@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 {2636,
	title = {Investigation of the Catalytic Mechanism of a Synthetic DNAzyme with Protein-like Functionality: An RNaseA Mimic?},
	journal = {Journal of the American Chemical Society},
	volume = {131},
	number = {15},
	year = {2009},
	note = {ISI Document Delivery No.: 434IJTimes Cited: 3Cited Reference Count: 108Thomas, Jason M. Yoon, Jung-Ki Perrin, David M.},
	month = {Apr},
	pages = {5648-5658},
	type = {Article},
	abstract = {The protein enzyme ribonuclease A (RNaseA) cleaves RNA with catalytic perfection, although with little sequence specificity, by a divalent metal ion (M2+)-independent mechanism in which a pair of imidazoles provides general acid and base catalysis, while a cationic amine provides electrostatic stabilization of the transition state. Synthetic imitation of this remarkable organo-catalyst ("RNaseA mimicry") has been a longstanding goal in biomimetic chemistry. The 9(25)-11 DNAzyme contains synthetically modified nucleotides presenting both imidazole and cationic amine side chains, and catalyzes RNA cleavage with turnover in the absence of M2+ similarly to RNaseA. Nevertheless, the catalytic roles, if any, of the "proteinlike" functional groups have not been defined, and hence the question remains whether 925-11 engages any of these functionalities to mimic aspects of the mechanism of RNaseA. To address this question, we report a mechanistic investigation Of 925-11 Catalysis wherein we have employed a variety of experiments, such as DNAzyme functional group deletion, mechanism-based affinity labeling, and bridging and nonbridging phosphorothioate substitution of the scissile phosphate. Several striking parallels exist between the results presented here for 925-11 and the results of analogous experiments applied previously to RNaseA. Specifically, our results implicate two particular imidazoles in general acid and base catalysis and suggest that a specific cationic amine stabilizes the transition state via diastereoselective interaction with the scissile phosphate. Overall, 925-11 appears to meet the minimal criteria of an RNaseA mimic; this demonstrates how added synthetic functionality can expand the mechanistic repertoire available to a synthetic DNA-based catalyst.},
	keywords = {ACID-BASE CATALYSIS, CLEAVING DNA ENZYME, COMPLEX, CYTOSOLIC FREE MAGNESIUM, DELTA VIRUS RIBOZYME, DINUCLEAR ZN(II), DIVALENT METAL-IONS, HAIRPIN RIBOZYME CATALYSIS, HDV GENOMIC, IN-VITRO SELECTION, RIBONUCLEASE-A, RIBOZYME},
	isbn = {0002-7863},
	url = {<Go to ISI>://000265268100049},
	author = {Thomas, J. M. and Yoon, J. K. and Perrin,David M.}
}
@article {1368,
	title = {Calcium ion exchange in crystalline gelsolin},
	journal = {Journal of Molecular Biology},
	volume = {357},
	number = {3},
	year = {2006},
	note = {ISI Document Delivery No.: 030IYTimes Cited: 6Cited Reference Count: 24},
	month = {Mar},
	pages = {773-782},
	type = {Article},
	abstract = {Gelsolin is a calcium and pH-sensitive modulator of actin filament length. Here, we use X-ray crystallography to examine the extraction and exchange of calcium ions from their binding sites in different crystalline forms of the activated N and C-terminal halves of gelsolin, G1-G3 and G4-G6, respectively. We demonstrate that the combination of calcium and low pH activating conditions do not induce conformational changes in G4-G6 beyond those elicited by calcium alone. EGTA is able to remove calcium ions bound to the type I and type II metal ion-binding sites in G4-G6. Constrained by crystal contacts and stabilized by interdomain interaction surfaces, the gross structure of calcium-depleted G4-G6 remains that of the activated form. However, high-resolution details of changes in the ion-binding sites may represent the initial steps toward restoration of the arrangement of domains found in the calcium-free inactive form of gelsolin in solution. Furthermore, bathing crystals with the trivalent calcium ion mimic, Tb3+, results in anomalous scattering data that permit unequivocal localization of terbium ions in each of the proposed type I and type II ion-binding sites of both halves of gelsolin. In contrast to predictions based on solution studies, we find that no calcium ion is immune to exchange. (c) 2006 Elsevier Ltd. All rights reserved.},
	keywords = {actin, ACTIN MONOMER, ACTIVATION, apoptosis, BINDING-SITE, C-TERMINAL HALF, calcium activation, COMPLEX, CONFORMATIONAL CHANGE, DOMAINS, ELECTRON-DENSITY MAPS, gelsolin, IDENTIFICATION, MECHANISMS, protein crystallography},
	isbn = {0022-2836},
	url = {<Go to ISI>://000236629300008},
	author = {Chumnarnsilpa, S. and Loonchanta, A. and Xue, B. and Choe, H. and Urosev, D. and Wang, H. and Lindberg, U. and Burtnick, L. D. and Robinson, R. C.}
}
@article {1489,
	title = {Crystal structures of protein phosphatase-1 bound to motuporin and dihydromicrocystin-LA: Elucidation of the mechanism of enzyme inhibition by cyanobacterial toxins},
	journal = {Journal of Molecular Biology},
	volume = {356},
	number = {1},
	year = {2006},
	note = {ISI Document Delivery No.: 007AFTimes Cited: 17Cited Reference Count: 42},
	month = {Feb},
	pages = {111-120},
	type = {Article},
	abstract = {The microcystins and nodularins are tumour promoting hepatotoxins that are responsible for global adverse human health effects and wildlife fatalities in countries where drinking water supplies contain cyanobacteria. The toxins function by inhibiting broad specificity Ser/Thr protein phosphatases in the host cells, thereby disrupting signal transduction pathways. A previous crystal structure of a microcystin bound to the catalytic subunit of protein phosphatase-1 (PP-1c) showed distinct changes in the active site region when compared with protein phosphatase-1 structures bound to other toxins. We have elucidated the crystal structures of the cyanotoxins, motuporin (nodularin-V) and dihydromicrocystin-LA bound to human protein phosphatase-1c (gamma isoform). The atomic structures of these complexes reveal the structural basis for inhibition of protein phosphatases by these toxins. Comparisons of the structures of the cyanobacterial toxin:phosphatase complexes explain the biochemical mechanism by which microcystins but not nodularins permanently modify their protein phosphatase targets by covalent addition to an active site cysteine residue. (c) 2005 Elsevier Ltd. All rights reserved.},
	keywords = {CATALYTIC SUBUNIT, COMPLEX, crystal structure, cyanobacteria, IN-VIVO, microcystin, MICROCYSTIN-LR, MOLECULAR-MECHANISMS, nodularin, POTENT, PROGRAM, TUMOR-PROMOTER, TYPE-1},
	isbn = {0022-2836},
	url = {<Go to ISI>://000234938600010},
	author = {Maynes, J. T. and Luu, H. A. and Cherney, M. M. and Andersen, R. J. and Williams, D. and Holmes, C. F. B. and James, M. N. G.}
}
@article {1187,
	title = {A new arene-bridged diamidophosphine ligand and its coordination chemistry with zirconium(IV)},
	journal = {Organometallics},
	volume = {24},
	number = {6},
	year = {2005},
	note = {ISI Document Delivery No.: 904YFTimes Cited: 15Cited Reference Count: 48},
	month = {Mar},
	pages = {1112-1118},
	type = {Article},
	abstract = {The arene-bridged dilithium diamidophosphine ligand, [(2,4,6-Me3C6H2)NLi-2-(5-MeC6H3)](2)PPh, [NPN]*Li-2, was prepared from (2,4,6-Me3C6H2)(2-Br-4-MeC6H3)NH, (BuLi)-Bu-n, and PhPCl2 in Et2O and isolated as a dioxane adduct in similar to 85\% yield. The solid-state structure of [NPN]*Li-2(THF)2 as determined by X-ray diffraction shows both lithiums bridged by the amido nitrogens with one Li ion coordinated to the phosphine donor. The reaction of [NPN]*H-2 and Zr(NMe2)(4) in toluene produced [NPN]*Zr(NMe2)(2) in 90\% isolated yield. Addition of excess Me3SiCl to [NPN]*Zr(NMe2)(2) converts it to [NPN]*ZrCl2 in high yield. The solid-state structure of [NPN] *ZrCl2 as determined by X-ray diffraction shows the Zr center is a distorted trigonal bipyramid with the phosphine and the chloride apical. The ortho-Me{\textquoteright}s on the N-mesityl moiety are inequivalent in both the Li and Zr complexes of [NPN]* by NMR spectroscopy, while in [NPN]*H-2 MesN ortho-Me{\textquoteright}s appear as broad singlets. VT-NMR of [NPN]*H-2 indicated that Delta G(rot)(double dagger) of MesC(ipso)-N is approximately 15.5 +/- 0.3 kcal mol(-1). The thermally labile and light-sensitive zirconium dimethyl complex [NPN]*ZrMe2 was prepared from [NPN]*ZrCl2 and MeMgCl in Et2O in 80\% yield.},
	keywords = {CLEAVAGE, COMPLEX, COUPLING REACTIONS, DINITROGEN LIGAND, END-ON, METAL-COMPLEXES, MOLECULAR NITROGEN, N-2 UNIT, palladium, SIDE-ON, tantalum},
	isbn = {0276-7333},
	url = {<Go to ISI>://000227533800014},
	author = {MacLachlan, E. A. and Fryzuk,Michael D.}
}
@article {1010,
	title = {Complementary inhibition of synoviocyte, smooth muscle cell or mouse lymphoma cell proliferation by a vanadyl curcumin complex compared to curcumin alone},
	journal = {Journal of Inorganic Biochemistry},
	volume = {98},
	number = {12},
	year = {2004},
	note = {ISI Document Delivery No.: 876VBTimes Cited: 20Cited Reference Count: 62},
	month = {Dec},
	pages = {2063-2070},
	type = {Article},
	abstract = {A novel vanadyl curcumin complex (VO(cur)2) has been synthesized and and its physicochemical properties characterized. Biological characterization included in vitro testing for anti-rheumatic activity in synoviocytes, angiogenesis inhibition in smooth muscle cells and anti-cancer potential in mouse lymphoma cells; as well as in vivo testing for hypoglycemic activity by oral gavage in streptozotocin (STZ)-diabetic rats. VO(cur)2 was more effective as an anti-cancer agent, compared to uncomplexed curcumin or vanadyl ion alone, was more than twice as effective as curcumin alone as an anti-arthritic agent, and was more than four times as effective as curcumin alone in inhibiting smooth muscle cell proliferation. In both acute and chronic screening tests, VO(cur)2 was ineffective as an insulin mimetic agent; however, it also proved to be exceptionally non-toxic, with no evidence of negative symptornatology during a month-long treatment period, at doses up to and including 2.0 mmol kg(-1) day(-1). (C) 2004 Elsevier Inc. All rights reserved.},
	keywords = {antioxidant, apoptosis, arthritis lymphoma, BIS(MALTOLATO)OXOVANADIUM(IV), CELLS, COMPLEX, COORDINATION, curcurnin, DIABETIC-RATS, DIFERULOYL METHANE CURCUMIN, FREE-RADICALS, INDUCED LIPID-PEROXIDATION, INSULIN MIMICS, LEUKEMIA HL-60, METAL-IONS, OXIDATIVE STRESS, vanadyl ion},
	isbn = {0162-0134},
	url = {<Go to ISI>://000225525200010},
	author = {Thompson, K. H. and Bohmerle, K. and Polishchuk, E. and Martins, C. and Toleikis, P. and Tse, J. and Yuen, V. and McNeill, J. H. and Orvig, Chris}
}
@inbook {833,
	title = {Measuring the silion fluoride bond distance in zeolites},
	booktitle = {Recent Advances in the Science and Technology of Zeolites and Related Materials, Pts a - C},
	series = {Studies in Surface Science and Catalysis},
	volume = {154},
	year = {2004},
	note = {ISI Document Delivery No.: BBR47Times Cited: 0Cited Reference Count: 19Proceedings Paper14th International Zeolite Conference on Recent Advances in the Science and Technology of Zeolites and Related MaterialsAPR 25-30, 2004Cape Town, SOUTH AFRICASARA BURGERHARTSTRAAT 25, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	pages = {1319-1323},
	publisher = {Elsevier Science Bv},
	organization = {Elsevier Science Bv},
	address = {Amsterdam},
	abstract = {A common misconception is that X-ray diffraction is the best way to measure bond distances. However, in some cases where disorder is present it can yield incorrect answers. The silicon-fluoride bond distance in fluoride-containing zeolite SFF has been measured using two magic angle spinning NMR techniques. Both techniques, variable contact time cross polarization and spinning side hand intensity fitting give shorter Si-F bond distances than X-ray diffraction.},
	keywords = {5-COORDINATE SILICON, COMPLEX, IFR, IONS, LOCATION, MEDIA, MOLECULAR-SIEVES, SOLID-STATE NMR, STF, TEMPLATE},
	isbn = {0167-29910-444-51805-3},
	url = {<Go to ISI>://000227357201022},
	author = {Darton, R. J. and Brouwer, D. H. and Fyfe, C. A. and Villaescusa, L. A. and Morris, R. E.},
	editor = {VanSteen, E. and Claeys, M. and Callanan, L. H.}
}
@article {834,
	title = {Solid-state NMR studies of the fluoride-containing zeolite SSZ-44},
	journal = {Chemistry of Materials},
	volume = {16},
	number = {4},
	year = {2004},
	note = {ISI Document Delivery No.: 774YATimes Cited: 12Cited Reference Count: 21},
	month = {Feb},
	pages = {600-603},
	type = {Article},
	abstract = {Magic-angle spinning NMR has been used to probe the local structure of as-made zeolite SFF containing occluded fluoride and NN-diethyl-2,6-dimethylpiperidinium. The Si-F bond distance has been measured using two methods: variable contact time cross polarization studies (1.74 Angstrom) and spinning sideband intensity fitting at relatively slow spinning speeds (1.79 Angstrom). Both measurements yield results that are significantly shorter than the internuclear Si-F distance as measured by single-crystal X-ray diffraction (similar to1.9 Angstrom), which is based on the average positions of the atoms due to disorder and hence does not reflect the true bond distance.},
	keywords = {5-COORDINATE SILICON, COMPLEX, IFR, IONS, LOCATION, MEDIA, MOLECULAR-SIEVES, SPECTROSCOPY, STF, TEMPLATE},
	isbn = {0897-4756},
	url = {<Go to ISI>://000189012900008},
	author = {Darton, R. J. and Brouwer, D. H. and Fyfe, C. A. and Villaescusa, L. A. and Morris, R. E.}
}
@article {697,
	title = {Activation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin},
	journal = {Febs Letters},
	volume = {552},
	number = {2-3},
	year = {2003},
	note = {ISI Document Delivery No.: 726DKTimes Cited: 15Cited Reference Count: 23},
	month = {Sep},
	pages = {82-85},
	type = {Article},
	abstract = {Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 resolution in the presence of Ca2+ ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca2+ sites occupied. Neither actin nor the type-1 Ca2+, which normally is sandwiched between actin and G4, is required to achieve this conformation. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.},
	keywords = {actin, calcium-activation, COMPLEX, DOMAINS, F-ACTIN, gelsolin, PLASMA GELSOLIN, REGULATORY PROTEIN, TRANSFORMATION},
	isbn = {0014-5793},
	url = {<Go to ISI>://000185583000002},
	author = {Narayan, K. and Chumnarnsilpa, S. and Choe, H. and Irobi, E. and Urosev, D. and Lindberg, U. and Schutt, C. E. and Burtnick, L. D. and Robinson, R. C.}
}
@article {643,
	title = {From the first to the second domain of gelsolin: a common path on the surface of actin?},
	journal = {Febs Letters},
	volume = {552},
	number = {2-3},
	year = {2003},
	note = {ISI Document Delivery No.: 726DKTimes Cited: 22Cited Reference Count: 29},
	month = {Sep},
	pages = {86-90},
	type = {Article},
	abstract = {We present the 2.6. resolution crystal structure of a complex formed between G-actin and gelsolin fragment Met25-GIn160 (G1+). The structure differs from those of other gelsolin domain 1 (G1) complexes in that an additional six amino acid residues from the crucial linker region into gelsolin domain 2 (G2) are visible and are attached securely to the surface of actin. The linker segment extends away from G1 up the face of actin in a direction that infers G2 will bind along the same long-pitch helical strand as the actin bound to G1. This is consistent with a mechanism whereby G2 attaches gelsolin to the side of a filament and then directs G1 toward a position where it would disrupt actin-actin contacts. Alignment of the sequence of the structurally important residues within the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin beta4) suggests that the opposing activities of filament assembly and disassembly may exploit a common patch on the surface of actin. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.},
	keywords = {actin, BINDING, calcium, COMPLEX, crystal structure, DIFFRACTION DATA, F-ACTIN, FILAMENT, gelsolin, IDENTIFICATION, MODEL, MOTILITY, NUCLEATION, WH2 domain},
	isbn = {0014-5793},
	url = {<Go to ISI>://000185583000003},
	author = {Irobi, E. and Burtnick, L. D. and Urosev, D. and Narayan, K. and Robinson, R. C.}
}
@article {777,
	title = {Inner C-cyanide addition and nucleophilic addition to Ni(II) N-confused porphyrins},
	journal = {Chemical Communications},
	number = {9},
	year = {2003},
	note = {ISI Document Delivery No.: 668WMTimes Cited: 19Cited Reference Count: 9},
	pages = {1062-1063},
	type = {Article},
	abstract = {Inner C-cyanide addition and subsequent addition of a methoxy group were observed in the reactions of Ni(II) N-confused tetra(p-tolyl)porphyrin with sodium methoxide and DDQ.},
	keywords = {COMPLEX, ISOMER, RING},
	isbn = {1359-7345},
	url = {<Go to ISI>://000182316200017},
	author = {Xiao, Z. W. and Patrick, B. O. and Dolphin, D.}
}
@article {641,
	title = {The synthesis, structural characterization, and in vitro anti-cancer activity of chloro(p-cymene) complexes of ruthenium(II) containing a disulfoxide ligand},
	journal = {Inorganica Chimica Acta},
	volume = {352},
	year = {2003},
	note = {ISI Document Delivery No.: 711FATimes Cited: 39Cited Reference Count: 47},
	month = {Aug},
	pages = {238-246},
	type = {Article},
	abstract = {Two diruthenium(II) complexes [RuCl2(p-cymene)](2)(mu-BESE) (1), [RuCl2(p-cymene)](2)(mu-BESP) (2), and the mononuclear salt [RuCl(p-cymene)(BESE)]PF6 (3), containing the disulfoxides BESE and BESP, were synthesized and characterized by elemental analysis, and NMR and IR spectroscopies, and were shown to contain S-bound sulfoxide groups; the disulfoxides are EtS(O)(CH2)(n) S(O)Et, where n = 2 (BESE) or 3 (BESP). Complexes 1 and 3 were also characterized by X-ray crystallography. Preliminary in vitro tests of I and 3 were conducted using the MTT assay, which measures mitochondrial dehydrogenase activity as an indication of cell viability; these complexes showed in vitro anti-cancer activity against a human mammary cancer cell line (MDA-MB-435s) with IC50 values of 360 and 55 muM, respectively. (C) 2003 Elsevier B.V. All rights reserved.},
	keywords = {anti-cancer activity, arene complexes, CANCER, cell, COMPLEX, COORDINATION, crystal structures, CRYSTAL-STRUCTURE, DIMETHYL-SULFOXIDE LIGAND, DIRUTHENIUM(II), disulfoxide ligands, INHIBITION, p-Cymene complexes, RADIOSENSITIZING ACTIVITY, ruthenium complexes, SOLUTION CHEMISTRY},
	isbn = {0020-1693},
	url = {<Go to ISI>://000184727900029},
	author = {Huxham, L. A. and Cheu, E. L. S. and Patrick, B. O. and James, Brian R.}
}
@article {380,
	title = {Hydroboration of coordinated dinitrogen: A new reaction for the N-2 ligand that results in its functionalization and cleavage},
	journal = {Angewandte Chemie-International Edition},
	volume = {41},
	number = {19},
	year = {2002},
	note = {ISI Document Delivery No.: 604GZTimes Cited: 48Cited Reference Count: 30},
	pages = {3709-3712},
	type = {Article},
	keywords = {ACTIVATION, COMPLEX, DINITROGEN, END-ON, EXCHANGE, hydroboration, iron, MILD CONDITIONS, nitrides, NITROGEN, nitrogen fixation, REDUCTION, SIDE-ON, tantalum, TUNGSTEN},
	isbn = {1433-7851},
	url = {<Go to ISI>://000178609900046},
	author = {Fryzuk,Michael D. and MacKay, B. A. and Johnson, S. A. and Patrick, B. O.}
}
@article {541,
	title = {Inhibitory module of Ets-1 allosterically regulates DNA binding through a dipole-facilitated phosphate contact},
	journal = {Journal of Biological Chemistry},
	volume = {277},
	number = {3},
	year = {2002},
	note = {ISI Document Delivery No.: 514CWTimes Cited: 21Cited Reference Count: 50},
	month = {Jan},
	pages = {2225-2233},
	type = {Article},
	abstract = {DNA binding of the transcription factor Ets-1 is negatively regulated by three inhibitory helices that lie near the ETS domain. The current model suggests that this negative regulation, termed autoinhibition, is caused by the energetic expense of a DNA-induced structural transition that includes the unfolding of one inhibitory helix. This report investigates the role of helix H1 of the ETS domain in the autoinhibition mechanism. Previous structural studies modeled the inhibitory helices packing together and connecting with helix H1, suggesting a role of this helix in the configuration of an inhibitory module. Recently, high-resolution structures of the ETS domain-DNA interface indicate that the N terminus of helix H1 directly contacts DNA. The contact, which is augmented by the macrodipole of helix H1, consists of a hydrogen bond between the amide NH of leucine 337 in helix HI and the oxygen of a corresponding phosphate. We propose that this hydrogen bond positions helix H1 to be a link between autoinhibition and DNA binding. Four independent approaches tested this hypothesis. First, the hydrogen bond was disrupted by removal of the phosphate in a missing phosphate analysis. Second, base pairs that surround the helix HI-contacting phosphate and appear to dictate DNA backbone conformation were mutated. Next, a hydrophobic residue in helix H1 that is expected to position the N terminus of the helix was altered. Finally, a residue on the surface of helix 111 that may contact the inhibitory elements was changed. In each case DNA binding and autoinhibition was affected. Taken together, the results demonstrate the role of the dipole-facilitated phosphate contact in DNA binding. Furthermore, the findings support a model in which helix H1 links the inhibitory elements to the ETS domain. We speculate that this helix, which is conserved in all Ets proteins, provides a common route to regulation.},
	keywords = {ALPHA-HELIX, AUTO-INHIBITION, COMPLEX, DOMAIN, FACTORS ELK-1, INDIRECT READOUT, MURINE ETS-1, PROTEINS, RECOGNITION, TRANSCRIPTION FACTOR},
	isbn = {0021-9258},
	url = {<Go to ISI>://000173421300083},
	author = {Wang, H. and McIntosh, L. P. and Graves, B. J.}
}
@article {5031,
	title = {Artificial nucleases},
	journal = {Chembiochem},
	volume = {2},
	number = {10},
	year = {2001},
	note = {ISI Document Delivery No.: 479NGTimes Cited: 54Cited Reference Count: 25},
	month = {Oct},
	pages = {735-740},
	type = {Article},
	abstract = {The oxidation of DNA and RNA provides a facile approach for investigating the interaction of nucleic acids wit proteins and oligonucleotides In this article, we have outlined our understanding of the mechanism of DNA scission by 1,10-phenanthroline-copper(I) in the presence of hydrogen peroxide. We also discuss results obtained by using 1,10-phenanthroline - oligonucleotide conjugates in probing the size of the transcriptionally active open complex. Finally, we outline an effective method for converting DNA-binding proteins into site-specific modification agents by using 1,10-phenanthroline-copper(I).},
	keywords = {1, 10-PHENANTHROLINE-COPPER ION, chemical, COLI RNA-POLYMERASE, COMPLEX, copper, DNA, DNA cleavage, DNA recognition, ESCHERICHIA-COLI, NUCLEASE, nucleic acids, OLIGONUCLEOTIDES, PROTEIN, SITE-SPECIFIC NUCLEASE, TRANSCRIPTION INITIATION},
	isbn = {1439-4227},
	url = {<Go to ISI>://000171410000003},
	author = {Chen, C. H. B. and Milne, L. and Landgraf, R. and Perrin,David M. and Sigman, D. S.}
}
@article {4815,
	title = {Investigation of the viability of solid-state NMR distance determinations in multiple spin systems of unknown structure},
	journal = {Journal of Physical Chemistry B},
	volume = {104},
	number = {1},
	year = {2000},
	note = {ISI Document Delivery No.: 283BJTimes Cited: 26Cited Reference Count: 37},
	month = {Jan},
	pages = {48-55},
	type = {Article},
	abstract = {This paper presents theoretical rotational-echo double-resonance (REDOR) and transferred-echo double-resonance (TEDOR) curves calculated for several three-spin systems and explores the potential for determining reliable distances in multiple-spin systems of unknown geometry. These NMR techniques can provide distances which compare very well with those obtained by X-ray diffraction if the samples contain isolated heteronuclear (IS) spin pairs and are currently being used in structural investigations of solids including peptides, polymers, and inorganic materials. The situation is less clear when small clusters of spins (e.g., INS systems) are present, and although the multispin dephasing can be calculated, very few examples have been reported in the literature. In most cases the spin system geometry was known before analysis of the NMR data, thus it is unclear whether reliable distances can be determined when the geometry of the spin system is completely unknown. To investigate the uniqueness of distance determinations from fitting of multispin REDOR and TEDOR data, the theoretical dephasing was calculated for a selection of I2S systems. The effects of varying the two I-S dipolar couplings and the I-A-S-I-B angle, zeta, were studied. The full range of zeta (0 degrees less than or equal to zeta less than or equal to 180 degrees) was considered, and the magnitudes of the dipolar couplings selected are typical of couplings expected for commonly studied nuclei. A variation of 10 degrees or more is required to effect a noticeable change and the dephasing is identical for zeta and 180 degrees - zeta. The most distinctive behavior is observed when zeta is small (or close to 180 degrees), otherwise there are quite minor differences. Spin systems with quite different geometries may exhibit very similar dephasing, and in some cases the curves are identical to those for an isolated IS spin pair. These calculations indicate that it is highly unlikely that reliable distances can be obtained directly from REDOR and TEDOR experiments on multiple spin systems when the number of spins and their geometrical arrangement is completely unknown. Furthermore, it is possible to obtain incorrect distances if isolated spin pairs are assumed and multiple spins are present.},
	keywords = {COMPLEX, DOUBLE-RESONANCE NMR, ECHO DOUBLE-RESONANCE, NMR, NUCLEI, QUADRUPOLAR, REDOR, ROTATIONAL-ECHO, zeolites},
	isbn = {1089-5647},
	url = {<Go to ISI>://000085256000007},
	author = {Fyfe, C. A. and Lewis, A. R.}
}
@article {4646,
	title = {Domain movement in gelsolin: A calcium-activated switch},
	journal = {Science},
	volume = {286},
	number = {5446},
	year = {1999},
	note = {ISI Document Delivery No.: 261HHTimes Cited: 94Cited Reference Count: 18},
	month = {Dec},
	pages = {1939-1942},
	type = {Article},
	abstract = {The actin-binding protein gelsolin is involved in remodeling the actin cytoskeleton during growth-factor signaling, apoptosis, cytokinesis, and cell movement. Calcium-activated gelsolin severs and caps actin filaments, The 3.4 angstrom x-ray structure of the carboxyl-terminal half of gelsolin (G4-G6) in complex with actin reveals the basis for gelsolin activation. Calcium binding induces a conformational rearrangement in which domain G6 is flipped over and translated by about 40 angstroms relative to G4 and G5. The structural reorganization tears apart the continuous beta sheet core of G4 and G6. This exposes the actin-binding site on G4, enabling severing and capping of actin filaments to proceed.},
	keywords = {actin, BINDING-SITE, COMPLEX, FILAMENT, IDENTIFICATION, PLASMA GELSOLIN},
	isbn = {0036-8075},
	url = {<Go to ISI>://000084003400047},
	author = {Robinson, R. C. and Mejillano, M. and Le, V. P. and Burtnick, L. D. and Yin, H. L. and Choe, S.}
}
@article {4216,
	title = {The reductive coupling of 2-cyanopyrroles: A study pertaining to the mechanism of formation of porphocyanines},
	journal = {Tetrahedron},
	volume = {54},
	number = {10},
	year = {1998},
	note = {ISI Document Delivery No.: YW979Times Cited: 5Cited Reference Count: 45},
	month = {Mar},
	pages = {2021-2030},
	type = {Article},
	abstract = {2-Cyanopyrrole was found to form (2-pyrrolylmethene)-(2-pyrrolylmethyl)im when treated with lithium aluminum hydride (LAH), followed by a mild work-up. A plausible mechanism of this reductive coupling was inferred from a series of experiments, including Al-27-NMR deuteration experiments, and the reduction of variously substituted cyanopyrroles. The mechanism, a metal chelate mediated dimerization, may be the key to understanding porphocyanine synthesis via the LAH reduction of 1,9-dicyanodipyrromethanes. (C) 1998 Elsevier Science Ltd. All rights reserved.},
	keywords = {CENTERED TEMPLATE REACTIONS, COMPLEX, CONVENIENT, EXPANDED TETRAPYRROLIC MACROCYCLE},
	isbn = {0040-4020},
	url = {<Go to ISI>://000071994000004},
	author = {Bruckner, C. and Xie, L. Y. and Dolphin, D.}
}
@article {4028,
	title = {Cytochrome c folding kinetics studied by time-resolved electrospray ionization mass spectrometry},
	journal = {Biochemistry},
	volume = {36},
	number = {18},
	year = {1997},
	note = {ISI Document Delivery No.: WY063Times Cited: 82Cited Reference Count: 46},
	month = {May},
	pages = {5554-5559},
	type = {Article},
	abstract = {A new method for studying the folding kinetics of proteins is described. The method combines a continuous flow mixing technique with an electrospray mass spectrometer. Different protein conformations in solution are detected by the different charge states they produce during electrospray ionization. Unfolded proteins generally have more accessible protonation sites and give higher charge states than native proteins. The method is applied to study the refolding of acid-denatured cytochrome c. Global data analysis is used to obtain the exponential lifetimes which are associated with the refolding process. The kinetics can be described by two lifetimes of 0.17 +/- 0.02 and 8.1 +/- 0.9 s which are in accordance with the results of stopped flow experiments previously described in the literature. These lifetimes are associated with roughly 90 and 10\% of the total intensity changes in the mass spectrum, respectively, and most likely reflect fast and slow refolding subpopulations of cytochrome c in solution.},
	keywords = {COMPLEX, denaturation, FERRICYTOCHROME-C, IRON BLEOMYCIN, LIGANDS, MECHANISM, PATHWAYS, PROBING CONFORMATIONAL-CHANGES, PROTEINS, SPECTRA},
	isbn = {0006-2960},
	url = {<Go to ISI>://A1997WY06300029},
	author = {Konermann, L. and Collings, B. A. and Douglas, D. J.}
}
@article {3858,
	title = {Porphocyanines: Expanded aromatic tetrapyrrolic macrocycles},
	journal = {Journal of the American Chemical Society},
	volume = {118},
	number = {20},
	year = {1996},
	note = {ISI Document Delivery No.: UM416Times Cited: 18Cited Reference Count: 34},
	month = {May},
	pages = {4853-4859},
	type = {Article},
	abstract = {Porphocyanines are tetrapyrrolic macrocycles containing two dipyrromethene units linked together by two C=N-C bridges. The syntheses of 2,3,7,8,14,15,19,20-octaethylporphocyanine 5,17-diphenylporphocyanine, 2,3,7,8-tetraethyl-17-phenylporphocyanine and other meso-aryl and beta-alkyl, including a tetra-beta-propionate, derivatives and metal complexes are described. The physical and chemical properties of porphocyanines show them to be aromatic. The aromaticity is reflected in the large deshielding of the outer beta-protons and shielding of the inner pyrrolic protons in their NMR spectra. The optical spectra of these compounds exhibit Soret and Q bands similar to porphyrins but all significantly bathochromically shifted. The ability of porphocyanines to act as catalysts for the generation of singlet molecular oxygen was investigated using a cholesterol oxidation assay.},
	keywords = {COMPLEX, porphyrins},
	isbn = {0002-7863},
	url = {<Go to ISI>://A1996UM41600015},
	author = {Xie, L. Y. and Boyle, R. W. and Dolphin, D.}
}
@article {3293,
	title = {CHARACTERIZATION OF DECAMETHYL AND ETHOXYCARBONYL PENTAPHYRINS},
	journal = {Heterocycles},
	volume = {41},
	number = {11},
	year = {1995},
	note = {ISI Document Delivery No.: TF562Times Cited: 5Cited Reference Count: 23},
	month = {Nov},
	pages = {2553-2564},
	type = {Article},
	abstract = {The syntheses of decamethyl- and ethoxycarbonyl-pentaphyrins are described. Their spectroscopic characterizations are presented in comparison with the permethyl derivatives of porphyrin, sapphyrin and hexaphyrin. The ethoxycarbonyl containing pentaphyrins are the only examples, amongst the expanded polypyrrolic macrocycles, that have an electron withdrawing group directly attached to the macrocyclic ring system. Elimination of a pyrrole and methine carbon unit in the mass spectrometer has been observed as a common feature for the pentaphyrin free bases as well as their metal derivatives.},
	keywords = {COMPLEX, EXPANDED PORPHYRIN, macrocycles, SAPPHYRINS},
	isbn = {0385-5414},
	url = {<Go to ISI>://A1995TF56200017},
	author = {Dansodanquah, R. E. and Xie, L. Y. and Dolphin, D.}
}
@article {7258,
	title = {GENERATION OF AU2+ IONS IN THE SOLID-STATE OR IN FLUOROSULFURIC ACID-SOLUTION AND THEIR IDENTIFICATION BY ESR},
	journal = {Journal of the American Chemical Society},
	volume = {114},
	number = {4},
	year = {1992},
	note = {ISI Document Delivery No.: HD978Times Cited: 25Cited Reference Count: 64},
	month = {Feb},
	pages = {1271-1277},
	type = {Article},
	abstract = {{The partial pyrolysis of gold(III) fluorosulfate, Au(SO3F)3, at temperatures below 145-degrees-C allows the generation of Au2+ defects in the solid residue by reductive elimination of SO3F. radicals. Solvated Au2+ is obtained by the reduction of Au(SO3F)3 in HSO3F solution by gold powder at 65-degrees-C. Both systems are studied by ESR and identical high g(iso) values of g = 2.360 are found. Hyperfine splitting due to Au-197},
	keywords = {BR2+, bromine, CATIONS, COMPLEX, GOLD(III) FLUOROSULFATE, HSO3F, I2+, palladium, SILVER(II)},
	isbn = {0002-7863},
	url = {<Go to ISI>://A1992HD97800024},
	author = {Herring, F. G. and Hwang, G. and Lee, K. C. and Mistry, F. and Phillips, P. S. and Willner, H. and Aubke, F.}
}
@article {7352,
	title = {STABILIZATION OF THE STRUCTURE OF HORSE PLASMA VITAMIN-D BINDING-PROTEIN BY DISULFIDE BONDS},
	journal = {Biochemistry and Cell Biology-Biochimie Et Biologie Cellulaire},
	volume = {70},
	number = {1},
	year = {1992},
	note = {ISI Document Delivery No.: HG742Times Cited: 1Cited Reference Count: 27},
	month = {Jan},
	pages = {10-15},
	type = {Article},
	abstract = {Vitamin D binding protein (DBP) was isolated from horse plasma in a four-step procedure that involved Affi-Gel Blue affinity chromatography, gel filtration, hydroxylapatite chromatography, and anion exchange high-pressure liquid chromatography. The yield of DBP from 80 mL of plasma was 6-7 mg. Horse plasma DBP closely resembles other plasma DBPs, being a tryptophan-free protein of M(r) 53 000. It is able to bind to and block the polymerization of monomeric actin. The secondary structure of DBP was calculated from circular dichroism measurements to be 39\% alpha-helix, 42\% beta-sheet, and 19\% random coil. Circular dichroism and fluorescence studies revealed that the disulfide bonds of DBP contribute substantial structural stabilization to the molecule with respect to thermal denaturation. The thermal stability of DBP can be used to advantage. Incorporation of a brief treatment at 70-degrees-C into the preparative scheme enables omission of one chromatographic step, without detectable alteration of the purified product.},
	keywords = {actin, circular dichroism, CIRCULAR-DICHROISM, COMPLEX, denaturation, DISULFIDE BONDS, FLUORESCENCE, GC-GLOBULIN, POLYMERIZATION, RAT, SERUM, thermal, TROPOMYOSIN, VITAMIN-D BINDING PROTEIN},
	isbn = {0829-8211},
	url = {<Go to ISI>://A1992HG74200002},
	author = {Robinson, R. C. and Burtnick, L. D.}
}
@article {7233,
	title = {SYNTHESIS AND REACTIVITY OF THE IRIDIUM VINYLIDENE IR=C=CH2[N(SIME2CH2PPH2)2] - FORMATION OF CARBON-CARBON BONDS VIA MIGRATORY INSERTION OF A VINYLIDENE UNIT},
	journal = {Organometallics},
	volume = {11},
	number = {9},
	year = {1992},
	note = {ISI Document Delivery No.: JN066Times Cited: 75Cited Reference Count: 42},
	month = {Sep},
	pages = {2979-2990},
	type = {Article},
	abstract = {{The synthesis of the 16-electron iridium vinylidene complex Ir=C=CH2[N(SiMe2CH2PPh2)2] is described by starting from the cyclooctene derivative Ir(eta-2-C8H14)[N(SiMe2CH2PPh2)2] with addition of acetylene. This vinylidene complex reacts with a variety of electrophiles; thus, reaction with AlR3 (R = Me, Et) or GaMe3 leads to the formation of the new derivatives Ir(ER2)CR=CH2[N(SiMe2CH2PPh2)2] (E = Al},
	keywords = {ACETYLIDE COMPLEXES, ALKYNE, CARBENE, COMPLEX, FISCHER-TROPSCH REACTION, LIGAND, MECHANISM, PHOTOINDUCED RING EXPANSION, REARRANGEMENT, SATURATED CARBON, TRANSITION-METAL},
	isbn = {0276-7333},
	url = {<Go to ISI>://A1992JN06600009},
	author = {Fryzuk,Michael D. and Huang, L. and McManus, N. T. and Paglia, P. and Rettig, S. J. and White, G. S.}
}
