@article {2630,
	title = {A new [4]carceplex, and a crystal structure and dynamic combinatorial chemistry of a [5]carceplex},
	journal = {Tetrahedron},
	volume = {65},
	number = {35},
	year = {2009},
	note = {ISI Document Delivery No.: 485CQTimes Cited: 1Cited Reference Count: 16Sun, Jianyu Patrick, Brian O. Sherman, John C.},
	month = {Aug},
	pages = {7296-7302},
	type = {Article},
	abstract = {A new [4]carceplex (2-guest) is reported. It is composed of two cavitands linked by four disulfide bonds. It forms twistomers, which interconvert on a millisecond timescale. The energy barrier for interconversion of twistomers is guest-dependent. Formation of [4]carceplex 2-guest is template dependent. The selectivity in templates is flat relative to most previous related template work. Larger kin [5]carceplex 1.guests were reinvestigated. A crystal structure confirms the twist between the hemispherical cavitands. Use of a redox buffer allowed dynamic combinatorial chemistry to be performed between pairs of templates. (C) 2009 Elsevier Ltd. All rights reserved.},
	keywords = {carceplex, Disulfide, Dynamic combinatorial chemistry, Guest release, HEMICARCEPLEXES, MOLECULES, supramolecular, TEMPLATION},
	isbn = {0040-4020},
	url = {<Go to ISI>://000269098700012},
	author = {Sun, J. Y. and Patrick, B. O. and Sherman, J. C.}
}
@article {4236,
	title = {Stability and oligosaccharide binding of the N1 cellulose-binding domain of Cellulomonas fimi endoglucanase CenC},
	journal = {Biochemistry},
	volume = {37},
	number = {10},
	year = {1998},
	note = {ISI Document Delivery No.: ZC900Times Cited: 16Cited Reference Count: 75},
	month = {Mar},
	pages = {3529-3537},
	type = {Article},
	abstract = {Differential scanning calorimetry has been used to study the thermal stability and oligosaccharide-binding thermodynamics of the N-terminal cellulose-binding domain of Cellulomonas fimi beta-1,4-glucanase CenC (CBDN1) CBDN1 has a relatively low maximum stability (Delta G(max) = 33 kJ/mol = 216 J/residue at 1 degrees C and pH 6.1) compared to other small single-domain globular proteins. The unfolding is fully reversible between pH 5.5 and 9 and in accordance with the two-state equilibrium model between pH 5.5 and 11. When the single disulfide bond in CBDN1 is reduced, the protein remains unfolded at all conditions, as judged by NMR spectroscopy. This indicates that the intramolecular cross-link makes a major contribution to the stability of CBDN1. The measured heat capacity change of unfolding (Delta C-p = 7.5 kJ mol(-1) K-1) agrees well with that calculated from the predicted changes in the solvent accessible nonpolar and polar surface areas upon unfolding. Extrapolation of the specific enthalpy and entropy of unfolding to their respective convergence temperature indicates that per residue unfolding energies for CBDN1, an isolated domain, are in accordance with those found by Privalov (1) for many single-domain globular proteins. DSC thermograms of the unfolding of CBDN1 in the presence of various concentrations of cellopentaose were fit to a thermodynamic model describing the linkage between protein-ligand binding and protein unfolding. A global two-dimensional minimization routine is used to regress the binding enthalpy, binding constant, and unfolding thermodynamics for the CBDN1-cellopentaose system. Extrapolated binding constants are in quantitative agreement with those determined by isothermal titration calorimetry at 35 degrees C.},
	keywords = {ASPERGILLUS-NIGER, BRIDGES, differential scanning calorimetry, Disulfide, ESCHERICHIA-COLI, GLOBULAR-PROTEINS, INHIBITOR BINDING, LIGAND-BINDING, PROTEIN-FOLDING THERMODYNAMICS, THERMAL-DENATURATION, TITRATION CALORIMETRY},
	isbn = {0006-2960},
	url = {<Go to ISI>://000072630300034},
	author = {Creagh, A. L. and Koska, J. and Johnson, P. E. and Tomme, P. and Joshi, M. D. and McIntosh, L. P. and Kilburn, D. G. and Haynes, C. A.}
}
@article {4139,
	title = {Comparative inhibition of yeast glutathione reductase by arsenicals and arsenothiols},
	journal = {Chemical Research in Toxicology},
	volume = {10},
	number = {1},
	year = {1997},
	note = {ISI Document Delivery No.: WD805Times Cited: 165Cited Reference Count: 30},
	month = {Jan},
	pages = {27-33},
	type = {Article},
	abstract = {Tri(gamma-glutamylcysteinylglycinyl)trithioarsenite (As-III(GS)(3)) is formed in cells and is a more potent mixed-type inhibitor of the reduction of glutathione disulfide (GSSG) by yeast glutathione (GSH) reductase than either arsenite (As-III) or GSH. The present work examines the effects of valence and complexation of arsenicals with GSH or L-cysteine (Cys) upon potency as competitive inhibitors of the reduction of GSH disulfide (GSSG) by yeast GSH reductase. Trivalent arsenicals were more potent inhibitors than their pentavalent analogs, and methylated trivalent arsenicals were more potent inhibitors than was inorganic trivalent As. Complexation of either inorganic trivalent As or methylarsonous diiodide ((CH3AsI2)-I-III) with Cys or GSH produced inhibitors of GSH reductase that were severalfold more potent than the parent arsenicals. In contrast, dimethylarsinous iodide ((CH3)(2)(AsI)-I-III) was a more potent inhibitor than its complexes with either GSH or Cys. Complexes of CH3AsIII with GSH (CH3AsIII(GS)(2)) or with Cys (CH3AsIII(Cys)(2)) were the most potent inhibitors, with K-i{\textquoteright}s of 0.009 and 0.018 mM, respectively. Inhibition of GSH reductase by arsenicals or arsenothiols was prevented by addition of meso-2,3-dimercaptosuccinic acid (DMSA) to a mixture of enzyme, GSSG, and inhibitor before addition of NADPH. DMSA added to the reaction mixture after NADPH reversed inhibition by (CH3)(2)(AsI)-I-III but had little effect on inhibition by (CH3AsI2)-I-III, CH3AsIII(GS)(2), CH3AsIII(Cys)(2), Or AS(III)(GS)(3). Partial redox inactivation of the enzyme with NADPH increased the inhibitory potency of (CH3AsI2)-I-III and (CH3)(2)(AsI)-I-III and changed the mode of inhibition for (CH3AsI2)-I-III from competitive to noncompetitive. The greater potency of methylated trivalent arsenicals and arsenothiols than of inorganic trivalent As suggests that biomethylation of As could yield species that inhibit reduction of GSSG and alter the redox status of cells.},
	keywords = {BINDING, DIMERCAPTOSUCCINIC ACID, Disulfide, MAGNETIC-RESONANCE, MICE, PHENYLDICHLOROARSINE, RABBIT ERYTHROCYTES},
	isbn = {0893-228X},
	url = {<Go to ISI>://A1997WD80500004},
	author = {Styblo, M. and Serves, S. V. and Cullen, W. R. and Thomas, D. J.}
}
