGD immobilized on either polystyrene or cellulose acetate. The attachment of many cell lines to CBD/RGD was comparable with attachment of these cells to fibronectin. (C) 1995 John Wiley \& Sons, Inc.},
	keywords = {ALPHA-V, ARG-GLY-ASP, CELL ATTACHMENT, CELLULASE, CELLULOMONAS FIMI, FIBRONECTIN, FRAGMENT, GROWTH, HEPARIN-BINDING, IMAGE ANALYSIS, MAMMALIAN CELLS, RECEPTOR, RECOGNITION SIGNAL, SURFACES, VITRONECTIN},
	isbn = {0006-3592},
	url = {<Go to ISI>://A1995QR82100001},
	author = {Wierzba, A. and Reichl, U. and Turner, R. F. B. and Warren, R. A. J. and Kilburn, D. G.}
}
