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397 results on '"Bishop, G."'

5. The thermal architecture of the ESA ARIEL payload at the end of phase B1

Author

Morgante, G., Terenzi, L., Desjonqueres, L., Eccleston, P., Bishop, G., Caldwell, A., Crook, M., Drummond, R., Hills, M., Hunt, T., Rust, D., Puig, L., Tirolien, T., Focardi, M., Zuppella, P., Holmes, W., Amiaux, J., Czupalla, M., Rataj, M., Jessen, N. C., Pedersen, S. M., Pascale, E., Pace, E., Malaguti, G., and Micela, G.

Published
2022
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7. Characterizing Foxp3+ and Foxp3- T cells in the homeostatic state and after allo-activation: resting CD4+Foxp3+ Tregs have molecular characteristics of activated T cells.

Author

Zilei Liu, Baines, Katherine J., Niessen, Natalie M., Heer, Munish K., Clark, David, Bishop, G. Alexander, and Trevillian, Paul R.

Subjects
T cells, REGULATORY T cells, BIOMARKERS, GENE expression, CYTOTOXIC T lymphocyte-associated molecule-4
Abstract

Due to the intracellular expression of Foxp3 it is impossible to purify viable Foxp3+ cells on the basis of Foxp3 staining. Consequently CD4+Foxp3+ regulatory T cells (Tregs) in mice have mostly been characterized using CD4+CD25+ T cells or GFPFoxp3 reporter T cells. However, these two populations cannot faithfully represent Tregs as the expression of CD25 and Foxp3 does not completely overlap and GFP+Foxp3+ reporter T cells have been reported to be functionally altered. The aim of this study was to characterize normal Tregs without separating Foxp3+ and Foxp3-cells for the expression of themain functional molecules and proliferation behaviors by flow cytometry and to examine their gene expression characteristics through differential gene expression. Our data showed that the expressions of Foxp3, CD25, CTLA-4 (both intracellular and cell surface) and PD-1 wasmostly confined to CD4+ T cells and the expression of Foxp3 did not completely overlap with the expression of CD25, CTLA-4 or PD-1. Despite higher levels of expression of the T cell inhibitory molecules CTLA-4 and PD-1, Tregs maintained higher levels of Ki-67 expression in the homeostatic state and had greater proliferation in vivo after allo-activation than Tconv. Differential gene expression analysis revealed that resting Tregs exhibited immune activation markers characteristic of activated Tconv. This is consistent with the flow data that the T cell activation markers CD25, CTLA-4, PD-1, and Ki-67 were much more strongly expressed by Tregs than Tconv in the homeostatic state. [ABSTRACT FROM AUTHOR]

Published
2024
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9. The ARIEL Instrument Control Unit design: For the M4 Mission Selection Review of the ESA’s Cosmic Vision Program

Author

Focardi, M., Pace, E., Farina, M., Di Giorgio, A. M., Ferrer, J. Colomé, Ribas, I., Roig, C. Sierra, Bote, L. Gesa, Morales, J. C., Amiaux, J., Cara, C., Augurés, J. L., Pascale, E., Morgante, G., Da Deppo, V., Pancrazzi, M., Noce, V., Pezzuto, S., Frericks, M., Zwart, F., Bishop, G., Middleton, K., Eccleston, P., Micela, G., and Tinetti, G.

Published
2018
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15. Conrad and the Reviewers: "The Secret Agent" on Stage

Author

Hand, Richard J., Charlton, Randall, Conrad, Joseph, Morrison, G. E., Titterton, W. R., Littlewood, S. R., Cowen, Louis, FARJEON, HERBERT, Carroll, S. W., Bishop, G. W., Grein, J. T., Francis, René, and Moult, Thomas

Published
2001

32. Triplex selective 2-(2-naphthyl)quinoline compounds: origins of affinity and new design principles

Author

Chaires, Jonathan B., Ren, Jinsong, Henary, Maged, Zegrocka, Oliwia, Bishop, G. Reid, and Strekowski, Lucjan

Subjects
Nucleic acids -- Structure, Nucleic acids -- Research, Dialysis -- Usage, Chemistry
Abstract

A study was conducted on the interaction of 14 compounds with 13 different nucleic acid sequences and structures. Quantitative analysis of the competition dialysis binding data using newly developed metrics revealed that these compounds were among the most selective triple-binding agents synthesized to date.

Published
2003

36. Electron transfer from the aminosemiquinone reaction intermediate of methylamine dehydrogenase to amicyanin

Author

Bishop, G. Reid and Davidson, Victor L.

Subjects
Oxidation-reduction reaction -- Research, Chemical reactions -- Research, Proteins -- Research, Biological sciences, Chemistry
Abstract

A thorough analysis was conducted to study the electron transfer reaction from the N-semiquinone methylamine deghydrogenase reaction intermediate to amicyanin. It will be shown that the integration of the substrate-derived N into tryptophan tryptophylquinone influences the rate of the electron transfer reaction from the N-semiquinone relative to the O-semiquinone by transforming the driving force for the electron transfer reaction.

Published
1998

38. Catalytic role of monovalent cations in the mechanism of proton transfer which gates an interprotein electron transfer reaction

Author

Bishop, G. Reid and Davidson, Victor L.

Subjects
Cations -- Research, Catalysis -- Research, Oxidation-reduction reaction -- Research, Electron transport -- Research, Biological sciences, Chemistry
Abstract

The nature of the rate-limiting proton transfer step which gates an intermolecular electron transfer from N-quinol tryptophan tryptophylquinone of methylamine dehydrogenase to amicyanin was investigated. Specifically, the role of monovalent cations in the mechanism of proton transfer was examined. Results showed that the rate of proton transfer is catalyzed by pH and monovalent cations and that proton transfer is rate-limiting for the interprotein electron transfer reaction over a certain range of both pH and monovalent cation concentrations.

Published
1997

39. Evidence for a tryptophan tryptophylquinone aminosemiquinone intermediate in the physiologic reaction between methylamine dehydrogenase and amicyanin

Author

Bishop, G. Reid, Brooks, Harold B., and Davidson, Victor L.

Subjects
Quinone -- Physiological aspects, Chemical reaction, Rate of -- Physiological aspects, Dehydrogenases -- Research, Biological sciences, Chemistry
Abstract

The complete oxidation of the substrate-reduced enzyme N-quinol methylamine dehydrogenase (MADH) yields N-semiquinone which is a physiologically significant reaction intermediate. The enzyme is oxidized in two sequential one-electron steps by amicyanin. Amicyanin oxidizes another form of this enzyme, O-quinol MADH, through similar one-electron steps. The rate of reaction between N-semiquinone and amicyanin is slower than the reaction rate between O-semiquinone and amicyanin. This results in an accumulation of N-semiquinone, whereas the intermediate O-semiquinone does not accumulate.

Published
1996

43. Intermolecular electron transfer from substrate-reduced methylamine dehydrogenase to amicyanin is linked to proton transfer

Author

Bishop, G. Reid and Davidson, Victor L.

Subjects
Electron transport -- Observations, Dehydrogenases -- Analysis, Biological sciences, Chemistry
Abstract

The intermolecular electron transfer (ET) among tryptophan tryptophylquinone (TTQ) and copper takes place in the methylamine dehydrogenase-amicyanin complex. For the redox system of quinol TTQ and copper, the ET process is the rate limiting step. The proton transfer occurs during the rate-limiting step of ET from the substrate-reduced enzyme as obtained from by the solvent kinetic isotope effect studies.

Published
1995

48. Antecedents to hospital deaths

Author

HILLMAN, K. M., BRISTOW, P. J., CHEY, T., DAFFURN, K., JACQUES, T., NORMAN, S. L., BISHOP, G. F., and SIMMONS, G.

Published
2001

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