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Journal articles on the topic 'Fluorophosphine ligands'

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Author: Grafiati

Published: 10 March 2023

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1

Peterson, Louis K., and Shangjun Huang. "Preferential displacement of fluorophosphine ligands from fluorophosphinetungstencarbonyl complexes by reaction with trimethylamine oxide." Inorganica Chimica Acta 203, no. 1 (January 1993): 87–91. http://dx.doi.org/10.1016/s0020-1693(00)82909-6.

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2

Bell, Graeme A., and David W. H. Rankin. "Instant ligands. Part 1. Preparation of some bidentate fluorophosphine ligands derived from straight chain organic substrates, and their reactions to form molybdenum complexes." Journal of the Chemical Society, Dalton Transactions, no. 8 (1986): 1689. http://dx.doi.org/10.1039/dt9860001689.

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3

Fey, Natalie, Michael Garland, Jonathan P. Hopewell, Claire L. McMullin, Sergio Mastroianni, A. Guy Orpen, and Paul G. Pringle. "Stable Fluorophosphines: Predicted and Realized Ligands for Catalysis." Angewandte Chemie 124, no. 1 (November 11, 2011): 122–26. http://dx.doi.org/10.1002/ange.201105954.

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4

Fey, Natalie, Michael Garland, Jonathan P. Hopewell, Claire L. McMullin, Sergio Mastroianni, A. Guy Orpen, and Paul G. Pringle. "Stable Fluorophosphines: Predicted and Realized Ligands for Catalysis." Angewandte Chemie International Edition 51, no. 1 (November 11, 2011): 118–22. http://dx.doi.org/10.1002/anie.201105954.

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5

Miles-Hobbs, Alexandra M., Eliza Hunt, Paul G. Pringle, and Hazel A. Sparkes. "Ring size effects in cyclic fluorophosphites: ligands that span the bonding space between phosphites and PF3." Dalton Transactions 48, no. 26 (2019): 9712–24. http://dx.doi.org/10.1039/c9dt00893d.

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6

Schwierking, Jake R., Laird W. Menzel, and E. Roland Menzel. "Organophosphate Nerve Agent Detection with Europium Complexes." Scientific World JOURNAL 4 (2004): 948–55. http://dx.doi.org/10.1100/tsw.2004.194.

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We explore the detection of paraoxon, a model compound for nonvolatile organophosphate nerve agents such as VX. The detection utilizes europium complexes with 1,10 phenanthroline and thenoyltrifluoroacetone as sensitizing ligands. Both europium luminescence quenching and luminescence enhancement modalities are involved in the detection, which is simple, rapid, and sensitive. It is adaptable as well to the more volatile fluorophosphate nerve agents. It involves nothing more than visual luminescence observation under sample illumination by an ordinary hand-held ultraviolet lamp.

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7

Ibrahim, Malek Y. S., Jeffrey A. Bennett, Dawn Mason, Jody Rodgers, and Milad Abolhasani. "Flexible homogeneous hydroformylation: on-demand tuning of aldehyde branching with a cyclic fluorophosphite ligand." Journal of Catalysis 409 (May 2022): 105–17. http://dx.doi.org/10.1016/j.jcat.2022.03.030.

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8

Schumann, Hans, and Liliana Eguren. "Synthese neuer Phosphan- und Fluorophosphankomplexe durch Ligandmodifikation in der Koordinationssphäre von kationischen Cyclopentadienyleisen-bis(phosphan)-Komplexen / Synthesis of New Phosphane and Fluorophosphane Complexes by Ligand Modification in the Coordination Sphere of Cationic Cyclopentadienyliron Bis(phosphane) Complexes." Zeitschrift für Naturforschung B 46, no. 7 (July 1, 1991): 887–95. http://dx.doi.org/10.1515/znb-1991-0707.

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The reaction of nitrile solvate complexes [(C5H5)(P(OCH3)3)2(NCCH3)Fe]PF6 (Ia) and [(C5H5)(DPPE)(NCCH3)Fe]PF6 (Ib, DPPE = [(C6H5)2PCH2]2) with halogenophosphanes, -arsines or -stibines L′ afford the cationic complexes [(C5H5)(L2)(L′)Fe]PF6 (II, L2 = (P(OCH3)3)2, L′ = PCl3, P(CH3)Cl2, P(t-C4H9)Cl2, P(C6H5)Cl2, P(C6H5)2Cl, PBr3, AsCl3, SbCl3; III, L2 = DPPE, L′ = PCl3, AsCl3, SbCl3) in high yield. Spectroscopic data are given together with the characterization of [(C5H5)(P(OCH3)3)2(P(t-C4H9)Cl2)Fe]PF6 (IIc) by single crystals X-ray diffraction analysis. Through reduction of coordinated P– Cl ligands in selected complexes II and III complexes bearing PH3, P(C6H5)H2 and P(C6H5)2H ligands are available. With anhydrous KF in acetonitrile solution in the presence of dibenzo-18-crown-6, the coordinated P– Cl ligands in selected complexes II and HIII undergo Cl/F-exchange with formation of related complexes with P(CH3)ClF, P(CH3)F2, PF2Cl and PF3 ligands.

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9

Cunningham, Allan F., and E. Peter Kuendig. "An efficient synthesis of both enantiomers of trans-1,2-cyclopentanediol and their conversion to two novel bidentate phosphite and fluorophosphinite ligands." Journal of Organic Chemistry 53, no. 8 (April 1988): 1823–25. http://dx.doi.org/10.1021/jo00243a048.

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10

COHEN, Ofer, Chanoch KRONMAN, Theodor CHITLARU, Arie ORDENTLICH, Baruch VELAN, and Avigdor SHAFFERMAN. "Effect of chemical modification of recombinant human acetylcholinesterase by polyethylene glycol on its circulatory longevity." Biochemical Journal 357, no. 3 (July 25, 2001): 795–802. http://dx.doi.org/10.1042/bj3570795.

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Post-translational modifications were recently shown to be responsible for the short circulatory mean residence time (MRT) of recombinant human acetylcholinesterase (rHuAChE) [Kronman, Velan, Marcus, Ordentlich, Reuveny and Shafferman (1995) Biochem. J. 311, 959–967; Chitlaru, Kronman, Zeevi, Kam, Harel, Ordentlich, Velan and Shafferman (1998) Biochem. J. 336, 647–658; Chitlaru, Kronman, Velan and Shafferman (2001) Biochem. J. 354, 613–625], which is one of the major obstacles to the fulfilment of its therapeutic potential as a bioscavenger. In the present study we demonstrate that the MRT of rHuAChE can be significantly increased by the controlled attachment of polyethylene glycol (PEG) side chains to lysine residues. Attachment of as many as four PEG molecules to monomeric rHuAChE had minimal effects, if any, on either the catalytic activity (Km = 0.09mM and kcat = 3.9×105min−1) or the reactivity of the modified enzyme towards active-centre inhibitors, such as edrophonium and di-isopropyl fluorophosphate, or to peripheral-site ligands, such as propidium, BW284C51 and even the bulky snake-venom toxin fasciculin-II. The increase in MRT of the PEG-modified monomeric enzyme is linearly dependent, in the tested range, on the number of attached PEG molecules, as well as on their size. It appears that even low level PEG-conjugation can overcome the deleterious effect of under-sialylation on the pharmacokinetic performance of rHuAChE. At the highest tested ratio of attached PEG-20000/rHuAChE (4:1), an MRT of over 2100min was attained, a value unmatched by any other known form of recombinant or native serum-derived AChE reported to date.

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11

Schick, B., and K. F. Austen. "Rat serosal mast cell degranulation mediated by chymase, an endogenous secretory granule protease: active site-dependent initiation at 1 degree C." Journal of Immunology 136, no. 10 (May 15, 1986): 3812–18. http://dx.doi.org/10.4049/jimmunol.136.10.3812.

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Abstract Exposure at 37 degrees C of rat serosal mast cells (RSMC) to chymase, an endogenous secretory granule serine protease, results in exocytosis as determined by the release of another secretory granule enzyme, beta-hexosaminidase. Chymase-mediated RSMC degranulation does not occur at 1 degree C; however, exposure of RSMC to chymase at 1 degree C followed by the removal of buffer and the resuspension of the cells in buffer alone at 37 degrees C results in exocytosis equivalent to that obtained by direct exposure of RSMC to chymase at 37 degrees C. Maximal chymase-mediated RSMC degranulation at 37 degrees C is Ca2+-dependent and Mg2+-independent. The dose-dependent degranulation-inducing interaction of chymase and alpha-chymotrypsin with RSMC at 1 degree C is Ca2+-independent, whereas subsequent exocytosis at 37 degrees C in new buffer without added enzyme still requires Ca2+. Specific binding of 125I-labeled alpha-chymotrypsin to RSMC does not occur at 1 degree C, implying that the inducing action of chymase is not a simple ligand-receptor binding. The enzyme inhibitors diisopropyl fluorophosphate and lima bean trypsin inhibitor inhibit subsequent exocytosis at 37 degrees C only if they are added within the first 10 min of the interaction of RSMC and chymase at 1 degree C, implying that an active site-dependent inducing event occurs between RSMC and chymase at 1 degree C. Thus, chymase-induced coupled activation-secretion can be divided into a cation- and temperature-independent initiation phase, which is dependent on the active site of exogenously added chymase and a subsequent temperature-dependent and calcium-augmented cellular secretion phase.

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12

Plesner, T., M. Ploug, V. Ellis, E. Ronne, G. Hoyer-Hansen, M. Wittrup, TL Pedersen, T. Tscherning, K. Dano, and NE Hansen. "The receptor for urokinase-type plasminogen activator and urokinase is translocated from two distinct intracellular compartments to the plasma membrane on stimulation of human neutrophils." Blood 83, no. 3 (February 1, 1994): 808–15. http://dx.doi.org/10.1182/blood.v83.3.808.808.

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Abstract The cellular receptor for urokinase-type plasminogen activator (uPAR) binds pro-urokinase (pro-uPA) and facilitates its conversion to enzymatically active urokinase (uPA). uPA in turn activates surface-bound plasminogen to plasmin, a process of presumed importance for a number of biologic processes including cell migration and resolution of thrombi. We have previously shown that uPAR is expressed on the plasma membrane of circulating neutrophils, and we now report that stimulation with phorbol myristate acetate (PMA), FMLP, or tumor necrosis factor-alpha results in a rapid increase in the expression of uPAR. This process is accompanied by an increased cell-associated plasminogen activation after preincubation of neutrophils with pro-uPA in vitro. By subcellular fractionation of unstimulated neutrophils, 50% of uPAR is recovered in fractions containing latent alkaline phosphatase, corresponding to an intracellular compartment of easily mobilizable secretory vesicles distinct from both primary and specific granules, whereas the remaining 50% of uPAR is associated with a compartment eluting close to the specific granules. In contrast, the ligand pro-uPA is primarily (approximately 80%) found in the specific granules, but small amounts of pro-uPA/uPA (approximately 20%) coelute with latent alkaline phosphatase. Stimulation of neutrophils with FMLP results in translocation of uPAR as well as of pro-uPA from the secretory vesicles, whereas stimulation with PMA is required to translocate material from specific granules. Flow cytometry of neutrophils saturated with exogenous diisopropyl fluorophosphate-uPA shows a large excess (approximately 90%) of unoccupied uPAR on resting as well as FMLP- and PMA-stimulated neutrophils, suggesting a possible role for exogenous pro-uPA in providing neutrophils with a potential for plasminogen activation. These processes may be important for neutrophil extravasation and migration through extracellular matrix and for the contribution of neutrophils to resolution of thrombi.

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13

Plesner, T., M. Ploug, V. Ellis, E. Ronne, G. Hoyer-Hansen, M. Wittrup, TL Pedersen, T. Tscherning, K. Dano, and NE Hansen. "The receptor for urokinase-type plasminogen activator and urokinase is translocated from two distinct intracellular compartments to the plasma membrane on stimulation of human neutrophils." Blood 83, no. 3 (February 1, 1994): 808–15. http://dx.doi.org/10.1182/blood.v83.3.808.bloodjournal833808.

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The cellular receptor for urokinase-type plasminogen activator (uPAR) binds pro-urokinase (pro-uPA) and facilitates its conversion to enzymatically active urokinase (uPA). uPA in turn activates surface-bound plasminogen to plasmin, a process of presumed importance for a number of biologic processes including cell migration and resolution of thrombi. We have previously shown that uPAR is expressed on the plasma membrane of circulating neutrophils, and we now report that stimulation with phorbol myristate acetate (PMA), FMLP, or tumor necrosis factor-alpha results in a rapid increase in the expression of uPAR. This process is accompanied by an increased cell-associated plasminogen activation after preincubation of neutrophils with pro-uPA in vitro. By subcellular fractionation of unstimulated neutrophils, 50% of uPAR is recovered in fractions containing latent alkaline phosphatase, corresponding to an intracellular compartment of easily mobilizable secretory vesicles distinct from both primary and specific granules, whereas the remaining 50% of uPAR is associated with a compartment eluting close to the specific granules. In contrast, the ligand pro-uPA is primarily (approximately 80%) found in the specific granules, but small amounts of pro-uPA/uPA (approximately 20%) coelute with latent alkaline phosphatase. Stimulation of neutrophils with FMLP results in translocation of uPAR as well as of pro-uPA from the secretory vesicles, whereas stimulation with PMA is required to translocate material from specific granules. Flow cytometry of neutrophils saturated with exogenous diisopropyl fluorophosphate-uPA shows a large excess (approximately 90%) of unoccupied uPAR on resting as well as FMLP- and PMA-stimulated neutrophils, suggesting a possible role for exogenous pro-uPA in providing neutrophils with a potential for plasminogen activation. These processes may be important for neutrophil extravasation and migration through extracellular matrix and for the contribution of neutrophils to resolution of thrombi.

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14

BELL, G. A., and D. W. H. RANKIN. "ChemInform Abstract: Instant Ligands. Part 1. Preparation of Some Bidentate Fluorophosphine Ligands Derived from Straight Chain Organic Substrates, and Their Reactions to Form Molybdenum Complexes." Chemischer Informationsdienst 17, no. 51 (December 23, 1986). http://dx.doi.org/10.1002/chin.198651258.

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15

CUNNINGHAM, A. F. JUN, and E. P. KUENDIG. "ChemInform Abstract: An Efficient Synthesis of Both Enantiomers of trans-1,2-Cyclopentanediol and Their Conversion to Two Novel Bidentate Phosphite and Fluorophosphinite Ligands." ChemInform 19, no. 41 (October 11, 1988). http://dx.doi.org/10.1002/chin.198841246.

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