@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 {2653,
	title = {Helix Straightening as an Activation Mechanism in the Gelsolin Superfamily of Actin Regulatory Proteins},
	journal = {Journal of Biological Chemistry},
	volume = {284},
	number = {32},
	year = {2009},
	note = {ISI Document Delivery No.: 478CCTimes Cited: 4Cited Reference Count: 23Wang, Hui Chumnarnsilpa, Sakesit Loonchanta, Anantasak Li, Qiang Kuan, Yang-Mei Robine, Sylvie Larsson, Marten Mihalek, Ivana Burtnick, Leslie D. Robinson, Robert C.},
	month = {Aug},
	pages = {21265-21269},
	type = {Article},
	abstract = {Villin and gelsolin consist of six homologous domains of the gelsolin/cofilin fold (V1-V6 and G1-G6, respectively). Villin differs from gelsolin in possessing at its C terminus an unrelated seventh domain, the villin headpiece. Here, we present the crystal structure of villin domain V6 in an environment in which intact villin would be inactive, in the absence of bound Ca2+ or phosphorylation. The structure of V6 more closely resembles that of the activated form of G6, which contains one bound Ca2+, rather than that of the calcium ion-free form of G6 within intact inactive gelsolin. Strikingly apparent is that the long helix in V6 is straight, as found in the activated form of G6, as opposed to the kinked version in inactive gelsolin. Molecular dynamics calculations suggest that the preferable conformation for this helix in the isolated G6 domain is also straight in the absence of Ca2+ and other gelsolin domains. However, the G6 helix bends in intact calcium ion-free gelsolin to allow interaction with G2 and G4. We suggest that a similar situation exists in villin. Within the intact protein, a bent V6 helix, when triggered by Ca2+, straightens and helps push apart adjacent domains to expose actin-binding sites within the protein. The sixth domain in this superfamily of proteins serves as a keystone that locks together a compact ensemble of domains in an inactive state. Perturbing the keystone initiates reorganization of the structure to reveal previously buried actin-binding sites.},
	keywords = {BINDING PROTEINS, calcium, COMPLEX, DOMAINS, F-ACTIN, HEADPIECE, SITES, SWITCH, TERMINAL HALF, VILLIN},
	isbn = {0021-9258},
	url = {<Go to ISI>://000268564400020},
	author = {Wang, H. and Chumnarnsilpa, S. and Loonchanta, A. and Li, Q. and Kuan, Y. M. and Robine, S. and Larsson, M. and Mihalek, I. and Burtnick, L. D. and Robinson, R. C.}
}
@article {1233,
	title = {Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region},
	journal = {Science},
	volume = {309},
	number = {5731},
	year = {2005},
	note = {ISI Document Delivery No.: 941KDTimes Cited: 66Cited Reference Count: 30},
	month = {Jul},
	pages = {142-145},
	type = {Article},
	abstract = {Cell signaling that culminates in posttranslational modifications directs protein activity. Here we report how multiple Ca2+-dependent phosphorylation sites within the transcription activator Ets-1 act additively to produce graded DNA binding affinity. Nuclear magnetic resonance spectroscopic analyses show that phosphorylation shifts Ets-1 from a dynamic conformation poised to bind DNA to a well-folded inhibited state. These phosphates lie in an unstructured flexible region that functions as the allosteric effector of autoinhibition. Variable phosphorylation thus serves as a "rheostat" for cell signaling to fine-tune transcription at the level of DNA binding.},
	keywords = {allosteric regulation, AUTOINHIBITION, DOMAIN, DYNAMICS, NMR-SPECTROSCOPY, PHOSPHORYLATION, PROTEIN, SITES, TRANSACTIVATION, TRANSCRIPTION FACTOR NFAT1},
	isbn = {0036-8075},
	url = {<Go to ISI>://000230212800079},
	author = {Pufall, M. A. and Lee, G. M. and Nelson, M. L. and Kang, H. S. and Velyvis, A. and Kay, L. E. and McIntosh, L. P. and Graves, B. J.}
}
@article {940,
	title = {Covalent Schiff base catalysis and turnover by a DNAzyme: A M2+ independent AP-endonuclease mimic},
	journal = {Journal of the American Chemical Society},
	volume = {126},
	number = {13},
	year = {2004},
	note = {ISI Document Delivery No.: 809LBTimes Cited: 44Cited Reference Count: 117},
	month = {Apr},
	pages = {4145-4156},
	type = {Review},
	abstract = {A DNAzyme, synthetically modified with both primary amines and imidazoles, is found to act as a M2+ -independent AP lyase-endonuclease. In the course of the cleavage reaction, this DNAzyme forms a covalent Schiff base intermediate with an abasic site on a complementary oligodeoxyribonucleotide. This intermediate, which is inferred from NaCNBH3 trapping as well as cyanide inhibition, does not evidently accumulate because the second step, dehydrophosphorylative elimination, is fast compared to Schiff base formation. The 5{\textquoteright}-product that remains linked to the catalyst hydrolyzes slowly to regenerate free catalyst. The use of duly modified DNAzymes to perform Schiff base catalysis demonstrates the value of modified nucleotides for enhancing the catalytic repertoire of nucleic acids. This work suggests that DNAzymes will be capable of catalyzing aldol condensation reactions.},
	keywords = {ALDEHYDIC ABASIC, APURINIC SITES, BETA-ELIMINATION, DIVALENT METAL-ION, FUNCTIONALITIES, IMIDAZOLYL, IN-VITRO SELECTION, NUCLEIC-ACIDS, RNA CLEAVAGE, SITES, TETRAHYMENA RIBOZYME, THERMOSTABLE DNA-POLYMERASES},
	isbn = {0002-7863},
	url = {<Go to ISI>://000220637100042},
	author = {May, J. P. and Ting, R. and Lermer, L. and Thomas, J. M. and Roupioz, Y. and Perrin,David M.}
}
@article {4313,
	title = {Unfolding of proteins monitored by electrospray ionization mass spectrometry: A comparison of positive and negative ion modes},
	journal = {Journal of the American Society for Mass Spectrometry},
	volume = {9},
	number = {12},
	year = {1998},
	note = {ISI Document Delivery No.: 141FPTimes Cited: 72Cited Reference Count: 56},
	month = {Dec},
	pages = {1248-1254},
	type = {Article},
	abstract = {Electrospray ionization (ESI) mass spectrometry (MS) in both the positive and negative ion mode has been used to study protein unfolding transitions of lysozyme, cytochrome c (cyt c), and ubiquitin in solution. As expected, ESI of unfolded lysozyme leads to the formation of substantially higher charge states than the tightly folded protein in both modes of operation. Surprisingly, the acid-induced unfolding of cyt c as well as the acid and the base-induced unfolding of ubiquitin show different behavior: In these three cases protein unfolding only leads to marginal changes in the negative ion charge state distributions, whereas in the positive ion mode pronounced shifts to higher charge states are observed. This shows that ESI MS in the negative ion mode as a method for probing conformational changes of proteins in solution should be treated with caution. The data presented in this work provide further evidence that the conformation of a protein in solution not its charge state is the predominant factor for determining the ESI charge slate distribution in the positive ion mode. Furthermore, these data support the hypothesis of a recent study (Konermann and Douglas, Biochemistry 1997, 36, 12296-12302) which suggested that ESI in the positive ion mode is not sensitive to changes in the secondary structure of proteins but only to changes in the tertiary structure. (C) 1998 American Society for Mass Spectrometry.},
	keywords = {A-STATE, BINDING, CIRCULAR-DICHROISM, CYTOCHROME-C, HYDROGEN-DEUTERIUM EXCHANGE, INDUCED CONFORMATIONAL-CHANGES, MYOGLOBIN, NUCLEAR-MAGNETIC-RESONANCE, SITES, SPECTRA, UBIQUITIN},
	isbn = {1044-0305},
	url = {<Go to ISI>://000077132600002},
	author = {Konermann, L. and Douglas, D. J.}
}
@article {4330,
	title = {XPS studies of the nitridation of MoO3 thin films on alumina and silica supports},
	journal = {Applied Surface Science},
	volume = {136},
	number = {3},
	year = {1998},
	note = {ISI Document Delivery No.: 140QWTimes Cited: 3Cited Reference Count: 40},
	month = {Nov},
	pages = {178-188},
	type = {Article},
	abstract = {X-ray photoelectron spectroscopy has been used to characterize thin films of MoO3 formed on planar oxidized supports, namely AlOx (from aluminum strip) and SiO2 (from silicon wafer). Comparisons are made with behaviour for MoO3 on metallic Mo substrate. It is observed that on calcination at 450 degrees C, the Mo 3d spectral features shift to higher binding energy for MoO3/AlOx and to lower binding energy for MoO3/SiO2, On nitridation by heating in NH3, it is found that the samples on the oxide supports show easier O-N replacement compared with the MoO3/Mo system. In general, the nitridation behaviour for MoO3/AlO, is similar to that of MoO3/Mo, but Mo species in MoO3/SiO2 seem to be more easily reduced (Mo(0) is detected for the SiO2 system but not for AlOx). Comparisons of heating rates for the second nitridation step from 350 to 450 degrees C were made for the MoO3/Mo and MoO3/AlOx samples. Differences between the high heating rate (100 K/h) and the low heating rate (40 K/h) are incremental but definite. The lower heating rate is favourable both for the O-N replacement and for the metal reduction. For example, more Mo(+3) is present after the nitridation to 450 degrees C when the low-heating rate regime is used, compared with that formed when the heating is done at the higher rate. (C) 1998 Elsevier Science B.V. All rights reserved.},
	keywords = {ADSORPTION, BEHAVIOR, CARBIDE, HYDRODENITROGENATION CATALYSTS, HYDRODESULFURIZATION, MOLYBDENUM NITRIDE, MoO3 thin films, nitridation, QUINOLINE, SITES, SURFACE-AREA, THIOPHENE, X-ray photoelectron, X-ray photoelectron spectroscopy},
	isbn = {0169-4332},
	url = {<Go to ISI>://000077100700002},
	author = {Leung, Y. L. and Wong, P. and Zhou, M. Y. and Mitchell, K. A. R. and Smith, K. J.}
}
@article {7022,
	title = {NATURAL ABUNDANCE, 2-DIMENSIONAL SI-29 MAS NMR INVESTIGATION OF THE 3-DIMENSIONAL BONDING CONNECTIVITIES IN THE HIGH-TEMPERATURE AND LOW-TEMPERATURE FORMS OF ZEOLITE ZSM-11},
	journal = {Journal of Physical Chemistry},
	volume = {95},
	number = {9},
	year = {1991},
	note = {ISI Document Delivery No.: FK322Times Cited: 20Cited Reference Count: 29},
	month = {May},
	pages = {3747-3751},
	type = {Article},
	abstract = {Two-dimensional 29Si solid-state NMR experiments have been used to investigate the three-dimensional bonding connectivities in ZSM-11 in both its high- and low-temperature forms, which are related to each other by a temperature-induced phase transition. The high-temperature form is known to have tetragonal symmetry with space group I4BARm2, while the details of the ZSM-11 structure at low temperatures are not known to date from diffraction measurements. 2-D INADEQUATE experiments at high temperature (340 K) confirmed the postulated structure. All of the nine expected connectivities were observed, permitting an unambiguous assignment of the spectrum. In the low-temperature (303 K) 2-D experiments, enough information was obtained that, combined with the knowledge of the high-temperature structure, a structure could be suggested for the low-temperature form. The complete connectivities of T sites in the structure were established, and at least one space group, I4BAR, is compatible with the NMR data.},
	keywords = {coherence, DIFFRACTION, LATTICE CONNECTIVITIES, SITES, SOLID-STATE NMR, SPECTROSCOPY},
	isbn = {0022-3654},
	url = {<Go to ISI>://A1991FK32200057},
	author = {Fyfe, C. A. and Feng, Y. and Grondey, H. and Kokotailo, G. T. and Mar, A.}
}
