@article {2547,
	title = {Design and Synthesis of Novel Phenothiazinium Photosensitiser Derivatives},
	journal = {European Journal of Organic Chemistry},
	number = {16},
	year = {2009},
	note = {ISI Document Delivery No.: 452FITimes Cited: 1Cited Reference Count: 39New, Olivia M. Dolphin, David},
	month = {Jun},
	pages = {2675-2686},
	type = {Article},
	abstract = {A high-yielding approach towards N-(2-aminoethyl)-Azure B has been established and extended towards the preparation of a functionalized peptide-dye synthetic precursor; Boc-protected 3-(alkylamino)phenothiazin-5-ium TFA. This has been utilized in a series of reactions with various amines towards nine novel 3,7-disubstituted phenothiazin-5-ium derivatives. Cleavage of the Boc group in the 3,7-disubstituted salts allowed a further seven novel dyes to be prepared and these have been utilized in a practical methodology designed for the synthesis of 13 novel phenothiazine-peptide conjugates. These peptide-photosensitizer vectors consist of a covalent attachment of a tethered dye to various protected amino acid moieties including the cell-penetrating peptide (CPP) octa-arginine and exhibit intense absorption maxima in the 623650 nm regions of the visible spectrum. The main goal of the studies is the design of cell-compatible photosensitisers that may be employed in photodynamic therapy. ((C) Wiley-VCH Verlag GmbH \& Co. KGaA, 69451 Weinheim, Germany, 2009)},
	keywords = {AMINATION, ANALOGS, Azure B, BENZOPHENOTHIAZINE, Cell-penetrating peptide, CELLULAR DELIVERY, Dye-peptide conjugate, Electronic spectra, METHYLENE-BLUE, Phenothiazine dye, PHOTODYNAMIC THERAPY, SERIES, TRANSDUCTION, TRANSLOCATION, TRANSPORTERS, TUMORS},
	isbn = {1434-193X},
	url = {<Go to ISI>://000266525100010},
	author = {New, O. M. and Dolphin, D.}
}
@article {2072,
	title = {Phage display and crystallographic analysis reveals potential substrate/binding site interactions in the protein secretion chaperone CsaA from Agrobacterium tumefaciens},
	journal = {Journal of Molecular Biology},
	volume = {379},
	number = {3},
	year = {2008},
	note = {ISI Document Delivery No.: 311FQTimes Cited: 0Cited Reference Count: 52Feldman, Anat R. Shapova, Yuliya A. Wu, Sampson S. T. Oliver, David C. Heller, Markus McIntosh, Lawrence P. Scott, Jamie K. Paetzel, Mark},
	month = {Jun},
	pages = {457-470},
	type = {Article},
	abstract = {The protein CsaA has been proposed to function as a protein secretion chaperone in bacteria that lack the Sec-dependent protein-targeting chaperone SecB. CsaA is a homodimer with two putative substrate-binding pockets, one in each monomer. To test the hypothesis that these cavities are indeed substrate-binding sites able to interact with other polypeptide chains, we selected a peptide that bound to CsaA from a random peptide library displayed on phage. Presented here is the structure of CsaA from Agrobacterium tumefaciens (AtCsaA) solved in the presence and absence of the selected peptide. To promote co-crystallization, the sequence for this peptide was genetically fused to the amino-terminus of AtCsaA. The resulting 1.65 angstrom resolution crystal structure reveals that the tethered peptide from one AtCsaA molecule binds to the proposed substrate-binding pocket of a symmetry-related molecule possibly mimicking the interaction between a pre-protein substrate and CsaA. The structure shows that the peptide lies in an extended conformation with alanine, proline and glutamine side chains pointing into the binding pocket. The peptide interacts with the atoms of the AtCsaA-binding pocket via seven direct hydrogen bonds. The side chain of a conserved pocket residue, Arg76, has an "up" conformation when the CsaA-binding site is empty and a "down" conformation when the CsaA-binding site is occupied, suggesting that this residue may function to stabilize the peptide in the binding cavity. The presented aggregation assays, phage-display analysis and structural analysis are consistent with AtCsaA being a general chaperone. The properties of the proposed CsaA-binding pocket/peptide interactions are compared to those from other structurally characterized molecular chaperones. (c) 2008 Elsevier Ltd. All rights reserved.},
	keywords = {BACILLUS-SUBTILIS CSAA, BACTERIAL SIGNAL PEPTIDASE, BINDING PROTEIN, CHANNEL, CRYSTAL-STRUCTURE, CsaA, DISPLAY, LIBRARIES, molecular chaperone, phage, PROTEIN SECRETION, protein targeting, SECA, SEQUENCE, STRUCTURAL SUPERPOSITION, TRANSLOCATION},
	isbn = {0022-2836},
	url = {<Go to ISI>://000256586500006},
	author = {Feldman, A. R. and Shapova, Y. A. and Wu, S. S. T. and Oliver, D. C. and Heller, M. and McIntosh, L. P. and Scott, J. K. and Paetzel, M.}
}
@article {1355,
	title = {Roles for the Drs2p-Cdc50p complex in protein transport and phosphatidylserine asymmetry of the yeast plasma membrane},
	journal = {Traffic},
	volume = {7},
	number = {11},
	year = {2006},
	note = {ISI Document Delivery No.: 093GOTimes Cited: 30Cited Reference Count: 76Chen, Sophie Wang, Jiyi Muthusamy, Baby-Periyanayaki Liu, Ke Zare, Sara Andersen, Raymond J. Graham, Todd R.},
	month = {Nov},
	pages = {1503-1517},
	type = {Article},
	abstract = {Drs2p, a P-type adenosine triphosphatase required for a phosphatidylserine (PS) flippase activity in the yeast trans Golgi network (TGN), was first implicated in protein trafficking by a screen for mutations synthetically lethal with arf1 (swa). Here, we show that SWA4 is allelic to CDC50, encoding a membrane protein previously shown to chaperone Drs2p from the endoplasmic reticulum to the Golgi complex. We find that cdc50 Delta exhibits the same clathrin-deficient phenotypes as drs2 Delta, including delayed transport of carboxypeptidase Y to the vacuole, mislocalization of resident TGN enzymes and the accumulation of aberrant membrane structures. These trafficking defects precede appearance of cell polarity defects in cdc50 Delta, suggesting that the latter are a secondary consequence of disrupting Golgi function. Involvement of Drs2p-Cdc50p in PS translocation suggests a role in restricting PS to the cytosolic leaflet of the Golgi and plasma membrane. Annexin V binding and papuamide B hypersensitivity indicate that drs2 Delta or cdc50 Delta causes a loss of plasma membrane PS asymmetry. However, clathrin and other endocytosis null mutants also exhibit a comparable loss of PS asymmetry, and studies with drs2-ts and clathrin (chc1-ts) conditional mutants suggest that loss of plasma membrane asymmetry is a secondary consequence of disrupting protein trafficking.},
	keywords = {annexin V, ATPase, B, CARBOXYPEPTIDASE-Y, Cdc50p, clathrin, CLATHRIN-COATED VESICLES, Drs2p, flippase, Golgi complex, GOLGI-COMPLEX, IN-VIVO, INTRAHEPATIC CHOLESTASIS, P-type, P-TYPE ATPASES, papuamide, phosphatidylserine, PHOSPHOLIPID, PUTATIVE AMINOPHOSPHOLIPID, SACCHAROMYCES-CEREVISIAE, TRANSLOCASES, TRANSLOCATION, VACUOLAR PROTEINS},
	isbn = {1398-9219},
	url = {<Go to ISI>://000241156500008},
	author = {Chen, S. and Wang, J. Y. and Muthusamy, B. P. and Liu, K. and Zare, S. and Andersen, R. J. and Graham, T. R.}
}
@article {784,
	title = {Chronic glucose-lowering effects of rosiglitazone and bis(ethylmaltolato)oxovanadium(IV) in ZDF rats},
	journal = {Canadian Journal of Physiology and Pharmacology},
	volume = {81},
	number = {11},
	year = {2003},
	note = {ISI Document Delivery No.: 749AHTimes Cited: 3Cited Reference Count: 47},
	month = {Nov},
	pages = {1049-1055},
	type = {Article},
	abstract = {The aim of this study was to determine if there was a synergistic or additive effect of a thiazolidinedione derivative (rosiglitazone (ROS)) and a vanadium compound (bis(ethylmaltolato)oxovanadium(IV) (BEOV)) on plasma glucose and insulin levels following chronic oral administration to Zucker diabetic fatty (ZDF) rats. Whole-blood vanadium levels were determined at time 0 and at days 1, 6, and 18. The doses of BEOV (0.1 mmol/kg) and ROS (2.8 mumol/kg) were selected to produce a glucose-lowering effect in 30\% (ED30) of animals. Both drugs were administered daily by oral gavage as suspensions in 1\% carboxymethylcellulose (CMC) in a volume of 2.5 mL/kg. The total volume administered to all rats was 5 mL/(kg-day). The combination of BEOV and ROS was effective in lowering plasma glucose levels to <9 mmol/L in 60\% of fatty animals as compared with 30\% for BEOV and 10\% for ROS alone. The age-dependent decrease in plasma insulin levels associated with \&beta;-cell failure in the ZDF rats did not occur in the BEOV-treated fatty groups. There was no effect of any treatment on body weight; however, there was a significant reduction in both food and fluid intake in fatty groups treated with BEOV. There were no overt signs of toxicity and no mortality in this study. Both BEOV and ROS were effective in lowering plasma glucose levels, as stated above, and there was at least an additive effect when BEOV and ROS were used in combination.},
	keywords = {ACTIVATED-RECEPTOR-GAMMA, bis(ethylmaltolato)oxovanadium(IV), diabetes, GLUT4, IN-VIVO, INSULIN SENSITIVITY, ORAL VANADYL, PHOSPHOENOLPYRUVATE-CARBOXYKINASE, RATS, rosigitazone, SKELETAL-MUSCLE, STREPTOZOTOCIN-DIABETIC RATS, TRANSLOCATION, VANADYL SULFATE, ZDF rats, ZUCKER FATTY},
	isbn = {0008-4212},
	url = {<Go to ISI>://000186896100007},
	author = {Yuen, V. G. and Bhanot, S. and Battell, M. L. and Orvig, Chris and McNeill, J. H.}
}
@article {4694,
	title = {An iron-based molecular redox switch as a model for iron release from enterobactin via the salicylate binding mode},
	journal = {Inorganic Chemistry},
	volume = {38},
	number = {22},
	year = {1999},
	note = {ISI Document Delivery No.: 255LLTimes Cited: 18Cited Reference Count: 51},
	month = {Nov},
	pages = {5007-5017},
	type = {Article},
	abstract = {The iron release mechanism from protonated ferric enterobactin [Fe-III(enterobactinH(3))] via the salicylate binding mode was probed. For this purpose, a tripodal dodecadentate Ligand incorporating three salicylamide (OO) and three bipyridine (NN) binding sites was synthesized as well as iron complexes thereof. It was shown that a ferric ion coordinates selectively to the hard salicylamides and a ferrous ion binds to the softer bipyridines. Upon reduction or oxidation, the iron translocates reversibly and intramolecularly from one site to the other, thus displaying switchlike properties. Both states were characterized by cyclic voltammetry and visible and Mossbauer spectroscopy. The Mossbauer spectrum for the ferric complex is fully consistent with that obtained by Pecoraro et al. upon lowering the pH of [Fe-III(enterobactin)](3-) solutions (Pecoraro, V. L., et al. J. Am. Chern. Sec. 1983, 105, 4617), thus supporting the alternative iron release mechanism from enterobactin via the salicylate binding mode.},
	keywords = {COORDINATION CHEMISTRY, ESCHERICHIA-COLI, FERRIC ENTEROBACTIN, IRON(III) COORDINATION, LIGAND, METAL-COMPLEXES, SEQUESTERING AGENTS, SYNTHETIC ANALOGS, TRANSLOCATION, TRANSPORT COMPOUNDS},
	isbn = {0020-1669},
	url = {<Go to ISI>://000083670200015},
	author = {Ward, T. R. and Lutz, A. and Parel, S. P. and Ensling, J. and Gutlich, P. and Buglyo, P. and Orvig, Chris}
}
@article {4405,
	title = {Structure of the Ets-1 pointed domain and mitogen-activated protein kinase phosphorylation site},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {95},
	number = {21},
	year = {1998},
	note = {ISI Document Delivery No.: 129DLTimes Cited: 84Cited Reference Count: 37},
	month = {Oct},
	pages = {12129-12134},
	type = {Article},
	abstract = {The Pointed (PNT) domain and an adjacent mitogen-activated protein (MAP) kinase phosphorylation site are defined by sequence conservation among a subset of ets transcription factors and are implicated in two regulatory strategies, protein interactions and posttranslational modifications, respectively. By using NMR, we have determined the structure of a 110-residue fragment of murine Ets-1 that includes the PNT domain and MAP kinase site. The Ets-1 PNT domain forms a monomeric five-helix bundle. The architecture is distinct from that of any known DNA- or protein-binding module, including the helix-loop-helix fold proposed for the PNT domain of the ets protein TEL. The MAP kinase site is in a highly flexible region of both the unphosphorylated and phosphorylated forms of the Ets-1 fragment. Phosphorylation alters neither the structure nor monomeric state of the PNT domain. These results suggest that the Ets-1 PNT domain functions in heterotypic protein interactions and support the possibility that target recognition is coupled to structuring of the MAP kinase site.},
	keywords = {beta, CHRONIC MYELOMONOCYTIC LEUKEMIA, FUSION, GENE, NMR, OLIGOMERIZATION, TEL, TRANSCRIPTION FACTORS, TRANSLOCATION, TROPONIN-C},
	isbn = {0027-8424},
	url = {<Go to ISI>://000076447900013},
	author = {Slupsky, C. M. and Gentile, L. N. and Donaldson, L. W. and Mackereth, C. D. and Seidel, J. J. and Graves, B. J. and McIntosh, L. P.}
}
