@article {2401,
	title = {Arabidopsis LTPG Is a Glycosylphosphatidylinositol-Anchored Lipid Transfer Protein Required for Export of Lipids to the Plant Surface},
	journal = {Plant Cell},
	volume = {21},
	number = {4},
	year = {2009},
	note = {ISI Document Delivery No.: 448XRTimes Cited: 13Cited Reference Count: 42DeBono, Allan Yeats, Trevor H. Rose, Jocelyn K. C. Bird, David Jetter, Reinhard Kunst, Ljerka Samuelsa, Lacey},
	month = {Apr},
	pages = {1230-1238},
	type = {Article},
	abstract = {Plant epidermal cells dedicate more than half of their lipid metabolism to the synthesis of cuticular lipids, which seal and protect the plant shoot. The cuticle is made up of a cutin polymer and waxes, diverse hydrophobic compounds including very-long-chain fatty acids and their derivatives. How such hydrophobic compounds are exported to the cuticle, especially through the hydrophilic plant cell wall, is not known. By performing a reverse genetic screen, we have identified LTPG, a glycosylphosphatidylinositol-anchored lipid transfer protein that is highly expressed in the epidermis during cuticle biosynthesis in Arabidopsis thaliana inflorescence stems. Mutant plant lines with decreased LTPG expression had reduced wax load on the stem surface, showing that LTPG is involved either directly or indirectly in cuticular lipid deposition. In vitro 2-p-toluidinonaphthalene-6-sulfonate assays showed that recombinant LTPG has the capacity to bind to this lipid probe. LTPG was primarily localized to the plasma membrane on all faces of stem epidermal cells in the growing regions of inflorescence stems where wax is actively secreted. These data suggest that LTPG may function as a component of the cuticular lipid export machinery.},
	keywords = {ABC TRANSPORTER, BINDING, CELLS, CUTICULAR WAX, GENE, GENOME-WIDE, MEMBRANE-PROTEINS, PHOSPHOLIPASE-D, PREDICTION SERVER, SEQUENCE TAGS},
	isbn = {1040-4651},
	url = {<Go to ISI>://000266295800020},
	author = {DeBono, A. and Yeats, T. H. and Rose, J. K. C. and Bird, D. and Jetter, R. and Kunst, L. and Samuelsa, L.}
}
@article {2366,
	title = {Calorimetric studies of the interaction between the insulin-enhancing drug candidate bis(maltolato)oxovanadium(IV) (BMOV) and human serum apo-transferrin},
	journal = {Journal of Inorganic Biochemistry},
	volume = {103},
	number = {4},
	year = {2009},
	note = {ISI Document Delivery No.: 429EUTimes Cited: 8Cited Reference Count: 31Bordbar, Abdol-Khalegh Creagh, A. Louise Mohammadi, Fakhrossadat Haynes, Charles A. Orvig, Chris6th International Vanadium SymposiumJUL 17-19, 2008Lisbon, PORTUGALSp. Iss. SI},
	month = {Apr},
	pages = {643-647},
	type = {Proceedings Paper},
	abstract = {Bis(maltolato)oxovanadium(IV) (BMOV), and its ethylmaltol analog, bis(ethymaltolato)oxovanadium(IV) (BEOV), are candidate insulin-enhancing agents for the treatment of type 2 diabetes mellitus; in mid-2008, BEOV advanced to phase 11 clinical testing. The interactions of BMOV and its inorganic congener, vanadyl Sulfate (VOSO4), with human serum apo-transferrin (hTf) were investigated using differential scanning calorimetry (DSC). Addition of BMOV or VOSO4 to apo-hTf resulted in an increase in thermal stability of both the C- and N-lobes of transferrin as a result of binding to either vanadyl compound. A series of DSC thermograms of hTf Solutions containing different molar ratios of BMOV and VOSO4 were used to determine binding constants: at 25 degrees C the binding constants of BMOV to the C- and N-lobes of apo-hTf were found to be 3 (+/- 1) x 10(5) and 1.8 (+/- 0.7) x 10(5) M-1, respectively. The cot-responding values for VOSO4 were 1.7 (+/- 0.3) x 10(5) and 7 (+/- 2) x 10(4) M-1. The results show that the vanadium species initially presented as either BMOV or VOSO4 had similar affinities for human serum transferrin due to oxidation of solvated vanadyl(IV) prior to complexation to transferrin. Binding of metavanadate (VO3-) was confirmed by DSC and isothermal titration calorimetry (ITC) experiments of the interaction between sodium metavanadate (NaVO3) and hTf. (C) 2008 Elsevier Inc. All rights reserved.},
	keywords = {Apo-transferrin, BINDING, BIS(MALTOLATO)OXOVANADIUM(IV), CHEMISTRY, COMPLEXES, Insulin-enhancing, iron, MALTOL, MOLYBDENUM, NICKEL, RATS, STABILITY, VANADIUM},
	isbn = {0162-0134},
	url = {<Go to ISI>://000264904400022},
	author = {Bordbar, A. K. and Creagh, A. L. and Mohammadi, F. and Haynes, C. A. and Orvig, Chris}
}
@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 {2456,
	title = {Nanomechanical Properties of Tenascin-X Revealed by Single-Molecule Force Spectroscopy},
	journal = {Journal of Molecular Biology},
	volume = {385},
	number = {4},
	year = {2009},
	note = {ISI Document Delivery No.: 403HJTimes Cited: 4Cited Reference Count: 35Jollymore, Ashlee Lethias, Claire Peng, Qing Cao, Yi Li, Hongbin},
	month = {Jan},
	pages = {1277-1286},
	type = {Article},
	abstract = {Tenascin-X is an extracellular matrix protein and binds a variety of molecules in extracellular matrix and on cell membrane. Tenascin-X plays important roles in regulating the structure and mechanical properties of connective tissues. Using single-molecule atomic force microscopy, we have investigated the mechanical properties of bovine tenascin-X in detail. Our results indicated that tenascin-X is an elastic protein and the fibronectin type III (FnIII) domains can unfold under a stretching force and refold to regain their mechanical stability upon the removal of the stretching force. All the 30 FnIII domains of tenascin-X show similar mechanical stability, mechanical unfolding kinetics, and contour length increment upon domain unfolding, despite their large sequence diversity. In contrast to the homogeneity in their mechanical unfolding behaviors, FnIII domains fold at different rates. Using the 10th FnIII domain of tenascin-X (TNXfn10) as a model system, we constructed a polyprotein chimera composed of alternating TNXfn10 and GB1 domains and used. atomic force microscopy to confirm that the mechanical properties of TNXfn10 are consistent with those of the FnIII domains of tenascin-X These results lay the foundation to further study the mechanical properties of individual FnIII domains and establish the relationship between point mutations and mechanical phenotypic effect on tenascin-X Moreover, our results provided the opportunity to compare the mechanical properties and design of different forms of tenascins. The comparison between tenascin-X and tenascin-C revealed interesting common as well as distinguishing features for mechanical unfolding and folding of tenascin-C and tenascin-X and will open up new avenues to investigate the mechanical. functions and architectural design of different forms of tenascins. (C) 2008 Elsevier Ltd. All rights reserved.},
	keywords = {AFM, BINDING, DEFICIENCY, DOMAINS, FAMILY, FnIII domains, IDENTIFICATION, III MODULES, MECHANICAL STABILITY, mechanical unfolding, microscopy, PROTEIN, single molecule force spectroscopy, tenascin},
	isbn = {0022-2836},
	url = {<Go to ISI>://000263073400022},
	author = {Jollymore, A. and Lethias, C. and Peng, Q. and Cao, Y. and Li, H. B.}
}
@article {2141,
	title = {The affinity of Ets-1 for DNA is modulated by phosphorylation through transient interactions of an unstructured region},
	journal = {Journal of Molecular Biology},
	volume = {382},
	number = {4},
	year = {2008},
	note = {ISI Document Delivery No.: 359YPTimes Cited: 3Cited Reference Count: 42Lee, Gregory M. Pufall, Miles A. Meeker, Charles A. Kang, Hyun-Seo Graves, Barbara J. McIntosh, Lawrence P.},
	month = {Oct},
	pages = {1014-1030},
	type = {Article},
	abstract = {Binding of the transcription factor Ets-1 to DNA is allosterically regulated by a serine-rich region (SRR) that modulates the dynamic character of the adjacent structured DNA-binding ETS domain and its flanking autoinhibitory elements. Multi-site phosphorylation of the flexible SRR in response to Ca2+ signaling mediates variable regulation of Ets-1 DNA-binding affinity. In this study, we further investigated the mechanism of this regulation. First, thermal and urea denaturation experiments demonstrated that phosphorylation of the predominantly unstructured SRR imparts enhanced thermodynamic stability on the well-folded ETS domain and its inhibitory module. We next identified a minimal fragment (residues 279-440) that exhibits both enhanced autoinhibition of Ets-1 DNA-binding and allosteric reinforcement by phosphorylation. To test for intramolecular interactions between the SRR and the rest of the fragment that were not detectable by H-1-H-1 NOE measurements, paramagnetic relaxation enhancements were performed using Cu2+ bound to the N-terminal ATCUN motif. Increased relaxation detected for specific amide and methyl groups revealed a preferential interaction surface for the flexible SRR extending from the inhibitory module to the DNA-binding interface. Phosphorylation enhanced the localization of the SRR to this surface. We therefore hypothesize that the positioning of the SRR at the DNA-binding interface and its role in shifting Ets-1 to an inhibited conformation are linked. In particular, transient interactions dampen the conformational flexibility of the ETS domain and inhibitory module required for high-affinity binding, as well as possibly occlude the DNA interaction site. Surprisingly, the phosphorylation-dependent effects were relatively insensitive to changes in ionic strength, suggesting that electrostatic forces are not the dominant mechanism for mediating these interactions. The results of this study highlight the role of flexibility and transient binding in the variable regulation of Ets-1 activity. (C) 2008 Elsevier Ltd. All rights reserved.},
	keywords = {allosteric regulation, ATCUN MOTIF, AUTOINHIBITION, BINDING, CHEMICAL-SHIFTS, DISORDERED PROTEIN, DOMAIN, DYNAMICS, GROUP HYDROGEN-EXCHANGE, NMR, paramagnetic relaxation, PARAMAGNETIC RELAXATION ENHANCEMENT, protein dynamics, SPECTROSCOPY, transcription},
	isbn = {0022-2836},
	url = {<Go to ISI>://000260024500017},
	author = {Lee, G. M. and Pufall, M. A. and Meeker, C. A. and Kang, H. S. and Graves, B. J. and McIntosh, L. P.}
}
@article {2033,
	title = {Engineered elastomeric proteins with dual elasticity can be controlled by a molecular regulator},
	journal = {Nature Nanotechnology},
	volume = {3},
	number = {8},
	year = {2008},
	note = {ISI Document Delivery No.: 335WZTimes Cited: 12Cited Reference Count: 29Cao, Yi Li, Hongbin},
	month = {Aug},
	pages = {512-516},
	type = {Article},
	abstract = {Elastomeric proteins are molecular springs that confer excellent mechanical properties(1-5) to many biological tissues and biomaterials. Depending on the role performed by the tissue or biomaterial, elastomeric proteins can behave as molecular springs(1,2,6,7) or shock absorbers(3-5,8-10). Here we combine single-molecule atomic force microscopy and protein engineering techniques to create elastomeric proteins that can switch between two distinct types of mechanical behaviour in response to the binding of a molecular regulator. The proteins are mechanically labile by design and behave as entropic springs with an elasticity that is governed by their configurational entropy. However, when a molecular regulator binds to the protein, it switches into a mechanically stable state and can act as a shock absorber. These engineered proteins effectively mimic and combine the two extreme forms of elastic behaviour found in natural elastomeric proteins, and thus represent a new type of smart nanomaterial that will find potential applications in nanomechanics and material sciences.},
	keywords = {BINDING, BIOLOGICAL ROLES, DESIGN, DOMAINS, FORCE-SPECTROSCOPY, MECHANICAL-PROPERTIES, STABILITY, TITINS, TOPOLOGY},
	isbn = {1748-3387},
	url = {<Go to ISI>://000258325800018},
	author = {Cao, Y. and Li, H. B.}
}
@article {2277,
	title = {Phosphorylation of U24 from Human Herpes Virus type 6 (HHV-6) and its potential role in mimicking myelin basic protein (MBP) in multiple sclerosis},
	journal = {Febs Letters},
	volume = {582},
	number = {18},
	year = {2008},
	note = {ISI Document Delivery No.: 332UKTimes Cited: 2Cited Reference Count: 31Tait, Andrew R. Straus, Suzana K.},
	month = {Aug},
	pages = {2685-2688},
	type = {Article},
	abstract = {Myelin basic protein (MBP) from multiple sclerosis ( MS) patients contains lower levels of phosphorylation at Thr97 than normal individuals. The significance of phosphorylation at this site is not fully understood, but it is proposed to play a role in the normal functioning of MBP. Human Herpesvirus Type 6 encodes the protein U24, which has tentatively been implicated in the pathology of MS. U24 shares a 7 amino acid stretch encompassing the Thr97 phosphorylation site of MBP: PRTPPPS. We demonstrate using a combination of mass spectrometry, thin layer chromatography and autoradiography, that U24 can be phosphorylated at the equivalent threonine. Phospho-U24 may confound signalling or other pathways in which phosphorylated MBP may participate, precipitating a pathological process.},
	keywords = {BINDING, EXPRESSION, HUMAN-HERPESVIRUS-6, IDENTIFICATION, KINASE, MEMBRANE MICRODOMAINS, mimicry, myelin, PHOSPHORYLATION, POSTTRANSLATIONAL MODIFICATIONS, SITE, T-ANTIGEN, U24},
	isbn = {0014-5793},
	url = {<Go to ISI>://000258108400002},
	author = {Tait, A. R. and Straus, S. K.}
}
@article {2035,
	title = {Protein-protein interaction regulates proteins{\textquoteright} mechanical stability},
	journal = {Journal of Molecular Biology},
	volume = {378},
	number = {5},
	year = {2008},
	note = {ISI Document Delivery No.: 305IOTimes Cited: 10Cited Reference Count: 38Cao, Yi Yoo, Teri Zhuang, Shulin Li, Hongbin},
	month = {May},
	pages = {1132-1141},
	type = {Article},
	abstract = {Elastomeric proteins are molecular springs found not only in a variety of biological machines and tissues, but also in biomaterials of superb mechanical properties. Regulating the mechanical stability of elastomeric proteins is not only important for a range of biological processes, but also critical for the use of engineered elastomeric proteins as building blocks to construct nanomechanical devices and novel materials of well-defined mechanical properties. Here we demonstrate that protein-protein interactions can potentially serve as an effective means to regulate the mechanical properties of elastomeric proteins. We show that the binding of fragments of IgG antibody to a small protein, GB1, can significantly enhance the mechanical stability of GB1. The regulation of the mechanical stability of GB1 by IgG fragments is not through direct modification of the interactions in the mechanically key region of GB1; instead, it is accomplished via the long-range coupling between the IgG binding site and the mechanically key region of GB1. Although Fc and Fab bind GB1 at different regions of GB1, their binding to GB1 can increase the mechanical stability of GB1 significantly. Using alanine point mutants of GB1, we show that the amplitude of mechanical stability enhancement of GB1 by Fc does not correlate with the binding affinity, suggesting that binding affinity only affects the population of GB1/human Fc (hFc) complex at a given concentration of hFc, but does not affect the intrinsic mechanical stability of the GB1/hFc complex. Furthermore, our results indicate that the mechanical stability enhancement by IgG fragments is robust and can tolerate sequence/structural perturbation to GB1. Our results demonstrate that the protein-protein interaction is an efficient approach to regulate the mechanical stability of GB1-like proteins and we anticipate that this new methodology will help to develop novel elastomeric proteins with tunable mechanical stability and compliance. (C) 2008 Elsevier Ltd. All rights reserved.},
	keywords = {BINDING, BIOLOGICAL ROLES, CRYSTAL-STRUCTURE, DIHYDROFOLATE-REDUCTASE, DOMAIN, ENGINEERING PROTEINS, FORCE SPECTROSCOPY, FRAGMENT, HUMAN-IGG, MECHANICAL STABILITY, mechanical unfolding, MOLECULAR ELASTICITY, protein-protein interaction, single molecule atomic force microscopy, STABILIZATION},
	isbn = {0022-2836},
	url = {<Go to ISI>://000256171900015},
	author = {Cao, Y. and Yoo, T. and Zhuang, S. L. and Li, H. B.}
}
@article {1290,
	title = {Spontaneous formation of core/shell bimetallic nanoparticles: A calorimetric study},
	journal = {Journal of Physical Chemistry B},
	volume = {109},
	number = {34},
	year = {2005},
	note = {ISI Document Delivery No.: 959DQTimes Cited: 23Cited Reference Count: 41},
	month = {Sep},
	pages = {16326-16331},
	type = {Article},
	abstract = {We showed recently that low entropy core/shell structured nanoparticles form spontaneously from the physical mixture of a dispersion of Ag nanoparticles and that of another noble metal (Rh. Pd, or Pt) at room, temperature. Here we use isothermal titration calorimetry (ITC) and show that the initial step of such a spontaneous process is strongly exothermic. When the alcohol dispersion of poly(N-vinyl-2-pyrrolidone) (PVP)-protected Rh nanoparticles (average diameter 2.3 nm) was titrated into the alcoholic dispersion of PVP-protected Ag nanoparticles, a strong exothermic enthalpy change, Delta H. was observed: Delta H = -908 kJ/mol for Ag(S) nanoparticle (average diameter 10.8 nm) and -963 kJ/mol for Ag(L) nanoparticles (average diameter 22.5 nm). The strength of interaction increases in the order of Rh/Ag > Pd/Ag > Pt/Ag. This strong exothermic interaction is considered as a driving force to from low entropy bimetallic nanoparticles by simple mixing of two kinds of monometallic nanoparticles. We show also that exothermic interactions occur between a pair of noble metal nanoparticles themselves by using ITC.},
	keywords = {ABSORPTION FINE-STRUCTURE, BINDING, CATALYTIC-ACTIVITY, CLUSTERS, CORE-SHELL, GOLD NANOPARTICLES, isothermal titration calorimetry, NANOPARTICLES, PD, REDUCTION, STRUCTURAL-ANALYSIS},
	isbn = {1520-6106},
	url = {<Go to ISI>://000231497500015},
	author = {Toshima, N. and Kanemaru, M. and Shiraishi, Y. and Koga,Yoshikata}
}
@article {1204,
	title = {Synthesis and characterization of dual function vanadyl, gallium and indium curcumin complexes for medicinal applications},
	journal = {Journal of Inorganic Biochemistry},
	volume = {99},
	number = {11},
	year = {2005},
	note = {ISI Document Delivery No.: 984RUTimes Cited: 22Cited Reference Count: 41},
	month = {Nov},
	pages = {2217-2225},
	type = {Article},
	abstract = {Novel bis[4-hydroxy-3-methoxyphenyl]-1,6-heptadiene-3,5-dione (curcumin) complexes with the formula, ML3, where M is Ga(III) or In(III), or of the formula, ML2 where M is [Vo](2+), have been synthesized and characterized by mass spectrometry, infrared and absorption spectroscopies, and elemental analysis. A new ligand, bis[4-acetyl-3-hydroxyphenyl]-1,6-heptadiene-3,5-dione (diacetylbisdemethoxycurcumin, DABC) was similarly characterized; an X-ray structure analysis was performed. Vanadyl complexes tested in an acute i.p. testing protocol in STZ-diabetic rats showed a lack of insulin enhancing potential. Vanadyl complexes were, however, more cytotoxic than were the ligands alone in standard MTT (3-[4,5-dimethylthiazole-2-yl]ate, -2.5-diphenyl-tetrazolium bromide) cytotoxicity testing, using mouse lymphoma cells. With the exception of DABC, that was not different from VO(DABC)(2), the complexes were not significantly different from one another, with IC50 values in the 5-10 mu M range. Gallium and indium curcumin complexes had IC50 values in the same 5-10 mu M range; whereas Ga(DAC)(3) and In(DAC)(3) (where DAC = diacetylcurcumin) were much less cytotoxiC (IC50 = 20-30 mu M). Antioxidant capacity was decreased in VO(DAC)(2), Ga(DAC)(3), and In(DAC)(3),, compared to vanadyl, gallium and indium curcumin, corroborating the importance of curcumin{\textquoteright}s free phenolic OH groups for scavenging oxidants, and correlated with reduced cytotoxic potential. (c) 2005 Elsevier Inc. All rights reserved.},
	keywords = {ANALOGS, antioxidant capacity, ANTIOXIDANT MECHANISM, ANTITUMOR ACTIVITY, BINDING, COORDINATION CHEMISTRY, curcumin, cytotoxicity, DERIVATIVES, diacetylcurcumin, gallium, GROUP, indium, INSULIN MIMICS, MANGANESE COMPLEXES, RADICAL SCAVENGING ABILITY, TOXICITY, VANADIUM},
	isbn = {0162-0134},
	url = {<Go to ISI>://000233322800012},
	author = {Mohammadi, K. and Thompson, K. H. and Patrick, B. O. and Storr, T. and Martins, C. and Polishchuk, E. and Yuen, V. G. and McNeill, J. H. and Orvig, Chris}
}
@article {1032,
	title = {Boneratamides A-C, new sesquiterpenoids isolated from the marine sponge Axinyssa aplysinoides},
	journal = {Journal of Natural Products},
	volume = {67},
	number = {10},
	year = {2004},
	note = {ISI Document Delivery No.: 865MRTimes Cited: 4Cited Reference Count: 14},
	month = {Oct},
	pages = {1752-1754},
	type = {Article},
	abstract = {Three new sesquiterpenoids, boneratamides A (1)-C (3), have been isolated as their methyl esters 4-6 from extracts of the marine sponge Axinyssa aplysinoides collected in Indonesia. The structures of methyl esters 4-6 were elucidated by analysis of spectroscopic data and confirmed by single-crystal X-ray diffraction analysis of 4.},
	keywords = {AGENT, ANALOGS, BINDING, HEMIASTERLIN, NATURAL-PRODUCTS, PACLITAXEL, TUBULIN},
	isbn = {0163-3864},
	url = {<Go to ISI>://000224707700025},
	author = {Williams, D. E. and Patrick, B. O. and Tahir, A. and Van Soest, R. and Roberge, M. and Andersen, R. J.}
}
@article {932,
	title = {Structural and dynamic independence of isopeptide-linked RanGAP1 and SUMO-1},
	journal = {Journal of Biological Chemistry},
	volume = {279},
	number = {47},
	year = {2004},
	note = {ISI Document Delivery No.: 870ZPTimes Cited: 14Cited Reference Count: 46},
	month = {Nov},
	pages = {49131-49137},
	type = {Article},
	abstract = {Although sumoylation regulates a diverse and growing number of recognized biological processes, the molecular mechanisms by which the covalent attachment of the ubiquitin-like protein SUMO can alter the properties of a target protein remain to be established. To address this question, we have used NMR spectroscopy to characterize the complex of mature SUMO-1 with the C-terminal domain of human RanGAP1. Based on amide chemical shift and N-15 relaxation measurements, we show that the C terminus of SUMO-1 and the loop containing the consensus sumoylation site in RanGAP1 are both conformationally flexible. Furthermore, the overall structure and backbone dynamics of each protein remain unchanged upon the covalent linkage of Lys(524) in RanGAP1 to the C-terminal Gly(97) of SUMO-1. Therefore, SUMO-1 and RanGAP1 behave as "beads-on-a-string," connected by a flexible isopeptide tether. Accordingly, the sumoylation-dependent interaction of RanGAP1 with the nucleoporin RanBP2 may arise through the bipartite recognition of both RanGAP1 and SUMO-1 rather than through a new binding surface induced in either individual protein upon their covalent linkage. We hypothesize that this conformational flexibility may be a general feature contributing to the recognition of ubiquitin-like modified proteins by their downstream effector machineries.},
	keywords = {BACKBONE DYNAMICS, BINDING, CONJUGATION, CRYSTAL-STRUCTURE, GTPASE-ACTIVATING PROTEIN, IN-VIVO, MOLYBDOPTERIN, NUCLEAR-PORE COMPLEX, SYNTHASE, UBC9, UBIQUITIN},
	isbn = {0021-9258},
	url = {<Go to ISI>://000225098100078},
	author = {Macauley, M. S. and Errington, W. J. and Okon, M. and Scharpf, M. and Mackereth, C. D. and Schulman, B. A. and McIntosh, L. P.}
}
@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 {620,
	title = {Molecular interaction in capillary electrophoresis},
	journal = {Current Opinion in Biotechnology},
	volume = {14},
	number = {1},
	year = {2003},
	note = {ISI Document Delivery No.: 645XTTimes Cited: 37Cited Reference Count: 22},
	month = {Feb},
	pages = {126-130},
	type = {Review},
	abstract = {At the present time, affinity capillary electrophoresis is a well-established method for the measurement of binding constants involving 1:1 interactions. Many recent applications of this technique have illustrated its versatility. If affinity capillary electrophoresis is to be widely applied to the study of all types of interactions it is imperative that we consider that higher order interactions may be present. Applying proper equations or developing new models appropriate to the description of such systems is essential to obtaining reliable binding information.},
	keywords = {ANALYTE MIGRATION BEHAVIOR, BINDING, CONSTANTS, ERROR PROPAGATION, HUMAN SERUM-ALBUMIN, MONTE-CARLO, RANGE, RECTANGULAR HYPERBOLAE, SIMULATION},
	isbn = {0958-1669},
	url = {<Go to ISI>://000181006300018},
	author = {Galbusera, C. and Chen, D. D. Y.}
}
@article {717,
	title = {Non-ideality of methanol solution{\textquoteright}s of artificial serum in the mole fraction range from 5 x 10(-4) to 5 x 10(-3) at 25 degrees C},
	journal = {Fluid Phase Equilibria},
	volume = {207},
	number = {1-2},
	year = {2003},
	note = {ISI Document Delivery No.: 683WUTimes Cited: 0Cited Reference Count: 20},
	month = {May},
	pages = {301-317},
	type = {Article},
	abstract = {Vapour pressure and excess partial molar enthalpy were measured at 25 degreesC for solutions of methanol in H2O and artificial serum solutions. The mole fraction range studied was from 5 x 10(-4) to 5 x 10(-3). From the vapour pressure data, the partial pressures were determined by the Barker{\textquoteright}s and Boissonnas{\textquoteright} methods. Various thermodynamic functions were then calculated from them. The curve-fitting (Barker{\textquoteright}s method) gave the osmotic coefficients very close to unity in all the cases, including serum solutions. The purely numerical method without resorting to any fitting function (Boissonnas{\textquoteright} method), on the other hand, produced the osmotic coefficient significantly larger than unity in serum solutions studied. This is consistent with the findings by the earlier freezing point depression study on ethanol in human blood serum solutions. The partial molar enthalpy data indicated highly non-ideal behaviours also, particularly in serum solutions. The detailed mechanism causing non-ideality even at this dilute concentration range is yet to be elucidated. (C) 2003 Elsevier Science B.V. All rights reserved.},
	keywords = {ALBUMIN, AQUEOUS-SOLUTIONS, Barker{\textquoteright}s and Boissonnas methods, BINDING, chemical potential, data analysis by, DILUTE, LAW REGION, methanol in H2O and serum with bovine serum, osmotic coefficient, partial molar enthalpy, VAPOR-PRESSURES, WATER},
	isbn = {0378-3812},
	url = {<Go to ISI>://000183174700020},
	author = {Ralloff, K. P. G. and Westh, P. and Purssell, R. A. and Pudek, M. and Koga,Yoshikata}
}
@article {593,
	title = {Sialic acid biosynthesis: Stereochemistry and mechanism of the reaction catalyzed by the mammalian UDP-N-acetylglucosamine 2-epimerase},
	journal = {Journal of the American Chemical Society},
	volume = {125},
	number = {9},
	year = {2003},
	note = {ISI Document Delivery No.: 649YPTimes Cited: 19Cited Reference Count: 44},
	month = {Mar},
	pages = {2455-2461},
	type = {Article},
	abstract = {The bifunctional enzyme, UDP-N-acetylglucosamine 2-epimerase/ManNAc kinase, catalyzes the first two steps in the biosynthesis of the sialic acids in mammals. The epimerase domain converts UDP-GlcNAc into ManNAc and UDP. This paper demonstrates that a-ManNAc is the first formed anomer and therefore the reaction proceeds with a net retention of configuration at C-1. Studies in deuterated buffer show that solvent-derived deuterium is quantitatively incorporated into the C-2 position of the product during catalysis, but it is not incorporated into the remaining pool of substrate. This indicates that the inversion of stereochemistry is ultimately brought about by the removal and replacement of a proton at C-2 and is consistent with a two-base mechanism. Studies with O-18-labeled UDP-GlcNAc show that the anomeric oxygen of the glycosyl phosphate bond departs with the UDP product and therefore the net hydrolysis reaction involves C-O bond cleavage. Incubation of the putative intermediate, 2-acetamidoglucal, with the enzyme resulted in a slow hydration reaction to give the product, ManNAc. Additional kinetic isotope effect and positional isotope exchange (PIX) experiments address the nature of the rate-determining step of the reaction and show that C-H bond cleavage is not rate limiting. Overall, these results support a reaction mechanism involving an anti-elimination of UDP to give 2-acetamidoglucal, followed by a syn-addition of water.},
	keywords = {2-EPIMERASE/N-ACETYLMANNOSAMINE KINASE, BIFUNCTIONAL ENZYME CATALYZES, BINDING, CELL-SURFACE SIALYLATION, EPIMERIZATION, FIRST 2 STEPS, GLUTAMATE RACEMASE, POSITIONAL ISOTOPE EXCHANGE, RAT-LIVER},
	isbn = {0002-7863},
	url = {<Go to ISI>://000181235800030},
	author = {Chou, W. K. and Hinderlich, S. and Reutter, W. and Tanner, M. E.}
}
@article {678,
	title = {Template effect where 1-3 molecules drive formation of a trimer carceplex},
	journal = {Chemistry-a European Journal},
	volume = {9},
	number = {14},
	year = {2003},
	note = {ISI Document Delivery No.: 706XATimes Cited: 6Cited Reference Count: 46},
	month = {Jul},
	pages = {3253-3262},
	type = {Article},
	abstract = {The template effect in the formation of a trimer carceplex using 1-3 molecules as templates is explored. Thirteen different templates were studied and template ratios were measured for templates of like and unlike molecularity. Five transition-state models were studied for their binding abilities to see if these mirror the template ratios. The chemical shifts of the guests and the thermodynamic and kinetic values for templation suggest that binding is key, often tight, and that the guest determining step is formation of the last covalent bond. The molecular dynamics of guests as well as the conformational dynamics of both hosts and guests further addresses nature of the recognition between host and guest. Finally, we were surprised to discover that water can bind reversibly to the trimer carceplexes, which will have ramifications to any inner phase reactions conducted inside the cage.},
	keywords = {AMPLIFICATION, BARRIER, BINDING, CAPTURE, carceplex, CHEMISTRY, DIELS-ALDER REACTION, DYNAMICS, ELUCIDATION, ENCAPSULATION, HOST-GUEST COMPLEXATION, host-guest systems, molecular recognition, RESORCINARENE CAPSULE, REVERSIBLE, supramolecular, TEMPLATE SYNTHESIS},
	isbn = {0947-6539},
	url = {<Go to ISI>://000184479300009},
	author = {Makeiff, D. A. and Sherman, J. C.}
}
@article {384,
	title = {Affinity capillary electrophoresis using a low-concentration additive with the consideration of relative mobilities},
	journal = {Analytical Chemistry},
	volume = {74},
	number = {8},
	year = {2002},
	note = {ISI Document Delivery No.: 541BPTimes Cited: 24Cited Reference Count: 28},
	month = {Apr},
	pages = {1903-1914},
	type = {Article},
	abstract = {Most affinity studies in capillary electrophoresis assume that the analyte concentration is much smaller than the additive concentration so that the migration of the analyte has no effect on the concentration of the additive in the capillary. However, in most medium- to high-affinity interactions, the additive concentration has to be kept rather low to observe the changes in analyte mobility before saturation is reached. In this paper, a mathematical model is developed to describe the migration behavior of the analyte in a system where the complex formed becomes concentrated to levels much greater than the original concentration of the additive due to the differences in the mobilities of the analyte, additive, and complex. The analyte is flurbiprofen, the additive is transthyretin, and the stoichiometry of the reaction between the two is 1:2. This study also provides a new algorithm to determine medium- to high-affinity binding interaction constants by CE.},
	keywords = {BINDING, CONSTANTS, DRUG-PROTEIN, ERROR PROPAGATION, LIGANDS, MONTE-CARLO SIMULATION, RANGE, RECTANGULAR HYPERBOLAE, SURFACE-PLASMON RESONANCE, TRANSTHYRETIN},
	isbn = {0003-2700},
	url = {<Go to ISI>://000174965600022},
	author = {Galbusera, C. and Thachuk, M. and De Lorenzi, E. and Chen, D. D. Y.}
}
@article {332,
	title = {A differential vapor-pressure equipment for investigations of biopolymer interactions},
	journal = {Journal of Biochemical and Biophysical Methods},
	volume = {50},
	number = {2-3},
	year = {2002},
	note = {ISI Document Delivery No.: 510CETimes Cited: 7Cited Reference Count: 47},
	month = {Jan},
	pages = {269-288},
	type = {Article},
	abstract = {The design and performance of an equipment for the measurement of vapor pressures over liquid or solid samples is presented. The equilibrium pressure difference, DeltaP, between a sample and a reference of known vapor pressure is recorded as a function of composition and/or temperature. Through the use of high-accuracy capacitance manometers and a leak-tight system of stainless steel pipes, below-scaled valves and metal-gasket fittings, DeltaP can be measured with a resolution of about 0.5 mubar (0.05 Pa) in some applications. This sensitivity level, along with other features of the equipment, particularly a "gas-phase titration" routine for changing the cell composition, makes it effective for the investigations of several types of biopolymer interactions. These include isothermal studies of net affinities such as the adsorption of water to proteins or membranes, the preferential interaction of biopolymers with the components of a mixed solvent. the partitioning of solutes between a membrane and the aqueous bulk and the weak. specific binding of ligands to macromolecules. Furthermore, a temperature-scanning mode allows real-time elucidation of such interactions at thermally induced conformational changes in biopolymers. Selected examples of these applications are presented and discussed. (C) 2002 Elsevier Science B.V. All rights reserved.},
	keywords = {25-DEGREES-C, ALCOHOLS, BINDING, BOVINE SERUM-ALBUMIN, CALORIMETER, differential, hydration, LIQUID-EQUILIBRIA, preferential interaction, static vapor pressure, temperature scanning, TEMPERATURES, THERMODYNAMICS, titration, WATER, weak binding},
	isbn = {0165-022X},
	url = {<Go to ISI>://000173190500016},
	author = {Andersen, K. B. and Koga,Yoshikata and Westh, P.}
}
@article {442,
	title = {Tandem mass spectrometry of protein-protein complexes: Cytochrome c-cytochrome b(5)},
	journal = {Journal of the American Society for Mass Spectrometry},
	volume = {13},
	number = {1},
	year = {2002},
	note = {ISI Document Delivery No.: 504QXTimes Cited: 31Cited Reference Count: 53},
	month = {Jan},
	pages = {59-71},
	type = {Article},
	abstract = {An improved method to interpret triple quadrupole MS/MS experiments of complexes of large ions is presented and applied to a study of the complex formed by the proteins cytochrome c and cytochrome b(5). Modeling of the activation and dissociation process shows that most of the reaction occurs near the collision cell exit where ions have the highest internal energies. Experiments at different collision cell pressures or with different collision gases (Ne, Ar, Kr) are interpreted with a previously proposed collision model (Chen et al., Rapid Commun. Mass Spectrom. 1998, 12, 1003-1010) to calculate the internal energy added to ions to cause dissociation. Small but systematic differences under different experimental conditions are attributed to different times available for reaction. A method to correct for this is presented. Ne, Ar, and Kr are found to have similar energy transfer efficiencies. Complexes of cytochrome c and cytochrome b5 are detected in ESI mass spectra but with abundances less than expected from the solution equilibrium. Dissociation of the cytochrome c-cytochrome b(5) complexes with charge k gives as the most abundant fragments, cytochrome b(5)(+3) and cytochrome c(+(k+3)). Adding charges to the complex destabilizes it. A series of cytochrome c variants with Lys residues thought to be involved in solution binding replaced by Ala showed no differences in the energy required to induce dissociation of the gas phase complex. The implications for the binding of the gas phase ions are inconclusive. (J Am Soc Mass Spectrom 2002, 13, 59-71) ((C)) 2002 American Society for Mass Spectrometry.},
	keywords = {ACTIVATION, BINDING, COLLISION-INDUCED DISSOCIATION, CROSS-SECTIONS, ELECTROSPRAY-IONIZATION, GAS-PHASE, INTERNAL ENERGY, ION-TRAP, NONCOVALENT COMPLEXES, YEAST ISO-1-FERRICYTOCHROME-C},
	isbn = {1044-0305},
	url = {<Go to ISI>://000172868300007},
	author = {Mauk, M. R. and Mauk, A. G. and Chen, Y. L. and Douglas, D. J.}
}
@article {5048,
	title = {Cdc4p, a contractile ring protein essential for cytokinesis in Schizosaccharomyces pombe, interacts with a phosphatidylinositol 4-kinase},
	journal = {Journal of Biological Chemistry},
	volume = {276},
	number = {8},
	year = {2001},
	note = {ISI Document Delivery No.: 404RUTimes Cited: 27Cited Reference Count: 35},
	month = {Feb},
	pages = {5932-5942},
	type = {Article},
	abstract = {The proposed function of Cdc4p, an essential contractile ring protein in Schizosaccharomyces pombe, is that of a myosin essential light chain. However, five conditionally lethal cdc4 alleles exhibit complementation in diploids. Such interallelic complementation is not readily explained if the sole function of Cde4p is that of a myosin essential light chain. Complementation of cdc4 alleles could occur only if different mutant forms can assemble into an active oligomeric complex or if Cdc4p has more than one essential function. To search for other proteins that may interact with Cdc4p, we performed a two-hybrid screen and identified two such candidates: one similar to Saccharomyces cerevisiae Vps27p and the other a putative phosphatidylinositol (PI) 4-kinase. finding of Cdc4p to the latter and to myosin heavy chain (Myo2p) was confirmed by immunosorbent assays. Deletion studies demonstrated interaction between the Cdc4p C-terminal domain and the PI 4-kinase C-terminal domain. Furthermore, interaction was abolished by the Cdc4p C-terminal domain point mutation, Gly(107) to Ser. This allele also causes failure of cytokinesis. Ectopic expression of the PI 4-kinase C-terminal domain caused cytokinesis defects that were most extreme in cells carrying the G107S allele. We suggest that Cdc4p plays multiple roles in cytokinesis and that interaction with a PI I-kinase may be important for contractile ring assembly and/or function.},
	keywords = {ACTOMYOSIN RING, BINDING, CELL-DIVISION CYCLE, F-ACTIN, FISSION YEAST, GENE, IDENTIFICATION, LIGHT-CHAIN, LOCALIZATION, MYOSIN HEAVY-CHAIN},
	isbn = {0021-9258},
	url = {<Go to ISI>://000167115100071},
	author = {Desautels, M. and Den Haese, J. P. and Slupsky, C. M. and McIntosh, L. P. and Hemmingsen, S. M.}
}
@article {5053,
	title = {Detection of noncovalent complex between alpha-amylase and its microbial inhibitor tendamistat by electrospray ionization mass spectrometry},
	journal = {Rapid Communications in Mass Spectrometry},
	volume = {15},
	number = {2},
	year = {2001},
	note = {ISI Document Delivery No.: 396KYTimes Cited: 11Cited Reference Count: 58},
	pages = {89-96},
	type = {Article},
	abstract = {Electrospray ionization mass spectrometry (ESI-MS) is now routinely used for detection of noncovalent complexes. However, detection of noncovalent protein-protein complexes is not a widespread practice and still produces some challenges for mass spectrometrists. Here we demonstrate the detection of a noncovalent protein-protein complex between alpha -amylase and its microbial inhibitor tendamistat using ESI-MS. Crude porcine pancreatic alpha -amylase was purified using a glycogen precipitation method. Noncovalent complexes between porcine pancreatic alpha -amylase and its microbial inhibitor tendamistat are probed and detected using ESI-MS. The atmosphere-vacuum ESI conditions along with solution conditions and the ratio of inhibitor over enzyme strongly affect the detection of noncovalent complexes in the gas phase. ESI mass spectra of alpha -amylase at pH 7 exhibited charge states significantly lower than that reported previously, which is indicative of a native protein conformation necessary to produce a noncovalent complex. Detection of noncovalent complexes in the gas phase suggests that further use of conventional biochemical approaches to provide a qualitative, and in some cases even quantitative, characterization of equilibria of noncovalent complexes in solution is possible. Copyright (C) 2001 John Wiley \& Sons, Ltd.},
	keywords = {ANALYTICAL ULTRACENTRIFUGATION, BINDING, CRYSTAL-STRUCTURE, CYTOCHROME-C, GAS-PHASE, HEME, MYOGLOBIN, PROBING CONFORMATIONAL-CHANGES, PROTEIN PROTEINASE-INHIBITORS, RECOGNITION SITES},
	isbn = {0951-4198},
	url = {<Go to ISI>://000166636600003},
	author = {Douglas, D. J. and Collings, B. A. and Numao, S. and Nesatyy, V. J.}
}
@article {4780,
	title = {Analysis of the dynamic properties of Bacillus circulans xylanase upon formation of a covalent glycosyl-enzyme intermediate},
	journal = {Protein Science},
	volume = {9},
	number = {3},
	year = {2000},
	note = {ISI Document Delivery No.: 295XWTimes Cited: 16Cited Reference Count: 56},
	month = {Mar},
	pages = {512-524},
	type = {Article},
	abstract = {NMR spectroscopy was used to search for mechanistically significant differences in the local mobility of the main-chain amides of Bacillus circulans xylanase (BCX) in its native and catalytically competent covalent glycosyl-enzyme intermediate states. N-15 T-1, T-2, and N-15{H-1} NOE values were measured for similar to 120 out of 178 peptide groups in both the apo form of the protein and in BCX covalently modified at position Glu78 with a mechanism-based 2-deoxy-2-fluoro-beta-xylobioside inactivator. Employing the model-free formalism of Lipari and Szabo, the measured relaxation parameters were used to calculate a global correlation time ( tau(m)) for the protein in each form (9.2 +/- 0.2 ns for apo-BCX; 9.8 +/- 0.3 ns for the modified protein), as well as individual order parameters for the main-chain NH bond vectors. Average values of the order parameters for the protein in the apo and complexed forms were S-2 = 0.86 +/- 0.04 and S-2 = 0.91 +/- 0.04, respectively. No correlation is observed between these order parameters and the secondary structure, solvent accessibility, or hydrogen bonding patterns of amides in either form of the protein. These results demonstrate that the backbone of BCX is well ordered in both states and that formation of the,glycosyl-enzyme intermediate leads to little change, in any, in the dynamic properties of BCX on the time scales sampled by N-15-NMR relaxation measurements.},
	keywords = {ACTIVE-SITE NUCLEOPHILE, ANISOTROPIC ROTATIONAL, BACKBONE DYNAMICS, BINDING, BURIED NEUTRAL HISTIDINE, DIFFUSION, glucanase, GLYCOSYL-ENZYME INTERMEDIATE, MAGNETIC-RESONANCE RELAXATION, MODEL-FREE APPROACH, N-15 NMR RELAXATION, NMR, order parameter, PROTEIN, PROTEINS, relaxation dynamics, SIDE-CHAIN RESONANCES, STRUCTURE},
	isbn = {0961-8368},
	url = {<Go to ISI>://000085994800009},
	author = {Connelly, G. P. and Withers, S. G. and McIntosh, L. P.}
}
@article {4916,
	title = {Cell-based screen for antimitotic agents and identification of analogues of rhizoxin, eleutherobin, and paclitaxel in natural extracts},
	journal = {Cancer Research},
	volume = {60},
	number = {18},
	year = {2000},
	note = {ISI Document Delivery No.: 358GQTimes Cited: 62Cited Reference Count: 55},
	month = {Sep},
	pages = {5052-5058},
	type = {Article},
	abstract = {We describe a cell-based assay for antimitotic compounds that is suitable for drug discovery and for quantitative determination of antimitotic activity, In the assay, cells arrested in mitosis as a result of exposure to antimitotic agents in pure form or in crude natural extracts are detected by ELISA using the monoclonal antibody TG-3, The assay was used to screen >24,000 extracts of marine microorganisms and invertebrates and terrestrial plants and to guide the purification of active compounds from 5 of 119 positive extracts. A new rhizoxin analogue was found in a Pseudomonas species, six new eleutherobin analogues were identified from the octocoral Erythropodium caribaeorum, and two paclitaxel analogues were found in the stem bark of the tree Ilex macrophylla. The assay was also used for quantitative comparison of the antimitotic activity of different analogues. It revealed the importance of the C-11 to C-13 segment of the diterpene core of eleutherobin for its antimitotic activity. The identification of antimitotic compounds in very low abundance and their high (0.5\%) occurrence in natural extracts indicates that drug discovery efforts using this cell-based assay may lead to the identification of structurally novel antimitotic agents.},
	keywords = {AGENT, ANTITUMOR, BINDING, fungus, INHIBITION, MACROCYCLIC LACTONE ANTIBIOTICS, MICROTUBULE-STABILIZING AGENTS, MITOTIC SPINDLES, RHIZOPUS-CHINENSIS, TAXOL, TUBULIN POLYMERIZATION},
	isbn = {0008-5472},
	url = {<Go to ISI>://000089550600013},
	author = {Roberge, M. and Cinel, B. and Anderson, H. J. and Lim, L. and Jiang, X. X. and Xu, L. and Bigg, C. M. and Kelly, M. T. and Andersen, R. J.}
}
@article {4942,
	title = {Comparative toxicity of trivalent and pentavalent inorganic and methylated arsenicals in rat and human cells},
	journal = {Archives of Toxicology},
	volume = {74},
	number = {6},
	year = {2000},
	note = {ISI Document Delivery No.: 349ZATimes Cited: 358Cited Reference Count: 37},
	month = {Aug},
	pages = {289-299},
	type = {Article},
	abstract = {Biomethylation is considered a major detoxification pathway for inorganic arsenicals (iAs). According to the postulated metabolic scheme, the methylation of iAs yields methylated metabolites in which arsenic is present in both pentavalent and trivalent forms. Pentavalent mono- and dimethylated arsenicals are less acutely toxic than iAs. However, little is known about the toxicity of trivalent methylated species. In the work reported here the toxicities of iAs and trivalent and pentavalent methylated arsenicals were examined in cultured human cells derived from tissues that are considered a major site for iAs methylation (liver) or targets for carcinogenic effects associated with exposure to iAs (skin, urinary bladder, and lung). To characterize the role of methylation in the protection against toxicity of arsenicals, the capacities of cells to produce methylated metabolites were also examined. In addition to human cells, primary rat hepatocytes were used as methylating controls. Among the arsenicals examined, trivalent monomethylated species were the most cytotoxic in all cell types. Trivalent dimethylated arsenicals were at least as cytotoxic as trivalent iAs (arsenite) for most cell types. Pentavalent arsenicals were significantly less cytotoxic than their trivalent analogs. Among the cell types examined, primary rat hepatocytes exhibited the greatest methylation capacity for iAs followed by primary human hepatocytes, epidermal keratinocytes, and bronchial epithelial cells. Cells derived from human bladder did not methylate iAs. There was no apparent correlation between susceptibility of cells to arsenic toxicity and their capacity to methylate iAs. These results suggest that (1) trivalent methylated arsenicals, intermediary products of arsenic methylation, may significantly contribute to the adverse effects associated with exposure to iAs, and (2) high methylation capacity does not protect cells from the acute toxicity of trivalent arsenicals.},
	keywords = {ARSENATE, arsenic, ARSENITE, BINDING, bladder, cell culture, CELLULAR UPTAKE, DIMETHYLARSINIC ACID, dimethylarsinous acid, DRINKING-WATER, ENZYMATIC METHYLATION, GLUTATHIONE, HEPATOCYTES, HUMAN, IN-VITRO METHYLATION, LIVER, lung, METABOLISM, methylarsonic acid, methylarsonous acid, METHYLATION, RABBIT LIVER, SKIN, TOXICITY},
	isbn = {0340-5761},
	url = {<Go to ISI>://000089074500001},
	author = {Styblo, M. and Del Razo, L. M. and Vega, L. and Germolec, D. R. and LeCluyse, E. L. and Hamilton, G. A. and Reed, W. and Wang, C. and Cullen, W. R. and Thomas, D. J.}
}
@article {4711,
	title = {Enzymatic methylation of arsenic compounds. VII. Monomethylarsonous acid (MMA(III)) is the substrate for MMA methyltransferase of rabbit liver and human hepatocytes},
	journal = {Toxicology and Applied Pharmacology},
	volume = {158},
	number = {1},
	year = {1999},
	note = {ISI Document Delivery No.: 216QCTimes Cited: 80Cited Reference Count: 33},
	month = {Jul},
	pages = {9-15},
	type = {Article},
	abstract = {Inorganic arsenite is methylated by some, but not all, animal species to dimethylarsinic acid (DMA), The monomethyl compound containing arsenic in an oxidation state of +3 has been proposed as an intermediate. Using highly purified arsenic methyltransferase from rabbit liver and the partially purified enzyme from Chang human liver hepatocytes, the activity of methylarsonic acid (MMA(V)) and methylarsonous acid (MMA(III)) as a substrate has been characterized by Michaelis-Menten kinetics. The rabbit liver enzyme has a greater affinity for MMA(III) (K-m = 0.92 x 10(-5) M) than MMA(V) (K-m = 7.0 x 10(-5) M) since the smaller the K, the greater the affinity. In addition, a dithiol, reduced lipoic acid or dithiothreitol, appears to be more active than GSH in satisfying the thiol requirement of the enzyme. Although investigators have been unable to detect the arsenic methyltransferase in surgically removed human liver, its presence in Chang human hepatocytes now has been established. The K-m for MMA(III), 3.04 x 10(-6), using MMAIII methyltransferase from Chang human hepatocytes was not greatly different from that of the rabbit liver enzyme, (C) 1999 Academic Press.},
	keywords = {BINDING, CYTOSOL, IN-VITRO, INVITRO, METABOLISM, TOXICITY, WATER, WEST-BENGAL},
	isbn = {0041-008X},
	url = {<Go to ISI>://000081452500002},
	author = {Zakharyan, R. A. and Ayala-Fierro, F. and Cullen, W. R. and Carter, D. M. and Aposhian, H. V.}
}
@article {4207,
	title = {Dynamic complexation of solutes in capillary electrophoresis},
	journal = {Electrophoresis},
	volume = {19},
	number = {3},
	year = {1998},
	note = {ISI Document Delivery No.: ZD713Times Cited: 12Cited Reference Count: 28},
	month = {Mar},
	pages = {383-387},
	type = {Article},
	abstract = {The analyte migration behavior in any chemical separation system can be described using a single equation that unifies all areas of separation science. This equation can be used in capillary electrophoresis (CE) to design separation systems, and to study interactions between analytes and additives. By using individual capacity factors for each analyte species present in the system, and with the knowledge of the characteristics of each interaction, one can predict the analyte migration behavior in complicated CE systems, including systems with multiple 1:1 interactions and/or higher order interactions.},
	keywords = {AFFINITY, BETA-CYCLODEXTRIN, BINDING, capacity factor, CHIRAL SEPARATIONS, dynamic complexation capillary electrophoresis, ENANTIOMERS, higher order interactions, MICELLAR ELECTROKINETIC CHROMATOGRAPHY, multiple equilibria, OPTIMIZATION, RESOLUTION, SELECTIVITY, separation theory, TIOCONAZOLE, ZONE ELECTROPHORESIS},
	isbn = {0173-0835},
	url = {<Go to ISI>://000072716000003},
	author = {Bowser, M. T. and Chen, D. D. Y.}
}
@article {4190,
	title = {An effective synthetic route to EF5},
	journal = {Synthetic Communications},
	volume = {28},
	number = {19},
	year = {1998},
	note = {ISI Document Delivery No.: 117KHTimes Cited: 2Cited Reference Count: 17},
	pages = {3701-3709},
	type = {Article},
	abstract = {EF5 (a 2-nitroimidazole containing an N-(pentafluoropropyl) acetamide substituent) is a very sensitive probe for quantifying the amount of hypoxia within cells; a much improved, short step, synthetic procedure is described for EF5, whose X-ray structure is also presented.},
	keywords = {ANTIBODIES, BINDING, CELLS, COMPLEXES, CRYSTAL, HYPOXIA, TUMORS},
	isbn = {0039-7911},
	url = {<Go to ISI>://000075780100021},
	author = {Baird, I. R. and Skov, K. A. and James, Brian R. and Rettig, S. J. and Koch, C. J.}
}
@article {4205,
	title = {Higher order equilibria and their effect on analyte migration behavior in capillary electrophoresis},
	journal = {Analytical Chemistry},
	volume = {70},
	number = {15},
	year = {1998},
	note = {ISI Document Delivery No.: 107VQTimes Cited: 38Cited Reference Count: 31},
	month = {Aug},
	pages = {3261-3270},
	type = {Article},
	abstract = {This paper presents a quantitative investigation into the effect of analyte-additive interactions on analyte migration behavior in capillary electrophoresis (CE) when both 1:1 and 1:2 stoichiometries are present. Equations based on the individual capacity factors for each interaction are derived to account for the effect of both first- and second-order equilibria. The analyte migration behavior is described using these equations with a full account of how the microscopic equilibrium constants and microscopic mobilities are combined to give the macroscopic values. The binding isotherms of interactions with both 1:1 and 1:2 stoichiometries are compared with those of a 1:1 stoichiometry. 4,4{\textquoteright}-Biphenol and 4-phenylphenol were chosen as analytes that undergo complexation with one and two hydroxypropyl-beta-cyclodextrin (HP-beta-CD) molecules; phenol was used as an analyte that interacts with only one HP-beta-CD molecule. The process of calculating higher order equilibrium constants and complex mobilities from the binding isotherms is demonstrated. The effects of experimental conditions, such as the additive concentration range and the number of data points, on the error in the calculated constants and the ability of the equations to accurately describe the experimental data are discussed. A comparison of the linear transformations of the binding isotherm with respect to their ability to detect higher order equilibria is made, and the advantage of using the capacity factor in CE is illustrated.},
	keywords = {AFFINITY, BETA-CYCLODEXTRIN, BINDING, CHIRAL SEPARATION, METAL-IONS, SELECTIVITY, SELECTORS, THEORETICAL ASPECTS, TIOCONAZOLE ENANTIOMERS, ZONE ELECTROPHORESIS},
	isbn = {0003-2700},
	url = {<Go to ISI>://000075232000034},
	author = {Bowser, M. T. and Chen, D. D. Y.}
}
@article {4305,
	title = {Optimization and immunological characterization of a photochemically coupled lysergic acid diethylamide (LSD) immunogen},
	journal = {Bioconjugate Chemistry},
	volume = {9},
	number = {5},
	year = {1998},
	note = {ISI Document Delivery No.: 125MYTimes Cited: 2Cited Reference Count: 41},
	month = {Sep-Oct},
	pages = {596-603},
	type = {Article},
	abstract = {A photoreactive heterobifunctional linker was used to prepare an immunogen in which lysergic acid diethylamide was indirectly coupled to keyhole limpet hemocyanin at multiple sites on the drug. It was possible to attach approximately 35 drug molecules to each protein using approximately equal amounts of both species during the reaction. The presence of buffer components or water severely compromised reaction efficiency, as estimated from the molar substitution ratio. Factors such as excess linker, pH, irradiation of dry matrix in the absence of buffer, and the drug/protein ratio used during photolysis were shown to have pronounced effects on reaction efficiency. Structural insights regarding immunogen coupling were obtained by determining the specificities of antibodies which were raised against the immunogen. Cross-reactivity data indicated that haptenation of protein likely occurred at positions N1 and N6 of lysergic acid diethylamide, which is plausible given the electrophilicity of the photogenerated aryl nitrene.},
	keywords = {BINDING, CROSS-LINKING REAGENTS, EPITOPE, FUNCTIONALIZED PERFLUOROPHENYL AZIDES, IMMUNOASSAY, IONIZATION MASS-SPECTROMETRY, photolysis, PROTEIN, RADIOIMMUNOASSAY, SERUM-ALBUMIN},
	isbn = {1043-1802},
	url = {<Go to ISI>://000076242400008},
	author = {Kerrigan, S. and Brooks, D. E.}
}
@article {4224,
	title = {Reversible molecular capsules composed of two cavitands linked via an assortment of charged-hydrogen bonds and covalent bonds},
	journal = {Journal of the American Chemical Society},
	volume = {120},
	number = {38},
	year = {1998},
	note = {ISI Document Delivery No.: 125EVTimes Cited: 42Cited Reference Count: 29},
	month = {Sep},
	pages = {9818-9826},
	type = {Article},
	abstract = {Six new cavitand bowls are reported (6, 7, 8, 9, 11, and 12), as are three bis-bowl compounds (4, 13, and 14). Eight new complexes (4.guest, 7C.guest, 8C.guest, 9C.guest, 14.guest, 15.guest, 15C.guest, and 16C.guest) that reversibly encapsulate small molecules are reported. Two or more charged-hydrogen bonds (CHBs) or covalent linkages between the bowls are required to form stable complexes. Guest exchange rates vary from milliseconds to days. Thermodynamically, these complexes display an enthalpy-entropy compensation. The relative stability of complex 3.pyrazine versus complex 3.chloroform is 170000 in nitrobenzene-d(5) at 298 It. Apparent stability constants in nitrobenzene-d(5) at 298 K yield 1.1 x 10(9) M-1 for complex 3.pyrazine. The absolute stability constant for complex 4.pyrazine in nitrobenzene-d(5) at 333 K is 3.5 x 10(6) M-1.},
	keywords = {BINDING, carceplex, CHEMISTRY, ENCAPSULATION, HEMICARCERANDS, HOST-GUEST COMPLEXATION, ORGANIC-MOLECULES, RELEASE, TEMPLATION},
	isbn = {0002-7863},
	url = {<Go to ISI>://000076225200012},
	author = {Chapman, R. G. and Sherman, J. C.}
}
@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 {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.}
}
@article {3911,
	title = {Prediction of the migration behavior of analytes in capillary electrophoresis based on three fundamental parameters},
	journal = {Journal of Chromatography A},
	volume = {781},
	number = {1-2},
	year = {1997},
	note = {ISI Document Delivery No.: YC198Times Cited: 11Cited Reference Count: 309th International Symposium on High Performance Capillary Electrophoresis and Related Microscale TechniquesJAN 26-30, 1997ORLANDO, FL},
	month = {Sep},
	pages = {23-34},
	type = {Proceedings Paper},
	abstract = {The prediction of analyte migration behavior in capillary electrophoresis (CE) is essential for rapid method development. The dynamic complexation model, based on 1:1 interactions, was used to accurately predict the apparent electrophoretic mobilities and the migration times of a group of deoxyribonucleotides (dNPs) at various concentrations of beta-cyclodextrin (beta-CD). The electrophoretic mobility of the analyte, the electrophoretic mobility of the analyte-additive complex and the equilibrium constant are the three fundamental parameters required to determine the mobility of an analyte. The apparent migration time of the analyte can be predicted once the electroosmotic mobility and relative viscosity of the solution are known. Optimum separation conditions can be determined based on these parameters. Excellent agreement between observed analyte migration behavior and predicted values was demonstrated, with relative errors being often less than 1\%. The theory was tested repeatedly under various conditions in order to assess its predictive capabilities and limitations. Analysis by molecular modelling, in conjunction with calculated electrophoretic parameters and equilibrium constants, provided deeper insight into the probable mechanisms of the separation process at the molecular level. (C) 1997 Elsevier Science B.V.},
	keywords = {AFFINITY, BETA-CYCLODEXTRIN, BINDING, CHIRAL SEPARATION, CONSTANTS, deoxyribonucleotides, ELECTROKINETIC CHROMATOGRAPHY, ENANTIOMERS, migration behaviour, migration time prediction, MODEL, OPTIMIZATION, SELECTORS, TIOCONAZOLE},
	isbn = {0021-9673},
	url = {<Go to ISI>://A1997YC19800005},
	author = {BritzMcKibbin, P. and Chen, D. D. Y.}
}
@article {4099,
	title = {Quantitative description of analyte migration behavior based on the dynamic complexation model in capillary electrophoresis},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {75},
	number = {5},
	year = {1997},
	note = {ISI Document Delivery No.: XF492Times Cited: 20Cited Reference Count: 27},
	month = {May},
	pages = {507-517},
	type = {Article},
	abstract = {A theory based on dynamic complexation is used to describe analyte migration behavior in capillary electrophoresis (CE). This theory is based on a one-phase system, instead of the commonly accepted two-phase system. The migration behavior of an analyte is described by three parameters (the electrophoretic mobility of the free analyte, the electrophoretic mobility of the analyte-additive complex, and the equilibrium constant (formation constant) that determines the fractions of the free analyte and the complex at a certain additive concentration). Varying the additive concentration shifts the equilibrium and changes the viscosity of the background electrolyte. Viscosity correction is crucial in interpreting the observed migration behavior of analytes. While electroosmotic flow in a capillary often varies from one capillary to another, the viscosity of a buffer is characteristic of the buffer composition and is constant for each buffer. The electrophoretic mobility of a certain species and the equilibrium constant are intrinsic properties and are less sensitive to changes in the environment. Understanding these relationships is indispensable in CE method development and method validation. A universal resolution equation is proposed, with a separation factor that has taken both the electrophoretic mobilities and equilibria into consideration. This resolution equation gives clear guidance for the optimization of CE separations. A group of nucleosides and their phosphates are used as analytes, and P-cyclodextrin is used as the additive in the model system studied in this paper. Both the observed analyte migration behavior and the resolution of analytes agree well with this theory.},
	keywords = {ACIDS, BETA-CYCLODEXTRIN, BINDING, capacity factor, CHIRAL SEPARATION, CORRECTION, dynamic complexation capillary electrophoresis, ELECTROKINETIC CHROMATOGRAPHY, mobility, nucleoside and, nucleotide separation, RESOLUTION, resolution equation, VISCOSITY},
	isbn = {0008-4042},
	url = {<Go to ISI>://A1997XF49200005},
	author = {Peng, X. J. and Bebault, G. M. and Sacks, S. L. and Chen, D. D. Y.}
}
@article {4100,
	title = {Quantitative description of analyte migration behavior based on dynamic complexation in capillary electrophoresis with one or more additives},
	journal = {Electrophoresis},
	volume = {18},
	number = {5},
	year = {1997},
	note = {ISI Document Delivery No.: XC565Times Cited: 48Cited Reference Count: 28},
	month = {May},
	pages = {706-716},
	type = {Article},
	abstract = {A comprehensive theory is proposed to describe the migration behavior of analytes in capillary electrophoresis (CE) when one or more additives are present in the buffer solution. This theory amalgamates and extends the previous work done by others. The capacity factor (k{\textquoteright}) in this theory is defined as the product of the equilibrium constant and the additive concentration, thus, k{\textquoteright} changes linearly with additive concentration, The net electrophoretic mobility of an analyte is a function of k{\textquoteright}, therefore, it can be changed by varying the additive concentration. Three parameters are needed to predict the mobility of an analyte in a one-additive CE system: the mobility of the free analyte, the mobility of the complex, and the equilibrium constant for the analyte-additive interaction (which determines the fraction of the free analyte at different additive concentrations). When additives are used, the change in viscosity obscures this relationship, therefore, a viscosity correction factor is required to convert all mobilities to an ideal state where the viscosity remains constant. The migration behavior of an analyte in a solution with multiple additives can be predicted and controlled, once the equilibrium constants of the interactions between the analyte and each of the additives are obtained separately. beta-Cyclodextrin and hydroxypropyl-beta-cyclodextrin are used as additives and the migration behavior of phenol, p-nitrophenol, and benzoic acid are studied as a model system to verify this theory. When the necessary viscosity correction factor is included, the net electrophoretic mobilities of the analytes obtained from experimental results agree with the values predicted by the theory based on dynamic complexation. Although only experiments with one and two additives were carried out to verify the theory, the equations apply to situations when more than two additives are used. The relationship between the theories of electrophoresis and chromatography is clarified.},
	keywords = {additives, analyte migration, BEHAVIOR, BETA-CYCLODEXTRIN, BINDING, capillary electrophoresis, CHIRAL RESOLUTION, DYNAMIC COMPLEXATION, ELECTROKINETIC CHROMATOGRAPHY, OPTIMIZATION, SELECTIVITY, SEPARATION, viscosity correction},
	isbn = {0173-0835},
	url = {<Go to ISI>://A1997XC56500008},
	author = {Peng, X. J. and Bowser, M. T. and BritzMcKibbin, P. and Bebault, G. M. and Morris, J. R. and Chen, D. D. Y.}
}
@article {3909,
	title = {Quantitative description of migration behavior of porphyrins based on the dynamic complexation model in a nonaqueous capillary electrophoresis system},
	journal = {Electrophoresis},
	volume = {18},
	number = {1},
	year = {1997},
	note = {ISI Document Delivery No.: WH231Times Cited: 47Cited Reference Count: 48},
	month = {Jan},
	pages = {82-91},
	type = {Article},
	abstract = {The effect of an additive (Brij 35) on the mobilities of a group of porphyrin acids is quantitatively characterized based on a 1:I dynamic complexation model. Varying additive concentration shifts the equilibrium and changes the viscosity of the background electrolyte. The equilibrium constant, the electrophoretic mobility of the free analyte, and the electrophoretic mobility of the complex are identified as the parameters necessary to describe the analytes{\textquoteright} migration behavior. Several statistical methods for obtaining these parameters are discussed. The equilibrium constants and complex mobilities are calculated using three different linear regression methods. The weighted y-recip-rocal method was preferred because it gives smaller error, and the data points are evenly distributed along the concentration axis. These values are confirmed using a nonlinear regression to ensure that the proper weighting was used in the linear regression plots. The parameters are then used to predict the apparent mobilities of the analytes over the entire additive concentration range, allowing the optimum separation conditions to be identified. For disclike molecules, such as porphyrins, the mobility is determined by the orientation of the molecule in an electric field, in addition to their size and charge. The strength of binding between the porphyrins and Brij 35 depends on the number of binding sites and the solvation shell.},
	keywords = {additives, AFFINITY, ANIONS, BETA-CYCLODEXTRIN, BINDING, CHIRAL SEPARATION, DYNAMIC COMPLEXATION, ENANTIOMERS, nonaqueous capillary electrophoresis, PARAMETERS, PORPHYRIN, SELECTIVITY, SELECTORS, separation theory, TIOCONAZOLE, ZONE ELECTROPHORESIS},
	isbn = {0173-0835},
	url = {<Go to ISI>://A1997WH23100016},
	author = {Bowser, M. T. and Sternberg, E. D. and Chen, D. D. Y.}
}
@article {4143,
	title = {Thermal alkane C-H bond activation by a tungsten alkylidene complex: The reversal of alpha-hydrogen elimination},
	journal = {Journal of the American Chemical Society},
	volume = {119},
	number = {21},
	year = {1997},
	note = {ISI Document Delivery No.: XB674Times Cited: 52Cited Reference Count: 36},
	month = {May},
	pages = {5071-5072},
	type = {Article},
	keywords = {ABSTRACTION, ADDUCTS, ARYL, BINDING, CHEMISTRY, DERIVATIVES, LIGANDS, METAL-COMPLEXES, REACTIVITY, tantalum},
	isbn = {0002-7863},
	url = {<Go to ISI>://A1997XB67400046},
	author = {Tran, E. and Legzdins,Peter}
}
@article {3927,
	title = {Tripodal aminophenolate ligand complexes of aluminum(III), gallium(III), and indium(III) in water},
	journal = {Inorganic Chemistry},
	volume = {36},
	number = {2},
	year = {1997},
	note = {ISI Document Delivery No.: WC887Times Cited: 34Cited Reference Count: 53},
	month = {Jan},
	pages = {236-248},
	type = {Article},
	abstract = {Four water-soluble amine phenols have been prepared: tris(((2-hydroxy-5-sulfobenzyl)amino)ethyl)amine (H(6)TRNS), 1,1,1-tris(((2-hydroxy-5-sulfobenzyl)amino)methyl)ethane (H(6)TAMS), 1,2,3-tris((2-hydroxy-5-sulfobenzyl)amino)propane (H(6)TAPS), and cis,cis-1,3,5-tris((2-hydroxy-5-sulfobenzyl)amino)cyclohexane (H(6)TACS). Complex formation constants have been measured at 25 degrees C (mu = 0.16 M NaCl): log K [M(TRNS)](3-) ([M(HTRNS)](2-)) M = Ga 28.55 (36.90), In 29.3 (34.9); log K [M(TAMS)](3-) ([M(HTAMS)](2-)) M = Al 22.5 (29.3), Ga 31.53, In 28.49; log K [M(TAPS)](3-) ([M(HTAPS)](2-)) M = Al 22.8 (29.0), Ga 31.54 (35.15), In 27.56 (31.93). The order of stability is Ga(III) > In(III) > Al(III) for H(6)TAMS and H(6)TAPS, while far H(6)TRNS it is Ga(III) approximate to In(lII) > Al(III). The solution structures of the complexes have been probed by multinuclear NMR (H-1, C-13, Al-27, Ga-71, In-115) and UV spectroscopic studies, and these solution structures are compared with solid state structures for analogous complexes. The H-1 NMR spectrum in D2O establishes TAPS to be preorganized for metal ion binding. H(6)TACS exists in the wrong conformation for metal ion binding, and this results in slow complexation kinetics and relatively weaker binding.},
	keywords = {ACID, BINDING, EQUILIBRIUM-CONSTANTS, GA(III), HUMAN-SERUM TRANSFERRIN, IN(III), IN-VIVO, METAL-IONS, SCHIFF-BASE LIGANDS, STABILITIES},
	isbn = {0020-1669},
	url = {<Go to ISI>://A1997WC88700021},
	author = {Caravan, P. and Orvig, Chris}
}
@article {3449,
	title = {ELECTROSTATIC EFFECTS ON THE ADSORPTION AND CARBODIIMIDE-MEDIATED COUPLING OF FERRICHROME-A TO AMINE-MODIFIED SILICA},
	journal = {Journal of Colloid and Interface Science},
	volume = {174},
	number = {2},
	year = {1995},
	note = {ISI Document Delivery No.: RV175Times Cited: 2Cited Reference Count: 26},
	month = {Sep},
	pages = {480-489},
	type = {Article},
	abstract = {The adsorption behavior and carbodiimide-mediated coupling were examined for a carboxyl-containing cyclic hexapeptide, ferrichrome A (FeA), on amine-modified silica beads. Adsorption decreased with increasing salt concentration and no adsorption was observed in 100 mM sodium chloride. Ferrichrome A in water adsorbs to amine-modified silica beads to a maximum surface concentration of 1.69 mg/m(2), corresponding to an area per molecule of 104 Angstrom(2); this adsorption is fully reversed by addition of salt. Carboxyl groups on the FeA were coupled to amine groups on silane-modified silica using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) to promote formation of a peptide bond. Ferrichrome A coupled in this way to the silica beads is not washed off in high salt. The isotherms of FeA coupled irreversibly to the beads as a function of solution concentration of FeA were measured using a constant EDC:FeA mole ratio of 50:1 and a constant EDC concentration of 20 mM. There were significant differences between the coupling and adsorption isotherms, particularly at low solution concentrations of FeA. Electrophoretic mobility measurements of the silica beads to which varying amounts of FeA had been covalently bound showed the surface was positively charged at all peptide surface concentrations. The results are consistent with a model of the surface in which FeA is coupled to a porous layer of oligomeric aminosilane through a reaction which is strongly influenced by electrostatic interactions between the surface and reagents. (C) 1995 Academic Press, Inc.},
	keywords = {BINDING, TEMPERATURE},
	isbn = {0021-9797},
	url = {<Go to ISI>://A1995RV17500024},
	author = {Melzak, K. A. and Janzen, J. and Brooks, D. E.}
}
@article {3272,
	title = {The kinetics and energetics of formation of a molecular hydrogen complex involving a dinuclear ruthenium(II) centre},
	journal = {Inorganica Chimica Acta},
	volume = {240},
	number = {1-2},
	year = {1995},
	note = {ISI Document Delivery No.: TV742Times Cited: 9Cited Reference Count: 32},
	month = {Dec},
	pages = {419-425},
	type = {Article},
	abstract = {The reversible equilibrium conversion under H-2 of [RuCl(dppb) (mu-Cl)](2) (1) to generate (eta(2)-H-2) (dppb) (mu-Cl)(3)RUCl( dppb) in CH2Cl2 (dppb = Ph(2)P(CH2)(4)PPh(2)) has been studied at 0-25 degrees C by UV-Vis and (31)p{H-1} NMR spectroscopy, and by stopped-how kinetics; the equilibrium constant and corresponding thermodynamic parameters, and the forward and reverse rate constants at 25 degrees C have been determined. A measured Delta H degrees value of similar to 0 kj mol(-1) allows for an estimation of an exothermicity of similar to 60 kj mol(-1) for binding an eta(2)-H-2 at an Ru(II) centre; a Delta S degrees value of similar to 60 J mol(-1) K-1 indicates that in solution 1 contains coordinated CH2Cl2. The kinetic and thermodynamic data are compared to those obtained from a previously studied hydrogenation of styrene catalyzed by 1. Preliminary findings on related systems containing Ph(2)P(CH2)(3)PPh(2) and (C6H11)(2)P(CH2)(4)P(C6H11)(2) are also noted.},
	keywords = {BINDING, DERIVATIVES, DIHYDROGEN, dihydrogen complexes, LIGANDS, MECHANISTIC ASPECTS, NITROGEN, PHOSPHINE COMPLEXES, ruthenium complexes, SELECTIVE HYDROGENATION},
	isbn = {0020-1693},
	url = {<Go to ISI>://A1995TV74200054},
	author = {Chau, Deky and James, Brian R.}
}
@article {3278,
	title = {TEMPLATION EFFECTS ON FORMATION OF A HEMICARCEPLEX},
	journal = {Supramolecular Chemistry},
	volume = {5},
	number = {1},
	year = {1995},
	note = {ISI Document Delivery No.: RX096Times Cited: 15Cited Reference Count: 36},
	pages = {31-37},
	type = {Article},
	abstract = {We have shown previously that the reaction to form carceplex 3 . guest has dramatic templation requirements where the best template molecule studied is one million times more effective at bridging the two bowl-shaped precursors than the poorest template. Here, we investigate the template requirements for the formation of hemicarceplex 4 . guest which is similar to carceplex 3 . guest in cavity size and shape. The two compounds differ in that 4 . guest lacks one of the four inter-bowl methylene bridges and thus has a portal and reduced symmetry relative to carceplex 3 . guest (C-2v vs D-4h). Thus, the template requirements for hemicarceplex 4 . guest are more stringent because the two howls can, in principle, misalign. We have found that despite these differences, the same template effect holds. We conclude that the same forces are at play in each reaction. These forces include 1) favorable van der Waals interactions between the template molecule and the forming cavity of the carceplex or hemicarceplex 2) unfavorable steric strain being imparted to the complex and 3) hydrogen bonds between the bowls. We also demonstrate the utility of matrix-assisted laser desorption ionization (MALDI) as a mild mass spectrometric technique for non-volatile organic compounds and complexes.},
	keywords = {4 PORTALS, BINDING, CAPTURE, CARCERANDS, CONSTRICTIVE, HOST-GUEST COMPLEXATION, LASER DESORPTION IONIZATION, MASS-SPECTROMETRY, POLYMERS, RECOGNITION, RELEASE},
	isbn = {1061-0278},
	url = {<Go to ISI>://A1995RX09600007},
	author = {Chopra, N. and Sherman, J. C.}
}
@article {3006,
	title = {DIOXYGEN AND CARBON-MONOXIDE BINDING TO APOLAR CYCLOPHANE HEMES - DURENE-CAPPED HEMES},
	journal = {Journal of the American Chemical Society},
	volume = {116},
	number = {1},
	year = {1994},
	note = {ISI Document Delivery No.: MT212Times Cited: 40Cited Reference Count: 48},
	month = {Jan},
	pages = {6-14},
	type = {Article},
	abstract = {Detailed solution kinetic and equilibria data (mainly in toluene) are presented for the reversible binding of CO and O2 to the five-coordinate hemes Fe(por)B, where B is 1,5-dicyclohexylimidazole or 1,2-dimethylimidazole (chosen to mimic the R- and T-states, respectively) and por = the dianion of some durene-capped porphyrins with variable length linking methylene straps on either side of the durene moiety (4/4, 5/5, or 7/7 methylenes). Use of spectrophotometric equilibrium titrations from 30 to -50-degrees-C, stopped-flow data, and laser flash photolysis under either CO or CO/O2 mixtures, has allowed for determination of on and off rates, equilibrium constants, and, in the case of the 4/4-system, thermodynamic constants for the binding. Increasing steric hindrance provided by the durene cap, in the order 7/7 < 5/5 < 4/4, is generally less than expected from studies with other heme derivatives; in combination with the complete absence of polarity effects, as within nonpolar distal sites, the durene hemes exhibit poor differentiation between CO and O2. However, the distorted 4/4-derivative discriminates between CO and O2 in a novel way through a {\textquoteright}{\textquoteright}proximal effect{\textquoteright}{\textquoteright} associated with deformation of the porphyrin skeleton from planarity, the effect being largely reflected by an increased CO dissociation rate.},
	keywords = {BINDING, CO, CRYSTAL-STRUCTURE, FREE-BASE, HEMOGLOBIN, IRON(II) PORPHYRINS, LIGAND-BINDING, O-2, O2 BINDING, SPERM WHALE, T-STATE},
	isbn = {0002-7863},
	url = {<Go to ISI>://A1994MT21200002},
	author = {David, S. and James, Brian R. and Dolphin, D. and Traylor, T. G. and Lopez, M. A.}
}
@article {7358,
	title = {MONOMER AND EXCIMER FLUORESCENCE OF HORSE PLASMA GELSOLIN LABELED WITH N-(1-PYRENYL)IODOACETAMIDE},
	journal = {Biochemistry and Cell Biology-Biochimie Et Biologie Cellulaire},
	volume = {70},
	number = {7},
	year = {1992},
	note = {ISI Document Delivery No.: JP667Times Cited: 3Cited Reference Count: 27},
	month = {Jul},
	pages = {573-578},
	type = {Article},
	abstract = {Horse plasma gelsolin was labelled with the sulfhydryl-specific fluorescent reagent N-(1-pyrenyl)iodoacetamide. The level of incorporation of probe was 1.6 +/- 0.3 mol pyrene/mol gelsolin. The circular dichroism spectrum of pyrenyl-gelsolin and its ability to interact with muscle actin were not different from that found for unmodified gelsolin. The emission from pyrenyl-gelsolin was dominated by a broad emission band centred near 483 nm, characteristic of the presence of pyrene excimers. Analysis of excitation spectra for the monomer and excimer-type fluorescence suggested that ground-state interactions may occur between adjacent pyrenes in the gelsolin structure. In the case either of excimer formation or of ground-state pyrene-pyrene interactions in doubly labelled gelsolin molecules, the modified Cys residues must be in close proximity in the folded protein structure. Thermal denaturation of gelsolin could be monitored by observing the decrease in excimer emission that accompanied heating and unfolding of the tertiary structure. While heat treatment alone did not eliminate excimer fluorescence, digestion of gelsolin with chymotrypsin completely abolished such emission. Also, pyrenyl-gelsolin prepared and studied in 6 M guanidine-HCl exhibited fluorescence characteristic of pyrene monomers exclusively.},
	keywords = {ACTIN-FILAMENTS, BINDING, CIRCULAR-DICHROISM, denaturation, FLUORESCENCE LIFETIME, gelsolin, POLYMERIZATION, PROBE, PROTEIN, PYRENE EXCIMER FLUORESCENCE, PYRENE-ACTIN, STATE, thermal, TROPOMYOSIN},
	isbn = {0829-8211},
	url = {<Go to ISI>://A1992JP66700008},
	author = {Silva, B. E. R. and Koepf, E. K. and Burtnick, L. D. and Turro, N. J.}
}
@article {7369,
	title = {SYNTHESIS AND CHARACTERIZATION OF DERIVATIZED CAPPED PORPHYRINS},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {70},
	number = {5},
	year = {1992},
	note = {ISI Document Delivery No.: JL870Times Cited: 4Cited Reference Count: 31},
	month = {May},
	pages = {1366-1374},
	type = {Article},
	abstract = {{The syntheses of porphyrins carrying either a fully hydrophobic cavity with a benzene moiety (32a,b) or a polar cavity with an amidobenzene (32c-d) are described. Terephthaldehyde (1) was converted to benzene-bisalkanoic acids (8, 10) and nitrobenzene-bisalkanoic acids (13 and 16) by using standard methods. The corresponding diacid chlorides 17a-d were used to acylate two equivalents of a beta-unsubstituted pyrrole, and the ketonic groups were reduced by diborane. Following the transformation of the nitro function to the acetamide, appropriate modifications of the ethyl ester functions afforded the key bisformylpyrroles 25a-d. The cyanoacrylate-protected formyl pyrrole derivatives were mono-chlorinated at the alpha-methyl groups and condensed with two equivalents of an alpha-unsubstitutued pyrrole to give the dipyrromethane dimers. Strong aqueous alkali caused saponification of the two ester groups and deprotection of the formyl functions to produce the dipyrromethane dimer 30, which, after thermal decarboxylation, was cyclized intramolecularly in acidic medium to give the porphyrins 32 (n = 4 or 5},
	keywords = {BINDING, CO, HUMAN OXYHEMOGLOBIN, IRON(II), O-2, RESOLUTION, STEREOCHEMISTRY},
	isbn = {0008-4042},
	url = {<Go to ISI>://A1992JL87000017},
	author = {Tang, H. and Wijesekera, T. P. and Dolphin, D.}
}
@article {6992,
	title = {HYBRIDIZATION OF RABBIT CARDIAC TROPOMYOSIN WITH NONPOLYMERIZABLE TROPOMYOSIN SPECIES},
	journal = {Biochemistry International},
	volume = {23},
	number = {4},
	year = {1991},
	note = {ISI Document Delivery No.: FR332Times Cited: 0Cited Reference Count: 19},
	month = {Mar},
	pages = {801-807},
	type = {Article},
	keywords = {ALPHA-TROPOMYOSIN, AMINO-ACID-SEQUENCE, BETA-TROPOMYOSIN, BINDING, EQUINE PLATELET TROPOMYOSIN, EXCIMER FLUORESCENCE, F-ACTIN, MUSCLE},
	isbn = {0158-5231},
	url = {<Go to ISI>://A1991FR33200022},
	author = {Clark, I. D. and Burtnick, L. D.}
}
@article {7110,
	title = {INTERACTION OF HORSE PLASMA GELSOLIN WITH THE HYDROPHOBIC FLUORESCENT-PROBE 2-(N-METHYLANILINO)NAPHTHALENE-6-SULFONIC ACID},
	journal = {Biochemistry International},
	volume = {23},
	number = {5},
	year = {1991},
	note = {ISI Document Delivery No.: FR334Times Cited: 2Cited Reference Count: 15},
	month = {Mar},
	pages = {905-913},
	type = {Article},
	keywords = {2-AMINONAPHTHALENE-6-SULFONATE, actin, BINDING, Electronic spectra, MOLECULES, PROTEIN},
	isbn = {0158-5231},
	url = {<Go to ISI>://A1991FR33400011},
	author = {Silva, B. E. R. and Burtnick, L. D. and Turro, N. J.}
}
